ID ANK1_HUMAN Reviewed; 1881 AA. AC P16157; A0PJN8; A6NJ23; E5RFL7; O43400; Q13768; Q53ER1; Q59FP2; Q8N604; AC Q99407; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 02-SEP-2026, entry version 252. DE RecName: Full=Ankyrin-1 {ECO:0000305}; DE Short=ANK-1; DE AltName: Full=Ankyrin-R; DE AltName: Full=Erythrocyte ankyrin; GN Name=ANK1 {ECO:0000312|HGNC:HGNC:492}; Synonyms=ANK; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ER1 AND ER2), PROTEIN SEQUENCE OF RP 3-30; 733-753; 828-871; 959-1003; 1106-1128; 1149-1168; 1282-1288; RP 1345-1367; 1383-1427; 1601-1626; 1686-1700 AND 1763-1772, AND VARIANTS RP ALA-750 AND ILE-1075. RC TISSUE=Hematopoietic; RX PubMed=2137557; DOI=10.1038/344036a0; RA Lux S.E., John K.M., Bennett V.; RT "Analysis of cDNA for human erythrocyte ankyrin indicates a repeated RT structure with homology to tissue-differentiation and cell-cycle control RT proteins."; RL Nature 344:36-42(1990). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ER1; ER5 AND ER16), AND VARIANTS RP ILE-1075 AND ILE-1546. RX PubMed=1689849; DOI=10.1073/pnas.87.5.1730; RA Lambert S., Yu H., Prchal J.T., Lawler J., Ruff P., Speicher D., RA Cheung M.C., Kan Y.W., Palek J.; RT "cDNA sequence for human erythrocyte ankyrin."; RL Proc. Natl. Acad. Sci. U.S.A. 87:1730-1734(1990). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, AND VARIANTS RP LEU-991 AND ILE-1075. RX PubMed=9235914; DOI=10.1074/jbc.272.31.19220; RA Gallagher P.G., Tse W.T., Scarpa A.L., Lux S.E., Forget B.G.; RT "Structure and organization of the human ankyrin-1 gene. Basis for RT complexity of pre-mRNA processing."; RL J. Biol. Chem. 272:19220-19228(1997). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS MU17; MU18; MU19 AND MU20), TISSUE RP SPECIFICITY, AND SUBCELLULAR LOCATION. RC TISSUE=Skeletal muscle; RX PubMed=9430667; DOI=10.1074/jbc.273.3.1339; RA Gallagher P.G., Forget B.G.; RT "An alternate promoter directs expression of a truncated, muscle-specific RT isoform of the human ankyrin 1 gene."; RL J. Biol. Chem. 273:1339-1348(1998). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BR21), AND VARIANT RP ILE-1075. RC TISSUE=Brain; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., RA Ohara O., Nagase T., Kikuno R.F.; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16421571; DOI=10.1038/nature04406; RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., RA Platzer M., Shimizu N., Lander E.S.; RT "DNA sequence and analysis of human chromosome 8."; RL Nature 439:331-335(2006). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS MU17; 22 AND 23). RC TISSUE=B-cell, and Skeletal muscle; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP PROTEIN SEQUENCE OF 5-12; 403-422; 797-814; 862-877 AND 899-912, DOMAINS RP SPTB AND SLC4A1 BINDING, AND VARIANT ASP-1286. RX PubMed=2141335; DOI=10.1016/s0021-9258(18)86987-3; RA Davis L.H., Bennett V.; RT "Mapping the binding sites of human erythrocyte ankyrin for the anion RT exchanger and spectrin."; RL J. Biol. Chem. 265:10589-10596(1990). RN [10] RP PROTEIN SEQUENCE OF 99-110; 129-169 AND 233-248, INTERACTION WITH HIF1AN, RP AND HYDROXYLATION AT ASN-105; ASN-233; ASN-431; ASN-464; ASN-629; ASN-662; RP ASP-695; ASN-728 AND ASN-761. RX PubMed=21177872; DOI=10.1074/jbc.m110.193540; RA Yang M., Ge W., Chowdhury R., Claridge T.D., Kramer H.B., Schmierer B., RA McDonough M.A., Gong L., Kessler B.M., Ratcliffe P.J., Coleman M.L., RA Schofield C.J.; RT "Asparagine and aspartate hydroxylation of the cytoskeletal ankyrin family RT is catalyzed by factor-inhibiting hypoxia-inducible factor."; RL J. Biol. Chem. 286:7648-7660(2011). RN [11] RP INTERACTION WITH SLC4A1. RX PubMed=7665627; DOI=10.1074/jbc.270.37.22050; RA Michaely P., Bennett V.; RT "The ANK repeats of erythrocyte ankyrin form two distinct but cooperative RT binding sites for the erythrocyte anion exchanger."; RL J. Biol. Chem. 270:22050-22057(1995). RN [12] RP INTERACTION WITH TTN. RX PubMed=12444090; DOI=10.1074/jbc.m209012200; RA Kontrogianni-Konstantopoulos A., Bloch R.J.; RT "The hydrophilic domain of small ankyrin-1 interacts with the two N- RT terminal immunoglobulin domains of titin."; RL J. Biol. Chem. 278:3985-3991(2003). RN [13] RP SUBCELLULAR LOCATION, INTERACTION WITH OBSCN, MUTAGENESIS OF THR-1824; RP LYS-1826; ARG-1829 AND LYS-1830, AND FUNCTION. RX PubMed=12527750; DOI=10.1083/jcb.200208109; RA Bagnato P., Barone V., Giacomello E., Rossi D., Sorrentino V.; RT "Binding of an ankyrin-1 isoform to obscurin suggests a molecular link RT between the sarcoplasmic reticulum and myofibrils in striated muscles."; RL J. Cell Biol. 160:245-253(2003). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Platelet; RX PubMed=18088087; DOI=10.1021/pr0704130; RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., RA Schuetz C., Walter U., Gambaryan S., Sickmann A.; RT "Phosphoproteome of resting human platelets."; RL J. Proteome Res. 7:526-534(2008). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-429; SER-759; SER-781; RP SER-856; THR-1378; THR-1380; SER-1396; SER-1486; SER-1666; SER-1671; RP SER-1686; SER-1690 AND SER-1696, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-781; SER-817; SER-834; RP SER-856; SER-1428; SER-1523 AND SER-1533, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [19] RP PROTEOLYTIC CLEAVAGE (MICROBIAL INFECTION). RX PubMed=29459732; DOI=10.1038/s41564-018-0111-0; RA Thomas J.A., Tan M.S.Y., Bisson C., Borg A., Umrekar T.R., Hackett F., RA Hale V.L., Vizcay-Barrena G., Fleck R.A., Snijders A.P., Saibil H.R., RA Blackman M.J.; RT "A protease cascade regulates release of the human malaria parasite RT Plasmodium falciparum from host red blood cells."; RL Nat. Microbiol. 3:447-455(2018). RN [20] {ECO:0007744|PDB:1N11} RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 402-827, AND FUNCTION OF ANK RP REPEAT DOMAIN. RX PubMed=12456646; DOI=10.1093/emboj/cdf651; RA Michaely P., Tomchick D.R., Machius M., Anderson R.G.; RT "Crystal structure of a 12 ANK repeat stack from human ankyrinR."; RL EMBO J. 21:6387-6396(2002). RN [21] RP STRUCTURE BY NMR OF 1392-1497. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the DEATH domain of ankyrin-1."; RL Submitted (APR-2008) to the PDB data bank. RN [22] {ECO:0007744|PDB:3UD1, ECO:0007744|PDB:3UD2} RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 911-1233, AND DOMAINS ZU5. RX PubMed=22310050; DOI=10.1016/j.jmb.2012.01.041; RA Yasunaga M., Ipsaro J.J., Mondragon A.; RT "Structurally similar but functionally diverse ZU5 domains in human RT erythrocyte ankyrin."; RL J. Mol. Biol. 417:336-350(2012). RN [23] {ECO:0007744|PDB:7UZQ, ECO:0007744|PDB:7UZU, ECO:0007744|PDB:7V0K, ECO:0007744|PDB:7V0M, ECO:0007744|PDB:7V0S, ECO:0007744|PDB:7V0X, ECO:0007744|PDB:8CS9, ECO:0007744|PDB:8CSL, ECO:0007744|PDB:8CSV, ECO:0007744|PDB:8CTE} RP STRUCTURE BY ELECTRON MICROSCOPY (2.17 ANGSTROMS) OF 1-201, FUNCTION, RP SUBUNIT, ANKYRIN-1 COMPLEX IDENTIFICATION, DOMAIN, AND INTERACTION WITH RP RHCE; AQP1; EPB42 AND SLC4A1. RX PubMed=35835865; DOI=10.1038/s41594-022-00792-w; RA Vallese F., Kim K., Yen L.Y., Johnston J.D., Noble A.J., Cali T., RA Clarke O.B.; RT "Architecture of the human erythrocyte ankyrin-1 complex."; RL Nat. Struct. Mol. Biol. 29:706-718(2022). RN [24] RP VARIANT SPH1 ILE-463. RX PubMed=8640229; DOI=10.1038/ng0696-214; RA Eber S.W., Gonzalez J.M., Lux M.L., Scarpa A.L., Tse W.T., Dornwell M., RA Herbers J., Kugler W., Oezcan R., Pekrun A., Gallagher P.G., Schroeter W., RA Forget B.G., Lux S.E.; RT "Ankyrin-1 mutations are a major cause of dominant and recessive hereditary RT spherocytosis."; RL Nat. Genet. 13:214-218(1996). RN [25] RP VARIANTS SPH1 ARG-276 AND THR-1054. RX PubMed=11102985; RX DOI=10.1002/1098-1004(200012)16:6<529::aid-humu13>3.0.co;2-n; RA Leite R.C.A., Basseres D.S., Ferreira J.S., Alberto F.L., Costa F.F., RA Saad S.T.O.; RT "Low frequency of ankyrin mutations in hereditary spherocytosis: RT identification of three novel mutations."; RL Hum. Mutat. 16:529-529(2000). RN [26] RP VARIANT [LARGE SCALE ANALYSIS] HIS-332. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Component of the ankyrin-1 complex, a multiprotein complex CC involved in the stability and shape of the erythrocyte membrane CC (PubMed:35835865). Attaches integral membrane proteins to cytoskeletal CC elements; binds to the erythrocyte membrane protein band 4.2, to Na-K CC ATPase, to the lymphocyte membrane protein GP85, and to the CC cytoskeletal proteins fodrin, tubulin, vimentin and desmin. Erythrocyte CC ankyrins also link spectrin (beta chain) to the cytoplasmic domain of CC the erythrocytes anion exchange protein; they retain most or all of CC these binding functions. {ECO:0000269|PubMed:12456646, CC ECO:0000269|PubMed:35835865}. CC -!- FUNCTION: [Isoform Mu17]: Together with obscurin in skeletal muscle may CC provide a molecular link between the sarcoplasmic reticulum and CC myofibrils. {ECO:0000269|PubMed:12527750}. CC -!- SUBUNIT: Component of the ankyrin-1 complex in the erythrocyte, CC composed of ANK1, RHCE, RHAG, SLC4A1, EPB42, GYPA, GYPB and AQP1 CC (PubMed:35835865). Interacts with a number of integral membrane CC proteins and cytoskeletal proteins. Interacts (via N-terminus) with CC SPTB/spectrin (beta chain). Also interacts with TTN/titin. Isoform Mu17 CC interacts with OBSCN isoform 3/obscurin. Interacts with HIF1AN. CC Interacts (via ANK 1-5 repeats) with RHCE; this interaction mediates CC the primary membrane attachment site for ANK1 (PubMed:35835865). CC Interacts (via ANK 1-2 repeats) with AQP1 (via the N-terminal) CC (PubMed:35835865). Interacts (via ANK 1-13 repeats) with EPB42 CC (PubMed:35835865). Interacts directly with SLC4A1 (via the cytoplasmic CC domain); this interaction is mediated by the SLC4A1 Band 3-II and Band CC 3-III dimers (PubMed:35835865, PubMed:7665627). CC {ECO:0000269|PubMed:12444090, ECO:0000269|PubMed:12527750, CC ECO:0000269|PubMed:21177872, ECO:0000269|PubMed:35835865, CC ECO:0000269|PubMed:7665627}. CC -!- INTERACTION: CC P16157; Q5VST9-3: OBSCN; NbExp=3; IntAct=EBI-941686, EBI-941921; CC P16157-17; P50402: EMD; NbExp=3; IntAct=EBI-941819, EBI-489887; CC P16157-17; P54849: EMP1; NbExp=3; IntAct=EBI-941819, EBI-4319440; CC P16157-17; Q14802-3: FXYD3; NbExp=3; IntAct=EBI-941819, EBI-12175685; CC P16157-17; Q8IXM6: NRM; NbExp=3; IntAct=EBI-941819, EBI-10262547; CC P16157-17; Q5VST9-3: OBSCN; NbExp=8; IntAct=EBI-941819, EBI-941921; CC P16157-17; Q8N0V3: RBFA; NbExp=3; IntAct=EBI-941819, EBI-3232108; CC P16157-17; Q5QGT7: RTP2; NbExp=3; IntAct=EBI-941819, EBI-10244780; CC P16157-17; Q8IWU4: SLC30A8; NbExp=3; IntAct=EBI-941819, EBI-10262251; CC P16157-17; P0DN84: STRIT1; NbExp=3; IntAct=EBI-941819, EBI-12200293; CC P16157-17; Q969S6: TMEM203; NbExp=3; IntAct=EBI-941819, EBI-12274070; CC -!- SUBCELLULAR LOCATION: [Isoform Er1]: Cytoplasm, cytoskeleton. CC Note=Probably the other erythrocyte (Er) isoforms, are located near the CC surface of erythrocytic plasma membrane. CC -!- SUBCELLULAR LOCATION: [Isoform Mu17]: Membrane. Cytoplasm, myofibril, CC sarcomere, M line. Note=Colocalizes with OBSCN isoform 3/obscurin at CC the M line in differentiated skeletal muscle cells. CC -!- SUBCELLULAR LOCATION: [Isoform Mu18]: Sarcoplasmic reticulum CC {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: [Isoform Mu19]: Sarcoplasmic reticulum CC {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: [Isoform Mu20]: Sarcoplasmic reticulum CC {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=23; CC Name=Er1; Synonyms=1, 2.1; CC IsoId=P16157-1; Sequence=Displayed; CC Name=Er2; Synonyms=2, 2.2; CC IsoId=P16157-4; Sequence=VSP_018442; CC Name=Er3; Synonyms=3; CC IsoId=P16157-5; Sequence=VSP_018449; CC Name=Er4; Synonyms=4; CC IsoId=P16157-6; Sequence=VSP_018442, VSP_018449; CC Name=Er5; Synonyms=5; CC IsoId=P16157-3; Sequence=VSP_000266; CC Name=Er6; Synonyms=6; CC IsoId=P16157-7; Sequence=VSP_018442, VSP_000266; CC Name=Er7; Synonyms=7; CC IsoId=P16157-8; Sequence=VSP_018447; CC Name=Er8; Synonyms=8; CC IsoId=P16157-9; Sequence=VSP_018442, VSP_018447; CC Name=Er9; Synonyms=9; CC IsoId=P16157-10; Sequence=VSP_018445; CC Name=Er10; Synonyms=10; CC IsoId=P16157-11; Sequence=VSP_018442, VSP_018445; CC Name=Er11; Synonyms=11; CC IsoId=P16157-12; Sequence=VSP_018450; CC Name=Er12; Synonyms=12; CC IsoId=P16157-13; Sequence=VSP_018442, VSP_018450; CC Name=Er13; Synonyms=13; CC IsoId=P16157-14; Sequence=VSP_018451; CC Name=Er14; Synonyms=14; CC IsoId=P16157-15; Sequence=VSP_018442, VSP_018451; CC Name=Er15; Synonyms=15; CC IsoId=P16157-16; Sequence=VSP_018448; CC Name=Er16; CC IsoId=P16157-2; Sequence=VSP_000264, VSP_000265; CC Name=Mu17; Synonyms=ank1.5, muscle-specific 1; CC IsoId=P16157-17; Sequence=VSP_018440, VSP_018443, VSP_000266; CC Name=Mu18; Synonyms=ank1.6, muscle-specific 2; CC IsoId=P16157-18; Sequence=VSP_018440, VSP_018443, VSP_018448; CC Name=Mu19; Synonyms=muscle-specific 3; CC IsoId=P16157-19; Sequence=VSP_018440, VSP_018443, VSP_018445; CC Name=Mu20; Synonyms=muscle-specific 4; CC IsoId=P16157-20; Sequence=VSP_018440, VSP_018444, VSP_018446; CC Name=Br21; CC IsoId=P16157-21; Sequence=VSP_018439, VSP_018441, VSP_018449; CC Name=22; CC IsoId=P16157-22; Sequence=VSP_018440, VSP_018443, VSP_045439; CC Name=23; CC IsoId=P16157-23; Sequence=VSP_018440, VSP_018443; CC -!- TISSUE SPECIFICITY: Isoform Mu17, isoform Mu18, isoform Mu19 and CC isoform Mu20 are expressed in skeletal muscle. Isoform Br21 is CC expressed in brain. {ECO:0000269|PubMed:9430667}. CC -!- DOMAIN: The 55 kDa regulatory domain is involved in regulating binding CC of SPTB/spectrin (beta chain) and SLC4A1/erythrocyte membrane protein CC band 3. CC -!- DOMAIN: The ANK repeat region forms a spiral around a large central CC cavity and is involved in binding of ion transporters. Adopts a T- CC shaped arrangement, in the ankyrin-1 complex, in which ANK 1-5 repeats CC are orthogonal to ANK 6-24 repeats, with the peptide binding groove of CC ANK 1-5 repeats oriented toward the membrane (PubMed:35835865). The CC rearrangement of the ANK 1-5 repeats orients the canonical protein CC binding groove to directly face the membrane, to interact the membrane- CC embedded targets RHCE and AQP1 (PubMed:35835865). CC {ECO:0000269|PubMed:35835865}. CC -!- DOMAIN: The tandem configuration of the two ZU5 and the UPA domains CC forms a structural supramodule termed ZZU. ZU5-1 mediates interaction CC with beta-spectrin, and the ZU5-1/UPA interface is required for CC ankyrin's function other than binding to spectrin (By similarity). CC {ECO:0000250}. CC -!- PTM: Regulated by phosphorylation. CC -!- PTM: Palmitoylated. CC -!- PTM: Hydroxylated by HIF1AN at several asparagine and 1 aspartate CC residue within ANK repeat region. Hydroxylation seems to increase the CC conformational stability of this region and may also modulate protein- CC protein interactions mediated by the ANK repeat region. CC {ECO:0000269|PubMed:21177872}. CC -!- PTM: (Microbial infection) Probably cleaved by P.falciparum SERA6; the CC cleavage probably causes the disruption of the actin cytoskeleton and CC the rupture of the erythrocyte cell membrane releasing the merozoites. CC {ECO:0000269|PubMed:29459732}. CC -!- DISEASE: Spherocytosis 1 (SPH1) [MIM:182900]: A form of spherocytosis, CC a hematologic disorder leading to chronic hemolytic anemia and CC characterized by numerous abnormally shaped erythrocytes which are CC generally spheroidal. SPH1 is characterized by severe hemolytic anemia. CC Inheritance can be autosomal dominant or autosomal recessive. Patients CC with homozygous mutations have a more severe disorder. CC {ECO:0000269|PubMed:11102985, ECO:0000269|PubMed:8640229}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- MISCELLANEOUS: [Isoform Er1]: Major erythrocyte-specific isoform. CC Produced by alternative promoter usage. CC -!- MISCELLANEOUS: [Isoform Er2]: Predominant form of minor erythrocyte- CC specific isoforms. Produced by alternative splicing of isoform Er1. CC {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform Er3]: Produced by alternative splicing of CC isoform Er1. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform Er4]: Produced by alternative splicing of CC isoform Er1. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform Er5]: Produced by alternative splicing of CC isoform Er1. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform Er6]: Produced by alternative splicing of CC isoform Er1. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform Er7]: Produced by alternative splicing of CC isoform Er1. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform Er9]: Produced by alternative splicing of CC isoform Er1. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform Er10]: Produced by alternative splicing of CC isoform Er1. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform Er11]: Produced by alternative splicing of CC isoform Er1. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform Er12]: Produced by alternative splicing of CC isoform Er1. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform Er13]: Produced by alternative splicing of CC isoform Er1. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform Er14]: Produced by alternative splicing of CC isoform Er1. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform Er15]: Produced by alternative splicing of CC isoform Er1. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform Er16]: Produced by alternative splicing of CC isoform Er1. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform Mu17]: Produced by alternative promoter usage. CC {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform Mu18]: Produced by alternative splicing of CC isoform Mu17. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform Mu19]: Produced by alternative splicing of CC isoform Mu17. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform Mu20]: Produced by alternative splicing of CC isoform Mu17. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform Br21]: Produced by alternative splicing of CC isoform Er1. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 22]: Produced by alternative splicing. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB47805.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Wikipedia; Note=Ankyrin entry; CC URL="https://en.wikipedia.org/wiki/Ankyrin"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X16609; CAA34610.1; -; mRNA. DR EMBL; X16609; CAA34611.1; -; mRNA. DR EMBL; M28880; AAA51732.1; -; mRNA. DR EMBL; U50133; AAB47805.1; ALT_SEQ; Genomic_DNA. DR EMBL; U50092; AAB47805.1; JOINED; Genomic_DNA. DR EMBL; U50093; AAB47805.1; JOINED; Genomic_DNA. DR EMBL; U50094; AAB47805.1; JOINED; Genomic_DNA. DR EMBL; U50095; AAB47805.1; JOINED; Genomic_DNA. DR EMBL; U50096; AAB47805.1; JOINED; Genomic_DNA. DR EMBL; U50097; AAB47805.1; JOINED; Genomic_DNA. DR EMBL; U50098; AAB47805.1; JOINED; Genomic_DNA. DR EMBL; U50099; AAB47805.1; JOINED; Genomic_DNA. DR EMBL; U50100; AAB47805.1; JOINED; Genomic_DNA. DR EMBL; U50101; AAB47805.1; JOINED; Genomic_DNA. DR EMBL; U50102; AAB47805.1; JOINED; Genomic_DNA. DR EMBL; U50103; AAB47805.1; JOINED; Genomic_DNA. DR EMBL; U50104; AAB47805.1; JOINED; Genomic_DNA. DR EMBL; U50105; AAB47805.1; JOINED; Genomic_DNA. DR EMBL; U50106; AAB47805.1; JOINED; Genomic_DNA. DR EMBL; U50107; AAB47805.1; JOINED; Genomic_DNA. DR EMBL; U50108; AAB47805.1; JOINED; Genomic_DNA. DR EMBL; U50109; AAB47805.1; JOINED; Genomic_DNA. DR EMBL; U50110; AAB47805.1; JOINED; Genomic_DNA. DR EMBL; U50111; AAB47805.1; JOINED; Genomic_DNA. DR EMBL; U50112; AAB47805.1; JOINED; Genomic_DNA. DR EMBL; U50113; AAB47805.1; JOINED; Genomic_DNA. DR EMBL; U50114; AAB47805.1; JOINED; Genomic_DNA. DR EMBL; U50115; AAB47805.1; JOINED; Genomic_DNA. DR EMBL; U50116; AAB47805.1; JOINED; Genomic_DNA. DR EMBL; U50117; AAB47805.1; JOINED; Genomic_DNA. DR EMBL; U50118; AAB47805.1; JOINED; Genomic_DNA. DR EMBL; U50119; AAB47805.1; JOINED; Genomic_DNA. DR EMBL; U50120; AAB47805.1; JOINED; Genomic_DNA. DR EMBL; U50121; AAB47805.1; JOINED; Genomic_DNA. DR EMBL; U50122; AAB47805.1; JOINED; Genomic_DNA. DR EMBL; U50123; AAB47805.1; JOINED; Genomic_DNA. DR EMBL; U50124; AAB47805.1; JOINED; Genomic_DNA. DR EMBL; U50125; AAB47805.1; JOINED; Genomic_DNA. DR EMBL; U50126; AAB47805.1; JOINED; Genomic_DNA. DR EMBL; U50127; AAB47805.1; JOINED; Genomic_DNA. DR EMBL; U50128; AAB47805.1; JOINED; Genomic_DNA. DR EMBL; U50129; AAB47805.1; JOINED; Genomic_DNA. DR EMBL; U50130; AAB47805.1; JOINED; Genomic_DNA. DR EMBL; U50131; AAB47805.1; JOINED; Genomic_DNA. DR EMBL; U50132; AAB47805.1; JOINED; Genomic_DNA. DR EMBL; AF005213; AAC01950.1; -; mRNA. DR EMBL; AB209418; BAD92655.1; -; mRNA. DR EMBL; AK223578; BAD97298.1; -; mRNA. DR EMBL; AC027702; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC113133; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471080; EAW63243.1; -; Genomic_DNA. DR EMBL; CH471080; EAW63244.1; -; Genomic_DNA. DR EMBL; BC030957; AAH30957.1; -; mRNA. DR EMBL; BC117121; AAI17122.1; -; mRNA. DR EMBL; BC014467; -; NOT_ANNOTATED_CDS; mRNA. DR CCDS; CCDS47849.1; -. [P16157-21] DR CCDS; CCDS55227.1; -. [P16157-23] DR CCDS; CCDS6119.1; -. [P16157-1] DR CCDS; CCDS6120.1; -. [P16157-22] DR CCDS; CCDS6121.1; -. [P16157-3] DR CCDS; CCDS6122.1; -. [P16157-17] DR PIR; A35049; A35049. DR PIR; S08275; SJHUK. DR RefSeq; NP_000028.3; NM_000037.4. [P16157-3] DR RefSeq; NP_001135917.1; NM_001142445.2. [P16157-23] DR RefSeq; NP_001135918.1; NM_001142446.2. [P16157-21] DR RefSeq; NP_065208.2; NM_020475.3. [P16157-5] DR RefSeq; NP_065209.2; NM_020476.3. [P16157-1] DR RefSeq; NP_065210.2; NM_020477.3. [P16157-4] DR RefSeq; NP_065211.2; NM_020478.5. [P16157-17] DR RefSeq; NP_065213.2; NM_020480.5. [P16157-22] DR PDB; 1N11; X-ray; 2.70 A; A=401-827. DR PDB; 2YQF; NMR; -; A=1394-1497. DR PDB; 2YVI; X-ray; 1.92 A; A=1393-1497. DR PDB; 3F59; X-ray; 2.00 A; A/B/C/D=911-1068. DR PDB; 3KBT; X-ray; 2.75 A; C/D=911-1068. DR PDB; 3KBU; X-ray; 2.75 A; C/D=911-1068. DR PDB; 3UD1; X-ray; 2.00 A; A/B/C=911-1233. DR PDB; 3UD2; X-ray; 2.21 A; A/B/C=911-1233. DR PDB; 7TW3; EM; 4.40 A; G=1-1881. DR PDB; 7TW5; EM; 5.70 A; G/H=1-1881. DR PDB; 7TW6; EM; 5.60 A; G=1-1881. DR PDB; 7UZQ; EM; 2.17 A; J=1-201. DR PDB; 7UZU; EM; 2.30 A; A=1-1881. DR PDB; 7V0K; EM; 2.40 A; H=1-1881. DR PDB; 7V0M; EM; 2.70 A; A=1-1881. DR PDB; 7V0S; EM; 2.50 A; J=1-1881. DR PDB; 7V0X; EM; 3.00 A; J=1-1881. DR PDB; 8CS9; EM; 2.74 A; A=1-1881. DR PDB; 8CSL; EM; 25.00 A; A=1-1881. DR PDB; 8CSV; EM; 2.70 A; A=1-1881. DR PDB; 8CTE; EM; 2.90 A; A=1-1881. DR AlphaFoldDB; P16157; -. DR BMRB; P16157; -. DR EMDB; EMD-26149; -. DR EMDB; EMD-26151; -. DR EMDB; EMD-26153; -. DR EMDB; EMD-26916; -. DR EMDB; EMD-26918; -. DR EMDB; EMD-26943; -. DR EMDB; EMD-26944; -. DR EMDB; EMD-26949; -. DR EMDB; EMD-26952; -. DR EMDB; EMD-26960; -. DR EMDB; EMD-26965; -. DR EMDB; EMD-26972; -. DR EMDB; EMD-26988; -. DR SMR; P16157; -. DR BioGRID; 106783; 49. DR FunCoup; P16157; 422. DR IntAct; P16157; 35. DR STRING; 9606.ENSP00000265709; -. DR TCDB; 8.A.28.1.2; the ankyrin (ankyrin) family. DR GlyConnect; P16157; 1 O-GlcNAc glycan (4 sites). DR GlyCosmos; P16157; 4 sites, 1 glycan. DR GlyGen; P16157; 5 sites, 1 O-linked glycan (4 sites). DR iPTMnet; P16157; -. DR MetOSite; P16157; -. DR PhosphoSitePlus; P16157; -. DR BioMuta; ANK1; -. DR DMDM; 116241246; -. DR jPOST; P16157; -. DR MassIVE; P16157; -. DR PaxDb; 9606-ENSP00000265709; -. DR PeptideAtlas; P16157; -. DR ProteomicsDB; 15386; -. DR ProteomicsDB; 53299; -. [P16157-1] DR ProteomicsDB; 53300; -. [P16157-10] DR ProteomicsDB; 53301; -. [P16157-11] DR ProteomicsDB; 53302; -. [P16157-12] DR ProteomicsDB; 53303; -. [P16157-13] DR ProteomicsDB; 53304; -. [P16157-14] DR ProteomicsDB; 53305; -. [P16157-15] DR ProteomicsDB; 53306; -. [P16157-16] DR ProteomicsDB; 53307; -. [P16157-17] DR ProteomicsDB; 53308; -. [P16157-18] DR ProteomicsDB; 53309; -. [P16157-19] DR ProteomicsDB; 53310; -. [P16157-2] DR ProteomicsDB; 53311; -. [P16157-20] DR ProteomicsDB; 53312; -. [P16157-21] DR ProteomicsDB; 53313; -. [P16157-3] DR ProteomicsDB; 53314; -. [P16157-4] DR ProteomicsDB; 53315; -. [P16157-5] DR ProteomicsDB; 53316; -. [P16157-6] DR ProteomicsDB; 53317; -. [P16157-7] DR ProteomicsDB; 53318; -. [P16157-8] DR ProteomicsDB; 53319; -. [P16157-9] DR ProteomicsDB; 62; -. DR ProteomicsDB; 62447; -. DR Pumba; P16157; -. DR ABCD; P16157; 3 sequenced antibodies. DR Antibodypedia; 4229; 436 antibodies from 36 providers. DR DNASU; 286; -. DR Ensembl; ENST00000265709.14; ENSP00000265709.8; ENSG00000029534.22. [P16157-21] DR Ensembl; ENST00000289734.13; ENSP00000289734.8; ENSG00000029534.22. [P16157-3] DR Ensembl; ENST00000314214.12; ENSP00000319123.8; ENSG00000029534.22. [P16157-17] DR Ensembl; ENST00000347528.8; ENSP00000339620.4; ENSG00000029534.22. [P16157-1] DR Ensembl; ENST00000348036.8; ENSP00000297744.5; ENSG00000029534.22. [P16157-22] DR Ensembl; ENST00000522543.6; ENSP00000430368.1; ENSG00000029534.22. [P16157-23] DR GeneID; 286; -. DR KEGG; hsa:286; -. DR MANE-Select; ENST00000289734.13; ENSP00000289734.8; NM_000037.4; NP_000028.3. [P16157-3] DR UCSC; uc003xoc.4; human. [P16157-1] DR AGR; HGNC:492; -. DR ClinPGx; PA24798; -. DR CTD; 286; -. DR DisGeNET; 286; -. DR GeneCards; ANK1; -. DR HGNC; HGNC:492; ANK1. DR HPA; ENSG00000029534; Group enriched (skeletal muscle, tongue). DR MalaCards; ANK1; -. DR MIM; 182900; phenotype. DR MIM; 612641; gene. DR OpenTargets; ENSG00000029534; -. DR Orphanet; 251066; 8p11.2 deletion syndrome. DR Orphanet; 822; Hereditary spherocytosis. DR VEuPathDB; HostDB:ENSG00000029534; -. DR eggNOG; KOG4177; Eukaryota. DR GeneTree; ENSGT00940000155760; -. DR HOGENOM; CLU_1694857_0_0_1; -. DR InParanoid; P16157; -. DR OMA; YWSEVAI; -. DR OrthoDB; 20872at2759; -. DR PAN-GO; P16157; 6 GO annotations based on evolutionary models. DR PhylomeDB; P16157; -. DR PathwayCommons; P16157; -. DR Reactome; R-HSA-445095; Interaction between L1 and Ankyrins. DR Reactome; R-HSA-447038; NrCAM interactions. DR Reactome; R-HSA-447041; CHL1 interactions. DR Reactome; R-HSA-447043; Neurofascin interactions. DR Reactome; R-HSA-6807878; COPI-mediated anterograde transport. DR SignaLink; P16157; -. DR SIGNOR; P16157; -. DR Agora; ENSG00000029534; -. DR BioGRID-ORCS; 286; 14 hits in 1158 CRISPR screens. DR CD-CODE; FB4E32DD; Presynaptic clusters and postsynaptic densities. DR ChiTaRS; ANK1; human. DR EvolutionaryTrace; P16157; -. DR GeneWiki; ANK1; -. DR GenomeRNAi; 286; -. DR Pharos; P16157; Tbio. DR PRO; PR:P16157; -. DR Proteomes; UP000005640; Chromosome 8. DR RNAct; P16157; protein. DR Bgee; ENSG00000029534; Expressed in skeletal muscle tissue of rectus abdominis and 162 other cell types or tissues. DR ExpressionAtlas; P16157; baseline and differential. DR GO; GO:0170014; C:ankyrin-1 complex; IDA:UniProtKB. DR GO; GO:0030673; C:axolemma; IEA:Ensembl. DR GO; GO:0016323; C:basolateral plasma membrane; NAS:UniProtKB. DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:ARUK-UCL. DR GO; GO:0005856; C:cytoskeleton; NAS:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0031430; C:M band; IEA:UniProtKB-SubCell. DR GO; GO:0043005; C:neuron projection; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL. DR GO; GO:0045211; C:postsynaptic membrane; IEA:Ensembl. DR GO; GO:0042383; C:sarcolemma; IEA:Ensembl. DR GO; GO:0016529; C:sarcoplasmic reticulum; IEA:UniProtKB-SubCell. DR GO; GO:0014731; C:spectrin-associated cytoskeleton; IDA:BHF-UCL. DR GO; GO:0030018; C:Z disc; IEA:Ensembl. DR GO; GO:0051117; F:ATPase binding; IPI:BHF-UCL. DR GO; GO:0008093; F:cytoskeletal adaptor activity; IDA:BHF-UCL. DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB. DR GO; GO:0019903; F:protein phosphatase binding; IPI:ARUK-UCL. DR GO; GO:0030507; F:spectrin binding; IDA:ARUK-UCL. DR GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:ProtInc. DR GO; GO:0005198; F:structural molecule activity; NAS:UniProtKB. DR GO; GO:0044325; F:transmembrane transporter binding; IBA:GO_Central. DR GO; GO:0007010; P:cytoskeleton organization; NAS:UniProtKB. DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IDA:BHF-UCL. DR GO; GO:0006887; P:exocytosis; NAS:UniProtKB. DR GO; GO:0045199; P:maintenance of epithelial cell apical/basal polarity; TAS:UniProtKB. DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:BHF-UCL. DR GO; GO:0007165; P:signal transduction; IEA:InterPro. DR CDD; cd08805; Death_ank1; 1. DR FunFam; 1.10.533.10:FF:000010; Ankyrin 1; 1. DR FunFam; 1.25.40.20:FF:000003; Ankyrin, isoform B; 1. DR FunFam; 2.60.40.2660:FF:000002; Ankyrin-1 isoform B; 1. DR FunFam; 1.25.40.20:FF:000001; Ankyrin-2 isoform 2; 1. DR FunFam; 1.25.40.20:FF:000002; Ankyrin-2 isoform 2; 1. DR FunFam; 2.60.220.30:FF:000001; Ankyrin-3 isoform 2; 1. DR FunFam; 2.60.220.30:FF:000002; Ankyrin-3 isoform 2; 1. DR Gene3D; 2.60.220.30; -; 2. DR Gene3D; 2.60.40.2660; -; 1. DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 3. DR Gene3D; 1.10.533.10; Death Domain, Fas; 1. DR InterPro; IPR002110; Ankyrin_rpt. DR InterPro; IPR036770; Ankyrin_rpt-contain_sf. DR InterPro; IPR040745; Ankyrin_UPA. DR InterPro; IPR011029; DEATH-like_dom_sf. DR InterPro; IPR000488; Death_dom. DR InterPro; IPR051165; Multifunctional_ANK_Repeat. DR InterPro; IPR000906; ZU5_dom. DR PANTHER; PTHR24123:SF71; ANKYRIN 1, ERYTHROCYTIC A ISOFORM X1; 1. DR PANTHER; PTHR24123; ANKYRIN REPEAT-CONTAINING; 1. DR Pfam; PF00023; Ank; 5. DR Pfam; PF12796; Ank_2; 6. DR Pfam; PF13637; Ank_4; 1. DR Pfam; PF00531; Death; 1. DR Pfam; PF17809; UPA_2; 1. DR Pfam; PF00791; ZU5; 1. DR PRINTS; PR01415; ANKYRIN. DR SMART; SM00248; ANK; 23. DR SMART; SM00005; DEATH; 1. DR SMART; SM00218; ZU5; 1. DR SUPFAM; SSF48403; Ankyrin repeat; 2. DR SUPFAM; SSF47986; DEATH domain; 1. DR PROSITE; PS50297; ANK_REP_REGION; 1. DR PROSITE; PS50088; ANK_REPEAT; 20. DR PROSITE; PS50017; DEATH_DOMAIN; 1. DR PROSITE; PS51145; ZU5; 2. DR PDBsum; 1N11; -. DR PDBsum; 2YQF; -. DR PDBsum; 2YVI; -. DR PDBsum; 3F59; -. DR PDBsum; 3KBT; -. DR PDBsum; 3KBU; -. DR PDBsum; 3UD1; -. DR PDBsum; 3UD2; -. DR PDBsum; 7TW3; -. DR PDBsum; 7TW5; -. DR PDBsum; 7TW6; -. DR PDBsum; 7UZQ; -. DR PDBsum; 7UZU; -. DR PDBsum; 7V0K; -. DR PDBsum; 7V0M; -. DR PDBsum; 7V0S; -. DR PDBsum; 7V0X; -. DR PDBsum; 8CS9; -. DR PDBsum; 8CSL; -. DR PDBsum; 8CSV; -. DR PDBsum; 8CTE; -. PE 1: Evidence at protein level; KW 3D-structure; Alternative promoter usage; Alternative splicing; ANK repeat; KW Cytoplasm; Cytoskeleton; Direct protein sequencing; Disease variant; KW Elliptocytosis; Hereditary hemolytic anemia; Hydroxylation; Lipoprotein; KW Membrane; Phosphoprotein; Proteomics identification; Reference proteome; KW Repeat; Sarcoplasmic reticulum. FT CHAIN 1..1881 FT /note="Ankyrin-1" FT /id="PRO_0000066883" FT REPEAT 44..73 FT /note="ANK 1" FT REPEAT 77..106 FT /note="ANK 2" FT REPEAT 110..139 FT /note="ANK 3" FT REPEAT 143..172 FT /note="ANK 4" FT REPEAT 174..201 FT /note="ANK 5" FT REPEAT 205..234 FT /note="ANK 6" FT REPEAT 238..267 FT /note="ANK 7" FT REPEAT 271..300 FT /note="ANK 8" FT REPEAT 304..333 FT /note="ANK 9" FT REPEAT 337..366 FT /note="ANK 10" FT REPEAT 370..399 FT /note="ANK 11" FT REPEAT 403..432 FT /note="ANK 12" FT REPEAT 436..465 FT /note="ANK 13" FT REPEAT 469..498 FT /note="ANK 14" FT REPEAT 502..531 FT /note="ANK 15" FT REPEAT 535..564 FT /note="ANK 16" FT REPEAT 568..597 FT /note="ANK 17" FT REPEAT 601..630 FT /note="ANK 18" FT REPEAT 634..663 FT /note="ANK 19" FT REPEAT 667..696 FT /note="ANK 20" FT REPEAT 700..729 FT /note="ANK 21" FT REPEAT 733..762 FT /note="ANK 22" FT REPEAT 766..795 FT /note="ANK 23" FT DOMAIN 913..1068 FT /note="ZU5 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00485" FT DOMAIN 1070..1216 FT /note="ZU5 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00485" FT DOMAIN 1403..1487 FT /note="Death" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00064" FT REGION 1..827 FT /note="89 kDa domain" FT REGION 875..904 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1234..1362 FT /note="UPA domain" FT /evidence="ECO:0000250" FT REGION 1383..1881 FT /note="55 kDa regulatory domain" FT REGION 1486..1510 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1583..1613 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1637..1703 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1718..1791 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1840..1859 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 890..904 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1493..1504 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1588..1612 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1642..1658 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1683..1694 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1718..1739 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1758..1771 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1772..1781 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 105 FT /note="(3S)-3-hydroxyasparagine; by HIF1AN; partial" FT /evidence="ECO:0000269|PubMed:21177872" FT MOD_RES 233 FT /note="(3S)-3-hydroxyasparagine; by HIF1AN; partial" FT /evidence="ECO:0000269|PubMed:21177872" FT MOD_RES 429 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 431 FT /note="(3S)-3-hydroxyasparagine; by HIF1AN; partial" FT /evidence="ECO:0000269|PubMed:21177872" FT MOD_RES 464 FT /note="(3S)-3-hydroxyasparagine; by HIF1AN; partial" FT /evidence="ECO:0000269|PubMed:21177872" FT MOD_RES 629 FT /note="(3S)-3-hydroxyasparagine; by HIF1AN; partial" FT /evidence="ECO:0000269|PubMed:21177872" FT MOD_RES 662 FT /note="(3S)-3-hydroxyasparagine; by HIF1AN; partial" FT /evidence="ECO:0000269|PubMed:21177872" FT MOD_RES 695 FT /note="(3S)-3-hydroxyaspartate; by HIF1AN; partial" FT /evidence="ECO:0000269|PubMed:21177872" FT MOD_RES 728 FT /note="(3S)-3-hydroxyasparagine; by HIF1AN; partial" FT /evidence="ECO:0000269|PubMed:21177872" FT MOD_RES 759 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 761 FT /note="(3S)-3-hydroxyasparagine; by HIF1AN; partial" FT /evidence="ECO:0000269|PubMed:21177872" FT MOD_RES 781 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 817 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 834 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 856 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 961 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q02357" FT MOD_RES 1073 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q02357" FT MOD_RES 1082 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q02357" FT MOD_RES 1378 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1380 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1390 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q02357" FT MOD_RES 1392 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q02357" FT MOD_RES 1396 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1400 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q02357" FT MOD_RES 1428 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 1486 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1523 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 1533 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 1617 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q02357" FT MOD_RES 1666 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1671 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1686 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1690 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1696 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 1..1725 FT /note="Missing (in isoform Mu17, isoform Mu18, isoform FT Mu19, isoform Mu20, isoform 22 and isoform 23)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:9430667" FT /id="VSP_018440" FT VAR_SEQ 1..9 FT /note="MPYSVGFRE -> MAQAAKQLKKIKDIEAQALQEQKEKEESNRKRRNRSRDR FT KKK (in isoform Br21)" FT /evidence="ECO:0000303|Ref.5" FT /id="VSP_018439" FT VAR_SEQ 820 FT /note="E -> EGTAHITIM (in isoform Br21)" FT /evidence="ECO:0000303|Ref.5" FT /id="VSP_018441" FT VAR_SEQ 1513..1874 FT /note="Missing (in isoform Er16)" FT /evidence="ECO:0000303|PubMed:1689849" FT /id="VSP_000264" FT VAR_SEQ 1514..1675 FT /note="Missing (in isoform Er2, isoform Er4, isoform Er6, FT isoform Er8, isoform Er10, isoform Er12 and isoform Er14)" FT /evidence="ECO:0000303|PubMed:2137557" FT /id="VSP_018442" FT VAR_SEQ 1726..1798 FT /note="TQGPHSFQGTSTMTEGLEPGGSQEYEKVLVSVSEHTWTEQPEAESSQADRDR FT RQQGQEEQVQEAKNTFTQVVQ -> MWTFVTQLLVTLVLLSFFLVSCQNVMHIVRGSLC FT FVLKHIHQELDKELGESEGLSDDEETISTRVVRRRVFLK (in isoform Mu17, FT isoform Mu18, isoform Mu19, isoform 22 and isoform 23)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:9430667" FT /id="VSP_018443" FT VAR_SEQ 1726..1798 FT /note="TQGPHSFQGTSTMTEGLEPGGSQEYEKVLVSVSEHTWTEQPEAESSQADRDR FT RQQGQEEQVQEAKNTFTQVVQ -> MWTFVTQLLVTLVLLSFFLVSCQNVMHIVRGSLC FT FVLKHIHQ (in isoform Mu20)" FT /evidence="ECO:0000303|PubMed:9430667" FT /id="VSP_018444" FT VAR_SEQ 1799..1881 FT /note="GNEFQNIPGEQVTEEQFTDEQGNIVTKKIIRKVVRQIDLSSADAAQEHEEVT FT VEGPLEDPSELEVDIDYFMKHSKDHTSTPNP -> VELRGSGLQPDLIEGRKGAQIVKR FT ASLKRGKQ (in isoform Mu20)" FT /evidence="ECO:0000303|PubMed:9430667" FT /id="VSP_018446" FT VAR_SEQ 1799..1873 FT /note="Missing (in isoform Er9, isoform Er10 and isoform FT Mu19)" FT /evidence="ECO:0000303|PubMed:9430667" FT /id="VSP_018445" FT VAR_SEQ 1826..1872 FT /note="Missing (in isoform 22)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_045439" FT VAR_SEQ 1827..1881 FT /note="IIRKVVRQIDLSSADAAQEHEEVTVEGPLEDPSELEVDIDYFMKHSKDHTST FT PNP -> VELRGSGLQPDLIEGRKGAQIVKRASLKRGKQ (in isoform Er15 FT and isoform Mu18)" FT /evidence="ECO:0000303|PubMed:9430667" FT /id="VSP_018448" FT VAR_SEQ 1827..1873 FT /note="Missing (in isoform Er7 and isoform Er8)" FT /evidence="ECO:0000305" FT /id="VSP_018447" FT VAR_SEQ 1849..1873 FT /note="Missing (in isoform Er3, isoform Er4 and isoform FT Br21)" FT /evidence="ECO:0000303|Ref.5" FT /id="VSP_018449" FT VAR_SEQ 1850..1881 FT /note="TVEGPLEDPSELEVDIDYFMKHSKDHTSTPNP -> ELRGSGLQPDLIEGRK FT GAQIVKRASLKRGKQ (in isoform Er5, isoform Er6 and isoform FT Mu17)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:1689849, ECO:0000303|PubMed:9430667" FT /id="VSP_000266" FT VAR_SEQ 1874..1881 FT /note="DHTSTPNP -> VELRGSGLQPDLIEGRKGAQIVKRASLKRGKQ (in FT isoform Er11 and isoform Er12)" FT /evidence="ECO:0000305" FT /id="VSP_018450" FT VAR_SEQ 1874..1881 FT /note="DHTSTPNP -> VLRRPRPWGTQRHHCCLALPGRLHDTSLHSPLYELSLQSL FT FSLVGSVSAPPCRSFRSSACVLPVFAICPAFCLCCCLQVELRGSGLQPDLIEGRKGAQI FT VKRASLKRGKQ (in isoform Er13 and isoform Er14)" FT /evidence="ECO:0000305" FT /id="VSP_018451" FT VAR_SEQ 1875 FT /note="H -> D (in isoform Er16)" FT /evidence="ECO:0000303|PubMed:1689849" FT /id="VSP_000265" FT VARIANT 21 FT /note="R -> T" FT /id="VAR_000595" FT VARIANT 276 FT /note="L -> R (in SPH1)" FT /evidence="ECO:0000269|PubMed:11102985" FT /id="VAR_054991" FT VARIANT 332 FT /note="D -> H (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035605" FT VARIANT 463 FT /note="V -> I (in SPH1; dbSNP:rs140085544)" FT /evidence="ECO:0000269|PubMed:8640229" FT /id="VAR_000596" FT VARIANT 619 FT /note="R -> H (in Brueggen; dbSNP:rs2304877)" FT /id="VAR_000597" FT VARIANT 733 FT /note="L -> I (in dbSNP:rs11778936)" FT /id="VAR_028769" FT VARIANT 750 FT /note="V -> A" FT /evidence="ECO:0000269|PubMed:2137557" FT /id="VAR_000598" FT VARIANT 832 FT /note="R -> Q (in dbSNP:rs34523608)" FT /id="VAR_061012" FT VARIANT 845 FT /note="D -> E" FT /id="VAR_000599" FT VARIANT 991 FT /note="V -> L (in dbSNP:rs758454168)" FT /evidence="ECO:0000269|PubMed:9235914" FT /id="VAR_026411" FT VARIANT 1054 FT /note="I -> T (in SPH1)" FT /evidence="ECO:0000269|PubMed:11102985" FT /id="VAR_054992" FT VARIANT 1075 FT /note="T -> I (in dbSNP:rs35213384)" FT /evidence="ECO:0000269|PubMed:1689849, FT ECO:0000269|PubMed:2137557, ECO:0000269|PubMed:9235914, FT ECO:0000269|Ref.5" FT /id="VAR_048263" FT VARIANT 1126 FT /note="A -> P (in dbSNP:rs504465)" FT /id="VAR_028770" FT VARIANT 1192 FT /note="T -> P (in dbSNP:rs486770)" FT /id="VAR_028771" FT VARIANT 1286 FT /note="E -> D (in dbSNP:rs2150589462)" FT /evidence="ECO:0000269|PubMed:2141335" FT /id="VAR_000601" FT VARIANT 1325 FT /note="M -> V (in dbSNP:rs10093583)" FT /id="VAR_028772" FT VARIANT 1392 FT /note="S -> T" FT /id="VAR_000600" FT VARIANT 1546 FT /note="V -> I (in dbSNP:rs1060130)" FT /evidence="ECO:0000269|PubMed:1689849" FT /id="VAR_028773" FT VARIANT 1592 FT /note="D -> N (in Duesseldorf; dbSNP:rs1457291305)" FT /id="VAR_000602" FT MUTAGEN 1824 FT /note="T->P: Abolishes interaction with OBSCN (in isoform FT Mu17)." FT /evidence="ECO:0000269|PubMed:12527750" FT MUTAGEN 1826 FT /note="K->E: Abolishes interaction with OBSCN (in isoform FT Mu17)." FT /evidence="ECO:0000269|PubMed:12527750" FT MUTAGEN 1829 FT /note="R->G: Abolishes interaction with OBSCN (in isoform FT Mu17)." FT /evidence="ECO:0000269|PubMed:12527750" FT MUTAGEN 1830 FT /note="K->E: Abolishes interaction with OBSCN (in isoform FT Mu17)." FT /evidence="ECO:0000269|PubMed:12527750" FT CONFLICT 230 FT /note="A -> S (in Ref. 2; AAA51732)" FT /evidence="ECO:0000305" FT CONFLICT 801 FT /note="K -> L (in Ref. 3; AAB47805)" FT /evidence="ECO:0000305" FT CONFLICT 845 FT /note="D -> R (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 902 FT /note="I -> T (in Ref. 3; AAB47805)" FT /evidence="ECO:0000305" FT HELIX 12..22 FT /evidence="ECO:0007829|PDB:7UZQ" FT HELIX 25..33 FT /evidence="ECO:0007829|PDB:7UZQ" FT HELIX 48..55 FT /evidence="ECO:0007829|PDB:7UZQ" FT HELIX 58..66 FT /evidence="ECO:0007829|PDB:7UZQ" FT HELIX 81..88 FT /evidence="ECO:0007829|PDB:7UZQ" FT HELIX 91..99 FT /evidence="ECO:0007829|PDB:7UZQ" FT HELIX 114..120 FT /evidence="ECO:0007829|PDB:7UZQ" FT HELIX 124..132 FT /evidence="ECO:0007829|PDB:7UZQ" FT HELIX 147..153 FT /evidence="ECO:0007829|PDB:7UZQ" FT HELIX 157..166 FT /evidence="ECO:0007829|PDB:7UZQ" FT HELIX 176..182 FT /evidence="ECO:0007829|PDB:7UZU" FT HELIX 186..195 FT /evidence="ECO:0007829|PDB:7UZU" FT HELIX 209..216 FT /evidence="ECO:0007829|PDB:7UZU" FT HELIX 219..227 FT /evidence="ECO:0007829|PDB:7UZU" FT HELIX 242..249 FT /evidence="ECO:0007829|PDB:7UZU" FT HELIX 252..260 FT /evidence="ECO:0007829|PDB:7UZU" FT HELIX 275..281 FT /evidence="ECO:0007829|PDB:7UZU" FT HELIX 285..293 FT /evidence="ECO:0007829|PDB:7UZU" FT HELIX 308..314 FT /evidence="ECO:0007829|PDB:7UZU" FT HELIX 318..326 FT /evidence="ECO:0007829|PDB:7UZU" FT HELIX 341..348 FT /evidence="ECO:0007829|PDB:7UZU" FT HELIX 351..359 FT /evidence="ECO:0007829|PDB:7UZU" FT HELIX 374..380 FT /evidence="ECO:0007829|PDB:7UZU" FT HELIX 384..392 FT /evidence="ECO:0007829|PDB:7UZU" FT HELIX 407..414 FT /evidence="ECO:0007829|PDB:7UZU" FT HELIX 417..425 FT /evidence="ECO:0007829|PDB:7UZU" FT STRAND 435..437 FT /evidence="ECO:0007829|PDB:7UZU" FT HELIX 440..447 FT /evidence="ECO:0007829|PDB:7UZU" FT HELIX 450..458 FT /evidence="ECO:0007829|PDB:7UZU" FT HELIX 468..470 FT /evidence="ECO:0007829|PDB:8CS9" FT HELIX 473..480 FT /evidence="ECO:0007829|PDB:1N11" FT HELIX 483..492 FT /evidence="ECO:0007829|PDB:1N11" FT HELIX 498..500 FT /evidence="ECO:0007829|PDB:1N11" FT HELIX 506..513 FT /evidence="ECO:0007829|PDB:1N11" FT HELIX 516..524 FT /evidence="ECO:0007829|PDB:1N11" FT HELIX 539..545 FT /evidence="ECO:0007829|PDB:1N11" FT HELIX 549..557 FT /evidence="ECO:0007829|PDB:1N11" FT HELIX 572..578 FT /evidence="ECO:0007829|PDB:1N11" FT HELIX 582..588 FT /evidence="ECO:0007829|PDB:1N11" FT HELIX 589..591 FT /evidence="ECO:0007829|PDB:1N11" FT HELIX 605..611 FT /evidence="ECO:0007829|PDB:1N11" FT HELIX 615..623 FT /evidence="ECO:0007829|PDB:1N11" FT HELIX 638..644 FT /evidence="ECO:0007829|PDB:1N11" FT HELIX 648..655 FT /evidence="ECO:0007829|PDB:1N11" FT TURN 656..658 FT /evidence="ECO:0007829|PDB:1N11" FT HELIX 671..678 FT /evidence="ECO:0007829|PDB:1N11" FT HELIX 681..690 FT /evidence="ECO:0007829|PDB:1N11" FT HELIX 704..710 FT /evidence="ECO:0007829|PDB:1N11" FT HELIX 715..722 FT /evidence="ECO:0007829|PDB:1N11" FT HELIX 729..731 FT /evidence="ECO:0007829|PDB:1N11" FT HELIX 737..743 FT /evidence="ECO:0007829|PDB:1N11" FT HELIX 747..755 FT /evidence="ECO:0007829|PDB:1N11" FT STRAND 765..767 FT /evidence="ECO:0007829|PDB:1N11" FT HELIX 770..776 FT /evidence="ECO:0007829|PDB:1N11" FT HELIX 780..789 FT /evidence="ECO:0007829|PDB:1N11" FT STRAND 914..919 FT /evidence="ECO:0007829|PDB:3F59" FT STRAND 924..927 FT /evidence="ECO:0007829|PDB:3F59" FT TURN 930..932 FT /evidence="ECO:0007829|PDB:3UD1" FT STRAND 935..938 FT /evidence="ECO:0007829|PDB:3F59" FT STRAND 942..945 FT /evidence="ECO:0007829|PDB:3KBT" FT STRAND 947..954 FT /evidence="ECO:0007829|PDB:3F59" FT HELIX 956..958 FT /evidence="ECO:0007829|PDB:3F59" FT STRAND 959..961 FT /evidence="ECO:0007829|PDB:3KBU" FT HELIX 962..964 FT /evidence="ECO:0007829|PDB:3F59" FT STRAND 970..973 FT /evidence="ECO:0007829|PDB:3KBT" FT STRAND 975..980 FT /evidence="ECO:0007829|PDB:3F59" FT STRAND 984..994 FT /evidence="ECO:0007829|PDB:3F59" FT HELIX 996..998 FT /evidence="ECO:0007829|PDB:3KBU" FT STRAND 1000..1003 FT /evidence="ECO:0007829|PDB:3KBT" FT STRAND 1006..1015 FT /evidence="ECO:0007829|PDB:3F59" FT STRAND 1018..1020 FT /evidence="ECO:0007829|PDB:3KBT" FT HELIX 1026..1028 FT /evidence="ECO:0007829|PDB:3F59" FT HELIX 1029..1033 FT /evidence="ECO:0007829|PDB:3F59" FT HELIX 1040..1042 FT /evidence="ECO:0007829|PDB:3KBT" FT HELIX 1043..1049 FT /evidence="ECO:0007829|PDB:3F59" FT STRAND 1051..1058 FT /evidence="ECO:0007829|PDB:3F59" FT STRAND 1061..1067 FT /evidence="ECO:0007829|PDB:3F59" FT STRAND 1074..1076 FT /evidence="ECO:0007829|PDB:3UD1" FT STRAND 1081..1084 FT /evidence="ECO:0007829|PDB:3UD1" FT STRAND 1092..1095 FT /evidence="ECO:0007829|PDB:3UD1" FT STRAND 1099..1102 FT /evidence="ECO:0007829|PDB:3UD1" FT STRAND 1104..1111 FT /evidence="ECO:0007829|PDB:3UD1" FT HELIX 1115..1122 FT /evidence="ECO:0007829|PDB:3UD1" FT STRAND 1131..1138 FT /evidence="ECO:0007829|PDB:3UD1" FT STRAND 1140..1150 FT /evidence="ECO:0007829|PDB:3UD1" FT HELIX 1153..1157 FT /evidence="ECO:0007829|PDB:3UD1" FT STRAND 1165..1167 FT /evidence="ECO:0007829|PDB:3UD2" FT STRAND 1169..1175 FT /evidence="ECO:0007829|PDB:3UD1" FT STRAND 1195..1197 FT /evidence="ECO:0007829|PDB:3UD1" FT STRAND 1200..1207 FT /evidence="ECO:0007829|PDB:3UD1" FT STRAND 1210..1215 FT /evidence="ECO:0007829|PDB:3UD1" FT HELIX 1219..1221 FT /evidence="ECO:0007829|PDB:3UD1" FT HELIX 1222..1232 FT /evidence="ECO:0007829|PDB:3UD1" FT TURN 1398..1402 FT /evidence="ECO:0007829|PDB:2YVI" FT HELIX 1403..1414 FT /evidence="ECO:0007829|PDB:2YVI" FT HELIX 1415..1417 FT /evidence="ECO:0007829|PDB:2YVI" FT HELIX 1418..1424 FT /evidence="ECO:0007829|PDB:2YVI" FT HELIX 1429..1438 FT /evidence="ECO:0007829|PDB:2YVI" FT HELIX 1443..1458 FT /evidence="ECO:0007829|PDB:2YVI" FT HELIX 1459..1461 FT /evidence="ECO:0007829|PDB:2YVI" FT HELIX 1464..1473 FT /evidence="ECO:0007829|PDB:2YVI" FT HELIX 1477..1483 FT /evidence="ECO:0007829|PDB:2YVI" FT CONFLICT P16157-17:63 FT /note="T -> P (in Ref. 4; AAC01950)" FT /evidence="ECO:0000305" SQ SEQUENCE 1881 AA; 206265 MW; 49466F6F915019EC CRC64; MPYSVGFREA DAATSFLRAA RSGNLDKALD HLRNGVDINT CNQNGLNGLH LASKEGHVKM VVELLHKEII LETTTKKGNT ALHIAALAGQ DEVVRELVNY GANVNAQSQK GFTPLYMAAQ ENHLEVVKFL LENGANQNVA TEDGFTPLAV ALQQGHENVV AHLINYGTKG KVRLPALHIA ARNDDTRTAA VLLQNDPNPD VLSKTGFTPL HIAAHYENLN VAQLLLNRGA SVNFTPQNGI TPLHIASRRG NVIMVRLLLD RGAQIETKTK DELTPLHCAA RNGHVRISEI LLDHGAPIQA KTKNGLSPIH MAAQGDHLDC VRLLLQYDAE IDDITLDHLT PLHVAAHCGH HRVAKVLLDK GAKPNSRALN GFTPLHIACK KNHVRVMELL LKTGASIDAV TESGLTPLHV ASFMGHLPIV KNLLQRGASP NVSNVKVETP LHMAARAGHT EVAKYLLQNK AKVNAKAKDD QTPLHCAARI GHTNMVKLLL ENNANPNLAT TAGHTPLHIA AREGHVETVL ALLEKEASQA CMTKKGFTPL HVAAKYGKVR VAELLLERDA HPNAAGKNGL TPLHVAVHHN NLDIVKLLLP RGGSPHSPAW NGYTPLHIAA KQNQVEVARS LLQYGGSANA ESVQGVTPLH LAAQEGHAEM VALLLSKQAN GNLGNKSGLT PLHLVAQEGH VPVADVLIKH GVMVDATTRM GYTPLHVASH YGNIKLVKFL LQHQADVNAK TKLGYSPLHQ AAQQGHTDIV TLLLKNGASP NEVSSDGTTP LAIAKRLGYI SVTDVLKVVT DETSFVLVSD KHRMSFPETV DEILDVSEDE GEELISFKAE RRDSRDVDEE KELLDFVPKL DQVVESPAIP RIPCAMPETV VIRSEEQEQA SKEYDEDSLI PSSPATETSD NISPVASPVH TGFLVSFMVD ARGGSMRGSR HNGLRVVIPP RTCAAPTRIT CRLVKPQKLS TPPPLAEEEG LASRIIALGP TGAQFLSPVI VEIPHFASHG RGDRELVVLR SENGSVWKEH RSRYGESYLD QILNGMDEEL GSLEELEKKR VCRIITTDFP LYFVIMSRLC QDYDTIGPEG GSLKSKLVPL VQATFPENAV TKRVKLALQA QPVPDELVTK LLGNQATFSP IVTVEPRRRK FHRPIGLRIP LPPSWTDNPR DSGEGDTTSL RLLCSVIGGT DQAQWEDITG TTKLVYANEC ANFTTNVSAR FWLSDCPRTA EAVNFATLLY KELTAVPYMA KFVIFAKMND PREGRLRCYC MTDDKVDKTL EQHENFVEVA RSRDIEVLEG MSLFAELSGN LVPVKKAAQQ RSFHFQSFRE NRLAMPVKVR DSSREPGGSL SFLRKAMKYE DTQHILCHLN ITMPPCAKGS GAEDRRRTPT PLALRYSILS ESTPGSLSGT EQAEMKMAVI SEHLGLSWAE LARELQFSVE DINRIRVENP NSLLEQSVAL LNLWVIREGQ NANMENLYTA LQSIDRGEIV NMLEGSGRQS RNLKPDRRHT DRDYSLSPSQ MNGYSSLQDE LLSPASLGCA LSSPLRADQY WNEVAVLDAI PLAATEHDTM LEMSDMQVWS AGLTPSLVTA EDSSLECSKA EDSDATGHEW KLEGALSEEP RGPELGSLEL VEDDTVDSDA TNGLIDLLEQ EEGQRSEEKL PGSKRQDDAT GAGQDSENEV SLVSGHQRGQ ARITHSPTVS QVTERSQDRL QDWDADGSIV SYLQDAAQGS WQEEVTQGPH SFQGTSTMTE GLEPGGSQEY EKVLVSVSEH TWTEQPEAES SQADRDRRQQ GQEEQVQEAK NTFTQVVQGN EFQNIPGEQV TEEQFTDEQG NIVTKKIIRK VVRQIDLSSA DAAQEHEEVT VEGPLEDPSE LEVDIDYFMK HSKDHTSTPN P //