ID CAND2_HUMAN Reviewed; 1236 AA. AC O75155; B9EGM9; E9KL24; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 05-MAY-2009, sequence version 3. DT 10-JUN-2026, entry version 188. DE RecName: Full=Cullin-associated NEDD8-dissociated protein 2; DE AltName: Full=Cullin-associated and neddylation-dissociated protein 2; DE AltName: Full=Epididymis tissue protein Li 169; DE AltName: Full=TBP-interacting protein of 120 kDa B; DE Short=TBP-interacting protein 120B; DE AltName: Full=p120 CAND2; GN Name=CAND2; Synonyms=KIAA0667, TIP120B; 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], AND TISSUE SPECIFICITY. RC TISSUE=Epididymis; RX PubMed=20736409; DOI=10.1074/mcp.m110.001719; RA Li J., Liu F., Wang H., Liu X., Liu J., Li N., Wan F., Wang W., Zhang C., RA Jin S., Liu J., Zhu P., Liu Y.; RT "Systematic mapping and functional analysis of a family of human epididymal RT secretory sperm-located proteins."; RL Mol. Cell. Proteomics 9:2517-2528(2010). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [3] RP PROTEIN SEQUENCE OF 2-14 AND 864-878, CLEAVAGE OF INITIATOR METHIONINE, RP ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Embryonic kidney; RA Bienvenut W.V., Ramsay A., Leung H.Y.; RL Submitted (MAR-2009) to UniProtKB. RN [4] RP PROTEIN SEQUENCE OF 2-14 AND 606-620, CLEAVAGE OF INITIATOR METHIONINE, RP ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Embryonic kidney; RA Bienvenut W.V., Waridel P., Quadroni M.; RL Submitted (MAR-2009) to UniProtKB. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-1236 (ISOFORM 1), AND VARIANTS RP PRO-858 AND THR-1225. RC TISSUE=Testis; 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-1236 (ISOFORM 2), AND VARIANTS RP ARG-408 AND PRO-858. RC TISSUE=Brain; RX PubMed=9734811; DOI=10.1093/dnares/5.3.169; RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., RA Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. X. The RT complete sequences of 100 new cDNA clones from brain which can code for RT large proteins in vitro."; RL DNA Res. 5:169-176(1998). RN [7] 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). CC -!- FUNCTION: Probable assembly factor of SCF (SKP1-CUL1-F-box protein) E3 CC ubiquitin ligase complexes that promotes the exchange of the substrate- CC recognition F-box subunit in SCF complexes, thereby playing a key role CC in the cellular repertoire of SCF complexes. {ECO:0000250}. CC -!- SUBUNIT: Binds TBP, CNOT3 and UBE3C. {ECO:0000250}. CC -!- INTERACTION: CC O75155; Q9UHD4: CIDEB; NbExp=3; IntAct=EBI-5656182, EBI-7062247; CC O75155; Q14192: FHL2; NbExp=3; IntAct=EBI-5656182, EBI-701903; CC O75155; P43220: GLP1R; NbExp=2; IntAct=EBI-5656182, EBI-7466542; CC O75155; P08247: SYP; NbExp=3; IntAct=EBI-5656182, EBI-9071725; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O75155-1; Sequence=Displayed; CC Name=2; CC IsoId=O75155-2; Sequence=VSP_037240, VSP_037241, VSP_037242; CC -!- TISSUE SPECIFICITY: Expressed in epididymis (at protein level). CC {ECO:0000269|PubMed:20736409}. CC -!- PTM: Ubiquitinated and targeted for proteasomal degradation. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the CAND family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAI36593.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; GU727621; ADU87623.1; -; mRNA. DR EMBL; AC034198; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC136592; AAI36593.1; ALT_INIT; mRNA. DR EMBL; AB014567; BAA31642.1; -; mRNA. DR CCDS; CCDS43053.1; -. [O75155-2] DR CCDS; CCDS54554.1; -. [O75155-1] DR PIR; T01239; T01239. DR RefSeq; NP_001155971.1; NM_001162499.2. [O75155-1] DR RefSeq; NP_036430.1; NM_012298.3. [O75155-2] DR PDB; 8VVY; EM; 3.49 A; C=1-1236. DR PDBsum; 8VVY; -. DR AlphaFoldDB; O75155; -. DR EMDB; EMD-43572; -. DR SMR; O75155; -. DR BioGRID; 116701; 107. DR FunCoup; O75155; 2545. DR IntAct; O75155; 85. DR MINT; O75155; -. DR NDEx; IQUERY-CP-CAND2; 2 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000387641; -. DR GlyCosmos; O75155; 1 site, 2 glycans. DR GlyGen; O75155; 1 site, 2 O-linked glycans (1 site). DR iPTMnet; O75155; -. DR PhosphoSitePlus; O75155; -. DR BioMuta; CAND2; -. DR jPOST; O75155; -. DR MassIVE; O75155; -. DR PaxDb; 9606-ENSP00000387641; -. DR PeptideAtlas; O75155; -. DR ProteomicsDB; 49823; -. [O75155-1] DR ProteomicsDB; 49824; -. [O75155-2] DR Pumba; O75155; -. DR Antibodypedia; 5869; 66 antibodies from 21 providers. DR DNASU; 23066; -. DR Ensembl; ENST00000295989.9; ENSP00000295989.5; ENSG00000144712.14. [O75155-2] DR Ensembl; ENST00000456430.6; ENSP00000387641.2; ENSG00000144712.14. [O75155-1] DR GeneID; 23066; -. DR KEGG; hsa:23066; -. DR MANE-Select; ENST00000456430.6; ENSP00000387641.2; NM_001162499.2; NP_001155971.1. DR UCSC; uc003bxj.3; human. [O75155-1] DR AGR; HGNC:30689; -. DR ClinPGx; PA142672208; -. DR CTD; 23066; -. DR DisGeNET; 23066; -. DR GeneCards; CAND2; -. DR HGNC; HGNC:30689; CAND2. DR HPA; ENSG00000144712; Tissue enhanced (skeletal muscle, tongue). DR MIM; 610403; gene. DR OpenTargets; ENSG00000144712; -. DR VEuPathDB; HostDB:ENSG00000144712; -. DR eggNOG; KOG1824; Eukaryota. DR GeneTree; ENSGT00390000017740; -. DR HOGENOM; CLU_007157_1_0_1; -. DR InParanoid; O75155; -. DR OMA; WKLRMWA; -. DR OrthoDB; 6260732at2759; -. DR PAN-GO; O75155; 3 GO annotations based on evolutionary models. DR PhylomeDB; O75155; -. DR PathwayCommons; O75155; -. DR SignaLink; O75155; -. DR SIGNOR; O75155; -. DR Agora; ENSG00000144712; -. DR BioGRID-ORCS; 23066; 17 hits in 1162 CRISPR screens. DR CD-CODE; 91857CE7; Nucleolus. DR CD-CODE; FB4E32DD; Presynaptic clusters and postsynaptic densities. DR ChiTaRS; CAND2; human. DR GenomeRNAi; 23066; -. DR Pharos; O75155; Tbio. DR PRO; PR:O75155; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; O75155; protein. DR Bgee; ENSG00000144712; Expressed in skeletal muscle tissue of rectus abdominis and 183 other cell types or tissues. DR ExpressionAtlas; O75155; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:ARUK-UCL. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0017025; F:TBP-class protein binding; IEA:Ensembl. DR GO; GO:0006351; P:DNA-templated transcription; IEA:UniProtKB-KW. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISS:UniProtKB. DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central. DR GO; GO:0010265; P:SCF complex assembly; IBA:GO_Central. DR FunFam; 1.25.10.10:FF:000047; Cullin-associated NEDD8-dissociated protein 1; 1. DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR039852; CAND1/CAND2. DR InterPro; IPR013932; TATA-bd_TIP120. DR PANTHER; PTHR12696; TIP120; 1. DR Pfam; PF13513; HEAT_EZ; 1. DR Pfam; PF08623; TIP120; 1. DR Pfam; PF25782; TPR_CAND1; 1. DR SUPFAM; SSF48371; ARM repeat; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Direct protein sequencing; KW Nucleus; Proteomics identification; Reference proteome; Repeat; KW Transcription; Ubl conjugation; Ubl conjugation pathway. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|Ref.3, ECO:0000269|Ref.4" FT CHAIN 2..1236 FT /note="Cullin-associated NEDD8-dissociated protein 2" FT /id="PRO_0000089297" FT REPEAT 2..39 FT /note="HEAT 1" FT REPEAT 44..81 FT /note="HEAT 2" FT REPEAT 83..119 FT /note="HEAT 3" FT REPEAT 129..167 FT /note="HEAT 4" FT REPEAT 171..208 FT /note="HEAT 5" FT REPEAT 210..246 FT /note="HEAT 6" FT REPEAT 254..291 FT /note="HEAT 7" FT REPEAT 327..368 FT /note="HEAT 8" FT REPEAT 372..409 FT /note="HEAT 9" FT REPEAT 432..469 FT /note="HEAT 10" FT REPEAT 517..554 FT /note="HEAT 11" FT REPEAT 565..604 FT /note="HEAT 12" FT REPEAT 608..645 FT /note="HEAT 13" FT REPEAT 648..685 FT /note="HEAT 14" FT REPEAT 690..727 FT /note="HEAT 15" FT REPEAT 731..770 FT /note="HEAT 16" FT REPEAT 772..813 FT /note="HEAT 17" FT REPEAT 857..894 FT /note="HEAT 18" FT REPEAT 896..931 FT /note="HEAT 19" FT REPEAT 933..966 FT /note="HEAT 20" FT REPEAT 967..1003 FT /note="HEAT 21" FT REPEAT 1007..1044 FT /note="HEAT 22" FT REPEAT 1048..1084 FT /note="HEAT 23" FT REPEAT 1105..1141 FT /note="HEAT 24" FT REPEAT 1157..1194 FT /note="HEAT 25" FT REPEAT 1204..1236 FT /note="HEAT 26" FT REGION 315..346 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 317..346 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0000269|Ref.3, ECO:0000269|Ref.4" FT VAR_SEQ 71 FT /note="C -> W (in isoform 2)" FT /evidence="ECO:0000303|PubMed:9734811" FT /id="VSP_037240" FT VAR_SEQ 72..164 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:9734811" FT /id="VSP_037241" FT VAR_SEQ 1014..1037 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:9734811" FT /id="VSP_037242" FT VARIANT 408 FT /note="Q -> R (in dbSNP:rs2305398)" FT /evidence="ECO:0000269|PubMed:9734811" FT /id="VAR_055023" FT VARIANT 476 FT /note="P -> L (in dbSNP:rs2305397)" FT /id="VAR_055024" FT VARIANT 533 FT /note="S -> P (in dbSNP:rs3732675)" FT /id="VAR_055025" FT VARIANT 655 FT /note="H -> R (in dbSNP:rs9838943)" FT /id="VAR_055026" FT VARIANT 845 FT /note="L -> F (in dbSNP:rs17037287)" FT /id="VAR_055027" FT VARIANT 858 FT /note="H -> P (in dbSNP:rs3732678)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:9734811" FT /id="VAR_055028" FT VARIANT 990 FT /note="V -> I (in dbSNP:rs3817121)" FT /id="VAR_055029" FT VARIANT 1225 FT /note="A -> T (in dbSNP:rs12629133)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_055030" FT CONFLICT 204 FT /note="A -> T (in Ref. 6; BAA31642)" FT /evidence="ECO:0000305" FT HELIX 3..12 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 13..15 FT /evidence="ECO:0007829|PDB:8VVY" FT TURN 16..18 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 20..30 FT /evidence="ECO:0007829|PDB:8VVY" FT STRAND 31..33 FT /evidence="ECO:0007829|PDB:8VVY" FT TURN 35..37 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 44..53 FT /evidence="ECO:0007829|PDB:8VVY" FT STRAND 56..58 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 59..62 FT /evidence="ECO:0007829|PDB:8VVY" FT STRAND 63..65 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 66..77 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 81..95 FT /evidence="ECO:0007829|PDB:8VVY" FT STRAND 96..98 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 102..116 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 126..143 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 148..162 FT /evidence="ECO:0007829|PDB:8VVY" FT TURN 166..172 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 173..180 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 182..185 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 189..202 FT /evidence="ECO:0007829|PDB:8VVY" FT TURN 207..209 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 210..221 FT /evidence="ECO:0007829|PDB:8VVY" FT STRAND 225..227 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 231..248 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 249..251 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 253..267 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 272..288 FT /evidence="ECO:0007829|PDB:8VVY" FT TURN 290..293 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 294..296 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 297..307 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 348..365 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 367..369 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 370..376 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 378..383 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 384..386 FT /evidence="ECO:0007829|PDB:8VVY" FT STRAND 388..390 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 391..407 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 408..410 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 422..441 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 443..446 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 450..466 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 472..474 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 475..486 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 493..509 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 512..515 FT /evidence="ECO:0007829|PDB:8VVY" FT TURN 516..518 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 519..530 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 535..552 FT /evidence="ECO:0007829|PDB:8VVY" FT STRAND 555..557 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 564..578 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 585..606 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 607..609 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 610..620 FT /evidence="ECO:0007829|PDB:8VVY" FT STRAND 623..626 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 627..639 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 647..649 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 650..662 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 666..683 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 689..696 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 699..701 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 709..724 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 726..729 FT /evidence="ECO:0007829|PDB:8VVY" FT TURN 730..732 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 733..745 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 751..766 FT /evidence="ECO:0007829|PDB:8VVY" FT STRAND 774..776 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 777..787 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 795..797 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 798..814 FT /evidence="ECO:0007829|PDB:8VVY" FT TURN 816..819 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 820..830 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 837..853 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 862..870 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 875..891 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 893..906 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 911..924 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 927..929 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 931..941 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 950..964 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 968..980 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 984..996 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 1006..1017 FT /evidence="ECO:0007829|PDB:8VVY" FT TURN 1018..1021 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 1025..1041 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 1044..1047 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 1050..1052 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 1054..1061 FT /evidence="ECO:0007829|PDB:8VVY" FT TURN 1065..1067 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 1084..1100 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 1102..1104 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 1107..1118 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 1122..1138 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 1140..1159 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 1168..1189 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 1193..1196 FT /evidence="ECO:0007829|PDB:8VVY" FT HELIX 1198..1208 FT /evidence="ECO:0007829|PDB:8VVY" SQ SEQUENCE 1236 AA; 135256 MW; 38F43A7C1B8322A8 CRC64; MSTAAFHISS LLEKMTSSDK DFRFMATSDL MSELQKDSIQ LDEDSERKVV KMLLRLLEDK NGEVQNLAVK CLGPLVVKVK EYQVETIVDT LCTNMRSDKE QLRDIAGIGL KTVLSELPPA ATGSGLATNV CRKITGQLTS AIAQQEDVAV QLEALDILSD MLSRLGVPLG AFHASLLHCL LPQLSSPRLA VRKRAVGALG HLAAACSTDL FVELADHLLD RLPGPRVPTS PTAIRTLIQC LGSVGRQAGH RLGAHLDRLV PLVEDFCNLD DDELRESCLQ AFEAFLRKCP KEMGPHVPNV TSLCLQYIKH DPNYNYDSDE DEEQMETEDS EFSEQESEDE YSDDDDMSWK VRRAAAKCIA ALISSRPDLL PDFHCTLAPV LIRRFKEREE NVKADVFTAY IVLLRQTQPP KGWLEAMEEP TQTGSNLHML RGQVPLVVKA LQRQLKDRSV RARQGCFSLL TELAGVLPGS LAEHMPVLVS GIIFSLADRS SSSTIRMDAL AFLQGLLGTE PAEAFHPHLP ILLPPVMACV ADSFYKIAAE ALVVLQELVR ALWPLHRPRM LDPEPYVGEM SAVTLARLRA TDLDQEVKER AISCMGHLVG HLGDRLGDDL EPTLLLLLDR LRNEITRLPA IKALTLVAVS PLQLDLQPIL AEALHILASF LRKNQRALRL ATLAALDALA QSQGLSLPPS AVQAVLAELP ALVNESDMHV AQLAVDFLAT VTQAQPASLV EVSGPVLSEL LRLLRSPLLP AGVLAAAEGF LQALVGTRPP CVDYAKLISL LTAPVYEQAV DGGPGLHKQV FHSLARCVAA LSAACPQEAA STASRLVCDA RSPHSSTGVK VLAFLSLAEV GQVAGPGHQR ELKAVLLEAL GSPSEDVRAA ASYALGRVGA GSLPDFLPFL LEQIEAEPRR QYLLLHSLRE ALGAAQPDSL KPYAEDIWAL LFQRCEGAEE GTRGVVAECI GKLVLVNPSF LLPRLRKQLA AGRPHTRSTV ITAVKFLISD QPHPIDPLLK SFIGEFMESL QDPDLNVRRA TLAFFNSAVH NKPSLVRDLL DDILPLLYQE TKIRRDLIRE VEMGPFKHTV DDGLDVRKAA FECMYSLLES CLGQLDICEF LNHVEDGLKD HYDIRMLTFI MVARLATLCP APVLQRVDRL IEPLRATCTA KVKAGSVKQE FEKQDELKRS AMRAVAALLT IPEVGKSPIM ADFSSQIRSN PELAALFESI QKDSASAPST DSMELS //