ID HYPK_HUMAN Reviewed; 121 AA. AC Q9NX55; C9JKJ0; O75408; Q8WUW8; Q9P024; DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot. DT 23-FEB-2022, sequence version 3. DT 28-JAN-2026, entry version 156. DE RecName: Full=Huntingtin-interacting protein K {ECO:0000305}; DE AltName: Full=Huntingtin yeast partner K; GN Name=HYPK {ECO:0000312|HGNC:HGNC:18418}; Synonyms=C15orf63; GN ORFNames=HSPC136; 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 [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT PRO-97. RC TISSUE=Umbilical cord blood; RX PubMed=11042152; DOI=10.1101/gr.140200; RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.; RT "Cloning and functional analysis of cDNAs with open reading frames for 300 RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor RT cells."; RL Genome Res. 10:1546-1560(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16572171; DOI=10.1038/nature04601; RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S., RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.; RT "Analysis of the DNA sequence and duplication history of human chromosome RT 15."; RL Nature 440:671-675(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Placenta; 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 [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-121 (ISOFORM 2), AND POSSIBLE INTERACTION RP WITH HTT. RC TISSUE=Testis; RX PubMed=9700202; DOI=10.1093/hmg/7.9.1463; RA Faber P.W., Barnes G.T., Srinidhi J., Chen J., Gusella J.F., RA MacDonald M.E.; RT "Huntingtin interacts with a family of WW domain proteins."; RL Hum. Mol. Genet. 7:1463-1474(1998). RN [6] RP FUNCTION, INTERACTION WITH HTT, AND SUBCELLULAR LOCATION. RX PubMed=17947297; DOI=10.1093/hmg/ddm301; RA Raychaudhuri S., Sinha M., Mukhopadhyay D., Bhattacharyya N.P.; RT "HYPK, a Huntingtin interacting protein, reduces aggregates and apoptosis RT induced by N-terminal Huntingtin with 40 glutamines in Neuro2a cells and RT exhibits chaperone-like activity."; RL Hum. Mol. Genet. 17:240-255(2008). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBUNIT, IDENTIFICATION IN RP THE N-TERMINAL ACETYLTRANSFERASE A/HYPK COMPLEX, INTERACTION WITH NAA15, RP AND SUBCELLULAR LOCATION. RX PubMed=20154145; DOI=10.1128/mcb.01199-09; RA Arnesen T., Starheim K.K., Van Damme P., Evjenth R., Dinh H., Betts M.J., RA Ryningen A., Vandekerckhove J., Gevaert K., Anderson D.; RT "The chaperone-like protein HYPK acts together with NatA in cotranslational RT N-terminal acetylation and prevention of Huntingtin aggregation."; RL Mol. Cell. Biol. 30:1898-1909(2010). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [9] 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 [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=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 [11] RP IDENTIFICATION BY MASS 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 [12] {ECO:0007744|PDB:6C95} RP X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) OF 27-121 IN COMPLEX WITH NAA10 AND RP NAA15, FUNCTION, IDENTIFICATION IN THE N-TERMINAL ACETYLTRANSFERASE A/HYPK RP COMPLEX, IDENTIFICATION IN THE N-TERMINAL ACETYLTRANSFERASE E/HYPK COMPLEX, RP INTERACTION WITH NAA10 AND NAA15, AND MUTAGENESIS OF HIS-28; LEU-35; VAL-38 RP AND 52-LEU--ASN-121. RX PubMed=29754825; DOI=10.1016/j.str.2018.04.003; RA Gottlieb L., Marmorstein R.; RT "Structure of Human NatA and Its Regulation by the Huntingtin Interacting RT Protein HYPK."; RL Structure 26:925-935.e8(2018). RN [13] {ECO:0007744|PDB:6C95} RP STRUCTURE BY ELECTRON MICROSCOPY (4.03 ANGSTROMS), FUNCTION, IDENTIFICATION RP IN THE N-TERMINAL ACETYLTRANSFERASE A/HYPK COMPLEX, IDENTIFICATION IN THE RP N-TERMINAL ACETYLTRANSFERASE E/HYPK COMPLEX, AND INTERACTION WITH NAA10 AND RP NAA15. RX PubMed=32042062; DOI=10.1038/s41467-020-14584-7; RA Deng S., McTiernan N., Wei X., Arnesen T., Marmorstein R.; RT "Molecular basis for N-terminal acetylation by human NatE and its RT modulation by HYPK."; RL Nat. Commun. 11:818-818(2020). CC -!- FUNCTION: Component of several N-terminal acetyltransferase complexes CC (PubMed:20154145, PubMed:29754825, PubMed:32042062). Inhibits the N- CC terminal acetylation activity of the N-terminal acetyltransferase CC NAA10-NAA15 complex (also called the NatA complex) (PubMed:29754825, CC PubMed:32042062). Has chaperone-like activity preventing polyglutamine CC (polyQ) aggregation of HTT in neuronal cells probably while associated CC with the NatA complex (PubMed:17947297, PubMed:20154145). May play a CC role in the NatA complex-mediated N-terminal acetylation of PCNP CC (PubMed:20154145). {ECO:0000269|PubMed:17947297, CC ECO:0000269|PubMed:20154145, ECO:0000269|PubMed:29754825, CC ECO:0000269|PubMed:32042062}. CC -!- SUBUNIT: Component of the N-terminal acetyltransferase A (NatA)/HYPK CC complex at least composed of NAA10, NAA15 and HYPK, which has N- CC terminal acetyltransferase activity (PubMed:20154145, PubMed:29754825, CC PubMed:32042062). Within the complex interacts with NAA10 CC (PubMed:29754825, PubMed:32042062). Within the complex interacts with CC NAA15 (PubMed:20154145, PubMed:29754825, PubMed:32042062). CC Predominantly interacts with NAA15 in the NAA10-NAA15 complex (also CC called the NatA complex); the interaction with the NatA complex reduces CC the acetylation activity of the NatA complex (PubMed:29754825, CC PubMed:32042062). Interacts with HTT (via N-terminus) CC (PubMed:17947297). The NatA complex is required for HYPK stability and CC for reducing polyQ aggregation of HTT (PubMed:20154145, CC PubMed:29754825, PubMed:32042062). Component of the N-terminal CC acetyltransferase E (NatE)/HYPK complex at least composed of NAA10, CC NAA15, NAA50 and HYPK (PubMed:32042062). Within the complex interacts CC with NAA10 and NAA15 (PubMed:32042062). Does not interact with NAA50 CC (PubMed:29754825, PubMed:32042062). Interaction with NAA15 reduces the CC capacity of NAA15 to interact with NAA50 (PubMed:29754825, CC PubMed:32042062). Its capacity to interact with the NatA complex is CC reduced by NAA50 (PubMed:32042062). Does not interact with the N- CC terminal acetyltransferase B (NatB) complex component NAA25 or the N- CC terminal acetyltransferase C (NatC) complex component NAA35 CC (PubMed:20154145). {ECO:0000269|PubMed:17947297, CC ECO:0000269|PubMed:20154145, ECO:0000269|PubMed:29754825, CC ECO:0000269|PubMed:32042062}. CC -!- INTERACTION: CC Q9NX55; Q2NKX9: C2orf68; NbExp=5; IntAct=EBI-1048743, EBI-11603468; CC Q9NX55; P42858: HTT; NbExp=4; IntAct=EBI-1048743, EBI-466029; CC Q9NX55; P43355: MAGEA1; NbExp=3; IntAct=EBI-1048743, EBI-740978; CC Q9NX55; Q9BXJ9: NAA15; NbExp=8; IntAct=EBI-1048743, EBI-1042540; CC Q9NX55; P40222: TXLNA; NbExp=6; IntAct=EBI-1048743, EBI-359793; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20154145}. Cytoplasm CC {ECO:0000269|PubMed:20154145}. Note=Within the NatA/HYPK complex, may CC localize to ribosomes. {ECO:0000269|PubMed:20154145}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=2; CC IsoId=Q9NX55-2; Sequence=Displayed; CC Name=3; CC IsoId=Q9NX55-3; Sequence=VSP_040677, VSP_040678; CC -!- SEQUENCE CAUTION: CC Sequence=AAH19262.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAA91165.1; Type=Miscellaneous discrepancy; Note=Readthrough transcript SERF2-HYPK/C15orf63.; 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; AF161485; AAF29100.1; -; mRNA. DR EMBL; AK000438; BAA91165.1; ALT_SEQ; mRNA. DR EMBL; AK022435; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AC018512; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC019262; AAH19262.2; ALT_INIT; mRNA. DR EMBL; AF049613; AAC26849.1; -; mRNA. DR CCDS; CCDS10104.2; -. [Q9NX55-2] DR RefSeq; NP_001186814.1; NM_001199885.1. DR PDB; 6C95; X-ray; 3.15 A; D=27-121. DR PDB; 6PW9; EM; 4.03 A; D=1-121. DR PDB; 9F1D; EM; 3.26 A; DD=1-121. DR PDBsum; 6C95; -. DR PDBsum; 6PW9; -. DR PDBsum; 9F1D; -. DR AlphaFoldDB; Q9NX55; -. DR EMDB; EMD-20501; -. DR EMDB; EMD-50126; -. DR SMR; Q9NX55; -. DR BioGRID; 117304; 125. DR CORUM; Q9NX55; -. DR FunCoup; Q9NX55; 2061. DR IntAct; Q9NX55; 27. DR MINT; Q9NX55; -. DR STRING; 9606.ENSP00000384474; -. DR iPTMnet; Q9NX55; -. DR MetOSite; Q9NX55; -. DR PhosphoSitePlus; Q9NX55; -. DR BioMuta; HYPK; -. DR DMDM; 325511335; -. DR jPOST; Q9NX55; -. DR MassIVE; Q9NX55; -. DR PaxDb; 9606-ENSP00000384474; -. DR PeptideAtlas; Q9NX55; -. DR ProteomicsDB; 83042; -. [Q9NX55-2] DR ProteomicsDB; 83043; -. [Q9NX55-3] DR Pumba; Q9NX55; -. DR TopDownProteomics; Q9NX55-2; -. [Q9NX55-2] DR Antibodypedia; 65071; 7 antibodies from 5 providers. DR DNASU; 25764; -. DR Ensembl; ENST00000406925.7; ENSP00000384474.2; ENSG00000242028.9. [Q9NX55-2] DR Ensembl; ENST00000442995.4; ENSP00000401155.3; ENSG00000242028.9. [Q9NX55-2] DR GeneID; 25764; -. DR KEGG; hsa:25764; -. DR MANE-Select; ENST00000442995.4; ENSP00000401155.3; NM_016400.4; NP_057484.4. DR UCSC; uc059inn.1; human. [Q9NX55-2] DR AGR; HGNC:18418; -. DR ClinPGx; PA165478509; -. DR CTD; 25764; -. DR DisGeNET; 25764; -. DR GeneCards; HYPK; -. DR HGNC; HGNC:18418; HYPK. DR HPA; ENSG00000242028; Low tissue specificity. DR MIM; 612784; gene. DR OpenTargets; ENSG00000242028; -. DR VEuPathDB; HostDB:ENSG00000242028; -. DR eggNOG; KOG3450; Eukaryota. DR GeneTree; ENSGT00390000008502; -. DR HOGENOM; CLU_128817_1_1_1; -. DR InParanoid; Q9NX55; -. DR OMA; IIGDRRN; -. DR OrthoDB; 285219at2759; -. DR PAN-GO; Q9NX55; 2 GO annotations based on evolutionary models. DR PhylomeDB; Q9NX55; -. DR PathwayCommons; Q9NX55; -. DR SABIO-RK; Q9NX55; -. DR SignaLink; Q9NX55; -. DR Agora; ENSG00000242028; -. DR BioGRID-ORCS; 25764; 712 hits in 1167 CRISPR screens. DR GenomeRNAi; 25764; -. DR Pharos; Q9NX55; Tbio. DR PRO; PR:Q9NX55; -. DR Proteomes; UP000005640; Chromosome 15. DR RNAct; Q9NX55; protein. DR Bgee; ENSG00000242028; Expressed in hindlimb stylopod muscle and 96 other cell types or tissues. DR ExpressionAtlas; Q9NX55; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:CAFA. DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:CAFA. DR GO; GO:0032991; C:protein-containing complex; IDA:CAFA. DR GO; GO:0044183; F:protein folding chaperone; IDA:DisProt. DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:CAFA. DR GO; GO:0050821; P:protein stabilization; IDA:CAFA. DR CDD; cd14361; UBA_HYPK; 1. DR DisProt; DP00546; -. DR FunFam; 1.10.8.10:FF:000052; Huntingtin-interacting protein K (Predicted); 1. DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1. DR InterPro; IPR052617; Huntingtin-int_K. DR InterPro; IPR038922; HYPK_UBA. DR InterPro; IPR044034; NAC-like_UBA. DR PANTHER; PTHR31184:SF2; HUNTINGTIN-INTERACTING PROTEIN K; 1. DR PANTHER; PTHR31184; HUNTINGTIN-INTERACTING PROTEIN K FAMILY MEMBER; 1. DR Pfam; PF19026; UBA_HYPK; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Coiled coil; Cytoplasm; Nucleus; KW Phosphoprotein; Proteomics identification; Reference proteome. FT CHAIN 1..121 FT /note="Huntingtin-interacting protein K" FT /id="PRO_0000274605" FT REGION 1..75 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 52..121 FT /note="Required for association with the NAA10-NAA15 FT complex" FT /evidence="ECO:0000269|PubMed:29754825" FT COILED 62..107 FT /evidence="ECO:0000255" FT COMPBIAS 1..13 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 20..47 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 60..75 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 30 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT VAR_SEQ 55..74 FT /note="AMSVIGDRRSREQKAKQERE -> GERTGKSHYQEGRSGANSEW (in FT isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_040677" FT VAR_SEQ 78..121 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_040678" FT VARIANT 97 FT /note="S -> P (in dbSNP:rs12702)" FT /evidence="ECO:0000269|PubMed:11042152" FT /id="VAR_030335" FT MUTAGEN 28 FT /note="H->A: Reduces ability to inhibit NAA10-NAA15 FT complex-mediated N-terminal acetylation, which results in FT increased N-terminal acetylation." FT /evidence="ECO:0000269|PubMed:29754825" FT MUTAGEN 35 FT /note="L->A: Reduces ability to inhibit NAA10-NAA15 FT complex-mediated N-terminal acetylation, which results in FT increased N-terminal acetylation; when associated with FT A-38." FT /evidence="ECO:0000269|PubMed:29754825" FT MUTAGEN 38 FT /note="V->A: Reduces ability to inhibit NAA10-NAA15 FT complex-mediated N-terminal acetylation, which results in FT increased N-terminal acetylation; when associated with FT A-35." FT /evidence="ECO:0000269|PubMed:29754825" FT MUTAGEN 52..121 FT /note="Missing: Abolishes interaction with NAA10 and FT NAA15." FT /evidence="ECO:0000269|PubMed:29754825" FT TURN 30..35 FT /evidence="ECO:0007829|PDB:6C95" FT HELIX 36..39 FT /evidence="ECO:0007829|PDB:6C95" FT HELIX 52..78 FT /evidence="ECO:0007829|PDB:6C95" FT HELIX 84..93 FT /evidence="ECO:0007829|PDB:6C95" FT HELIX 98..107 FT /evidence="ECO:0007829|PDB:6C95" FT TURN 108..110 FT /evidence="ECO:0007829|PDB:6C95" FT HELIX 112..120 FT /evidence="ECO:0007829|PDB:6C95" SQ SEQUENCE 121 AA; 13651 MW; 27028987B3FE6EE8 CRC64; MATEGDVELE LETETSGPER PPEKPRKHDS GAADLERVTD YAEEKEIQSS NLETAMSVIG DRRSREQKAK QEREKELAKV TIKKEDLELI MTEMEISRAA AERSLREHMG NVVEALIALT N //