HYPK_HUMAN
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 03-AUG-2022, entry version 141.
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=5; 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};
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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; CCDS10104.1; -. [Q9NX55-2]
DR RefSeq; NP_001186814.1; NM_001199885.1.
DR RefSeq; NP_057484.3; NM_016400.3.
DR PDB; 6C95; X-ray; 3.15 A; D=27-121.
DR PDB; 6PW9; EM; 4.03 A; D=1-121.
DR PDBsum; 6C95; -.
DR PDBsum; 6PW9; -.
DR AlphaFoldDB; Q9NX55; -.
DR SMR; Q9NX55; -.
DR BioGRID; 117304; 108.
DR IntAct; Q9NX55; 19.
DR MINT; Q9NX55; -.
DR STRING; 9606.ENSP00000384474; -.
DR iPTMnet; Q9NX55; -.
DR MetOSite; Q9NX55; -.
DR PhosphoSitePlus; Q9NX55; -.
DR BioMuta; HYPK; -.
DR DMDM; 325511335; -.
DR EPD; Q9NX55; -.
DR jPOST; Q9NX55; -.
DR MassIVE; Q9NX55; -.
DR MaxQB; Q9NX55; -.
DR PaxDb; Q9NX55; -.
DR PeptideAtlas; Q9NX55; -.
DR PRIDE; Q9NX55; -.
DR ProteomicsDB; 83042; -. [Q9NX55-2]
DR ProteomicsDB; 83043; -. [Q9NX55-3]
DR TopDownProteomics; Q9NX55-2; -. [Q9NX55-2]
DR Antibodypedia; 65071; 7 antibodies from 5 providers.
DR DNASU; 25764; -.
DR Ensembl; ENST00000406925.6; ENSP00000384474.2; ENSG00000242028.8. [Q9NX55-2]
DR Ensembl; ENST00000442995.4; ENSP00000401155.3; ENSG00000242028.8. [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 CTD; 25764; -.
DR DisGeNET; 25764; -.
DR GeneCards; HYPK; -.
DR HGNC; HGNC:18418; HYPK.
DR HPA; ENSG00000242028; Low tissue specificity.
DR MIM; 612784; gene.
DR neXtProt; NX_Q9NX55; -.
DR OpenTargets; ENSG00000242028; -.
DR PharmGKB; PA165478509; -.
DR VEuPathDB; HostDB:ENSG00000242028; -.
DR eggNOG; KOG3450; Eukaryota.
DR GeneTree; ENSGT00390000008502; -.
DR HOGENOM; CLU_128817_1_1_1; -.
DR InParanoid; Q9NX55; -.
DR PhylomeDB; Q9NX55; -.
DR TreeFam; TF325606; -.
DR PathwayCommons; Q9NX55; -.
DR SignaLink; Q9NX55; -.
DR BioGRID-ORCS; 25764; 679 hits in 1087 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 94 other tissues.
DR ExpressionAtlas; Q9NX55; baseline and differential.
DR Genevisible; Q9NX55; HS.
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:0047485; F:protein N-terminus binding; IPI:CAFA.
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 InterPro; IPR038922; HYPK_UBA.
DR InterPro; IPR044034; NAC-like_UBA.
DR Pfam; PF19026; HYPK_UBA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Cytoplasm; Nucleus;
KW Phosphoprotein; 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 13..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..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 A-
FT 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 A-
FT 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
