VATL_HUMAN
ID VATL_HUMAN Reviewed; 155 AA.
AC P27449; Q6FH26;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=V-type proton ATPase 16 kDa proteolipid subunit c {ECO:0000305};
DE Short=V-ATPase 16 kDa proteolipid subunit c {ECO:0000305};
DE AltName: Full=Vacuolar proton pump 16 kDa proteolipid subunit c {ECO:0000305};
GN Name=ATP6V0C; Synonyms=ATP6C, ATP6L, ATPL;
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].
RX PubMed=1709739; DOI=10.1073/pnas.88.10.4289;
RA Gillespie G.A.J., Somlo S., Germino G.G., Weinstat-Saslow D., Reeders S.T.;
RT "CpG island in the region of an autosomal dominant polycystic kidney
RT disease locus defines the 5' end of a gene encoding a putative proton
RT channel.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:4289-4293(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Muscle, and Skin;
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 28-155.
RX PubMed=1532310; DOI=10.1016/0006-291x(92)90562-y;
RA Hasebe M., Hanada H., Moriyama Y., Maeda M., Futai M.;
RT "Vacuolar type H(+)-ATPase genes: presence of four genes including
RT pseudogenes for the 16-kDa proteolipid subunit in the human genome.";
RL Biochem. Biophys. Res. Commun. 183:856-863(1992).
RN [6]
RP INTERACTION WITH HTLV-1 ACCESSORY PROTEIN P12I (MICROBIAL INFECTION).
RX PubMed=7636472; DOI=10.1099/0022-1317-76-8-1909;
RA Koralnik I.J., Mulloy J.C., Andresson T., Fullen J., Franchini G.;
RT "Mapping of the intermolecular association of human T cell
RT leukaemia/lymphotropic virus type I p12I and the vacuolar H+-ATPase 16 kDa
RT subunit protein.";
RL J. Gen. Virol. 76:1909-1916(1995).
RN [7]
RP INTERACTION WITH LASS2.
RX PubMed=11543633; DOI=10.1006/geno.2001.6614;
RA Pan H., Qin W.-X., Huo K.-K., Wan D.-F., Yu Y., Xu Z.-G., Hu Q.-D.,
RA Gu K.T., Zhou X.-M., Jiang H.-Q., Zhang P.-P., Huang Y., Li Y.-Y.,
RA Gu J.-R.;
RT "Cloning, mapping, and characterization of a human homologue of the yeast
RT longevity assurance gene LAG1.";
RL Genomics 77:58-64(2001).
RN [8]
RP INTERACTION WITH RNF182, AND UBIQUITINATION.
RX PubMed=18298843; DOI=10.1186/1750-1326-3-4;
RA Liu Q.Y., Lei J.X., Sikorska M., Liu R.;
RT "A novel brain-enriched E3 ubiquitin ligase RNF182 is up regulated in the
RT brains of Alzheimer's patients and targets ATP6V0C for degradation.";
RL Mol. Neurodegener. 3:4-4(2008).
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].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [11] {ECO:0007744|PDB:6WLW, ECO:0007744|PDB:6WM2, ECO:0007744|PDB:6WM3, ECO:0007744|PDB:6WM4}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.00 ANGSTROMS), FUNCTION, AND
RP IDENTIFICATION IN THE V-ATPASE COMPLEX.
RX PubMed=33065002; DOI=10.1016/j.molcel.2020.09.029;
RA Wang L., Wu D., Robinson C.V., Wu H., Fu T.M.;
RT "Structures of a Complete Human V-ATPase Reveal Mechanisms of Its
RT Assembly.";
RL Mol. Cell 80:501-511.e3(2020).
CC -!- FUNCTION: Proton-conducting pore forming of the V0 complex of
CC vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a
CC peripheral complex (V1) that hydrolyzes ATP and a membrane integral
CC complex (V0) that translocates protons (PubMed:33065002). V-ATPase is
CC responsible for acidifying and maintaining the pH of intracellular
CC compartments and in some cell types, is targeted to the plasma
CC membrane, where it is responsible for acidifying the extracellular
CC environment (By similarity). {ECO:0000250|UniProtKB:P23956,
CC ECO:0000269|PubMed:33065002}.
CC -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme made up of two
CC complexes: the ATP-hydrolytic V1 complex and the proton translocation
CC V0 complex (PubMed:33065002). The V1 complex consists of three
CC catalytic AB heterodimers that form a heterohexamer, three peripheral
CC stalks each consisting of EG heterodimers, one central rotor including
CC subunits D and F, and the regulatory subunits C and H
CC (PubMed:33065002). The proton translocation complex V0 consists of the
CC proton transport subunit a, a ring of proteolipid subunits c9c'',
CC rotary subunit d, subunits e and f, and the accessory subunits
CC ATP6AP1/Ac45 and ATP6AP2/PRR (PubMed:33065002). Interacts with the V0
CC complex V-ATPase subunit a4 ATP6V0A4 (By similarity). Interacts with
CC LASS2 (PubMed:11543633). Interacts with RNF182; this interaction leads
CC to ubiquitination and degradation via the proteasome pathway
CC (PubMed:18298843). {ECO:0000250|UniProtKB:P63082,
CC ECO:0000269|PubMed:11543633, ECO:0000269|PubMed:18298843,
CC ECO:0000269|PubMed:33065002}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HTLV-1 accessory protein
CC p12I. {ECO:0000269|PubMed:7636472}.
CC -!- INTERACTION:
CC P27449; Q13520: AQP6; NbExp=3; IntAct=EBI-721179, EBI-13059134;
CC P27449; P07307-3: ASGR2; NbExp=3; IntAct=EBI-721179, EBI-12808270;
CC P27449; P19397: CD53; NbExp=3; IntAct=EBI-721179, EBI-6657396;
CC P27449; Q07108: CD69; NbExp=3; IntAct=EBI-721179, EBI-2836595;
CC P27449; P11912: CD79A; NbExp=3; IntAct=EBI-721179, EBI-7797864;
CC P27449; Q96G23: CERS2; NbExp=3; IntAct=EBI-721179, EBI-1057080;
CC P27449; Q86T13: CLEC14A; NbExp=3; IntAct=EBI-721179, EBI-17710733;
CC P27449; Q6ZS10: CLEC17A; NbExp=3; IntAct=EBI-721179, EBI-11977093;
CC P27449; Q9UHP7-3: CLEC2D; NbExp=3; IntAct=EBI-721179, EBI-11749983;
CC P27449; Q7Z7G2: CPLX4; NbExp=3; IntAct=EBI-721179, EBI-18013275;
CC P27449; Q9NR28: DIABLO; NbExp=3; IntAct=EBI-721179, EBI-517508;
CC P27449; Q96KC8: DNAJC1; NbExp=3; IntAct=EBI-721179, EBI-296550;
CC P27449; Q92838: EDA; NbExp=4; IntAct=EBI-721179, EBI-529425;
CC P27449; Q9HAV5: EDA2R; NbExp=3; IntAct=EBI-721179, EBI-526033;
CC P27449; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-721179, EBI-781551;
CC P27449; P84090: ERH; NbExp=3; IntAct=EBI-721179, EBI-711389;
CC P27449; P22794: EVI2A; NbExp=3; IntAct=EBI-721179, EBI-2870359;
CC P27449; Q96KR6: FAM210B; NbExp=3; IntAct=EBI-721179, EBI-18938272;
CC P27449; O15552: FFAR2; NbExp=3; IntAct=EBI-721179, EBI-2833872;
CC P27449; Q8TBE3: FNDC9; NbExp=3; IntAct=EBI-721179, EBI-12142257;
CC P27449; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-721179, EBI-13345167;
CC P27449; O00155: GPR25; NbExp=3; IntAct=EBI-721179, EBI-10178951;
CC P27449; O15529: GPR42; NbExp=3; IntAct=EBI-721179, EBI-18076404;
CC P27449; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-721179, EBI-18053395;
CC P27449; Q13651: IL10RA; NbExp=3; IntAct=EBI-721179, EBI-1031656;
CC P27449; P16871: IL7R; NbExp=3; IntAct=EBI-721179, EBI-80490;
CC P27449; Q92876: KLK6; NbExp=3; IntAct=EBI-721179, EBI-2432309;
CC P27449; P26715: KLRC1; NbExp=3; IntAct=EBI-721179, EBI-9018187;
CC P27449; Q8N386: LRRC25; NbExp=3; IntAct=EBI-721179, EBI-11304917;
CC P27449; Q8IX19: MCEMP1; NbExp=5; IntAct=EBI-721179, EBI-2816356;
CC P27449; P21757: MSR1; NbExp=6; IntAct=EBI-721179, EBI-1776976;
CC P27449; Q6P499: NIPAL3; NbExp=3; IntAct=EBI-721179, EBI-10252783;
CC P27449; P35372-10: OPRM1; NbExp=3; IntAct=EBI-721179, EBI-12807478;
CC P27449; Q9BQ51: PDCD1LG2; NbExp=3; IntAct=EBI-721179, EBI-16427978;
CC P27449; Q6UXB8: PI16; NbExp=3; IntAct=EBI-721179, EBI-12810028;
CC P27449; P25788: PSMA3; NbExp=3; IntAct=EBI-721179, EBI-348380;
CC P27449; Q9H6H4: REEP4; NbExp=3; IntAct=EBI-721179, EBI-7545592;
CC P27449; Q86VR2: RETREG3; NbExp=3; IntAct=EBI-721179, EBI-10192441;
CC P27449; Q9NY72: SCN3B; NbExp=3; IntAct=EBI-721179, EBI-17247926;
CC P27449; Q7Z769: SLC35E3; NbExp=3; IntAct=EBI-721179, EBI-13389236;
CC P27449; P30825: SLC7A1; NbExp=3; IntAct=EBI-721179, EBI-4289564;
CC P27449; Q9BZL3: SMIM3; NbExp=6; IntAct=EBI-721179, EBI-741850;
CC P27449; Q9HBV2: SPACA1; NbExp=3; IntAct=EBI-721179, EBI-17498703;
CC P27449; Q8WWF3: SSMEM1; NbExp=3; IntAct=EBI-721179, EBI-17280858;
CC P27449; P27105: STOM; NbExp=3; IntAct=EBI-721179, EBI-1211440;
CC P27449; Q96L08: SUSD3; NbExp=3; IntAct=EBI-721179, EBI-18194029;
CC P27449; Q8IV31: TMEM139; NbExp=3; IntAct=EBI-721179, EBI-7238458;
CC P27449; Q9P0T7: TMEM9; NbExp=3; IntAct=EBI-721179, EBI-723976;
CC P27449; Q9H7M9: VSIR; NbExp=3; IntAct=EBI-721179, EBI-744988;
CC P27449; Q6PEW1: ZCCHC12; NbExp=3; IntAct=EBI-721179, EBI-748373;
CC P27449; P0CK45: E5; Xeno; NbExp=2; IntAct=EBI-721179, EBI-7015490;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle
CC membrane {ECO:0000250|UniProtKB:P63081}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle
CC membrane {ECO:0000250|UniProtKB:P63081}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- PTM: Ubiquitinated by RNF182, leading to its degradation via the
CC ubiquitin-proteasome pathway. {ECO:0000269|PubMed:18298843}.
CC -!- SIMILARITY: Belongs to the V-ATPase proteolipid subunit family.
CC {ECO:0000305}.
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DR EMBL; M62762; AAA60039.1; -; mRNA.
DR EMBL; CR541930; CAG46728.1; -; mRNA.
DR EMBL; CR541951; CAG46749.1; -; mRNA.
DR EMBL; BT007155; AAP35819.1; -; mRNA.
DR EMBL; BC004537; AAH04537.1; -; mRNA.
DR EMBL; BC007389; AAH07389.1; -; mRNA.
DR EMBL; BC007759; AAH07759.1; -; mRNA.
DR EMBL; BC009290; AAH09290.1; -; mRNA.
DR CCDS; CCDS10470.1; -.
DR PIR; A39367; A39367.
DR RefSeq; NP_001185498.1; NM_001198569.1.
DR RefSeq; NP_001685.1; NM_001694.3.
DR PDB; 6WLW; EM; 3.00 A; 1/2/3/4/5/6/7/8/9=1-155.
DR PDB; 6WM2; EM; 3.10 A; 1/2/3/4/5/6/7/8/9=1-155.
DR PDB; 6WM3; EM; 3.40 A; 1/2/3/4/5/6/7/8/9=1-155.
DR PDB; 6WM4; EM; 3.60 A; 1/2/3/4/5/6/7/8/9=1-155.
DR PDBsum; 6WLW; -.
DR PDBsum; 6WM2; -.
DR PDBsum; 6WM3; -.
DR PDBsum; 6WM4; -.
DR AlphaFoldDB; P27449; -.
DR SMR; P27449; -.
DR BioGRID; 107010; 140.
DR ComplexPortal; CPX-2470; Vacuolar proton translocating ATPase complex, ATP6V0A1 variant.
DR ComplexPortal; CPX-6904; Vacuolar proton translocating ATPase complex, ATP6V0A2 variant.
DR ComplexPortal; CPX-6905; Vacuolar proton translocating ATPase complex, ATP6V0A3 variant.
DR ComplexPortal; CPX-6912; Vacuolar proton translocating ATPase complex, ATP6V0A4 variant.
DR CORUM; P27449; -.
DR IntAct; P27449; 72.
DR MINT; P27449; -.
DR STRING; 9606.ENSP00000329757; -.
DR DrugBank; DB01133; Tiludronic acid.
DR iPTMnet; P27449; -.
DR PhosphoSitePlus; P27449; -.
DR BioMuta; ATP6V0C; -.
DR DMDM; 137479; -.
DR EPD; P27449; -.
DR jPOST; P27449; -.
DR MassIVE; P27449; -.
DR MaxQB; P27449; -.
DR PaxDb; P27449; -.
DR PeptideAtlas; P27449; -.
DR PRIDE; P27449; -.
DR ProteomicsDB; 54393; -.
DR TopDownProteomics; P27449; -.
DR Antibodypedia; 23806; 83 antibodies from 18 providers.
DR DNASU; 527; -.
DR Ensembl; ENST00000330398.9; ENSP00000329757.4; ENSG00000185883.12.
DR GeneID; 527; -.
DR KEGG; hsa:527; -.
DR MANE-Select; ENST00000330398.9; ENSP00000329757.4; NM_001694.4; NP_001685.1.
DR UCSC; uc002cqn.4; human.
DR CTD; 527; -.
DR DisGeNET; 527; -.
DR GeneCards; ATP6V0C; -.
DR HGNC; HGNC:855; ATP6V0C.
DR HPA; ENSG00000185883; Low tissue specificity.
DR MalaCards; ATP6V0C; -.
DR MIM; 108745; gene.
DR neXtProt; NX_P27449; -.
DR OpenTargets; ENSG00000185883; -.
DR PharmGKB; PA25149; -.
DR VEuPathDB; HostDB:ENSG00000185883; -.
DR eggNOG; KOG0232; Eukaryota.
DR GeneTree; ENSGT00550000074873; -.
DR HOGENOM; CLU_085752_1_2_1; -.
DR InParanoid; P27449; -.
DR OMA; NFIQLGA; -.
DR OrthoDB; 1534092at2759; -.
DR PhylomeDB; P27449; -.
DR TreeFam; TF300025; -.
DR BioCyc; MetaCyc:MON66-34368; -.
DR PathwayCommons; P27449; -.
DR Reactome; R-HSA-1222556; ROS and RNS production in phagocytes.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-77387; Insulin receptor recycling.
DR Reactome; R-HSA-917977; Transferrin endocytosis and recycling.
DR Reactome; R-HSA-9639288; Amino acids regulate mTORC1.
DR Reactome; R-HSA-983712; Ion channel transport.
DR SignaLink; P27449; -.
DR BioGRID-ORCS; 527; 824 hits in 1087 CRISPR screens.
DR ChiTaRS; ATP6V0C; human.
DR GeneWiki; ATP6V0C; -.
DR GenomeRNAi; 527; -.
DR Pharos; P27449; Tbio.
DR PRO; PR:P27449; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P27449; protein.
DR Bgee; ENSG00000185883; Expressed in superior frontal gyrus and 93 other tissues.
DR ExpressionAtlas; P27449; baseline and differential.
DR Genevisible; P27449; HS.
DR GO; GO:0035577; C:azurophil granule membrane; TAS:Reactome.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0010008; C:endosome membrane; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IC:ComplexPortal.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0033176; C:proton-transporting V-type ATPase complex; IC:ComplexPortal.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome.
DR GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; ISS:UniProtKB.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; TAS:UniProtKB.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; TAS:ProtInc.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0048388; P:endosomal lumen acidification; IC:ComplexPortal.
DR GO; GO:0061795; P:Golgi lumen acidification; IC:ComplexPortal.
DR GO; GO:0051452; P:intracellular pH reduction; IC:ComplexPortal.
DR GO; GO:0007042; P:lysosomal lumen acidification; IC:ComplexPortal.
DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IMP:UniProtKB.
DR GO; GO:1902600; P:proton transmembrane transport; TAS:ProtInc.
DR GO; GO:0016241; P:regulation of macroautophagy; NAS:ParkinsonsUK-UCL.
DR GO; GO:0007035; P:vacuolar acidification; IC:ComplexPortal.
DR Gene3D; 1.20.120.610; -; 1.
DR InterPro; IPR002379; ATPase_proteolipid_c-like_dom.
DR InterPro; IPR000245; ATPase_proteolipid_csu.
DR InterPro; IPR011555; ATPase_proteolipid_su_C_euk.
DR InterPro; IPR035921; F/V-ATP_Csub_sf.
DR Pfam; PF00137; ATP-synt_C; 2.
DR PRINTS; PR00122; VACATPASE.
DR SUPFAM; SSF81333; SSF81333; 2.
DR TIGRFAMs; TIGR01100; V_ATP_synt_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasmic vesicle; Host-virus interaction;
KW Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW Synapse; Transmembrane; Transmembrane helix; Transport; Ubl conjugation.
FT CHAIN 1..155
FT /note="V-type proton ATPase 16 kDa proteolipid subunit c"
FT /id="PRO_0000071743"
FT TOPO_DOM 1..10
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 11..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..55
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 77..92
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 115..131
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 153..155
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT SITE 139
FT /note="Essential for proton translocation"
FT /evidence="ECO:0000250|UniProtKB:P63081"
FT HELIX 9..12
FT /evidence="ECO:0007829|PDB:6WLW"
FT HELIX 13..45
FT /evidence="ECO:0007829|PDB:6WLW"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:6WLW"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:6WLW"
FT HELIX 57..76
FT /evidence="ECO:0007829|PDB:6WLW"
FT HELIX 86..123
FT /evidence="ECO:0007829|PDB:6WLW"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:6WLW"
FT HELIX 128..137
FT /evidence="ECO:0007829|PDB:6WLW"
FT HELIX 140..152
FT /evidence="ECO:0007829|PDB:6WLW"
SQ SEQUENCE 155 AA; 15736 MW; 91141854A0492A5B CRC64;
MSESKSGPEY ASFFAVMGAS AAMVFSALGA AYGTAKSGTG IAAMSVMRPE QIMKSIIPVV
MAGIIAIYGL VVAVLIANSL NDDISLYKSF LQLGAGLSVG LSGLAAGFAI GIVGDAGVRG
TAQQPRLFVG MILILIFAEV LGLYGLIVAL ILSTK
