VPP1_HUMAN
ID VPP1_HUMAN Reviewed; 837 AA.
AC Q93050; B7Z3B7; Q8N5G7; Q9NSX0;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 3.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=V-type proton ATPase 116 kDa subunit a 1;
DE Short=V-ATPase 116 kDa subunit a 1;
DE AltName: Full=Clathrin-coated vesicle/synaptic vesicle proton pump 116 kDa subunit;
DE AltName: Full=Vacuolar adenosine triphosphatase subunit Ac116;
DE AltName: Full=Vacuolar proton pump subunit 1;
DE AltName: Full=Vacuolar proton translocating ATPase 116 kDa subunit a isoform 1;
GN Name=ATP6V0A1; Synonyms=ATP6N1, ATP6N1A, VPP1;
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] (ISOFORM 2).
RC TISSUE=Pancreas;
RA Fehr C.N., Gillies R.J., Wang H.-Y., Ullrich A.;
RT "Sequence and alternative splicing in human 115 kDa subunit of vacuolar-
RT type H(+)-ATPase.";
RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Hippocampus, and Placenta;
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=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 675-837 (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Melanoma;
RX PubMed=12643545; DOI=10.1021/pr025562r;
RA Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K., Valencia J.,
RA Muller J., Vieira W.D., Watabe H., Shabanowitz J., Hearing V.J., Hunt D.F.,
RA Appella E.;
RT "Proteomic analysis of early melanosomes: identification of novel
RT melanosomal proteins.";
RL J. Proteome Res. 2:69-79(2003).
RN [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J.,
RA Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S.,
RA Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.;
RT "Proteomic and bioinformatic characterization of the biogenesis and
RT function of melanosomes.";
RL J. Proteome Res. 5:3135-3144(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-360, AND IDENTIFICATION BY
RP 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 [10]
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 [11]
RP INTERACTION WITH SPAAR.
RX PubMed=28024296; DOI=10.1038/nature21034;
RA Matsumoto A., Pasut A., Matsumoto M., Yamashita R., Fung J., Monteleone E.,
RA Saghatelian A., Nakayama K.I., Clohessy J.G., Pandolfi P.P.;
RT "mTORC1 and muscle regeneration are regulated by the LINC00961-encoded SPAR
RT polypeptide.";
RL Nature 541:228-232(2017).
RN [12] {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, IDENTIFICATION
RP IN THE V-ATPASE COMPLEX, AND GLYCOSYLATION AT ASN-488.
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: Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase),
CC a multisubunit enzyme composed of a peripheral complex (V1) that
CC hydrolyzes ATP and a membrane integral complex (V0) that translocates
CC protons (PubMed:33065002). V-ATPase is responsible for acidifying and
CC maintaining the pH of intracellular compartments and in some cell
CC types, is targeted to the plasma membrane, where it is responsible for
CC acidifying the extracellular environment (By similarity). Required for
CC assembly and activity of the vacuolar ATPase (By similarity).
CC {ECO:0000250|UniProtKB:P32563, ECO:0000250|UniProtKB:Q29466,
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 SPAAR
CC (PubMed:28024296). {ECO:0000269|PubMed:28024296,
CC ECO:0000269|PubMed:33065002}.
CC -!- INTERACTION:
CC Q93050; P06927: E5; Xeno; NbExp=3; IntAct=EBI-2891238, EBI-8561748;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle
CC membrane {ECO:0000250|UniProtKB:P25286}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle
CC membrane {ECO:0000250|UniProtKB:P25286}; Multi-pass membrane protein
CC {ECO:0000255}. Melanosome {ECO:0000269|PubMed:12643545,
CC ECO:0000269|PubMed:17081065}. Note=Identified by mass spectrometry in
CC melanosome fractions from stage I to stage IV.
CC {ECO:0000269|PubMed:12643545, ECO:0000269|PubMed:17081065}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=I;
CC IsoId=Q93050-2; Sequence=Displayed;
CC Name=2; Synonyms=II;
CC IsoId=Q93050-1; Sequence=VSP_012814;
CC Name=3;
CC IsoId=Q93050-3; Sequence=VSP_043532, VSP_012814;
CC -!- SIMILARITY: Belongs to the V-ATPase 116 kDa subunit family.
CC {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; Z71460; CAA96077.1; -; mRNA.
DR EMBL; AK295682; BAH12153.1; -; mRNA.
DR EMBL; AK316305; BAH14676.1; -; mRNA.
DR EMBL; AC067852; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC107993; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471152; EAW60830.1; -; Genomic_DNA.
DR EMBL; BC032398; AAH32398.1; -; mRNA.
DR EMBL; AL137683; CAB70874.1; -; mRNA.
DR CCDS; CCDS11426.1; -. [Q93050-1]
DR CCDS; CCDS45683.1; -. [Q93050-3]
DR CCDS; CCDS45684.1; -. [Q93050-2]
DR PIR; T46449; T46449.
DR RefSeq; NP_001123492.1; NM_001130020.1. [Q93050-3]
DR RefSeq; NP_001123493.1; NM_001130021.1. [Q93050-2]
DR RefSeq; NP_005168.2; NM_005177.3. [Q93050-1]
DR PDB; 6WLW; EM; 3.00 A; R=1-837.
DR PDB; 6WM2; EM; 3.10 A; R=1-837.
DR PDB; 6WM3; EM; 3.40 A; R=1-837.
DR PDB; 6WM4; EM; 3.60 A; R=1-837.
DR PDBsum; 6WLW; -.
DR PDBsum; 6WM2; -.
DR PDBsum; 6WM3; -.
DR PDBsum; 6WM4; -.
DR AlphaFoldDB; Q93050; -.
DR SMR; Q93050; -.
DR BioGRID; 107018; 202.
DR ComplexPortal; CPX-2470; Vacuolar proton translocating ATPase complex, ATP6V0A1 variant.
DR IntAct; Q93050; 66.
DR MINT; Q93050; -.
DR STRING; 9606.ENSP00000264649; -.
DR DrugBank; DB01133; Tiludronic acid.
DR TCDB; 3.A.2.2.4; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR iPTMnet; Q93050; -.
DR MetOSite; Q93050; -.
DR PhosphoSitePlus; Q93050; -.
DR SwissPalm; Q93050; -.
DR BioMuta; ATP6V0A1; -.
DR DMDM; 59803038; -.
DR EPD; Q93050; -.
DR jPOST; Q93050; -.
DR MassIVE; Q93050; -.
DR MaxQB; Q93050; -.
DR PaxDb; Q93050; -.
DR PeptideAtlas; Q93050; -.
DR PRIDE; Q93050; -.
DR ProteomicsDB; 75687; -. [Q93050-2]
DR ProteomicsDB; 75688; -. [Q93050-1]
DR ProteomicsDB; 75689; -. [Q93050-3]
DR Antibodypedia; 16938; 110 antibodies from 21 providers.
DR DNASU; 535; -.
DR Ensembl; ENST00000264649.10; ENSP00000264649.5; ENSG00000033627.17. [Q93050-3]
DR Ensembl; ENST00000343619.9; ENSP00000342951.3; ENSG00000033627.17. [Q93050-2]
DR Ensembl; ENST00000393829.6; ENSP00000377415.2; ENSG00000033627.17. [Q93050-1]
DR GeneID; 535; -.
DR KEGG; hsa:535; -.
DR MANE-Select; ENST00000343619.9; ENSP00000342951.3; NM_001130021.3; NP_001123493.1.
DR UCSC; uc002hzq.4; human. [Q93050-2]
DR CTD; 535; -.
DR DisGeNET; 535; -.
DR GeneCards; ATP6V0A1; -.
DR HGNC; HGNC:865; ATP6V0A1.
DR HPA; ENSG00000033627; Tissue enhanced (retina).
DR MIM; 192130; gene.
DR neXtProt; NX_Q93050; -.
DR OpenTargets; ENSG00000033627; -.
DR PharmGKB; PA25146; -.
DR VEuPathDB; HostDB:ENSG00000033627; -.
DR eggNOG; KOG2189; Eukaryota.
DR GeneTree; ENSGT00950000182881; -.
DR HOGENOM; CLU_005230_0_1_1; -.
DR InParanoid; Q93050; -.
DR OMA; FSYDRAR; -.
DR OrthoDB; 181796at2759; -.
DR PhylomeDB; Q93050; -.
DR TreeFam; TF300346; -.
DR BioCyc; MetaCyc:ENSG00000033627-MON; -.
DR PathwayCommons; Q93050; -.
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-983712; Ion channel transport.
DR SignaLink; Q93050; -.
DR BioGRID-ORCS; 535; 25 hits in 1085 CRISPR screens.
DR ChiTaRS; ATP6V0A1; human.
DR GeneWiki; ATPase,_H%2B_transporting,_lysosomal_V0_subunit_a1; -.
DR GenomeRNAi; 535; -.
DR Pharos; Q93050; Tbio.
DR PRO; PR:Q93050; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q93050; protein.
DR Bgee; ENSG00000033627; Expressed in right frontal lobe and 199 other tissues.
DR ExpressionAtlas; Q93050; baseline and differential.
DR Genevisible; Q93050; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
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:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005765; C:lysosomal membrane; TAS:ParkinsonsUK-UCL.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0033176; C:proton-transporting V-type ATPase complex; IC:ComplexPortal.
DR GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IBA:GO_Central.
DR GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; ISS:UniProtKB.
DR GO; GO:0051117; F:ATPase binding; IPI:UniProtKB.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0048388; P:endosomal lumen acidification; IC:ComplexPortal.
DR GO; GO:0007042; P:lysosomal lumen acidification; IC:ComplexPortal.
DR GO; GO:1902600; P:proton transmembrane transport; IC:ComplexPortal.
DR GO; GO:0016241; P:regulation of macroautophagy; IMP:ParkinsonsUK-UCL.
DR GO; GO:1901998; P:toxin transport; IEA:Ensembl.
DR GO; GO:0007035; P:vacuolar acidification; IBA:GO_Central.
DR InterPro; IPR002490; V-ATPase_116kDa_su.
DR InterPro; IPR026028; V-type_ATPase_116kDa_su_euka.
DR PANTHER; PTHR11629; PTHR11629; 1.
DR Pfam; PF01496; V_ATPase_I; 1.
DR PIRSF; PIRSF001293; ATP6V0A1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasmic vesicle; Glycoprotein;
KW Hydrogen ion transport; Ion transport; Membrane; Phosphoprotein;
KW Reference proteome; Synapse; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..837
FT /note="V-type proton ATPase 116 kDa subunit a 1"
FT /id="PRO_0000119211"
FT TOPO_DOM 1..388
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 389..407
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 408..409
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 410..426
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 427..441
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 442..471
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 472..534
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 535..554
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 555..572
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 573..593
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 594..638
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 639..658
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 659..724
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 725..749
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 750..770
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 771..809
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 810..837
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 250
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1G4"
FT MOD_RES 360
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 364
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1G4"
FT CARBOHYD 488
FT /note="N-linked (GalNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:33065002,
FT ECO:0000312|PDB:6WM3, ECO:0000312|PDB:6WM4"
FT VAR_SEQ 141
FT /note="E -> EAELHHQQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043532"
FT VAR_SEQ 705..710
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:17974005, ECO:0000303|Ref.1"
FT /id="VSP_012814"
FT CONFLICT 750..751
FT /note="QL -> HV (in Ref. 1; CAA96077)"
FT /evidence="ECO:0000305"
FT STRAND 10..18
FT /evidence="ECO:0007829|PDB:6WM2"
FT HELIX 19..32
FT /evidence="ECO:0007829|PDB:6WM2"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:6WM3"
FT HELIX 46..49
FT /evidence="ECO:0007829|PDB:6WM2"
FT HELIX 52..74
FT /evidence="ECO:0007829|PDB:6WM2"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:6WM3"
FT HELIX 94..132
FT /evidence="ECO:0007829|PDB:6WM2"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:6WM2"
FT HELIX 180..189
FT /evidence="ECO:0007829|PDB:6WM2"
FT STRAND 197..202
FT /evidence="ECO:0007829|PDB:6WM2"
FT TURN 209..211
FT /evidence="ECO:0007829|PDB:6WM2"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:6WM2"
FT HELIX 227..239
FT /evidence="ECO:0007829|PDB:6WM2"
FT HELIX 253..308
FT /evidence="ECO:0007829|PDB:6WM2"
FT STRAND 309..312
FT /evidence="ECO:0007829|PDB:6WM2"
FT STRAND 314..326
FT /evidence="ECO:0007829|PDB:6WM2"
FT HELIX 327..329
FT /evidence="ECO:0007829|PDB:6WM2"
FT HELIX 330..343
FT /evidence="ECO:0007829|PDB:6WM2"
FT STRAND 352..355
FT /evidence="ECO:0007829|PDB:6WM2"
FT HELIX 372..378
FT /evidence="ECO:0007829|PDB:6WLW"
FT TURN 379..381
FT /evidence="ECO:0007829|PDB:6WLW"
FT HELIX 392..405
FT /evidence="ECO:0007829|PDB:6WLW"
FT HELIX 410..425
FT /evidence="ECO:0007829|PDB:6WLW"
FT HELIX 427..431
FT /evidence="ECO:0007829|PDB:6WLW"
FT HELIX 438..445
FT /evidence="ECO:0007829|PDB:6WLW"
FT HELIX 447..464
FT /evidence="ECO:0007829|PDB:6WLW"
FT HELIX 484..487
FT /evidence="ECO:0007829|PDB:6WLW"
FT HELIX 491..496
FT /evidence="ECO:0007829|PDB:6WLW"
FT STRAND 498..501
FT /evidence="ECO:0007829|PDB:6WLW"
FT STRAND 515..518
FT /evidence="ECO:0007829|PDB:6WLW"
FT HELIX 520..523
FT /evidence="ECO:0007829|PDB:6WLW"
FT HELIX 528..553
FT /evidence="ECO:0007829|PDB:6WLW"
FT HELIX 556..561
FT /evidence="ECO:0007829|PDB:6WLW"
FT HELIX 565..567
FT /evidence="ECO:0007829|PDB:6WLW"
FT TURN 568..571
FT /evidence="ECO:0007829|PDB:6WLW"
FT HELIX 572..582
FT /evidence="ECO:0007829|PDB:6WLW"
FT HELIX 584..596
FT /evidence="ECO:0007829|PDB:6WLW"
FT HELIX 602..604
FT /evidence="ECO:0007829|PDB:6WM3"
FT HELIX 608..616
FT /evidence="ECO:0007829|PDB:6WLW"
FT STRAND 622..624
FT /evidence="ECO:0007829|PDB:6WLW"
FT HELIX 632..649
FT /evidence="ECO:0007829|PDB:6WLW"
FT HELIX 653..665
FT /evidence="ECO:0007829|PDB:6WLW"
FT HELIX 713..736
FT /evidence="ECO:0007829|PDB:6WLW"
FT HELIX 737..739
FT /evidence="ECO:0007829|PDB:6WLW"
FT HELIX 740..757
FT /evidence="ECO:0007829|PDB:6WLW"
FT STRAND 758..761
FT /evidence="ECO:0007829|PDB:6WLW"
FT HELIX 768..789
FT /evidence="ECO:0007829|PDB:6WLW"
FT TURN 790..792
FT /evidence="ECO:0007829|PDB:6WLW"
FT HELIX 793..807
FT /evidence="ECO:0007829|PDB:6WLW"
FT TURN 808..810
FT /evidence="ECO:0007829|PDB:6WLW"
FT HELIX 811..813
FT /evidence="ECO:0007829|PDB:6WLW"
SQ SEQUENCE 837 AA; 96413 MW; 80E4842CF6ADEE44 CRC64;
MGELFRSEEM TLAQLFLQSE AAYCCVSELG ELGKVQFRDL NPDVNVFQRK FVNEVRRCEE
MDRKLRFVEK EIRKANIPIM DTGENPEVPF PRDMIDLEAN FEKIENELKE INTNQEALKR
NFLELTELKF ILRKTQQFFD EMADPDLLEE SSSLLEPSEM GRGTPLRLGF VAGVINRERI
PTFERMLWRV CRGNVFLRQA EIENPLEDPV TGDYVHKSVF IIFFQGDQLK NRVKKICEGF
RASLYPCPET PQERKEMASG VNTRIDDLQM VLNQTEDHRQ RVLQAAAKNI RVWFIKVRKM
KAIYHTLNLC NIDVTQKCLI AEVWCPVTDL DSIQFALRRG TEHSGSTVPS ILNRMQTNQT
PPTYNKTNKF TYGFQNIVDA YGIGTYREIN PAPYTIITFP FLFAVMFGDF GHGILMTLFA
VWMVLRESRI LSQKNENEMF STVFSGRYII LLMGVFSMYT GLIYNDCFSK SLNIFGSSWS
VRPMFTYNWT EETLRGNPVL QLNPALPGVF GGPYPFGIDP IWNIATNKLT FLNSFKMKMS
VILGIIHMLF GVSLSLFNHI YFKKPLNIYF GFIPEIIFMT SLFGYLVILI FYKWTAYDAH
TSENAPSLLI HFINMFLFSY PESGYSMLYS GQKGIQCFLV VVALLCVPWM LLFKPLVLRR
QYLRRKHLGT LNFGGIRVGN GPTEEDAEII QHDQLSTHSE DADEPSEDEV FDFGDTMVHQ
AIHTIEYCLG CISNTASYLR LWALSLAHAQ LSEVLWTMVI HIGLSVKSLA GGLVLFFFFT
AFATLTVAIL LIMEGLSAFL HALRLHWVEF QNKFYSGTGF KFLPFSFEHI REGKFEE
