VATH_HUMAN
ID VATH_HUMAN Reviewed; 483 AA.
AC Q9UI12; B3KMR0; Q6PK44; Q9H3E3; Q9Y300;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=V-type proton ATPase subunit H;
DE Short=V-ATPase subunit H;
DE AltName: Full=Nef-binding protein 1;
DE Short=NBP1;
DE AltName: Full=Protein VMA13 homolog;
DE AltName: Full=V-ATPase 50/57 kDa subunits;
DE AltName: Full=Vacuolar proton pump subunit H;
DE AltName: Full=Vacuolar proton pump subunit SFD;
GN Name=ATP6V1H; ORFNames=CGI-11;
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=Heart;
RA Liu B., Liu Y.Q., Wang X.Y., Zhao B., Sheng H., Zhao X.W., Liu S., Xu Y.Y.,
RA Ye J., Song L., Gao Y., Zhang C.L., Zhang J., Wei Y.J., Cao H.Q., Zhao Y.,
RA Liu L.S., Ding J.F., Gao R.L., Wu Q.Y., Qiang B.Q., Yuan J.G., Liew C.C.,
RA Zhao M.S., Hui R.T.;
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND INTERACTION
RP WITH HIV-1 NEF (MICROBIAL INFECTION).
RC TISSUE=B-cell;
RX PubMed=9620685; DOI=10.1016/s1074-7613(00)80569-5;
RA Lu X., Yu H., Liu S.-H., Brodsky F.M., Peterlin B.M.;
RT "Interactions between HIV1 Nef and vacuolar ATPase facilitate the
RT internalization of CD4.";
RL Immunity 8:647-656(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Hypothalamus;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Mammary gland;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye, and Lymphoma;
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 [8]
RP FUNCTION, AND INTERACTION WITH HIV-1 NEF (MICROBIAL INFECTION) AND AP2M1.
RX PubMed=12032142; DOI=10.1074/jbc.m200522200;
RA Geyer M., Yu H., Mandic R., Linnemann T., Zheng Y.-H., Fackler O.T.,
RA Peterlin B.M.;
RT "Subunit H of the V-ATPase binds to the medium chain of adaptor protein
RT complex 2 and connects Nef to the endocytic machinery.";
RL J. Biol. Chem. 277:28521-28529(2002).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-483, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [10]
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 [11]
RP INTERACTION WITH MYCOBACTERIUM TUBERCULOSIS PTPA (MICROBIAL INFECTION).
RX PubMed=22087003; DOI=10.1073/pnas.1109201108;
RA Wong D., Bach H., Sun J., Hmama Z., Av-Gay Y.;
RT "Mycobacterium tuberculosis protein tyrosine phosphatase (PtpA) excludes
RT host vacuolar-H+-ATPase to inhibit phagosome acidification.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:19371-19376(2011).
RN [12]
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 [13]
RP INTERACTION WITH TM9SF4.
RX PubMed=25659576; DOI=10.1038/onc.2014.437;
RA Lozupone F., Borghi M., Marzoli F., Azzarito T., Matarrese P., Iessi E.,
RA Venturi G., Meschini S., Canitano A., Bona R., Cara A., Fais S.;
RT "TM9SF4 is a novel V-ATPase-interacting protein that modulates tumor pH
RT alterations associated with drug resistance and invasiveness of colon
RT cancer cells.";
RL Oncogene 34:5163-5174(2015).
RN [14] {ECO:0007744|PDB:6WM2, ECO:0007744|PDB:6WM3, ECO:0007744|PDB:6WM4}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.10 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: Subunit of the V1 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). Subunit H is
CC essential for V-ATPase activity, but not for the assembly of the
CC complex (By similarity). Involved in the endocytosis mediated by
CC clathrin-coated pits, required for the formation of endosomes
CC (PubMed:12032142). {ECO:0000250|UniProtKB:O46563,
CC ECO:0000250|UniProtKB:P41807, ECO:0000269|PubMed:12032142,
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 AP2M1
CC (PubMed:12032142). Interacts with TM9SF4 in colon cancer cells
CC (PubMed:25659576). {ECO:0000269|PubMed:12032142,
CC ECO:0000269|PubMed:25659576, ECO:0000269|PubMed:33065002}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 Nef protein.
CC {ECO:0000269|PubMed:12032142, ECO:0000269|PubMed:9620685}.
CC -!- SUBUNIT: (Microbial infection) Interacts with M.tuberculosis PtpA,
CC which blocks V-ATPase trafficking and phagosome acidification.
CC {ECO:0000269|PubMed:22087003}.
CC -!- INTERACTION:
CC Q9UI12; Q96IK1-2: BOD1; NbExp=3; IntAct=EBI-724719, EBI-18924329;
CC Q9UI12; P42772: CDKN2B; NbExp=3; IntAct=EBI-724719, EBI-711280;
CC Q9UI12; Q96Q35-2: FLACC1; NbExp=3; IntAct=EBI-724719, EBI-11533409;
CC Q9UI12; P42858: HTT; NbExp=3; IntAct=EBI-724719, EBI-466029;
CC Q9UI12; Q9BZL4: PPP1R12C; NbExp=3; IntAct=EBI-724719, EBI-721802;
CC Q9UI12; O15079: SNPH; NbExp=3; IntAct=EBI-724719, EBI-4401902;
CC Q9UI12; Q9UM82: SPATA2; NbExp=3; IntAct=EBI-724719, EBI-744066;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle
CC membrane {ECO:0000250|UniProtKB:O46563}; Peripheral membrane protein
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UI12-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UI12-2; Sequence=VSP_012274;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9620685}.
CC -!- SIMILARITY: Belongs to the V-ATPase H subunit family. {ECO:0000305}.
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DR EMBL; AF113222; AAG39293.1; -; mRNA.
DR EMBL; AF298777; AAG22809.1; -; mRNA.
DR EMBL; AF112204; AAF17192.1; -; mRNA.
DR EMBL; AF132945; AAD27720.1; -; mRNA.
DR EMBL; AK022345; BAG51072.1; -; mRNA.
DR EMBL; CH471068; EAW86727.1; -; Genomic_DNA.
DR EMBL; BC025275; AAH25275.1; -; mRNA.
DR CCDS; CCDS6153.1; -. [Q9UI12-1]
DR CCDS; CCDS6154.1; -. [Q9UI12-2]
DR RefSeq; NP_057025.2; NM_015941.3. [Q9UI12-1]
DR RefSeq; NP_998784.1; NM_213619.2. [Q9UI12-2]
DR RefSeq; NP_998785.1; NM_213620.2. [Q9UI12-1]
DR RefSeq; XP_006716518.1; XM_006716455.2. [Q9UI12-2]
DR PDB; 6WM2; EM; 3.10 A; P=1-483.
DR PDB; 6WM3; EM; 3.40 A; P=1-483.
DR PDB; 6WM4; EM; 3.60 A; P=1-483.
DR PDB; 7FDA; EM; 4.20 A; P=356-465.
DR PDB; 7FDB; EM; 4.80 A; P=356-465.
DR PDB; 7FDC; EM; 6.60 A; P=356-465.
DR PDBsum; 6WM2; -.
DR PDBsum; 6WM3; -.
DR PDBsum; 6WM4; -.
DR PDBsum; 7FDA; -.
DR PDBsum; 7FDB; -.
DR PDBsum; 7FDC; -.
DR AlphaFoldDB; Q9UI12; -.
DR SMR; Q9UI12; -.
DR BioGRID; 119635; 136.
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 IntAct; Q9UI12; 38.
DR MINT; Q9UI12; -.
DR STRING; 9606.ENSP00000352522; -.
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 GlyGen; Q9UI12; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UI12; -.
DR MetOSite; Q9UI12; -.
DR PhosphoSitePlus; Q9UI12; -.
DR SwissPalm; Q9UI12; -.
DR BioMuta; ATP6V1H; -.
DR DMDM; 12643371; -.
DR EPD; Q9UI12; -.
DR jPOST; Q9UI12; -.
DR MassIVE; Q9UI12; -.
DR MaxQB; Q9UI12; -.
DR PaxDb; Q9UI12; -.
DR PeptideAtlas; Q9UI12; -.
DR PRIDE; Q9UI12; -.
DR ProteomicsDB; 84451; -. [Q9UI12-1]
DR ProteomicsDB; 84452; -. [Q9UI12-2]
DR Antibodypedia; 4026; 152 antibodies from 25 providers.
DR DNASU; 51606; -.
DR Ensembl; ENST00000355221.7; ENSP00000347359.3; ENSG00000047249.18. [Q9UI12-2]
DR Ensembl; ENST00000359530.7; ENSP00000352522.2; ENSG00000047249.18. [Q9UI12-1]
DR Ensembl; ENST00000396774.6; ENSP00000379995.2; ENSG00000047249.18. [Q9UI12-1]
DR GeneID; 51606; -.
DR KEGG; hsa:51606; -.
DR MANE-Select; ENST00000359530.7; ENSP00000352522.2; NM_015941.4; NP_057025.2.
DR UCSC; uc003xrl.5; human. [Q9UI12-1]
DR CTD; 51606; -.
DR DisGeNET; 51606; -.
DR GeneCards; ATP6V1H; -.
DR HGNC; HGNC:18303; ATP6V1H.
DR HPA; ENSG00000047249; Low tissue specificity.
DR MIM; 608861; gene.
DR neXtProt; NX_Q9UI12; -.
DR OpenTargets; ENSG00000047249; -.
DR PharmGKB; PA38521; -.
DR VEuPathDB; HostDB:ENSG00000047249; -.
DR eggNOG; KOG2759; Eukaryota.
DR GeneTree; ENSGT00390000003289; -.
DR InParanoid; Q9UI12; -.
DR OMA; KDQNVRY; -.
DR PhylomeDB; Q9UI12; -.
DR TreeFam; TF313488; -.
DR BioCyc; MetaCyc:HS00586-MON; -.
DR PathwayCommons; Q9UI12; -.
DR Reactome; R-HSA-1222556; ROS and RNS production in phagocytes.
DR Reactome; R-HSA-167590; Nef Mediated CD4 Down-regulation.
DR Reactome; R-HSA-182218; Nef Mediated CD8 Down-regulation.
DR Reactome; R-HSA-77387; Insulin receptor recycling.
DR Reactome; R-HSA-917977; Transferrin endocytosis and recycling.
DR Reactome; R-HSA-9636467; Blockage of phagosome acidification.
DR Reactome; R-HSA-9639288; Amino acids regulate mTORC1.
DR Reactome; R-HSA-983712; Ion channel transport.
DR SignaLink; Q9UI12; -.
DR SIGNOR; Q9UI12; -.
DR BioGRID-ORCS; 51606; 649 hits in 1094 CRISPR screens.
DR ChiTaRS; ATP6V1H; human.
DR GeneWiki; ATP6V1H; -.
DR GenomeRNAi; 51606; -.
DR Pharos; Q9UI12; Tbio.
DR PRO; PR:Q9UI12; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q9UI12; protein.
DR Bgee; ENSG00000047249; Expressed in middle temporal gyrus and 200 other tissues.
DR ExpressionAtlas; Q9UI12; baseline and differential.
DR Genevisible; Q9UI12; HS.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0010008; C:endosome membrane; IC:ComplexPortal.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IC:ComplexPortal.
DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
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:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; ISS:UniProtKB.
DR GO; GO:0030234; F:enzyme regulator activity; NAS:UniProtKB.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; IDA: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:1902600; P:proton transmembrane transport; NAS:UniProtKB.
DR GO; GO:0016241; P:regulation of macroautophagy; NAS:ParkinsonsUK-UCL.
DR GO; GO:0007035; P:vacuolar acidification; NAS:UniProtKB.
DR Gene3D; 1.25.10.10; -; 1.
DR Gene3D; 1.25.40.150; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR004908; ATPase_V1-cplx_hsu.
DR InterPro; IPR011987; ATPase_V1-cplx_hsu_C.
DR InterPro; IPR038497; ATPase_V1-cplx_hsu_C_sf.
DR PANTHER; PTHR10698; PTHR10698; 1.
DR Pfam; PF11698; V-ATPase_H_C; 1.
DR Pfam; PF03224; V-ATPase_H_N; 1.
DR PIRSF; PIRSF032184; ATPase_V1_H; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasmic vesicle;
KW Host-virus interaction; Hydrogen ion transport; Ion transport; Membrane;
KW Phosphoprotein; Reference proteome; Transport.
FT CHAIN 1..483
FT /note="V-type proton ATPase subunit H"
FT /id="PRO_0000124193"
FT MOD_RES 483
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT VAR_SEQ 176..193
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_012274"
FT CONFLICT 129
FT /note="M -> I (in Ref. 4; AAD27720)"
FT /evidence="ECO:0000305"
FT HELIX 18..28
FT /evidence="ECO:0007829|PDB:6WM2"
FT TURN 34..40
FT /evidence="ECO:0007829|PDB:6WM2"
FT HELIX 44..48
FT /evidence="ECO:0007829|PDB:6WM2"
FT TURN 50..53
FT /evidence="ECO:0007829|PDB:6WM2"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:6WM3"
FT HELIX 59..63
FT /evidence="ECO:0007829|PDB:6WM2"
FT HELIX 65..68
FT /evidence="ECO:0007829|PDB:6WM2"
FT TURN 69..74
FT /evidence="ECO:0007829|PDB:6WM2"
FT HELIX 78..83
FT /evidence="ECO:0007829|PDB:6WM2"
FT HELIX 87..103
FT /evidence="ECO:0007829|PDB:6WM2"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:6WM2"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:6WM2"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:6WM3"
FT HELIX 117..120
FT /evidence="ECO:0007829|PDB:6WM2"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:6WM2"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:6WM2"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:6WM3"
FT TURN 133..138
FT /evidence="ECO:0007829|PDB:6WM2"
FT HELIX 139..144
FT /evidence="ECO:0007829|PDB:6WM2"
FT HELIX 146..150
FT /evidence="ECO:0007829|PDB:6WM2"
FT HELIX 159..162
FT /evidence="ECO:0007829|PDB:6WM2"
FT HELIX 169..172
FT /evidence="ECO:0007829|PDB:6WM2"
FT HELIX 196..208
FT /evidence="ECO:0007829|PDB:6WM2"
FT HELIX 213..219
FT /evidence="ECO:0007829|PDB:6WM2"
FT TURN 220..222
FT /evidence="ECO:0007829|PDB:6WM2"
FT HELIX 223..232
FT /evidence="ECO:0007829|PDB:6WM2"
FT HELIX 237..250
FT /evidence="ECO:0007829|PDB:6WM2"
FT HELIX 254..260
FT /evidence="ECO:0007829|PDB:6WM2"
FT HELIX 265..273
FT /evidence="ECO:0007829|PDB:6WM2"
FT HELIX 281..295
FT /evidence="ECO:0007829|PDB:6WM2"
FT TURN 299..301
FT /evidence="ECO:0007829|PDB:6WM2"
FT HELIX 304..310
FT /evidence="ECO:0007829|PDB:6WM2"
FT HELIX 315..323
FT /evidence="ECO:0007829|PDB:6WM2"
FT HELIX 329..349
FT /evidence="ECO:0007829|PDB:6WM2"
FT HELIX 352..361
FT /evidence="ECO:0007829|PDB:6WM2"
FT TURN 369..371
FT /evidence="ECO:0007829|PDB:6WM2"
FT HELIX 373..377
FT /evidence="ECO:0007829|PDB:6WM2"
FT HELIX 378..382
FT /evidence="ECO:0007829|PDB:6WM2"
FT HELIX 386..388
FT /evidence="ECO:0007829|PDB:6WM2"
FT HELIX 389..397
FT /evidence="ECO:0007829|PDB:6WM2"
FT HELIX 404..420
FT /evidence="ECO:0007829|PDB:6WM2"
FT HELIX 422..430
FT /evidence="ECO:0007829|PDB:6WM2"
FT HELIX 433..439
FT /evidence="ECO:0007829|PDB:6WM2"
FT HELIX 440..442
FT /evidence="ECO:0007829|PDB:6WM2"
FT HELIX 446..460
FT /evidence="ECO:0007829|PDB:6WM2"
SQ SEQUENCE 483 AA; 55883 MW; EAE0457C538AC906 CRC64;
MTKMDIRGAV DAAVPTNIIA AKAAEVRANK VNWQSYLQGQ MISAEDCEFI QRFEMKRSPE
EKQEMLQTEG SQCAKTFINL MTHICKEQTV QYILTMVDDM LQENHQRVSI FFDYARCSKN
TAWPYFLPML NRQDPFTVHM AARIIAKLAA WGKELMEGSD LNYYFNWIKT QLSSQKLRGS
GVAVETGTVS SSDSSQYVQC VAGCLQLMLR VNEYRFAWVE ADGVNCIMGV LSNKCGFQLQ
YQMIFSIWLL AFSPQMCEHL RRYNIIPVLS DILQESVKEK VTRIILAAFR NFLEKSTERE
TRQEYALAMI QCKVLKQLEN LEQQKYDDED ISEDIKFLLE KLGESVQDLS SFDEYSSELK
SGRLEWSPVH KSEKFWRENA VRLNEKNYEL LKILTKLLEV SDDPQVLAVA AHDVGEYVRH
YPRGKRVIEQ LGGKQLVMNH MHHEDQQVRY NALLAVQKLM VHNWEYLGKQ LQSEQPQTAA
ARS
