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 28-JAN-2026, entry version 216. 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}. 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; 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_213619.3. [Q9UI12-2] DR RefSeq; NP_998785.1; NM_213620.3. [Q9UI12-1] DR RefSeq; XP_006716518.1; XM_006716455.4. [Q9UI12-2] DR RefSeq; XP_054216619.1; XM_054360644.1. [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 PDB; 7U4T; EM; 3.60 A; P=1-483. DR PDB; 7UNF; EM; 4.08 A; H=1-483. DR PDBsum; 6WM2; -. DR PDBsum; 6WM3; -. DR PDBsum; 6WM4; -. DR PDBsum; 7FDA; -. DR PDBsum; 7FDB; -. DR PDBsum; 7FDC; -. DR PDBsum; 7U4T; -. DR PDBsum; 7UNF; -. DR AlphaFoldDB; Q9UI12; -. DR EMDB; EMD-21847; -. DR EMDB; EMD-21848; -. DR EMDB; EMD-21849; -. DR EMDB; EMD-26334; -. DR EMDB; EMD-26623; -. DR EMDB; EMD-31538; -. DR EMDB; EMD-31539; -. DR EMDB; EMD-31540; -. DR SMR; Q9UI12; -. DR BioGRID; 119635; 185. 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 FunCoup; Q9UI12; 3629. DR IntAct; Q9UI12; 127. 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 jPOST; Q9UI12; -. DR MassIVE; Q9UI12; -. DR PaxDb; 9606-ENSP00000352522; -. DR PeptideAtlas; Q9UI12; -. DR ProteomicsDB; 84451; -. [Q9UI12-1] DR ProteomicsDB; 84452; -. [Q9UI12-2] DR Pumba; Q9UI12; -. DR Antibodypedia; 4026; 152 antibodies from 25 providers. DR DNASU; 51606; -. DR Ensembl; ENST00000355221.7; ENSP00000347359.3; ENSG00000047249.19. [Q9UI12-2] DR Ensembl; ENST00000359530.7; ENSP00000352522.2; ENSG00000047249.19. [Q9UI12-1] DR Ensembl; ENST00000396774.6; ENSP00000379995.2; ENSG00000047249.19. [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 AGR; HGNC:18303; -. DR ClinPGx; PA38521; -. 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 OpenTargets; ENSG00000047249; -. DR VEuPathDB; HostDB:ENSG00000047249; -. DR eggNOG; KOG2759; Eukaryota. DR GeneTree; ENSGT00390000003289; -. DR InParanoid; Q9UI12; -. DR OMA; HSGHLRW; -. DR OrthoDB; 10263554at2759; -. DR PAN-GO; Q9UI12; 0 GO annotations based on evolutionary models. DR PhylomeDB; Q9UI12; -. DR BioCyc; MetaCyc:HS00586-MONOMER; -. 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 Reactome; R-HSA-9857377; Regulation of MITF-M-dependent genes involved in lysosome biogenesis and autophagy. DR SignaLink; Q9UI12; -. DR SIGNOR; Q9UI12; -. DR Agora; ENSG00000047249; Agora Nominated Target for Alzheimer's Disease. DR BioGRID-ORCS; 51606; 671 hits in 1192 CRISPR screens. DR CD-CODE; FB4E32DD; Presynaptic clusters and postsynaptic densities. 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 202 other cell types or tissues. DR ExpressionAtlas; Q9UI12; baseline and differential. 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; NAS:ComplexPortal. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0098850; C:extrinsic component of synaptic vesicle membrane; IEA:Ensembl. DR GO; GO:0000139; C:Golgi membrane; NAS: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; NAS: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; NAS:ComplexPortal. DR GO; GO:0061795; P:Golgi lumen acidification; NAS:ComplexPortal. DR GO; GO:0051452; P:intracellular pH reduction; NAS:ComplexPortal. DR GO; GO:0007042; P:lysosomal lumen acidification; NAS: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 CDD; cd00256; VATPase_H; 1. DR FunFam; 1.25.10.10:FF:000067; V-type proton ATPase subunit H; 1. DR FunFam; 1.25.40.150:FF:000001; V-type proton ATPase subunit H; 1. DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1. DR Gene3D; 1.25.40.150; V-type ATPase, subunit H, C-terminal domain; 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; V-TYPE PROTON ATPASE SUBUNIT H; 1. DR PANTHER; PTHR10698:SF0; V-TYPE PROTON ATPASE SUBUNIT H; 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; ARM repeat; 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; Proteomics identification; 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 //