Full text data of ATP6V1H
ATP6V1H
[Confidence: low (only semi-automatic identification from reviews)]
V-type proton ATPase subunit H; V-ATPase subunit H (Nef-binding protein 1; NBP1; Protein VMA13 homolog; V-ATPase 50/57 kDa subunits; Vacuolar proton pump subunit H; Vacuolar proton pump subunit SFD)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
V-type proton ATPase subunit H; V-ATPase subunit H (Nef-binding protein 1; NBP1; Protein VMA13 homolog; V-ATPase 50/57 kDa subunits; Vacuolar proton pump subunit H; Vacuolar proton pump subunit SFD)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9UI12
ID VATH_HUMAN Reviewed; 483 AA.
AC Q9UI12; B3KMR0; Q6PK44; Q9H3E3; Q9Y300;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-2000, sequence version 1.
DT 22-JAN-2014, entry version 129.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Xu Y.Y., Ye J., Song L., Gao Y., Zhang C.L., Zhang J., Wei Y.J.,
RA Cao H.Q., Zhao Y., Liu L.S., Ding J.F., Gao R.L., Wu Q.Y., Qiang B.Q.,
RA Yuan J.G., Liew C.C., 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
RP INTERACTION WITH HIV-1 NEF.
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.,
RA Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
RA Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
RA Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal
RT axis 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP INTERACTION WITH HIV-1 NEF 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
RT protein 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 MASS
RP SPECTROMETRY.
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
RT the 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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Subunit of the peripheral V1 complex of vacuolar ATPase.
CC Subunit H activates the ATPase activity of the enzyme and couples
CC ATPase activity to proton flow. Vacuolar ATPase is responsible for
CC acidifying a variety of intracellular compartments in eukaryotic
CC cells, thus providing most of the energy required for transport
CC processes in the vacuolar system (By similarity). Involved in the
CC endocytosis mediated by clathrin-coated pits, required for the
CC formation of endosomes.
CC -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a
CC peripheral catalytic V1 complex (components A to H) attached to an
CC integral membrane V0 proton pore complex (components: a, c, c',
CC c'' and d). Interacts with HIV-1 Nef protein and AP2M1.
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.
CC -!- SIMILARITY: Belongs to the V-ATPase H subunit family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs 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 RefSeq; NP_057025.2; NM_015941.3.
DR RefSeq; NP_998784.1; NM_213619.2.
DR RefSeq; NP_998785.1; NM_213620.2.
DR RefSeq; XP_005251314.1; XM_005251257.1.
DR UniGene; Hs.491737; -.
DR ProteinModelPortal; Q9UI12; -.
DR SMR; Q9UI12; 227-465.
DR IntAct; Q9UI12; 5.
DR MINT; MINT-5006690; -.
DR STRING; 9606.ENSP00000352522; -.
DR TCDB; 3.A.2.2.4; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR PhosphoSite; Q9UI12; -.
DR DMDM; 12643371; -.
DR PaxDb; Q9UI12; -.
DR PRIDE; Q9UI12; -.
DR DNASU; 51606; -.
DR Ensembl; ENST00000355221; ENSP00000347359; ENSG00000047249.
DR Ensembl; ENST00000359530; ENSP00000352522; ENSG00000047249.
DR Ensembl; ENST00000396774; ENSP00000379995; ENSG00000047249.
DR GeneID; 51606; -.
DR KEGG; hsa:51606; -.
DR UCSC; uc003xrk.4; human.
DR CTD; 51606; -.
DR GeneCards; GC08M054678; -.
DR HGNC; HGNC:18303; ATP6V1H.
DR HPA; CAB009532; -.
DR HPA; HPA023421; -.
DR MIM; 608861; gene.
DR neXtProt; NX_Q9UI12; -.
DR PharmGKB; PA38521; -.
DR eggNOG; COG5231; -.
DR HOGENOM; HOG000007240; -.
DR HOVERGEN; HBG000459; -.
DR InParanoid; Q9UI12; -.
DR KO; K02144; -.
DR OMA; DTLQENH; -.
DR OrthoDB; EOG7CCBQQ; -.
DR PhylomeDB; Q9UI12; -.
DR BioCyc; MetaCyc:HS00586-MONOMER; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_15518; Transmembrane transport of small molecules.
DR ChiTaRS; ATP6V1H; human.
DR GeneWiki; ATP6V1H; -.
DR GenomeRNAi; 51606; -.
DR NextBio; 55498; -.
DR PRO; PR:Q9UI12; -.
DR ArrayExpress; Q9UI12; -.
DR Bgee; Q9UI12; -.
DR CleanEx; HS_ATP6V1H; -.
DR Genevestigator; Q9UI12; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; NAS: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:0006200; P:ATP catabolic process; NAS:GOC.
DR GO; GO:0015991; P:ATP hydrolysis coupled proton transport; NAS:UniProtKB.
DR GO; GO:0006879; P:cellular iron ion homeostasis; TAS:Reactome.
DR GO; GO:0006897; P:endocytosis; IDA:UniProtKB.
DR GO; GO:0008286; P:insulin receptor signaling pathway; TAS:Reactome.
DR GO; GO:0051701; P:interaction with host; TAS:Reactome.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0090382; P:phagosome maturation; TAS:Reactome.
DR GO; GO:0050690; P:regulation of defense response to virus by virus; TAS:Reactome.
DR GO; GO:0033572; P:transferrin transport; TAS:Reactome.
DR GO; GO:0007035; P:vacuolar acidification; NAS:UniProtKB.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
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 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 Alternative splicing; Complete proteome; Host-virus interaction;
KW Hydrogen ion transport; Ion transport; Phosphoprotein;
KW Reference proteome; Transport.
FT CHAIN 1 483 V-type proton ATPase subunit H.
FT /FTId=PRO_0000124193.
FT MOD_RES 483 483 Phosphoserine.
FT VAR_SEQ 176 193 Missing (in isoform 2).
FT /FTId=VSP_012274.
FT CONFLICT 129 129 M -> I (in Ref. 4; AAD27720).
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
//
ID VATH_HUMAN Reviewed; 483 AA.
AC Q9UI12; B3KMR0; Q6PK44; Q9H3E3; Q9Y300;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-2000, sequence version 1.
DT 22-JAN-2014, entry version 129.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Xu Y.Y., Ye J., Song L., Gao Y., Zhang C.L., Zhang J., Wei Y.J.,
RA Cao H.Q., Zhao Y., Liu L.S., Ding J.F., Gao R.L., Wu Q.Y., Qiang B.Q.,
RA Yuan J.G., Liew C.C., 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
RP INTERACTION WITH HIV-1 NEF.
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.,
RA Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
RA Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
RA Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal
RT axis 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP INTERACTION WITH HIV-1 NEF 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
RT protein 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 MASS
RP SPECTROMETRY.
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
RT the 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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Subunit of the peripheral V1 complex of vacuolar ATPase.
CC Subunit H activates the ATPase activity of the enzyme and couples
CC ATPase activity to proton flow. Vacuolar ATPase is responsible for
CC acidifying a variety of intracellular compartments in eukaryotic
CC cells, thus providing most of the energy required for transport
CC processes in the vacuolar system (By similarity). Involved in the
CC endocytosis mediated by clathrin-coated pits, required for the
CC formation of endosomes.
CC -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a
CC peripheral catalytic V1 complex (components A to H) attached to an
CC integral membrane V0 proton pore complex (components: a, c, c',
CC c'' and d). Interacts with HIV-1 Nef protein and AP2M1.
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.
CC -!- SIMILARITY: Belongs to the V-ATPase H subunit family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs 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 RefSeq; NP_057025.2; NM_015941.3.
DR RefSeq; NP_998784.1; NM_213619.2.
DR RefSeq; NP_998785.1; NM_213620.2.
DR RefSeq; XP_005251314.1; XM_005251257.1.
DR UniGene; Hs.491737; -.
DR ProteinModelPortal; Q9UI12; -.
DR SMR; Q9UI12; 227-465.
DR IntAct; Q9UI12; 5.
DR MINT; MINT-5006690; -.
DR STRING; 9606.ENSP00000352522; -.
DR TCDB; 3.A.2.2.4; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR PhosphoSite; Q9UI12; -.
DR DMDM; 12643371; -.
DR PaxDb; Q9UI12; -.
DR PRIDE; Q9UI12; -.
DR DNASU; 51606; -.
DR Ensembl; ENST00000355221; ENSP00000347359; ENSG00000047249.
DR Ensembl; ENST00000359530; ENSP00000352522; ENSG00000047249.
DR Ensembl; ENST00000396774; ENSP00000379995; ENSG00000047249.
DR GeneID; 51606; -.
DR KEGG; hsa:51606; -.
DR UCSC; uc003xrk.4; human.
DR CTD; 51606; -.
DR GeneCards; GC08M054678; -.
DR HGNC; HGNC:18303; ATP6V1H.
DR HPA; CAB009532; -.
DR HPA; HPA023421; -.
DR MIM; 608861; gene.
DR neXtProt; NX_Q9UI12; -.
DR PharmGKB; PA38521; -.
DR eggNOG; COG5231; -.
DR HOGENOM; HOG000007240; -.
DR HOVERGEN; HBG000459; -.
DR InParanoid; Q9UI12; -.
DR KO; K02144; -.
DR OMA; DTLQENH; -.
DR OrthoDB; EOG7CCBQQ; -.
DR PhylomeDB; Q9UI12; -.
DR BioCyc; MetaCyc:HS00586-MONOMER; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_15518; Transmembrane transport of small molecules.
DR ChiTaRS; ATP6V1H; human.
DR GeneWiki; ATP6V1H; -.
DR GenomeRNAi; 51606; -.
DR NextBio; 55498; -.
DR PRO; PR:Q9UI12; -.
DR ArrayExpress; Q9UI12; -.
DR Bgee; Q9UI12; -.
DR CleanEx; HS_ATP6V1H; -.
DR Genevestigator; Q9UI12; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; NAS: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:0006200; P:ATP catabolic process; NAS:GOC.
DR GO; GO:0015991; P:ATP hydrolysis coupled proton transport; NAS:UniProtKB.
DR GO; GO:0006879; P:cellular iron ion homeostasis; TAS:Reactome.
DR GO; GO:0006897; P:endocytosis; IDA:UniProtKB.
DR GO; GO:0008286; P:insulin receptor signaling pathway; TAS:Reactome.
DR GO; GO:0051701; P:interaction with host; TAS:Reactome.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0090382; P:phagosome maturation; TAS:Reactome.
DR GO; GO:0050690; P:regulation of defense response to virus by virus; TAS:Reactome.
DR GO; GO:0033572; P:transferrin transport; TAS:Reactome.
DR GO; GO:0007035; P:vacuolar acidification; NAS:UniProtKB.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
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 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 Alternative splicing; Complete proteome; Host-virus interaction;
KW Hydrogen ion transport; Ion transport; Phosphoprotein;
KW Reference proteome; Transport.
FT CHAIN 1 483 V-type proton ATPase subunit H.
FT /FTId=PRO_0000124193.
FT MOD_RES 483 483 Phosphoserine.
FT VAR_SEQ 176 193 Missing (in isoform 2).
FT /FTId=VSP_012274.
FT CONFLICT 129 129 M -> I (in Ref. 4; AAD27720).
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
//
MIM
608861
*RECORD*
*FIELD* NO
608861
*FIELD* TI
*608861 ATPase, H+ TRANSPORTING, LYSOSOMAL, 50/57-KD, V1 SUBUNIT H; ATP6V1H
;;NEF-BINDING PROTEIN 1; NBP1;;
read moreVMA13, S. CEREVISIAE, HOMOLOG OF; VMA13
*FIELD* TX
DESCRIPTION
The vacuolar ATPase is a multisubunit enzyme that facilitates the
acidification of intracellular compartments and plays a role in
receptor-mediated endocytosis, intracellular trafficking, and protein
degradation. ATP6V1H is a subunit of the 570-kD V1 peripheral complex
responsible for hydrolysis of ATP (Geyer et al., 2002).
CLONING
Using human immunodeficiency virus (HIV)-1 Nef protein as bait in a
yeast 2-hybrid screen of a B-cell cDNA library, Lu et al. (1998) cloned
ATP6V1H, which they designated NBP1. The deduced 484-amino acid protein
has a calculated molecular mass of 56 kD. ATP6V1H contains 7 motifs that
contain tyrosine-polar-polar-hydrophobic residues and 4 dileucine
motifs, mostly in its C terminus. Lu et al. (1998) stated that ATP6V1H
is expressed ubiquitously as a 2.0-kb transcript.
Geyer et al. (2002) characterized the ATP6V1H protein. The all-helical
structure contains 8 armadillo (ARM) repeats that are also found in
importins (see KPNB1; 602738). A single ARM repeat consists of about 42
residues that fold into 3 alpha helices with an almost triangular cross
section. Multiple ARM repeats pack regularly side by side, forming
elongated molecules with a superhelical twist.
GENE FUNCTION
Lu et al. (1998) confirmed that ATP6B1H interacts directly with HIV-1
Nef. This interaction correlated with the ability of Nef to internalize
CD4 (186940), and expression of antisense ATP6V1H abrogated these
effects.
Geyer et al. (2002) determined that ATP6V1H binds to the C-terminal
flexible loop in Nef and to the medium chain (mu-2) of the adaptor
protein complex-2 (see 601024) in vitro and in vivo. The interaction
sites for ATP6V1H and mu-2 were mapped to the central region of ATP6V1H,
which contains 4 ARM repeats, and to the N-terminal adaptin-binding
domain of mu-2. Blocking expression of ATP6V1H decreased the enhancement
of virion infectivity by Nef.
Geyer et al. (2002) showed that the C-terminal 350-amino acids of
ATP6V1H share significant similarity with the N-terminal trunk portion
of beta-adaptins (see AP1B1; 600157). They found that expression of this
ATP6V1H fragment in cells blocked the internalization of transmembrane
proteins, which depend upon dileucine-based sorting motifs.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the ATP6V1H
gene to chromosome 8 (TMAP A003B09).
*FIELD* RF
1. Geyer, M.; Fackler, O. T.; Peterlin, B. M.: Subunit H of the V-ATPase
involved in endocytosis shows homology to beta-adaptins. Molec. Biol.
Cell 13: 2045-2056, 2002.
2. Geyer, M.; Yu, H.; Mandic, R.; Linnemann, T.; Zheng, Y.-H.; Fackler,
O. T.; Peterlin, B. M.: Subunit H of the V-ATPase binds to the medium
chain of adaptor protein complex 2 and connects Nef to the endocytic
machinery. J. Biol. Chem. 277: 28521-28529, 2002.
3. Lu, X.; Yu, H.; Liu, S.-H.; Brodsky, F. M.; Peterlin, B. M.: Interactions
between HIV1 Nef and vacuolar ATPase facilitate the internalization
of CD4. Immunity 8: 647-656, 1998.
*FIELD* CD
Patricia A. Hartz: 8/19/2004
*FIELD* ED
mgross: 08/19/2004
*RECORD*
*FIELD* NO
608861
*FIELD* TI
*608861 ATPase, H+ TRANSPORTING, LYSOSOMAL, 50/57-KD, V1 SUBUNIT H; ATP6V1H
;;NEF-BINDING PROTEIN 1; NBP1;;
read moreVMA13, S. CEREVISIAE, HOMOLOG OF; VMA13
*FIELD* TX
DESCRIPTION
The vacuolar ATPase is a multisubunit enzyme that facilitates the
acidification of intracellular compartments and plays a role in
receptor-mediated endocytosis, intracellular trafficking, and protein
degradation. ATP6V1H is a subunit of the 570-kD V1 peripheral complex
responsible for hydrolysis of ATP (Geyer et al., 2002).
CLONING
Using human immunodeficiency virus (HIV)-1 Nef protein as bait in a
yeast 2-hybrid screen of a B-cell cDNA library, Lu et al. (1998) cloned
ATP6V1H, which they designated NBP1. The deduced 484-amino acid protein
has a calculated molecular mass of 56 kD. ATP6V1H contains 7 motifs that
contain tyrosine-polar-polar-hydrophobic residues and 4 dileucine
motifs, mostly in its C terminus. Lu et al. (1998) stated that ATP6V1H
is expressed ubiquitously as a 2.0-kb transcript.
Geyer et al. (2002) characterized the ATP6V1H protein. The all-helical
structure contains 8 armadillo (ARM) repeats that are also found in
importins (see KPNB1; 602738). A single ARM repeat consists of about 42
residues that fold into 3 alpha helices with an almost triangular cross
section. Multiple ARM repeats pack regularly side by side, forming
elongated molecules with a superhelical twist.
GENE FUNCTION
Lu et al. (1998) confirmed that ATP6B1H interacts directly with HIV-1
Nef. This interaction correlated with the ability of Nef to internalize
CD4 (186940), and expression of antisense ATP6V1H abrogated these
effects.
Geyer et al. (2002) determined that ATP6V1H binds to the C-terminal
flexible loop in Nef and to the medium chain (mu-2) of the adaptor
protein complex-2 (see 601024) in vitro and in vivo. The interaction
sites for ATP6V1H and mu-2 were mapped to the central region of ATP6V1H,
which contains 4 ARM repeats, and to the N-terminal adaptin-binding
domain of mu-2. Blocking expression of ATP6V1H decreased the enhancement
of virion infectivity by Nef.
Geyer et al. (2002) showed that the C-terminal 350-amino acids of
ATP6V1H share significant similarity with the N-terminal trunk portion
of beta-adaptins (see AP1B1; 600157). They found that expression of this
ATP6V1H fragment in cells blocked the internalization of transmembrane
proteins, which depend upon dileucine-based sorting motifs.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the ATP6V1H
gene to chromosome 8 (TMAP A003B09).
*FIELD* RF
1. Geyer, M.; Fackler, O. T.; Peterlin, B. M.: Subunit H of the V-ATPase
involved in endocytosis shows homology to beta-adaptins. Molec. Biol.
Cell 13: 2045-2056, 2002.
2. Geyer, M.; Yu, H.; Mandic, R.; Linnemann, T.; Zheng, Y.-H.; Fackler,
O. T.; Peterlin, B. M.: Subunit H of the V-ATPase binds to the medium
chain of adaptor protein complex 2 and connects Nef to the endocytic
machinery. J. Biol. Chem. 277: 28521-28529, 2002.
3. Lu, X.; Yu, H.; Liu, S.-H.; Brodsky, F. M.; Peterlin, B. M.: Interactions
between HIV1 Nef and vacuolar ATPase facilitate the internalization
of CD4. Immunity 8: 647-656, 1998.
*FIELD* CD
Patricia A. Hartz: 8/19/2004
*FIELD* ED
mgross: 08/19/2004