Full text data of ATP6V0A1
ATP6V0A1
(ATP6N1, ATP6N1A, VPP1)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
V-type proton ATPase 116 kDa subunit a isoform 1; V-ATPase 116 kDa isoform a1 (Clathrin-coated vesicle/synaptic vesicle proton pump 116 kDa subunit; Vacuolar adenosine triphosphatase subunit Ac116; Vacuolar proton pump subunit 1; Vacuolar proton translocating ATPase 116 kDa subunit a isoform 1)
V-type proton ATPase 116 kDa subunit a isoform 1; V-ATPase 116 kDa isoform a1 (Clathrin-coated vesicle/synaptic vesicle proton pump 116 kDa subunit; Vacuolar adenosine triphosphatase subunit Ac116; Vacuolar proton pump subunit 1; Vacuolar proton translocating ATPase 116 kDa subunit a isoform 1)
Comments
Isoform Q93050-1 was detected.
Isoform Q93050-1 was detected.
UniProt
Q93050
ID VPP1_HUMAN Reviewed; 837 AA.
AC Q93050; B7Z3B7; Q8N5G7; Q9NSX0;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
read moreDT 15-FEB-2005, sequence version 3.
DT 22-JAN-2014, entry version 123.
DE RecName: Full=V-type proton ATPase 116 kDa subunit a isoform 1;
DE Short=V-ATPase 116 kDa isoform a1;
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT vacuolar-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.,
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 [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.,
RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA 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
RT the 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.,
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 [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
RT project: 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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., 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], AND MASS SPECTROMETRY.
RC TISSUE=Melanoma;
RX PubMed=12643545; DOI=10.1021/pr025562r;
RA Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K.,
RA Valencia J., Muller J., Vieira W.D., Watabe H., Shabanowitz J.,
RA Hearing V.J., Hunt D.F., 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], AND MASS SPECTROMETRY.
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
RA Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
RA Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
RA Hunt D.F.;
RT "Proteomic and bioinformatic characterization of the biogenesis and
RT function of melanosomes.";
RL J. Proteome Res. 5:3135-3144(2006).
CC -!- FUNCTION: Required for assembly and activity of the vacuolar
CC ATPase. Potential role in differential targeting and regulation of
CC the enzyme for a specific organelle (By similarity).
CC -!- SUBUNIT: The V-ATPase is a heteromultimeric enzyme composed of at
CC least thirteen different subunits. It has a membrane peripheral V1
CC sector for ATP hydrolysis and an integral V0 for proton
CC translocation. The V1 sector comprises subunits A-H, whereas V0
CC includes subunits a, d, c, c', and c''.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Multi-pass
CC membrane protein. Melanosome. Note=Coated vesicle. Identified by
CC mass spectrometry in melanosome fractions from stage I to stage
CC IV.
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 Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the V-ATPase 116 kDa subunit family.
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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 PIR; T46449; T46449.
DR RefSeq; NP_001123492.1; NM_001130020.1.
DR RefSeq; NP_001123493.1; NM_001130021.1.
DR RefSeq; NP_005168.2; NM_005177.3.
DR UniGene; Hs.463074; -.
DR ProteinModelPortal; Q93050; -.
DR IntAct; Q93050; 7.
DR MINT; MINT-3049850; -.
DR STRING; 9606.ENSP00000264649; -.
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; Q93050; -.
DR DMDM; 59803038; -.
DR PaxDb; Q93050; -.
DR PRIDE; Q93050; -.
DR Ensembl; ENST00000264649; ENSP00000264649; ENSG00000033627.
DR Ensembl; ENST00000343619; ENSP00000342951; ENSG00000033627.
DR Ensembl; ENST00000393829; ENSP00000377415; ENSG00000033627.
DR GeneID; 535; -.
DR KEGG; hsa:535; -.
DR UCSC; uc002hzr.3; human.
DR CTD; 535; -.
DR GeneCards; GC17P040610; -.
DR H-InvDB; HIX0013842; -.
DR HGNC; HGNC:865; ATP6V0A1.
DR HPA; HPA022144; -.
DR MIM; 192130; gene.
DR neXtProt; NX_Q93050; -.
DR PharmGKB; PA25146; -.
DR eggNOG; COG1269; -.
DR HOGENOM; HOG000037059; -.
DR HOVERGEN; HBG014606; -.
DR KO; K02154; -.
DR OMA; GHAIIML; -.
DR OrthoDB; EOG74FF04; -.
DR BioCyc; MetaCyc:ENSG00000033627-MONOMER; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_15518; Transmembrane transport of small molecules.
DR ChiTaRS; ATP6V0A1; human.
DR GeneWiki; ATPase,_H%2B_transporting,_lysosomal_V0_subunit_a1; -.
DR GenomeRNAi; 535; -.
DR NextBio; 2223; -.
DR PRO; PR:Q93050; -.
DR ArrayExpress; Q93050; -.
DR Bgee; Q93050; -.
DR CleanEx; HS_ATP6V0A1; -.
DR Genevestigator; Q93050; -.
DR GO; GO:0010008; C:endosome membrane; TAS:Reactome.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR GO; GO:0015078; F:hydrogen ion transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
DR GO; GO:0006879; P:cellular iron ion homeostasis; TAS:Reactome.
DR GO; GO:0008286; P:insulin receptor signaling pathway; TAS:Reactome.
DR GO; GO:0051701; P:interaction with host; TAS:Reactome.
DR GO; GO:0090382; P:phagosome maturation; TAS:Reactome.
DR GO; GO:0033572; P:transferrin transport; TAS:Reactome.
DR GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
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 Alternative splicing; Complete proteome; Cytoplasmic vesicle;
KW Hydrogen ion transport; Ion transport; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1 837 V-type proton ATPase 116 kDa subunit a
FT isoform 1.
FT /FTId=PRO_0000119211.
FT TOPO_DOM 1 388 Cytoplasmic (Potential).
FT TRANSMEM 389 407 Helical; (Potential).
FT TOPO_DOM 408 409 Vacuolar (Potential).
FT TRANSMEM 410 426 Helical; (Potential).
FT TOPO_DOM 427 441 Cytoplasmic (Potential).
FT TRANSMEM 442 471 Helical; (Potential).
FT TOPO_DOM 472 534 Vacuolar (Potential).
FT TRANSMEM 535 554 Helical; (Potential).
FT TOPO_DOM 555 572 Cytoplasmic (Potential).
FT TRANSMEM 573 593 Helical; (Potential).
FT TOPO_DOM 594 638 Vacuolar (Potential).
FT TRANSMEM 639 658 Helical; (Potential).
FT TOPO_DOM 659 724 Cytoplasmic (Potential).
FT TRANSMEM 725 749 Helical; (Potential).
FT TOPO_DOM 750 770 Vacuolar (Potential).
FT TRANSMEM 771 809 Helical; (Potential).
FT TOPO_DOM 810 837 Cytoplasmic (Potential).
FT MOD_RES 364 364 Phosphotyrosine (By similarity).
FT VAR_SEQ 141 141 E -> EAELHHQQ (in isoform 3).
FT /FTId=VSP_043532.
FT VAR_SEQ 705 710 Missing (in isoform 2 and isoform 3).
FT /FTId=VSP_012814.
FT CONFLICT 750 751 QL -> HV (in Ref. 1; CAA96077).
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
//
ID VPP1_HUMAN Reviewed; 837 AA.
AC Q93050; B7Z3B7; Q8N5G7; Q9NSX0;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
read moreDT 15-FEB-2005, sequence version 3.
DT 22-JAN-2014, entry version 123.
DE RecName: Full=V-type proton ATPase 116 kDa subunit a isoform 1;
DE Short=V-ATPase 116 kDa isoform a1;
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT vacuolar-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.,
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 [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.,
RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA 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
RT the 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.,
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 [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
RT project: 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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., 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], AND MASS SPECTROMETRY.
RC TISSUE=Melanoma;
RX PubMed=12643545; DOI=10.1021/pr025562r;
RA Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K.,
RA Valencia J., Muller J., Vieira W.D., Watabe H., Shabanowitz J.,
RA Hearing V.J., Hunt D.F., 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], AND MASS SPECTROMETRY.
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
RA Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
RA Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
RA Hunt D.F.;
RT "Proteomic and bioinformatic characterization of the biogenesis and
RT function of melanosomes.";
RL J. Proteome Res. 5:3135-3144(2006).
CC -!- FUNCTION: Required for assembly and activity of the vacuolar
CC ATPase. Potential role in differential targeting and regulation of
CC the enzyme for a specific organelle (By similarity).
CC -!- SUBUNIT: The V-ATPase is a heteromultimeric enzyme composed of at
CC least thirteen different subunits. It has a membrane peripheral V1
CC sector for ATP hydrolysis and an integral V0 for proton
CC translocation. The V1 sector comprises subunits A-H, whereas V0
CC includes subunits a, d, c, c', and c''.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Multi-pass
CC membrane protein. Melanosome. Note=Coated vesicle. Identified by
CC mass spectrometry in melanosome fractions from stage I to stage
CC IV.
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 Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the V-ATPase 116 kDa subunit family.
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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 PIR; T46449; T46449.
DR RefSeq; NP_001123492.1; NM_001130020.1.
DR RefSeq; NP_001123493.1; NM_001130021.1.
DR RefSeq; NP_005168.2; NM_005177.3.
DR UniGene; Hs.463074; -.
DR ProteinModelPortal; Q93050; -.
DR IntAct; Q93050; 7.
DR MINT; MINT-3049850; -.
DR STRING; 9606.ENSP00000264649; -.
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; Q93050; -.
DR DMDM; 59803038; -.
DR PaxDb; Q93050; -.
DR PRIDE; Q93050; -.
DR Ensembl; ENST00000264649; ENSP00000264649; ENSG00000033627.
DR Ensembl; ENST00000343619; ENSP00000342951; ENSG00000033627.
DR Ensembl; ENST00000393829; ENSP00000377415; ENSG00000033627.
DR GeneID; 535; -.
DR KEGG; hsa:535; -.
DR UCSC; uc002hzr.3; human.
DR CTD; 535; -.
DR GeneCards; GC17P040610; -.
DR H-InvDB; HIX0013842; -.
DR HGNC; HGNC:865; ATP6V0A1.
DR HPA; HPA022144; -.
DR MIM; 192130; gene.
DR neXtProt; NX_Q93050; -.
DR PharmGKB; PA25146; -.
DR eggNOG; COG1269; -.
DR HOGENOM; HOG000037059; -.
DR HOVERGEN; HBG014606; -.
DR KO; K02154; -.
DR OMA; GHAIIML; -.
DR OrthoDB; EOG74FF04; -.
DR BioCyc; MetaCyc:ENSG00000033627-MONOMER; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_15518; Transmembrane transport of small molecules.
DR ChiTaRS; ATP6V0A1; human.
DR GeneWiki; ATPase,_H%2B_transporting,_lysosomal_V0_subunit_a1; -.
DR GenomeRNAi; 535; -.
DR NextBio; 2223; -.
DR PRO; PR:Q93050; -.
DR ArrayExpress; Q93050; -.
DR Bgee; Q93050; -.
DR CleanEx; HS_ATP6V0A1; -.
DR Genevestigator; Q93050; -.
DR GO; GO:0010008; C:endosome membrane; TAS:Reactome.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR GO; GO:0015078; F:hydrogen ion transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
DR GO; GO:0006879; P:cellular iron ion homeostasis; TAS:Reactome.
DR GO; GO:0008286; P:insulin receptor signaling pathway; TAS:Reactome.
DR GO; GO:0051701; P:interaction with host; TAS:Reactome.
DR GO; GO:0090382; P:phagosome maturation; TAS:Reactome.
DR GO; GO:0033572; P:transferrin transport; TAS:Reactome.
DR GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
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 Alternative splicing; Complete proteome; Cytoplasmic vesicle;
KW Hydrogen ion transport; Ion transport; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1 837 V-type proton ATPase 116 kDa subunit a
FT isoform 1.
FT /FTId=PRO_0000119211.
FT TOPO_DOM 1 388 Cytoplasmic (Potential).
FT TRANSMEM 389 407 Helical; (Potential).
FT TOPO_DOM 408 409 Vacuolar (Potential).
FT TRANSMEM 410 426 Helical; (Potential).
FT TOPO_DOM 427 441 Cytoplasmic (Potential).
FT TRANSMEM 442 471 Helical; (Potential).
FT TOPO_DOM 472 534 Vacuolar (Potential).
FT TRANSMEM 535 554 Helical; (Potential).
FT TOPO_DOM 555 572 Cytoplasmic (Potential).
FT TRANSMEM 573 593 Helical; (Potential).
FT TOPO_DOM 594 638 Vacuolar (Potential).
FT TRANSMEM 639 658 Helical; (Potential).
FT TOPO_DOM 659 724 Cytoplasmic (Potential).
FT TRANSMEM 725 749 Helical; (Potential).
FT TOPO_DOM 750 770 Vacuolar (Potential).
FT TRANSMEM 771 809 Helical; (Potential).
FT TOPO_DOM 810 837 Cytoplasmic (Potential).
FT MOD_RES 364 364 Phosphotyrosine (By similarity).
FT VAR_SEQ 141 141 E -> EAELHHQQ (in isoform 3).
FT /FTId=VSP_043532.
FT VAR_SEQ 705 710 Missing (in isoform 2 and isoform 3).
FT /FTId=VSP_012814.
FT CONFLICT 750 751 QL -> HV (in Ref. 1; CAA96077).
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
//
MIM
192130
*RECORD*
*FIELD* NO
192130
*FIELD* TI
*192130 ATPase, H+ TRANSPORTING, LYSOSOMAL, V0 SUBUNIT A1; ATP6V0A1
;;ATPase, H+ TRANSPORTING, LYSOSOMAL, NONCATALYTIC ACCESSORY PROTEIN
read more1A; ATP6N1A;;
ATP6N1;;
VACUOLAR PROTON PUMP, SUBUNIT 1; VPP1
*FIELD* TX
ATP-driven proton pumps associated with the clathrin-coated vesicles and
synaptic vesicles are a group of polypeptides involved in basic cellular
processes through acidification of intracellular organelles. These
functions include intracellular targeting of enzymes to lysosomes and
secretory granules, and receptor-ligand dissociation in
receptor-mediated endocytosis. Eight or 9 polypeptides had been
identified from clathrin-coated vesicles. Using a rat cDNA clone for the
116-kD subunit of the vacuolar proton pump, Ozcelik et al. (1991) mapped
the gene to human chromosome 17 by study of rodent-human hybrid cell
lines and the homologous gene to mouse chromosome 11 by a study of
Chinese hamster or rat/mouse hybrid cell lines. In hybrid cell lines
with fragments of chromosome 17, the VPP1 gene was shown to be located
in region 17q21-qter.
In the course of constructing a transcription map of approximately 600
kb of genomic DNA surrounding the BRCA1 (113705) gene, Brody et al.
(1995) identified the VPP1 gene, thus regionalizing it to 17q21.
*FIELD* RF
1. Brody, L. C.; Abel, K. J.; Castilla, L. H.; Couch, F. J.; McKinley,
D. R.; Yin, G.-Y.; Ho, P. P.; Merajver, S.; Chandrasekharappa, S.
C.; Xu, J.; Cole, J. L.; Struewing, J. P.; Valdes, J. M.; Collins,
F. S.; Weber, B. L.: Construction of a transcription map surrounding
the BRCA1 locus of human chromosome 17. Genomics 25: 238-247, 1995.
2. Ozcelik, T.; Suedhof, T. C.; Francke, U.: Chromosomal assignments
of genes for vacuolar (endomembrane) proton pump subunits VPP1/Vpp-1
(116 kDa) and VPP3/Vpp-3 (58 kDa) in human and mouse. (Abstract) Cytogenet.
Cell Genet. 58: 2008-2009, 1991.
*FIELD* CD
Victor A. McKusick: 8/6/1991
*FIELD* ED
wwang: 01/07/2008
psherman: 3/31/2000
psherman: 10/8/1998
carol: 8/18/1998
terry: 2/10/1995
supermim: 3/16/1992
carol: 2/23/1992
carol: 8/6/1991
*RECORD*
*FIELD* NO
192130
*FIELD* TI
*192130 ATPase, H+ TRANSPORTING, LYSOSOMAL, V0 SUBUNIT A1; ATP6V0A1
;;ATPase, H+ TRANSPORTING, LYSOSOMAL, NONCATALYTIC ACCESSORY PROTEIN
read more1A; ATP6N1A;;
ATP6N1;;
VACUOLAR PROTON PUMP, SUBUNIT 1; VPP1
*FIELD* TX
ATP-driven proton pumps associated with the clathrin-coated vesicles and
synaptic vesicles are a group of polypeptides involved in basic cellular
processes through acidification of intracellular organelles. These
functions include intracellular targeting of enzymes to lysosomes and
secretory granules, and receptor-ligand dissociation in
receptor-mediated endocytosis. Eight or 9 polypeptides had been
identified from clathrin-coated vesicles. Using a rat cDNA clone for the
116-kD subunit of the vacuolar proton pump, Ozcelik et al. (1991) mapped
the gene to human chromosome 17 by study of rodent-human hybrid cell
lines and the homologous gene to mouse chromosome 11 by a study of
Chinese hamster or rat/mouse hybrid cell lines. In hybrid cell lines
with fragments of chromosome 17, the VPP1 gene was shown to be located
in region 17q21-qter.
In the course of constructing a transcription map of approximately 600
kb of genomic DNA surrounding the BRCA1 (113705) gene, Brody et al.
(1995) identified the VPP1 gene, thus regionalizing it to 17q21.
*FIELD* RF
1. Brody, L. C.; Abel, K. J.; Castilla, L. H.; Couch, F. J.; McKinley,
D. R.; Yin, G.-Y.; Ho, P. P.; Merajver, S.; Chandrasekharappa, S.
C.; Xu, J.; Cole, J. L.; Struewing, J. P.; Valdes, J. M.; Collins,
F. S.; Weber, B. L.: Construction of a transcription map surrounding
the BRCA1 locus of human chromosome 17. Genomics 25: 238-247, 1995.
2. Ozcelik, T.; Suedhof, T. C.; Francke, U.: Chromosomal assignments
of genes for vacuolar (endomembrane) proton pump subunits VPP1/Vpp-1
(116 kDa) and VPP3/Vpp-3 (58 kDa) in human and mouse. (Abstract) Cytogenet.
Cell Genet. 58: 2008-2009, 1991.
*FIELD* CD
Victor A. McKusick: 8/6/1991
*FIELD* ED
wwang: 01/07/2008
psherman: 3/31/2000
psherman: 10/8/1998
carol: 8/18/1998
terry: 2/10/1995
supermim: 3/16/1992
carol: 2/23/1992
carol: 8/6/1991