Full text data of ATP6V1A
ATP6V1A
(ATP6A1, ATP6V1A1, VPP2)
[Confidence: high (present in two of the MS resources)]
V-type proton ATPase catalytic subunit A; V-ATPase subunit A; 3.6.3.14 (V-ATPase 69 kDa subunit; Vacuolar ATPase isoform VA68; Vacuolar proton pump subunit alpha)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
V-type proton ATPase catalytic subunit A; V-ATPase subunit A; 3.6.3.14 (V-ATPase 69 kDa subunit; Vacuolar ATPase isoform VA68; Vacuolar proton pump subunit alpha)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00007682
IPI00007682 Vacuolar ATP synthase catalytic subunit A, ubiquitous isoform Noncatalytic subunit of the peripheral V1 complex of vacuolar ATPase soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a endomembrane n/a found at its expected molecular weight found at molecular weight
IPI00007682 Vacuolar ATP synthase catalytic subunit A, ubiquitous isoform Noncatalytic subunit of the peripheral V1 complex of vacuolar ATPase soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a endomembrane n/a found at its expected molecular weight found at molecular weight
UniProt
P38606
ID VATA_HUMAN Reviewed; 617 AA.
AC P38606; B2RBR8; D3DN75; Q53YD9; Q96DY6; Q9UHY3;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
read moreDT 02-AUG-2002, sequence version 2.
DT 22-JAN-2014, entry version 142.
DE RecName: Full=V-type proton ATPase catalytic subunit A;
DE Short=V-ATPase subunit A;
DE EC=3.6.3.14;
DE AltName: Full=V-ATPase 69 kDa subunit;
DE AltName: Full=Vacuolar ATPase isoform VA68;
DE AltName: Full=Vacuolar proton pump subunit alpha;
GN Name=ATP6V1A; Synonyms=ATP6A1, ATP6V1A1, VPP2;
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].
RC TISSUE=Fetal adrenal gland, and Leukocyte;
RX PubMed=8463241;
RA van Hille B., Richener H., Evans D.B., Green J.R., Bilbe G.;
RT "Identification of two subunit A isoforms of the vacuolar H(+)-ATPase
RT in human osteoclastoma.";
RL J. Biol. Chem. 268:7075-7080(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Amygdala;
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 [5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [7]
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).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Catalytic subunit of the peripheral V1 complex of
CC vacuolar ATPase. V-ATPase vacuolar ATPase is responsible for
CC acidifying a variety of intracellular compartments in eukaryotic
CC cells.
CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(In) = ADP + phosphate +
CC H(+)(Out).
CC -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a
CC peripheral catalytic V1 complex (main components: subunits A, B,
CC C, D, E, and F) attached to an integral membrane V0 proton pore
CC complex (main component: the proteolipid protein).
CC -!- TISSUE SPECIFICITY: Present in all tissues analyzed.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
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DR EMBL; L09235; AAA83249.1; -; mRNA.
DR EMBL; AF113129; AAF14870.1; -; mRNA.
DR EMBL; BT006672; AAP35318.1; -; mRNA.
DR EMBL; AK314779; BAG37315.1; -; mRNA.
DR EMBL; CH471052; EAW79625.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79626.1; -; Genomic_DNA.
DR EMBL; BC013138; AAH13138.1; -; mRNA.
DR PIR; B46091; B46091.
DR RefSeq; NP_001681.2; NM_001690.3.
DR UniGene; Hs.477155; -.
DR ProteinModelPortal; P38606; -.
DR SMR; P38606; 40-587.
DR IntAct; P38606; 63.
DR MINT; MINT-224589; -.
DR STRING; 9606.ENSP00000273398; -.
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; P38606; -.
DR DMDM; 22096378; -.
DR PaxDb; P38606; -.
DR PeptideAtlas; P38606; -.
DR PRIDE; P38606; -.
DR DNASU; 523; -.
DR Ensembl; ENST00000273398; ENSP00000273398; ENSG00000114573.
DR GeneID; 523; -.
DR KEGG; hsa:523; -.
DR UCSC; uc003eao.3; human.
DR CTD; 523; -.
DR GeneCards; GC03P113465; -.
DR HGNC; HGNC:851; ATP6V1A.
DR HPA; CAB006910; -.
DR MIM; 607027; gene.
DR neXtProt; NX_P38606; -.
DR PharmGKB; PA25152; -.
DR eggNOG; COG1155; -.
DR HOGENOM; HOG000161057; -.
DR HOVERGEN; HBG053351; -.
DR InParanoid; P38606; -.
DR KO; K02145; -.
DR OMA; VNTSNMP; -.
DR OrthoDB; EOG7Q8CMM; -.
DR PhylomeDB; P38606; -.
DR BioCyc; MetaCyc:HS03781-MONOMER; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_15518; Transmembrane transport of small molecules.
DR ChiTaRS; ATP6V1A; human.
DR GeneWiki; ATP6V1A; -.
DR GenomeRNAi; 523; -.
DR NextBio; 2175; -.
DR PRO; PR:P38606; -.
DR ArrayExpress; P38606; -.
DR Bgee; P38606; -.
DR CleanEx; HS_ATP6V1A; -.
DR Genevestigator; P38606; -.
DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005887; C:integral to plasma membrane; TAS:ProtInc.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0005902; C:microvillus; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0016469; C:proton-transporting two-sector ATPase complex; TAS:ProtInc.
DR GO; GO:0033180; C:proton-transporting V-type ATPase, V1 domain; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; 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 Gene3D; 1.10.1140.10; -; 1.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR000793; ATPase_F1/V1/A1-cplx_a/bsu_C.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR004100; ATPase_F1_a/bsu_N.
DR InterPro; IPR024034; ATPase_F1_bsu/V1_C.
DR InterPro; IPR005725; ATPase_V1-cplx_asu.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR022878; V-ATPase_asu.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF00306; ATP-synt_ab_C; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR SUPFAM; SSF47917; SSF47917; 1.
DR SUPFAM; SSF50615; SSF50615; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01042; V-ATPase_V1_A; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Complete proteome; Hydrogen ion transport; Hydrolase;
KW Ion transport; Nucleotide-binding; Reference proteome; Transport.
FT CHAIN 1 617 V-type proton ATPase catalytic subunit A.
FT /FTId=PRO_0000144560.
FT NP_BIND 250 257 ATP (Potential).
FT CONFLICT 71 71 S -> C (in Ref. 1; AAA83249).
FT CONFLICT 89 90 EL -> DV (in Ref. 1; AAA83249).
FT CONFLICT 211 211 V -> A (in Ref. 1; AAA83249 and 2;
FT AAF14870).
SQ SEQUENCE 617 AA; 68304 MW; DB409A8731D772CB CRC64;
MDFSKLPKIL DEDKESTFGY VHGVSGPVVT ACDMAGAAMY ELVRVGHSEL VGEIIRLEGD
MATIQVYEET SGVSVGDPVL RTGKPLSVEL GPGIMGAIFD GIQRPLSDIS SQTQSIYIPR
GVNVSALSRD IKWDFTPCKN LRVGSHITGG DIYGIVSENS LIKHKIMLPP RNRGTVTYIA
PPGNYDTSDV VLELEFEGVK EKFTMVQVWP VRQVRPVTEK LPANHPLLTG QRVLDALFPC
VQGGTTAIPG AFGCGKTVIS QSLSKYSNSD VIIYVGCGER GNEMSEVLRD FPELTMEVDG
KVESIMKRTA LVANTSNMPV AAREASIYTG ITLSEYFRDM GYHVSMMADS TSRWAEALRE
ISGRLAEMPA DSGYPAYLGA RLASFYERAG RVKCLGNPER EGSVSIVGAV SPPGGDFSDP
VTSATLGIVQ VFWGLDKKLA QRKHFPSVNW LISYSKYMRA LDEYYDKHFT EFVPLRTKAK
EILQEEEDLA EIVQLVGKAS LAETDKITLE VAKLIKDDFL QQNGYTPYDR FCPFYKTVGM
LSNMIAFYDM ARRAVETTAQ SDNKITWSII REHMGDILYK LSSMKFKDPL KDGEAKIKSD
YAQLLEDMQN AFRSLED
//
ID VATA_HUMAN Reviewed; 617 AA.
AC P38606; B2RBR8; D3DN75; Q53YD9; Q96DY6; Q9UHY3;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
read moreDT 02-AUG-2002, sequence version 2.
DT 22-JAN-2014, entry version 142.
DE RecName: Full=V-type proton ATPase catalytic subunit A;
DE Short=V-ATPase subunit A;
DE EC=3.6.3.14;
DE AltName: Full=V-ATPase 69 kDa subunit;
DE AltName: Full=Vacuolar ATPase isoform VA68;
DE AltName: Full=Vacuolar proton pump subunit alpha;
GN Name=ATP6V1A; Synonyms=ATP6A1, ATP6V1A1, VPP2;
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].
RC TISSUE=Fetal adrenal gland, and Leukocyte;
RX PubMed=8463241;
RA van Hille B., Richener H., Evans D.B., Green J.R., Bilbe G.;
RT "Identification of two subunit A isoforms of the vacuolar H(+)-ATPase
RT in human osteoclastoma.";
RL J. Biol. Chem. 268:7075-7080(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Amygdala;
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 [5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [7]
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).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Catalytic subunit of the peripheral V1 complex of
CC vacuolar ATPase. V-ATPase vacuolar ATPase is responsible for
CC acidifying a variety of intracellular compartments in eukaryotic
CC cells.
CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(In) = ADP + phosphate +
CC H(+)(Out).
CC -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a
CC peripheral catalytic V1 complex (main components: subunits A, B,
CC C, D, E, and F) attached to an integral membrane V0 proton pore
CC complex (main component: the proteolipid protein).
CC -!- TISSUE SPECIFICITY: Present in all tissues analyzed.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
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DR EMBL; L09235; AAA83249.1; -; mRNA.
DR EMBL; AF113129; AAF14870.1; -; mRNA.
DR EMBL; BT006672; AAP35318.1; -; mRNA.
DR EMBL; AK314779; BAG37315.1; -; mRNA.
DR EMBL; CH471052; EAW79625.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79626.1; -; Genomic_DNA.
DR EMBL; BC013138; AAH13138.1; -; mRNA.
DR PIR; B46091; B46091.
DR RefSeq; NP_001681.2; NM_001690.3.
DR UniGene; Hs.477155; -.
DR ProteinModelPortal; P38606; -.
DR SMR; P38606; 40-587.
DR IntAct; P38606; 63.
DR MINT; MINT-224589; -.
DR STRING; 9606.ENSP00000273398; -.
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; P38606; -.
DR DMDM; 22096378; -.
DR PaxDb; P38606; -.
DR PeptideAtlas; P38606; -.
DR PRIDE; P38606; -.
DR DNASU; 523; -.
DR Ensembl; ENST00000273398; ENSP00000273398; ENSG00000114573.
DR GeneID; 523; -.
DR KEGG; hsa:523; -.
DR UCSC; uc003eao.3; human.
DR CTD; 523; -.
DR GeneCards; GC03P113465; -.
DR HGNC; HGNC:851; ATP6V1A.
DR HPA; CAB006910; -.
DR MIM; 607027; gene.
DR neXtProt; NX_P38606; -.
DR PharmGKB; PA25152; -.
DR eggNOG; COG1155; -.
DR HOGENOM; HOG000161057; -.
DR HOVERGEN; HBG053351; -.
DR InParanoid; P38606; -.
DR KO; K02145; -.
DR OMA; VNTSNMP; -.
DR OrthoDB; EOG7Q8CMM; -.
DR PhylomeDB; P38606; -.
DR BioCyc; MetaCyc:HS03781-MONOMER; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_15518; Transmembrane transport of small molecules.
DR ChiTaRS; ATP6V1A; human.
DR GeneWiki; ATP6V1A; -.
DR GenomeRNAi; 523; -.
DR NextBio; 2175; -.
DR PRO; PR:P38606; -.
DR ArrayExpress; P38606; -.
DR Bgee; P38606; -.
DR CleanEx; HS_ATP6V1A; -.
DR Genevestigator; P38606; -.
DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005887; C:integral to plasma membrane; TAS:ProtInc.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0005902; C:microvillus; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0016469; C:proton-transporting two-sector ATPase complex; TAS:ProtInc.
DR GO; GO:0033180; C:proton-transporting V-type ATPase, V1 domain; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; 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 Gene3D; 1.10.1140.10; -; 1.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR000793; ATPase_F1/V1/A1-cplx_a/bsu_C.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR004100; ATPase_F1_a/bsu_N.
DR InterPro; IPR024034; ATPase_F1_bsu/V1_C.
DR InterPro; IPR005725; ATPase_V1-cplx_asu.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR022878; V-ATPase_asu.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF00306; ATP-synt_ab_C; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR SUPFAM; SSF47917; SSF47917; 1.
DR SUPFAM; SSF50615; SSF50615; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01042; V-ATPase_V1_A; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Complete proteome; Hydrogen ion transport; Hydrolase;
KW Ion transport; Nucleotide-binding; Reference proteome; Transport.
FT CHAIN 1 617 V-type proton ATPase catalytic subunit A.
FT /FTId=PRO_0000144560.
FT NP_BIND 250 257 ATP (Potential).
FT CONFLICT 71 71 S -> C (in Ref. 1; AAA83249).
FT CONFLICT 89 90 EL -> DV (in Ref. 1; AAA83249).
FT CONFLICT 211 211 V -> A (in Ref. 1; AAA83249 and 2;
FT AAF14870).
SQ SEQUENCE 617 AA; 68304 MW; DB409A8731D772CB CRC64;
MDFSKLPKIL DEDKESTFGY VHGVSGPVVT ACDMAGAAMY ELVRVGHSEL VGEIIRLEGD
MATIQVYEET SGVSVGDPVL RTGKPLSVEL GPGIMGAIFD GIQRPLSDIS SQTQSIYIPR
GVNVSALSRD IKWDFTPCKN LRVGSHITGG DIYGIVSENS LIKHKIMLPP RNRGTVTYIA
PPGNYDTSDV VLELEFEGVK EKFTMVQVWP VRQVRPVTEK LPANHPLLTG QRVLDALFPC
VQGGTTAIPG AFGCGKTVIS QSLSKYSNSD VIIYVGCGER GNEMSEVLRD FPELTMEVDG
KVESIMKRTA LVANTSNMPV AAREASIYTG ITLSEYFRDM GYHVSMMADS TSRWAEALRE
ISGRLAEMPA DSGYPAYLGA RLASFYERAG RVKCLGNPER EGSVSIVGAV SPPGGDFSDP
VTSATLGIVQ VFWGLDKKLA QRKHFPSVNW LISYSKYMRA LDEYYDKHFT EFVPLRTKAK
EILQEEEDLA EIVQLVGKAS LAETDKITLE VAKLIKDDFL QQNGYTPYDR FCPFYKTVGM
LSNMIAFYDM ARRAVETTAQ SDNKITWSII REHMGDILYK LSSMKFKDPL KDGEAKIKSD
YAQLLEDMQN AFRSLED
//
MIM
607027
*RECORD*
*FIELD* NO
607027
*FIELD* TI
*607027 ATPase, H+ TRANSPORTING, LYSOSOMAL ALPHA POLYPEPTIDE, 70-KD, ISOFORM
1; ATP6V1A1
read more;;V-ATPase A SUBUNIT 1;;
VACUOLAR PROTON PUMP, ALPHA SUBUNIT 1;;
VA68
HO68, INCLUDED
*FIELD* TX
DESCRIPTION
The vacuolar-type H(+)-ATPase (V-ATPase) is responsible for the
acidification of endosomes, lysosomes, and other intracellular
organelles. It is also involved in hydrogen ion transport across the
plasma membrane into the extracellular space. The V-ATPase is a
multisubunit complex with cytosolic and transmembrane domains. The
cytosolic catalytic domain consists of 3 A subunits and 3 B subunits,
which bind and hydrolyze ATP, as well as regulatory accessory subunits.
CLONING
Van Hille et al. (1993) cloned a partial cDNA clone for an A subunit
isoform, which they designated VA68, from a human osteoclastoma tumor
cDNA library by PCR using degenerate primers based on the bovine
sequence. They obtained a full-length clone from a genomic library. The
deduced 617-amino acid protein has a predicted molecular mass of about
68 kD and shows 99% sequence identity with the bovine brain subunit A.
Northern blot analysis revealed ubiquitous expression of a major 4.8-kb
band and a minor 3.4-kb band. They also identified a variant, which they
designated HO68, encoding a 615-amino acid protein. By RNase protection
assays and in situ hybridization, van Hille et al. (1995) determined
that expression of the HO68 variant was specific to the osteoclastoma
originally used to construct the cDNA library.
GENE FUNCTION
Amino acids activate the Rag GTPases, which promote the translocation of
mTORC1 (see 601231) to the lysosomal surface, the site of mTORC1
activation. Zoncu et al. (2011) found that the v-ATPase is necessary for
amino acids to activate mTORC1. The v-ATPase engages in extensive
amino-acid sensitive interactions with the Ragulator, a scaffolding
complex that anchors the Rag GTPases to the lysosome. In a cell-free
system, ATP hydrolysis by the v-ATPase was necessary for amino acids to
regulate the v-ATPase-Ragulator interaction and promote mTORC1
translocation. The results obtained in vitro and in human cells
suggested that amino acid signaling begins within the lysosomal lumen.
Zoncu et al. (2011) concluded that their results identified the v-ATPase
as a component of the mTOR pathway and delineated a lysosome-associated
machinery for amino acid sensing.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the
ATP6V1A1 gene to chromosome 3 (TMAP stSG364).
*FIELD* RF
1. van Hille, B.; Richener, H.; Evans, D. B.; Green, J. R.; Bilbe,
G.: Identification of two subunit A isoforms of the vacuolar H(+)-ATPase
in human osteoclastoma. J. Biol. Chem. 268: 7075-7080, 1993.
2. van Hille, B.; Richener, H.; Green, J. R.; Bilbe, G.: The ubiquitous
VA68 isoform of subunit A of the vacuolar H(+)-ATPase is highly expressed
in human osteoclasts. Biochem. Biophys. Res. Commun. 214: 1108-1113,
1995.
3. Zoncu, R.; Bar-Peled, L.; Efeyan, A.; Wang, S.; Sancak, Y.; Sabatini,
D. M.: mTORC1 senses lysosomal amino acids through an inside-out
mechanism that requires the vacuolar H(+)-ATPase. Science 334: 678-683,
2011.
*FIELD* CN
Ada Hamosh - updated: 11/29/2011
*FIELD* CD
Patricia A. Hartz: 6/7/2002
*FIELD* ED
alopez: 11/30/2011
terry: 11/29/2011
carol: 7/7/2006
carol: 6/10/2002
*RECORD*
*FIELD* NO
607027
*FIELD* TI
*607027 ATPase, H+ TRANSPORTING, LYSOSOMAL ALPHA POLYPEPTIDE, 70-KD, ISOFORM
1; ATP6V1A1
read more;;V-ATPase A SUBUNIT 1;;
VACUOLAR PROTON PUMP, ALPHA SUBUNIT 1;;
VA68
HO68, INCLUDED
*FIELD* TX
DESCRIPTION
The vacuolar-type H(+)-ATPase (V-ATPase) is responsible for the
acidification of endosomes, lysosomes, and other intracellular
organelles. It is also involved in hydrogen ion transport across the
plasma membrane into the extracellular space. The V-ATPase is a
multisubunit complex with cytosolic and transmembrane domains. The
cytosolic catalytic domain consists of 3 A subunits and 3 B subunits,
which bind and hydrolyze ATP, as well as regulatory accessory subunits.
CLONING
Van Hille et al. (1993) cloned a partial cDNA clone for an A subunit
isoform, which they designated VA68, from a human osteoclastoma tumor
cDNA library by PCR using degenerate primers based on the bovine
sequence. They obtained a full-length clone from a genomic library. The
deduced 617-amino acid protein has a predicted molecular mass of about
68 kD and shows 99% sequence identity with the bovine brain subunit A.
Northern blot analysis revealed ubiquitous expression of a major 4.8-kb
band and a minor 3.4-kb band. They also identified a variant, which they
designated HO68, encoding a 615-amino acid protein. By RNase protection
assays and in situ hybridization, van Hille et al. (1995) determined
that expression of the HO68 variant was specific to the osteoclastoma
originally used to construct the cDNA library.
GENE FUNCTION
Amino acids activate the Rag GTPases, which promote the translocation of
mTORC1 (see 601231) to the lysosomal surface, the site of mTORC1
activation. Zoncu et al. (2011) found that the v-ATPase is necessary for
amino acids to activate mTORC1. The v-ATPase engages in extensive
amino-acid sensitive interactions with the Ragulator, a scaffolding
complex that anchors the Rag GTPases to the lysosome. In a cell-free
system, ATP hydrolysis by the v-ATPase was necessary for amino acids to
regulate the v-ATPase-Ragulator interaction and promote mTORC1
translocation. The results obtained in vitro and in human cells
suggested that amino acid signaling begins within the lysosomal lumen.
Zoncu et al. (2011) concluded that their results identified the v-ATPase
as a component of the mTOR pathway and delineated a lysosome-associated
machinery for amino acid sensing.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the
ATP6V1A1 gene to chromosome 3 (TMAP stSG364).
*FIELD* RF
1. van Hille, B.; Richener, H.; Evans, D. B.; Green, J. R.; Bilbe,
G.: Identification of two subunit A isoforms of the vacuolar H(+)-ATPase
in human osteoclastoma. J. Biol. Chem. 268: 7075-7080, 1993.
2. van Hille, B.; Richener, H.; Green, J. R.; Bilbe, G.: The ubiquitous
VA68 isoform of subunit A of the vacuolar H(+)-ATPase is highly expressed
in human osteoclasts. Biochem. Biophys. Res. Commun. 214: 1108-1113,
1995.
3. Zoncu, R.; Bar-Peled, L.; Efeyan, A.; Wang, S.; Sancak, Y.; Sabatini,
D. M.: mTORC1 senses lysosomal amino acids through an inside-out
mechanism that requires the vacuolar H(+)-ATPase. Science 334: 678-683,
2011.
*FIELD* CN
Ada Hamosh - updated: 11/29/2011
*FIELD* CD
Patricia A. Hartz: 6/7/2002
*FIELD* ED
alopez: 11/30/2011
terry: 11/29/2011
carol: 7/7/2006
carol: 6/10/2002