Full text data of ATP6AP1
ATP6AP1
(ATP6IP1, ATP6S1, VATPS1, XAP3)
[Confidence: low (only semi-automatic identification from reviews)]
V-type proton ATPase subunit S1; V-ATPase subunit S1 (Protein XAP-3; V-ATPase Ac45 subunit; V-ATPase S1 accessory protein; Vacuolar proton pump subunit S1; Flags: Precursor)
V-type proton ATPase subunit S1; V-ATPase subunit S1 (Protein XAP-3; V-ATPase Ac45 subunit; V-ATPase S1 accessory protein; Vacuolar proton pump subunit S1; Flags: Precursor)
UniProt
Q15904
ID VAS1_HUMAN Reviewed; 470 AA.
AC Q15904; A6ZKI4;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 11-JAN-2001, sequence version 2.
DT 22-JAN-2014, entry version 136.
DE RecName: Full=V-type proton ATPase subunit S1;
DE Short=V-ATPase subunit S1;
DE AltName: Full=Protein XAP-3;
DE AltName: Full=V-ATPase Ac45 subunit;
DE AltName: Full=V-ATPase S1 accessory protein;
DE AltName: Full=Vacuolar proton pump subunit S1;
DE Flags: Precursor;
GN Name=ATP6AP1; Synonyms=ATP6IP1, ATP6S1, VATPS1, XAP3;
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 [GENOMIC DNA / MRNA].
RX PubMed=8733135; DOI=10.1093/hmg/5.5.659;
RA Chen E.Y., Zollo M., Mazzarella R.A., Ciccodicola A., Chen C.-N.,
RA Zuo L., Heiner C., Burough F.W., Ripetto M., Schlessinger D.,
RA D'Urso M.;
RT "Long-range sequence analysis in Xq28: thirteen known and six
RT candidate genes in 219.4 kb of high GC DNA between the RCP/GCP and
RT G6PD loci.";
RL Hum. Mol. Genet. 5:659-668(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 97-470.
RC TISSUE=Brain;
RX PubMed=8034313; DOI=10.1006/geno.1994.1194;
RA Yokoi H., Hadano S., Kogi M., Kang X., Wakasa K., Ikeda J.;
RT "Isolation of expressed sequences encoded by the human Xq terminal
RT portion using microclone probes generated by laser microdissection.";
RL Genomics 20:404-411(1994).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-261 AND ASN-273, AND MASS
RP SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of
RT multiple enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [8]
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: Vacuolar ATPase is responsible for acidifying a variety
CC of intracellular compartments in eukaryotic cells (By similarity).
CC -!- SUBUNIT: Composed of at least 10 subunits.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane; Single-pass membrane
CC protein (By similarity).
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the vacuolar ATPase subunit S1 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA03938.1; Type=Erroneous initiation;
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; L44140; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK026519; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK289452; BAF82141.1; -; mRNA.
DR EMBL; BX936347; CAI43213.3; -; Genomic_DNA.
DR EMBL; BX936385; CAI43213.3; JOINED; Genomic_DNA.
DR EMBL; BX936385; CAI95782.2; -; Genomic_DNA.
DR EMBL; BX936347; CAI95782.2; JOINED; Genomic_DNA.
DR EMBL; CH471172; EAW72715.1; -; Genomic_DNA.
DR EMBL; BC000724; AAH00724.1; -; mRNA.
DR EMBL; D16469; BAA03938.1; ALT_INIT; mRNA.
DR RefSeq; NP_001174.2; NM_001183.5.
DR UniGene; Hs.633817; -.
DR UniGene; Hs.6551; -.
DR ProteinModelPortal; Q15904; -.
DR IntAct; Q15904; 5.
DR MINT; MINT-4722342; -.
DR STRING; 9606.ENSP00000358777; -.
DR BindingDB; Q15904; -.
DR ChEMBL; CHEMBL4790; -.
DR PhosphoSite; Q15904; -.
DR DMDM; 12230759; -.
DR PaxDb; Q15904; -.
DR PRIDE; Q15904; -.
DR DNASU; 537; -.
DR Ensembl; ENST00000369762; ENSP00000358777; ENSG00000071553.
DR Ensembl; ENST00000594478; ENSP00000472265; ENSG00000269668.
DR GeneID; 537; -.
DR KEGG; hsa:537; -.
DR UCSC; uc004flf.1; human.
DR CTD; 537; -.
DR GeneCards; GC0XP153657; -.
DR HGNC; HGNC:868; ATP6AP1.
DR HPA; CAB015218; -.
DR MIM; 300197; gene.
DR neXtProt; NX_Q15904; -.
DR PharmGKB; PA25145; -.
DR eggNOG; NOG322101; -.
DR HOGENOM; HOG000000706; -.
DR HOVERGEN; HBG001090; -.
DR InParanoid; Q15904; -.
DR KO; K03662; -.
DR OMA; GHITSDM; -.
DR BioCyc; MetaCyc:HS01034-MONOMER; -.
DR GeneWiki; ATP6AP1; -.
DR GenomeRNAi; 537; -.
DR NextBio; 2227; -.
DR PRO; PR:Q15904; -.
DR ArrayExpress; Q15904; -.
DR Bgee; Q15904; -.
DR CleanEx; HS_ATP6AP1; -.
DR Genevestigator; Q15904; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
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:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0005215; F:transporter activity; TAS:ProtInc.
DR GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
DR GO; GO:0015992; P:proton transport; TAS:ProtInc.
DR InterPro; IPR008388; ATPase_V1-cplx_s1su.
DR InterPro; IPR024722; BIG/ATPase_V1_suS1.
DR PANTHER; PTHR12471; PTHR12471; 1.
DR Pfam; PF05827; ATP-synt_S1; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Complete proteome; Glycoprotein; Hydrogen ion transport;
KW Ion transport; Membrane; Nucleotide-binding; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix; Transport; Vacuole.
FT SIGNAL 1 41 Potential.
FT CHAIN 42 470 V-type proton ATPase subunit S1.
FT /FTId=PRO_0000002543.
FT TRANSMEM 420 440 Helical; (Potential).
FT CARBOHYD 170 170 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 261 261 N-linked (GlcNAc...).
FT CARBOHYD 273 273 N-linked (GlcNAc...).
FT CARBOHYD 296 296 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 303 303 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 350 350 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 357 357 N-linked (GlcNAc...) (Potential).
FT CONFLICT 229 229 V -> A (in Ref. 2; AK026519).
FT CONFLICT 307 307 A -> T (in Ref. 2; AK026519).
FT CONFLICT 335 335 S -> F (in Ref. 2; AK026519).
SQ SEQUENCE 470 AA; 52026 MW; A71C7EF0E90D0652 CRC64;
MMAAMATARV RMGPRCAQAL WRMPWLPVFL SLAAAAAAAA AEQQVPLVLW SSDRDLWAPA
ADTHEGHITS DLQLSTYLDP ALELGPRNVL LFLQDKLSIE DFTAYGGVFG NKQDSAFSNL
ENALDLAPSS LVLPAVDWYA VSTLTTYLQE KLGASPLHVD LATLRELKLN ASLPALLLIR
LPYTASSGLM APREVLTGND EVIGQVLSTL KSEDVPYTAA LTAVRPSRVA RDVAVVAGGL
GRQLLQKQPV SPVIHPPVSY NDTAPRILFW AQNFSVAYKD QWEDLTPLTF GVQELNLTGS
FWNDSFARLS LTYERLFGTT VTFKFILANR LYPVSARHWF TMERLEVHSN GSVAYFNASQ
VTGPSIYSFH CEYVSSLSKK GSLLVARTQP SPWQMMLQDF QIQAFNVMGE QFSYASDCAS
FFSPGIWMGL LTSLFMLFIF TYGLHMILSL KTMDRFDDHK GPTISLTQIV
//
ID VAS1_HUMAN Reviewed; 470 AA.
AC Q15904; A6ZKI4;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 11-JAN-2001, sequence version 2.
DT 22-JAN-2014, entry version 136.
DE RecName: Full=V-type proton ATPase subunit S1;
DE Short=V-ATPase subunit S1;
DE AltName: Full=Protein XAP-3;
DE AltName: Full=V-ATPase Ac45 subunit;
DE AltName: Full=V-ATPase S1 accessory protein;
DE AltName: Full=Vacuolar proton pump subunit S1;
DE Flags: Precursor;
GN Name=ATP6AP1; Synonyms=ATP6IP1, ATP6S1, VATPS1, XAP3;
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 [GENOMIC DNA / MRNA].
RX PubMed=8733135; DOI=10.1093/hmg/5.5.659;
RA Chen E.Y., Zollo M., Mazzarella R.A., Ciccodicola A., Chen C.-N.,
RA Zuo L., Heiner C., Burough F.W., Ripetto M., Schlessinger D.,
RA D'Urso M.;
RT "Long-range sequence analysis in Xq28: thirteen known and six
RT candidate genes in 219.4 kb of high GC DNA between the RCP/GCP and
RT G6PD loci.";
RL Hum. Mol. Genet. 5:659-668(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 97-470.
RC TISSUE=Brain;
RX PubMed=8034313; DOI=10.1006/geno.1994.1194;
RA Yokoi H., Hadano S., Kogi M., Kang X., Wakasa K., Ikeda J.;
RT "Isolation of expressed sequences encoded by the human Xq terminal
RT portion using microclone probes generated by laser microdissection.";
RL Genomics 20:404-411(1994).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-261 AND ASN-273, AND MASS
RP SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of
RT multiple enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [8]
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: Vacuolar ATPase is responsible for acidifying a variety
CC of intracellular compartments in eukaryotic cells (By similarity).
CC -!- SUBUNIT: Composed of at least 10 subunits.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane; Single-pass membrane
CC protein (By similarity).
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the vacuolar ATPase subunit S1 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA03938.1; Type=Erroneous initiation;
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; L44140; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK026519; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK289452; BAF82141.1; -; mRNA.
DR EMBL; BX936347; CAI43213.3; -; Genomic_DNA.
DR EMBL; BX936385; CAI43213.3; JOINED; Genomic_DNA.
DR EMBL; BX936385; CAI95782.2; -; Genomic_DNA.
DR EMBL; BX936347; CAI95782.2; JOINED; Genomic_DNA.
DR EMBL; CH471172; EAW72715.1; -; Genomic_DNA.
DR EMBL; BC000724; AAH00724.1; -; mRNA.
DR EMBL; D16469; BAA03938.1; ALT_INIT; mRNA.
DR RefSeq; NP_001174.2; NM_001183.5.
DR UniGene; Hs.633817; -.
DR UniGene; Hs.6551; -.
DR ProteinModelPortal; Q15904; -.
DR IntAct; Q15904; 5.
DR MINT; MINT-4722342; -.
DR STRING; 9606.ENSP00000358777; -.
DR BindingDB; Q15904; -.
DR ChEMBL; CHEMBL4790; -.
DR PhosphoSite; Q15904; -.
DR DMDM; 12230759; -.
DR PaxDb; Q15904; -.
DR PRIDE; Q15904; -.
DR DNASU; 537; -.
DR Ensembl; ENST00000369762; ENSP00000358777; ENSG00000071553.
DR Ensembl; ENST00000594478; ENSP00000472265; ENSG00000269668.
DR GeneID; 537; -.
DR KEGG; hsa:537; -.
DR UCSC; uc004flf.1; human.
DR CTD; 537; -.
DR GeneCards; GC0XP153657; -.
DR HGNC; HGNC:868; ATP6AP1.
DR HPA; CAB015218; -.
DR MIM; 300197; gene.
DR neXtProt; NX_Q15904; -.
DR PharmGKB; PA25145; -.
DR eggNOG; NOG322101; -.
DR HOGENOM; HOG000000706; -.
DR HOVERGEN; HBG001090; -.
DR InParanoid; Q15904; -.
DR KO; K03662; -.
DR OMA; GHITSDM; -.
DR BioCyc; MetaCyc:HS01034-MONOMER; -.
DR GeneWiki; ATP6AP1; -.
DR GenomeRNAi; 537; -.
DR NextBio; 2227; -.
DR PRO; PR:Q15904; -.
DR ArrayExpress; Q15904; -.
DR Bgee; Q15904; -.
DR CleanEx; HS_ATP6AP1; -.
DR Genevestigator; Q15904; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
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:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0005215; F:transporter activity; TAS:ProtInc.
DR GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
DR GO; GO:0015992; P:proton transport; TAS:ProtInc.
DR InterPro; IPR008388; ATPase_V1-cplx_s1su.
DR InterPro; IPR024722; BIG/ATPase_V1_suS1.
DR PANTHER; PTHR12471; PTHR12471; 1.
DR Pfam; PF05827; ATP-synt_S1; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Complete proteome; Glycoprotein; Hydrogen ion transport;
KW Ion transport; Membrane; Nucleotide-binding; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix; Transport; Vacuole.
FT SIGNAL 1 41 Potential.
FT CHAIN 42 470 V-type proton ATPase subunit S1.
FT /FTId=PRO_0000002543.
FT TRANSMEM 420 440 Helical; (Potential).
FT CARBOHYD 170 170 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 261 261 N-linked (GlcNAc...).
FT CARBOHYD 273 273 N-linked (GlcNAc...).
FT CARBOHYD 296 296 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 303 303 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 350 350 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 357 357 N-linked (GlcNAc...) (Potential).
FT CONFLICT 229 229 V -> A (in Ref. 2; AK026519).
FT CONFLICT 307 307 A -> T (in Ref. 2; AK026519).
FT CONFLICT 335 335 S -> F (in Ref. 2; AK026519).
SQ SEQUENCE 470 AA; 52026 MW; A71C7EF0E90D0652 CRC64;
MMAAMATARV RMGPRCAQAL WRMPWLPVFL SLAAAAAAAA AEQQVPLVLW SSDRDLWAPA
ADTHEGHITS DLQLSTYLDP ALELGPRNVL LFLQDKLSIE DFTAYGGVFG NKQDSAFSNL
ENALDLAPSS LVLPAVDWYA VSTLTTYLQE KLGASPLHVD LATLRELKLN ASLPALLLIR
LPYTASSGLM APREVLTGND EVIGQVLSTL KSEDVPYTAA LTAVRPSRVA RDVAVVAGGL
GRQLLQKQPV SPVIHPPVSY NDTAPRILFW AQNFSVAYKD QWEDLTPLTF GVQELNLTGS
FWNDSFARLS LTYERLFGTT VTFKFILANR LYPVSARHWF TMERLEVHSN GSVAYFNASQ
VTGPSIYSFH CEYVSSLSKK GSLLVARTQP SPWQMMLQDF QIQAFNVMGE QFSYASDCAS
FFSPGIWMGL LTSLFMLFIF TYGLHMILSL KTMDRFDDHK GPTISLTQIV
//
MIM
300197
*RECORD*
*FIELD* NO
300197
*FIELD* TI
*300197 ATPase, H+ TRANSPORTING, LYSOSOMAL, ACCESSORY PROTEIN 1; ATP6AP1
;;ATP6IP1;;
read moreATP6S1;;
VACUOLAR ATPase SUBUNIT 1; VATPS1
*FIELD* TX
CLONING
The vacuolar proton-ATPase (V-ATPase) is composed of a catalytic and a
membrane sector. See 603717. Supek et al. (1994) identified a 45-kD
component of V-ATPase from bovine chromaffin granules and cloned the
corresponding gene. The predicted 468-amino acid bovine protein, which
they called Ac45, contains an N-terminal signal sequence and a
C-terminal transmembrane domain.
Independently, Sedlacek et al. (1993), Yokoi et al. (1994), and Chen et
al. (1996) identified the human homolog of Ac45 as an open reading frame
on chromosome Xq28. They designated the human gene XAP3, CF2, and
VATPS1, respectively. Using Northern blot analysis, Yokoi et al. (1994)
demonstrated that CF2 was expressed as a 2.6-kb mRNA in all tissues
tested.
GENE STRUCTURE
Chen et al. (1996) reported that the VATPS1 gene contains 9 exons with
an additional possible exon at the 3-prime end.
MAPPING
By sequence analysis, Sedlacek et al. (1993), Yokoi et al. (1994), and
Chen et al. (1996) mapped the ATP6AP1 gene to chromosome Xq28.
*FIELD* RF
1. Chen, E. Y.; Zollo, M.; Mazzarella, R.; Ciccodicola, A.; Chen,
C.; Zuo, L.; Heiner, C.; Burough, F.; Repetto, M.; Schlessinger, D.;
D'Urso, M.: Long-range sequence analysis in Xq28: thirteen known
and six candidate genes in 219.4 kb of high GC DNA between the RCP/GCP
and G6PD loci. Hum. Molec. Genet. 5: 659-668, 1996.
2. Sedlacek, Z.; Korn, B.; Konecki, D. S.; Siebenhaar, R.; Coy, J.
F.; Kioschis, P.; Poustka, A.: Construction of a transcription map
of a 300 kb region around the human G6PD locus by direct cDNA selection. Hum.
Molec. Genet. 2: 1865-1869, 1993.
3. Supek, F.; Supekova, L.; Mandiyan, S.; Pan, Y.-C. E.; Nelson, H.;
Nelson, N.: A novel accessory subunit for vacuolar H(+)-ATPase from
chromaffin granules. J. Biol. Chem. 269: 24102-24106, 1994.
4. Yokoi, H.; Hadano, S.; Kogi, M.; Kang, X.; Wakasa, K.; Ikeda, J.-E.
: Isolation of expressed sequences encoded by the human Xq terminal
portion using microclone probes generated by laser microdissection. Genomics 20:
404-411, 1994.
*FIELD* CD
Rebekah S. Rasooly: 6/21/1999
*FIELD* ED
mgross: 09/06/2005
carol: 7/29/2002
alopez: 6/23/1999
alopez: 6/22/1999
*RECORD*
*FIELD* NO
300197
*FIELD* TI
*300197 ATPase, H+ TRANSPORTING, LYSOSOMAL, ACCESSORY PROTEIN 1; ATP6AP1
;;ATP6IP1;;
read moreATP6S1;;
VACUOLAR ATPase SUBUNIT 1; VATPS1
*FIELD* TX
CLONING
The vacuolar proton-ATPase (V-ATPase) is composed of a catalytic and a
membrane sector. See 603717. Supek et al. (1994) identified a 45-kD
component of V-ATPase from bovine chromaffin granules and cloned the
corresponding gene. The predicted 468-amino acid bovine protein, which
they called Ac45, contains an N-terminal signal sequence and a
C-terminal transmembrane domain.
Independently, Sedlacek et al. (1993), Yokoi et al. (1994), and Chen et
al. (1996) identified the human homolog of Ac45 as an open reading frame
on chromosome Xq28. They designated the human gene XAP3, CF2, and
VATPS1, respectively. Using Northern blot analysis, Yokoi et al. (1994)
demonstrated that CF2 was expressed as a 2.6-kb mRNA in all tissues
tested.
GENE STRUCTURE
Chen et al. (1996) reported that the VATPS1 gene contains 9 exons with
an additional possible exon at the 3-prime end.
MAPPING
By sequence analysis, Sedlacek et al. (1993), Yokoi et al. (1994), and
Chen et al. (1996) mapped the ATP6AP1 gene to chromosome Xq28.
*FIELD* RF
1. Chen, E. Y.; Zollo, M.; Mazzarella, R.; Ciccodicola, A.; Chen,
C.; Zuo, L.; Heiner, C.; Burough, F.; Repetto, M.; Schlessinger, D.;
D'Urso, M.: Long-range sequence analysis in Xq28: thirteen known
and six candidate genes in 219.4 kb of high GC DNA between the RCP/GCP
and G6PD loci. Hum. Molec. Genet. 5: 659-668, 1996.
2. Sedlacek, Z.; Korn, B.; Konecki, D. S.; Siebenhaar, R.; Coy, J.
F.; Kioschis, P.; Poustka, A.: Construction of a transcription map
of a 300 kb region around the human G6PD locus by direct cDNA selection. Hum.
Molec. Genet. 2: 1865-1869, 1993.
3. Supek, F.; Supekova, L.; Mandiyan, S.; Pan, Y.-C. E.; Nelson, H.;
Nelson, N.: A novel accessory subunit for vacuolar H(+)-ATPase from
chromaffin granules. J. Biol. Chem. 269: 24102-24106, 1994.
4. Yokoi, H.; Hadano, S.; Kogi, M.; Kang, X.; Wakasa, K.; Ikeda, J.-E.
: Isolation of expressed sequences encoded by the human Xq terminal
portion using microclone probes generated by laser microdissection. Genomics 20:
404-411, 1994.
*FIELD* CD
Rebekah S. Rasooly: 6/21/1999
*FIELD* ED
mgross: 09/06/2005
carol: 7/29/2002
alopez: 6/23/1999
alopez: 6/22/1999