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VPP4_HUMAN
ID   VPP4_HUMAN              Reviewed;         840 AA.
AC   Q9HBG4; A4D1R4; A8KA80; Q32M47;
DT   14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 2.
DT   03-AUG-2022, entry version 174.
DE   RecName: Full=V-type proton ATPase 116 kDa subunit a 4;
DE            Short=V-ATPase 116 kDa isoform a 4;
DE   AltName: Full=Vacuolar proton translocating ATPase 116 kDa subunit a isoform 4;
DE   AltName: Full=Vacuolar proton translocating ATPase 116 kDa subunit a kidney isoform;
GN   Name=ATP6V0A4; Synonyms=ATP6N1B, ATP6N2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, VARIANTS DRTA3
RP   LEU-524; THR-580 AND ARG-820, AND VARIANT ALA-2.
RC   TISSUE=Kidney;
RX   PubMed=10973252; DOI=10.1038/79208;
RA   Smith A.N., Skaug J., Choate K.A., Nayir A., Bakkaloglu A., Ozen S.,
RA   Hulton S.A., Sanjad S.A., Al-Sabban E.A., Lifton R.P., Scherer S.W.,
RA   Karet F.E.;
RT   "Mutations in ATP6N1B, encoding a new kidney vacuolar proton pump 116-kD
RT   subunit, cause recessive distal renal tubular acidosis with preserved
RT   hearing.";
RL   Nat. Genet. 26:71-75(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-2.
RC   TISSUE=Trachea;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12853948; DOI=10.1038/nature01782;
RA   Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA   Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA   Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA   Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA   Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA   Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA   Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA   Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA   Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA   Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA   Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA   Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA   Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA   Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA   Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA   Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA   Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA   McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA   Wilson R.K.;
RT   "The DNA sequence of human chromosome 7.";
RL   Nature 424:157-164(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12690205; DOI=10.1126/science.1083423;
RA   Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA   Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA   Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA   Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA   Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA   Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA   Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA   Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA   Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA   Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA   Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA   Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA   Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA   Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA   Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA   Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA   Adams M.D., Tsui L.-C.;
RT   "Human chromosome 7: DNA sequence and biology.";
RL   Science 300:767-772(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   FUNCTION, AND VARIANTS DRTA3 ASP-175; LYS-237 DEL; HIS-449 AND GLN-807.
RX   PubMed=12414817; DOI=10.1136/jmg.39.11.796;
RA   Stover E.H., Borthwick K.J., Bavalia C., Eady N., Fritz D.M., Rungroj N.,
RA   Giersch A.B.S., Morton C.C., Axon P.R., Akil I., Al-Sabban E.A.,
RA   Baguley D.M., Bianca S., Bakkaloglu A., Bircan Z., Chauveau D.,
RA   Clermont M.-J., Guala A., Hulton S.A., Kroes H., Li Volti G., Mir S.,
RA   Mocan H., Nayir A., Ozen S., Rodriguez Soriano J., Sanjad S.A., Tasic V.,
RA   Taylor C.M., Topaloglu R., Smith A.N., Karet F.E.;
RT   "Novel ATP6V1B1 and ATP6V0A4 mutations in autosomal recessive distal renal
RT   tubular acidosis with new evidence for hearing loss.";
RL   J. Med. Genet. 39:796-803(2002).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
CC   -!- FUNCTION: Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase),
CC       a multisubunit enzyme composed of a peripheral complex (V1) that
CC       hydrolyzes ATP and a membrane integral complex (V0) that translocates
CC       protons (By similarity). V-ATPase is responsible for acidifying and
CC       maintaining the pH of intracellular compartments and in some cell
CC       types, is targeted to the plasma membrane, where it is responsible for
CC       acidifying the extracellular environment (By similarity). Involved in
CC       normal vectorial acid transport into the urine by the kidney
CC       (PubMed:10973252, PubMed:12414817). {ECO:0000250|UniProtKB:Q29466,
CC       ECO:0000250|UniProtKB:Q93050, ECO:0000269|PubMed:10973252,
CC       ECO:0000269|PubMed:12414817}.
CC   -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme made up of two
CC       complexes: the ATP-hydrolytic V1 complex and the proton translocation
CC       V0 complex (By similarity). The V1 complex consists of three catalytic
CC       AB heterodimers that form a heterohexamer, three peripheral stalks each
CC       consisting of EG heterodimers, one central rotor including subunits D
CC       and F, and the regulatory subunits C and H (By similarity). The proton
CC       translocation complex V0 consists of the proton transport subunit a, a
CC       ring of proteolipid subunits c9c'', rotary subunit d, subunits e and f,
CC       and the accessory subunits ATP6AP1/Ac45 and ATP6AP2/PRR (By
CC       similarity). Interacts with the V1 complex V-ATPase subunit A ATP6V1A
CC       (By similarity). Interacts with the V0 complex V-ATPase subunit c
CC       ATP6V0C (By similarity). {ECO:0000250|UniProtKB:Q920R6,
CC       ECO:0000250|UniProtKB:Q93050}.
CC   -!- INTERACTION:
CC       Q9HBG4; P02649: APOE; NbExp=3; IntAct=EBI-25832286, EBI-1222467;
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane
CC       {ECO:0000269|PubMed:10973252}; Multi-pass membrane protein
CC       {ECO:0000255}. Basolateral cell membrane
CC       {ECO:0000250|UniProtKB:Q920R6}; Multi-pass membrane protein
CC       {ECO:0000255}. Note=Localizes to the apical surface of alpha-
CC       intercalated cells in the cortical collecting ducts of the distal
CC       nephron (PubMed:10973252). Localizes to the basolateral surface of
CC       beta-intercalated cells in the cortical collecting ducts of the distal
CC       nephron (By similarity). {ECO:0000250|UniProtKB:Q920R6,
CC       ECO:0000269|PubMed:10973252}.
CC   -!- TISSUE SPECIFICITY: Expressed in adult and fetal kidney. Found in the
CC       inner ear. {ECO:0000269|PubMed:12414817}.
CC   -!- DISEASE: Renal tubular acidosis, distal, 3, with or without
CC       sensorineural hearing loss (DRTA3) [MIM:602722]: An autosomal recessive
CC       disease characterized by reduced ability to acidify urine, variable
CC       hyperchloremic hypokalemic metabolic acidosis, nephrocalcinosis, and
CC       nephrolithiasis. It is due to functional failure of alpha-intercalated
CC       cells of the cortical collecting duct of the distal nephron, where
CC       vectorial proton transport is required for urinary acidification.
CC       {ECO:0000269|PubMed:10973252, ECO:0000269|PubMed:12414817}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- SIMILARITY: Belongs to the V-ATPase 116 kDa subunit family.
CC       {ECO:0000305}.
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DR   EMBL; AF245517; AAG11415.1; -; mRNA.
DR   EMBL; AK292945; BAF85634.1; -; mRNA.
DR   EMBL; AC018663; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC020983; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH236950; EAL24043.1; -; Genomic_DNA.
DR   EMBL; CH471070; EAW83892.1; -; Genomic_DNA.
DR   EMBL; BC109304; AAI09305.1; -; mRNA.
DR   EMBL; BC109305; AAI09306.1; -; mRNA.
DR   CCDS; CCDS5849.1; -.
DR   RefSeq; NP_065683.2; NM_020632.2.
DR   RefSeq; NP_570855.2; NM_130840.2.
DR   RefSeq; NP_570856.2; NM_130841.2.
DR   RefSeq; XP_005250450.1; XM_005250393.1.
DR   RefSeq; XP_005250451.1; XM_005250394.3.
DR   AlphaFoldDB; Q9HBG4; -.
DR   SMR; Q9HBG4; -.
DR   BioGRID; 119097; 27.
DR   ComplexPortal; CPX-6912; Vacuolar proton translocating ATPase complex, ATP6V0A4 variant.
DR   IntAct; Q9HBG4; 1.
DR   STRING; 9606.ENSP00000308122; -.
DR   DrugBank; DB01133; Tiludronic acid.
DR   TCDB; 3.A.2.2.4; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR   iPTMnet; Q9HBG4; -.
DR   PhosphoSitePlus; Q9HBG4; -.
DR   BioMuta; ATP6V0A4; -.
DR   DMDM; 308153516; -.
DR   EPD; Q9HBG4; -.
DR   jPOST; Q9HBG4; -.
DR   MassIVE; Q9HBG4; -.
DR   MaxQB; Q9HBG4; -.
DR   PaxDb; Q9HBG4; -.
DR   PeptideAtlas; Q9HBG4; -.
DR   PRIDE; Q9HBG4; -.
DR   ProteomicsDB; 81539; -.
DR   Antibodypedia; 3120; 126 antibodies from 23 providers.
DR   DNASU; 50617; -.
DR   Ensembl; ENST00000310018.7; ENSP00000308122.2; ENSG00000105929.16.
DR   Ensembl; ENST00000353492.4; ENSP00000253856.6; ENSG00000105929.16.
DR   Ensembl; ENST00000393054.5; ENSP00000376774.1; ENSG00000105929.16.
DR   Ensembl; ENST00000645515.1; ENSP00000496421.1; ENSG00000105929.16.
DR   GeneID; 50617; -.
DR   KEGG; hsa:50617; -.
DR   MANE-Select; ENST00000310018.7; ENSP00000308122.2; NM_020632.3; NP_065683.2.
DR   UCSC; uc003vuf.4; human.
DR   CTD; 50617; -.
DR   DisGeNET; 50617; -.
DR   GeneCards; ATP6V0A4; -.
DR   GeneReviews; ATP6V0A4; -.
DR   HGNC; HGNC:866; ATP6V0A4.
DR   HPA; ENSG00000105929; Group enriched (kidney, salivary gland).
DR   MalaCards; ATP6V0A4; -.
DR   MIM; 602722; phenotype.
DR   MIM; 605239; gene.
DR   neXtProt; NX_Q9HBG4; -.
DR   OpenTargets; ENSG00000105929; -.
DR   Orphanet; 402041; Autosomal recessive distal renal tubular acidosis.
DR   PharmGKB; PA25147; -.
DR   VEuPathDB; HostDB:ENSG00000105929; -.
DR   eggNOG; KOG2189; Eukaryota.
DR   GeneTree; ENSGT00950000182881; -.
DR   HOGENOM; CLU_005230_0_2_1; -.
DR   InParanoid; Q9HBG4; -.
DR   OMA; GCKEFMF; -.
DR   OrthoDB; 181796at2759; -.
DR   PhylomeDB; Q9HBG4; -.
DR   TreeFam; TF300346; -.
DR   BioCyc; MetaCyc:ENSG00000105929-MON; -.
DR   PathwayCommons; Q9HBG4; -.
DR   Reactome; R-HSA-1222556; ROS and RNS production in phagocytes.
DR   Reactome; R-HSA-77387; Insulin receptor recycling.
DR   Reactome; R-HSA-917977; Transferrin endocytosis and recycling.
DR   Reactome; R-HSA-983712; Ion channel transport.
DR   SignaLink; Q9HBG4; -.
DR   BioGRID-ORCS; 50617; 17 hits in 1069 CRISPR screens.
DR   ChiTaRS; ATP6V0A4; human.
DR   GeneWiki; ATP6V0A4; -.
DR   GenomeRNAi; 50617; -.
DR   Pharos; Q9HBG4; Tbio.
DR   PRO; PR:Q9HBG4; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; Q9HBG4; protein.
DR   Bgee; ENSG00000105929; Expressed in metanephros cortex and 108 other tissues.
DR   ExpressionAtlas; Q9HBG4; baseline and differential.
DR   Genevisible; Q9HBG4; HS.
DR   GO; GO:0045177; C:apical part of cell; IDA:UniProtKB.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR   GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031526; C:brush border membrane; IDA:HGNC-UCL.
DR   GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR   GO; GO:0010008; C:endosome membrane; TAS:Reactome.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
DR   GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0033176; C:proton-transporting V-type ATPase complex; IC:ComplexPortal.
DR   GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IDA:HGNC-UCL.
DR   GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR   GO; GO:0051117; F:ATPase binding; IPI:UniProtKB.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR   GO; GO:0051452; P:intracellular pH reduction; IC:ComplexPortal.
DR   GO; GO:0001503; P:ossification; IMP:HGNC-UCL.
DR   GO; GO:1902600; P:proton transmembrane transport; IMP:HGNC-UCL.
DR   GO; GO:0006885; P:regulation of pH; IMP:HGNC-UCL.
DR   GO; GO:0097254; P:renal tubular secretion; IMP:HGNC-UCL.
DR   GO; GO:0007605; P:sensory perception of sound; IMP:HGNC-UCL.
DR   GO; GO:0007035; P:vacuolar acidification; IBA:GO_Central.
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   Cell membrane; Disease variant; Hydrogen ion transport; Ion transport;
KW   Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..840
FT                   /note="V-type proton ATPase 116 kDa subunit a 4"
FT                   /id="PRO_0000119219"
FT   TOPO_DOM        1..390
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        391..409
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        410..411
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        412..428
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        429..443
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        444..473
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        474..538
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        539..558
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        559..576
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        577..597
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        598..642
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        643..662
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        663..727
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        728..752
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        753..773
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        774..812
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        813..840
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          675..704
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        675..702
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VARIANT         2
FT                   /note="V -> A (in dbSNP:rs10258719)"
FT                   /evidence="ECO:0000269|PubMed:10973252,
FT                   ECO:0000269|PubMed:14702039"
FT                   /id="VAR_020992"
FT   VARIANT         175
FT                   /note="G -> D (in DRTA3)"
FT                   /evidence="ECO:0000269|PubMed:12414817"
FT                   /id="VAR_020993"
FT   VARIANT         237
FT                   /note="Missing (in DRTA3)"
FT                   /evidence="ECO:0000269|PubMed:12414817"
FT                   /id="VAR_020994"
FT   VARIANT         449
FT                   /note="R -> H (in DRTA3; dbSNP:rs1443883930)"
FT                   /evidence="ECO:0000269|PubMed:12414817"
FT                   /id="VAR_020995"
FT   VARIANT         524
FT                   /note="P -> L (in DRTA3; dbSNP:rs121908368)"
FT                   /evidence="ECO:0000269|PubMed:10973252"
FT                   /id="VAR_017255"
FT   VARIANT         554
FT                   /note="F -> L (in dbSNP:rs1026435)"
FT                   /id="VAR_066612"
FT   VARIANT         580
FT                   /note="M -> T (in DRTA3; dbSNP:rs3807153)"
FT                   /evidence="ECO:0000269|PubMed:10973252"
FT                   /id="VAR_017256"
FT   VARIANT         604
FT                   /note="H -> Q (in dbSNP:rs3807154)"
FT                   /id="VAR_066613"
FT   VARIANT         807
FT                   /note="R -> Q (in DRTA3; dbSNP:rs28939081)"
FT                   /evidence="ECO:0000269|PubMed:12414817"
FT                   /id="VAR_020996"
FT   VARIANT         820
FT                   /note="G -> R (in DRTA3; dbSNP:rs267606671)"
FT                   /evidence="ECO:0000269|PubMed:10973252"
FT                   /id="VAR_017257"
FT   CONFLICT        252
FT                   /note="P -> R (in Ref. 6; AAI09305/AAI09306)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   840 AA;  96386 MW;  449964EBC01D4649 CRC64;
     MVSVFRSEEM CLSQLFLQVE AAYCCVAELG ELGLVQFKDL NMNVNSFQRK FVNEVRRCES
     LERILRFLED EMQNEIVVQL LEKSPLTPLP REMITLETVL EKLEGELQEA NQNQQALKQS
     FLELTELKYL LKKTQDFFET ETNLADDFFT EDTSGLLELK AVPAYMTGKL GFIAGVINRE
     RMASFERLLW RICRGNVYLK FSEMDAPLED PVTKEEIQKN IFIIFYQGEQ LRQKIKKICD
     GFRATVYPCP EPAVERREML ESVNVRLEDL ITVITQTESH RQRLLQEAAA NWHSWLIKVQ
     KMKAVYHILN MCNIDVTQQC VIAEIWFPVA DATRIKRALE QGMELSGSSM APIMTTVQSK
     TAPPTFNRTN KFTAGFQNIV DAYGVGSYRE INPAPYTIIT FPFLFAVMFG DCGHGTVMLL
     AALWMILNER RLLSQKTDNE IWNTFFHGRY LILLMGIFSI YTGLIYNDCF SKSLNIFGSS
     WSVQPMFRNG TWNTHVMEES LYLQLDPAIP GVYFGNPYPF GIDPIWNLAS NKLTFLNSYK
     MKMSVILGIV QMVFGVILSL FNHIYFRRTL NIILQFIPEM IFILCLFGYL VFMIIFKWCC
     FDVHVSQHAP SILIHFINMF LFNYSDSSNA PLYKHQQEVQ SFFVVMALIS VPWMLLIKPF
     ILRASHRKSQ LQASRIQEDA TENIEGDSSS PSSRSGQRTS ADTHGALDDH GEEFNFGDVF
     VHQAIHTIEY CLGCISNTAS YLRLWALSLA HAQLSEVLWT MVMNSGLQTR GWGGIVGVFI
     IFAVFAVLTV AILLIMEGLS AFLHALRLHW VEFQNKFYVG DGYKFSPFSF KHILDGTAEE
 
 
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