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Database: UniProt
Entry: F1QE30_DANRE
LinkDB: F1QE30_DANRE
Original site: F1QE30_DANRE 
ID   F1QE30_DANRE            Unreviewed;       839 AA.
AC   F1QE30;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   07-JUN-2017, entry version 42.
DE   RecName: Full=V-type proton ATPase subunit a {ECO:0000256|RuleBase:RU361189};
GN   Name=atp6v0a1b {ECO:0000313|Ensembl:ENSDARP00000041713,
GN   ECO:0000313|ZFIN:ZDB-GENE-050522-215};
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Danio.
OX   NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000041713, ECO:0000313|Proteomes:UP000000437};
RN   [1] {ECO:0000313|Ensembl:ENSDARP00000041713}
RP   IDENTIFICATION.
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000041713};
RG   Ensembl;
RL   Submitted (JUL-2011) to UniProtKB.
RN   [2] {ECO:0000313|Ensembl:ENSDARP00000041713, ECO:0000313|Proteomes:UP000000437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000041713,
RC   ECO:0000313|Proteomes:UP000000437};
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C.,
RA   Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L.,
RA   McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C.,
RA   Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T.,
RA   Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T.,
RA   Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F.,
RA   Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H.,
RA   Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J.,
RA   Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P.,
RA   Barker N., Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G.,
RA   Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D.,
RA   Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K.,
RA   Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C.,
RA   Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J.,
RA   Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA   Saunders D., Wallis J., Babbage A., Hammond S.,
RA   Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A.,
RA   Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D.,
RA   Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z.,
RA   Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J.,
RA   Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C.,
RA   Raddatz G., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C.,
RA   Yang F., Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J.,
RA   Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C.,
RA   Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H.,
RA   Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J.,
RA   Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the
RT   human genome.";
RL   Nature 496:498-503(2013).
CC   -!- FUNCTION: Essential component of the vacuolar proton pump (V-
CC       ATPase), a multimeric enzyme that catalyzes the translocation of
CC       protons across the membranes. Required for assembly and activity
CC       of the V-ATPase. {ECO:0000256|RuleBase:RU361189}.
CC   -!- SIMILARITY: Belongs to the V-ATPase 116 kDa subunit family.
CC       {ECO:0000256|RuleBase:RU361189}.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data. {ECO:0000313|Ensembl:ENSDARP00000041713}.
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DR   EMBL; BX294185; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 7955.ENSDARP00000041713; -.
DR   PaxDb; F1QE30; -.
DR   Ensembl; ENSDART00000041714; ENSDARP00000041713; ENSDARG00000015174.
DR   ZFIN; ZDB-GENE-050522-215; atp6v0a1b.
DR   eggNOG; KOG2189; Eukaryota.
DR   eggNOG; COG1269; LUCA.
DR   GeneTree; ENSGT00390000004941; -.
DR   InParanoid; F1QE30; -.
DR   OMA; WTAYDAH; -.
DR   OrthoDB; EOG091G01BI; -.
DR   TreeFam; TF300346; -.
DR   Reactome; R-DRE-1222556; ROS, RNS production in phagocytes.
DR   Reactome; R-DRE-6798695; Neutrophil degranulation.
DR   Reactome; R-DRE-77387; Insulin receptor recycling.
DR   Reactome; R-DRE-917977; Transferrin endocytosis and recycling.
DR   Reactome; R-DRE-983712; Ion channel transport.
DR   Proteomes; UP000000437; Chromosome 24.
DR   Bgee; ENSDARG00000015174; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IBA:GO_Central.
DR   GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR   GO; GO:0051117; F:ATPase binding; IBA:GO_Central.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IBA:GO_Central.
DR   GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
DR   GO; GO:0015986; P:ATP synthesis coupled proton transport; IBA:GO_Central.
DR   GO; GO:0071466; P:cellular response to xenobiotic stimulus; IDA:ZFIN.
DR   GO; GO:0007035; P:vacuolar acidification; IBA:GO_Central.
DR   GO; GO:0070072; P:vacuolar proton-transporting V-type ATPase complex assembly; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000437};
KW   Hydrogen ion transport {ECO:0000256|RuleBase:RU361189};
KW   Ion transport {ECO:0000256|RuleBase:RU361189};
KW   Membrane {ECO:0000256|RuleBase:RU361189};
KW   Proteomics identification {ECO:0000213|PeptideAtlas:F1QE30};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW   Transmembrane {ECO:0000256|RuleBase:RU361189};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU361189};
KW   Transport {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    401    425       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    445    464       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    543    564       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    570    594       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    635    655       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    773    795       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   COILED       94    121       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   839 AA;  95708 MW;  78729D891EEE62B7 CRC64;
     MGELFRSEEM TLAQLFLQSE AAYCCVSELG ELGMVQFRDL NPDVNVFQRK FVNEVRRCEE
     MDRKLRFVEK EIKKANIPTM DTGENPEVPF PRDMIDLEAT FEKLENELKE INTNQEALKK
     NFLELTELKH ILRRTQQFFD EMEDPNLLEE SSSLLDPSEA GRGAPLRLGF VAGVINRERI
     PTFERMLWRV CRGNVFLRQT EIEDPLEDPT TGDQVHKSVF IIFFQGDQLK NRVKKICEGF
     RASLYPCPET PQERKEMASG VNTRIDDLQM VLNQTEDHRQ RVLQAAAKTM RVWFIKVRKM
     KAIYHTLNLC NIDVTQKCLI AEVWCPVSDL DSIQFALRRG TERSGSTVPS ILNRMQTKQT
     PPTYNKTNKF TSGFQNIVDA YGIGTYREIN PAPYTIITFP FLFAVMFGDM GHGVLMTSAA
     LYLVLRETRL LAQKSDNEMF NMIFAGRYII LLMGMFSVYT GLIYNDCFSK SLNMFSSGWS
     VRPMFAPNGN WTDQTLESNS VLQLNPSVSG VFGGPYPLGI DPIWNIAANK LTFLNSFKMK
     MSVILGVIHM LFGVTLSLFN HLYFKKPLNI FLNFIPEIVF MSSLFGYLIL LIFYKWIAYD
     AVTSKDAPSL LIAFINMCLF NYNDPTNKPL YRGQAGIQSL LVVIALACVP VMLVVKTMIL
     RRQHLWKKHL GTQKFGGVRV GNGPTEDEAE IIDHDQLSQH SEEGDEHSEE EPFNFGDMAV
     HQAIHTIEYC LGCISNTASY LRLWALSLAH AQLSEVLWGM VMRLGLSSRS GGGFFGLSII
     FSAFATLTVC ILLIMEGLSA FLHALRLHWV EFQNKFYTGQ GFKFVPFSFE SILEGRFDE
//
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