GenomeNet

Database: UniProt
Entry: F1PVU4_CANLF
LinkDB: F1PVU4_CANLF
Original site: F1PVU4_CANLF 
ID   F1PVU4_CANLF            Unreviewed;       839 AA.
AC   F1PVU4;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 2.
DT   30-AUG-2017, entry version 45.
DE   RecName: Full=V-type proton ATPase subunit a {ECO:0000256|RuleBase:RU361189};
GN   Name=ATP6V0A1 {ECO:0000313|Ensembl:ENSCAFP00000022163};
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
OC   Canis.
OX   NCBI_TaxID=9615 {ECO:0000313|Ensembl:ENSCAFP00000022163, ECO:0000313|Proteomes:UP000002254};
RN   [1] {ECO:0000313|Ensembl:ENSCAFP00000022163, ECO:0000313|Proteomes:UP000002254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000022163,
RC   ECO:0000313|Proteomes:UP000002254};
RX   PubMed=16341006; DOI=10.1038/nature04338;
RG   Broad Sequencing Platform;
RA   Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
RA   Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C.,
RA   Mauceli E., Xie X., Breen M., Wayne R.K., Ostrander E.A.,
RA   Ponting C.P., Galibert F., Smith D.R., deJong P.J., Kirkness E.F.,
RA   Alvarez P., Biagi T., Brockman W., Butler J., Chin C.-W., Cook A.,
RA   Cuff J., Daly M.J., DeCaprio D., Gnerre S., Grabherr M., Kellis M.,
RA   Kleber M., Bardeleben C., Goodstadt L., Heger A., Hitte C., Kim L.,
RA   Koepfli K.-P., Parker H.G., Pollinger J.P., Searle S.M.J.,
RA   Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
RA   Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
RA   Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L.,
RA   Bachantsang P., Barry A., Bayul T., Benamara M., Berlin A.,
RA   Bessette D., Blitshteyn B., Bloom T., Blye J., Boguslavskiy L.,
RA   Bonnet C., Boukhgalter B., Brown A., Cahill P., Calixte N.,
RA   Camarata J., Cheshatsang Y., Chu J., Citroen M., Collymore A.,
RA   Cooke P., Dawoe T., Daza R., Decktor K., DeGray S., Dhargay N.,
RA   Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N.,
RA   Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
RA   Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K.,
RA   Foley C., Franke A., Friedrich D., Gage D., Garber M., Gearin G.,
RA   Giannoukos G., Goode T., Goyette A., Graham J., Grandbois E.,
RA   Gyaltsen K., Hafez N., Hagopian D., Hagos B., Hall J., Healy C.,
RA   Hegarty R., Honan T., Horn A., Houde N., Hughes L., Hunnicutt L.,
RA   Husby M., Jester B., Jones C., Kamat A., Kanga B., Kells C.,
RA   Khazanovich D., Kieu A.C., Kisner P., Kumar M., Lance K., Landers T.,
RA   Lara M., Lee W., Leger J.-P., Lennon N., Leuper L., LeVine S., Liu J.,
RA   Liu X., Lokyitsang Y., Lokyitsang T., Lui A., Macdonald J., Major J.,
RA   Marabella R., Maru K., Matthews C., McDonough S., Mehta T.,
RA   Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T., Miller K.,
RA   Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A., Naylor J.,
RA   Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
RA   Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K.,
RA   Osman S., Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F.,
RA   Priest M., Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C.,
RA   Rege F., Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S.,
RA   Sharpe T., Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J.,
RA   Smith C., Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S.,
RA   Stone C., Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S.,
RA   Thoulutsang D., Thoulutsang Y., Topham K., Topping I., Tsamla T.,
RA   Vassiliev H., Venkataraman V., Vo A., Wangchuk T., Wangdi T.,
RA   Weiand M., Wilkinson J., Wilson A., Yadav S., Yang S., Yang X.,
RA   Young G., Yu Q., Zainoun J., Zembek L., Zimmer A., Lander E.S.;
RT   "Genome sequence, comparative analysis and haplotype structure of the
RT   domestic dog.";
RL   Nature 438:803-819(2005).
RN   [2] {ECO:0000313|Ensembl:ENSCAFP00000022163}
RP   IDENTIFICATION.
RC   STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000022163};
RG   Ensembl;
RL   Submitted (JUL-2011) to UniProtKB.
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:ENSCAFP00000022163}.
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DR   EMBL; AAEX03006446; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAEX03006447; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_859219.1; XM_854126.4.
DR   STRING; 9615.ENSCAFP00000022163; -.
DR   PaxDb; F1PVU4; -.
DR   Ensembl; ENSCAFT00000023874; ENSCAFP00000022163; ENSCAFG00000015017.
DR   GeneID; 607705; -.
DR   CTD; 535; -.
DR   eggNOG; KOG2189; Eukaryota.
DR   eggNOG; COG1269; LUCA.
DR   GeneTree; ENSGT00390000004941; -.
DR   InParanoid; F1PVU4; -.
DR   OMA; WTAYDAH; -.
DR   OrthoDB; EOG091G01BI; -.
DR   TreeFam; TF300346; -.
DR   Reactome; R-CFA-1222556; ROS, RNS production in phagocytes.
DR   Reactome; R-CFA-6798695; Neutrophil degranulation.
DR   Reactome; R-CFA-77387; Insulin receptor recycling.
DR   Reactome; R-CFA-917977; Transferrin endocytosis and recycling.
DR   Reactome; R-CFA-983712; Ion channel transport.
DR   Proteomes; UP000002254; Chromosome 9.
DR   Bgee; ENSCAFG00000015017; -.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
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:0016241; P:regulation of macroautophagy; IEA:Ensembl.
DR   GO; GO:1901998; P:toxin transport; IEA:Ensembl.
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   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002254};
KW   Hydrogen ion transport {ECO:0000256|RuleBase:RU361189};
KW   Ion transport {ECO:0000256|RuleBase:RU361189};
KW   Membrane {ECO:0000256|RuleBase:RU361189};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002254};
KW   Transmembrane {ECO:0000256|RuleBase:RU361189};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU361189};
KW   Transport {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    408    432       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    452    471       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    549    570       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    576    600       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    641    665       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    743    766       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    772    795       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   COILED       94    128       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   839 AA;  96565 MW;  59D0EAF0B234A2B1 CRC64;
     MGELFRSEEM TLAQLFLQSE AAYCCVSELG ELGKVQFRDL NPDVNVFQRK FVNEVRRCEE
     MDRKLRFVEK EIRKANIPIM DTGENPEVPF PRDMIDLEAN FEKIENELKE INTNQEALKR
     NFLELTELKF ILRKTQQFFD EAELHHQQMA DPDLLEESSS LLEPSEMGRG TPLRLGFVAG
     VINRERIPTF ERMLWRVCRG NVFLRQAEIE NPLEDPVTGD YVHKSVFIIF FQGDQLKNRV
     KKICEGFRAS LYPCPETPQE RKEMASGVNT RIDDLQMVLN QTEDHRQRVL QAAAKNIRVW
     FIKVRKMKAI YHTLNLCNID VTQKCLIAEV WCPVTDLDSI QFALRRGTEH SGSTVPSILN
     RMQTNQTPPT YNKTNKFTYG FQNIVDAYGI GTYREINPAP YTIITFPFLF AVMFGDFGHG
     ILMTLFAVWM VLRESRILSQ KNENEMFSTV FSGRYIILLM GVFSIYTGLI YNDCFSKSLN
     IFGSSWSVRP MFTIYNWTEE TLRGNPVLQL NPSVRGVFGG PYPFGIDPIW NIATNKLTFL
     NSFKMKTSVI LGIIHMMFGV TLSLFNHIYF KKPLNIYFGF IPEIIFMTSL FGYLVILIFY
     KWTAYNADTS EKAPSLLIHF INMFLFSYGD SSNSMLYSGQ KGIQCFLVVV ALLCVPWMLL
     FKPLVLRHQY LRRKHLGTLN FGGIRVGNGP TEEDAEIIQH DQLSTHSEDA EEFDFGDTMV
     HQAIHTIEYC LGCISNTASY LRLWALSLAH AQLSEVLWTM VIHIGLSVKS LAGGLALFFI
     FAAFATLTVA ILLIMEGLSA FLHALRLHWV EFQNKFYSGT GFKFLPFSFE HIREGKFDE
//
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