ID Q7ZYW7_DANRE Unreviewed; 139 AA.
AC Q7ZYW7;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 10-MAY-2017, entry version 111.
DE SubName: Full=ATP synthase, H+-transporting, mitochondrial Fo complex, subunit C3 (subunit 9), genome duplicate a {ECO:0000313|Ensembl:ENSDARP00000015997};
DE SubName: Full=Zgc:55970 {ECO:0000313|EMBL:AAH47199.1};
DE SubName: Full=Zgc:55970 protein {ECO:0000313|EMBL:AAH78654.1};
GN Name=atp5g3a {ECO:0000313|Ensembl:ENSDARP00000015997,
GN ECO:0000313|ZFIN:ZDB-GENE-040426-857};
GN Synonyms=zgc:55970 {ECO:0000313|EMBL:AAH47199.1};
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|EMBL:AAH47199.1};
RN [1] {ECO:0000313|EMBL:AAH47199.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB {ECO:0000313|EMBL:AAH47199.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:AAH47199.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AAH78654.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo {ECO:0000313|EMBL:AAH78654.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSDARP00000015997}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000015997};
RG Ensembl;
RL Submitted (JUL-2011) to UniProtKB.
RN [4] {ECO:0000313|Ensembl:ENSDARP00000015997, ECO:0000313|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000015997,
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).
RN [5] {ECO:0000313|Ensembl:ENSDARP00000106777}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000106777};
RG Ensembl;
RL Submitted (NOV-2014) to UniProtKB.
CC -!- SIMILARITY: Belongs to the ATPase C chain family.
CC {ECO:0000256|RuleBase:RU004221}.
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DR EMBL; CU639436; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC047199; AAH47199.1; -; mRNA.
DR EMBL; BC078654; AAH78654.1; -; mRNA.
DR RefSeq; NP_957470.1; NM_201176.1.
DR UniGene; Dr.29150; -.
DR STRING; 7955.ENSDARP00000015997; -.
DR Ensembl; ENSDART00000016417; ENSDARP00000015997; ENSDARG00000017775.
DR Ensembl; ENSDART00000123340; ENSDARP00000106777; ENSDARG00000017775.
DR GeneID; 394151; -.
DR KEGG; dre:394151; -.
DR CTD; 394151; -.
DR ZFIN; ZDB-GENE-040426-857; atp5g3a.
DR eggNOG; KOG3025; Eukaryota.
DR eggNOG; COG0636; LUCA.
DR GeneTree; ENSGT00390000006210; -.
DR HOGENOM; HOG000235246; -.
DR HOVERGEN; HBG050605; -.
DR KO; K02128; -.
DR OMA; VMPQNPL; -.
DR OrthoDB; EOG091G13J1; -.
DR TreeFam; TF300140; -.
DR Reactome; R-DRE-163210; Formation of ATP by chemiosmotic coupling.
DR Proteomes; UP000000437; Chromosome 9.
DR Bgee; ENSDARG00000017775; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IBA:GO_Central.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0046933; F:proton-transporting ATP synthase 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 Gene3D; 1.20.20.10; -; 1.
DR HAMAP; MF_01396; ATP_synth_c_bact; 1.
DR InterPro; IPR000454; ATP_synth_F0_csu.
DR InterPro; IPR020537; ATP_synth_F0_csu_DDCD_BS.
DR InterPro; IPR002379; ATPase_proteolipid_c-like_dom.
DR PANTHER; PTHR10031; PTHR10031; 1.
DR Pfam; PF00137; ATP-synt_C; 1.
DR PRINTS; PR00124; ATPASEC.
DR SUPFAM; SSF81333; SSF81333; 1.
DR PROSITE; PS00605; ATPASE_C; 1.
PE 2: Evidence at transcript level;
KW Complete proteome {ECO:0000313|Proteomes:UP000000437};
KW Hydrogen ion transport {ECO:0000256|RuleBase:RU004221};
KW Ion transport {ECO:0000256|RuleBase:RU004221};
KW Lipid-binding {ECO:0000256|RuleBase:RU004221};
KW Membrane {ECO:0000256|RuleBase:RU004221};
KW Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW Transmembrane {ECO:0000256|RuleBase:RU004221};
KW Transmembrane helix {ECO:0000256|RuleBase:RU004221};
KW Transport {ECO:0000256|RuleBase:RU004221}.
FT TRANSMEM 72 98 Helical. {ECO:0000256|RuleBase:RU004221}.
FT TRANSMEM 110 138 Helical. {ECO:0000256|RuleBase:RU004221}.
FT DOMAIN 73 135 ATP-synt_C. {ECO:0000259|Pfam:PF00137}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 73 135 ipfam:ATP-synt_C [T]
FT MYHIT 68 136 ihamap:ATP_synth_c_bact [T]
FT MYHIT 101 122 ipat:ATPASE_C [T]
SQ SEQUENCE 139 AA; 14373 MW; D7C8B981DE10AE58 CRC64;
MFTCAKFVST PALVRAGSRS VYRPVSAAVL SRPEAKPEVS TAAILQSPVA QMALRSFQTS
AVSRDIDTAA KFIGAGAATV GVAGSGAGIG TVFGSLIIGY ARNPSLKQQL FSYAILGFAL
SEAMGLFCLM VAFLILFAM
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