GenomeNet

Database: UniProt
Entry: Q7ZV76_DANRE
LinkDB: Q7ZV76_DANRE
Original site: Q7ZV76_DANRE 
ID   Q7ZV76_DANRE            Unreviewed;       254 AA.
AC   Q7ZV76;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 115.
DE   RecName: Full=Electron transfer flavoprotein subunit beta {ECO:0000256|ARBA:ARBA00016797, ECO:0000256|PIRNR:PIRNR000090};
DE            Short=Beta-ETF {ECO:0000256|PIRNR:PIRNR000090};
GN   Name=etfb {ECO:0000313|EMBL:AAH45971.1,
GN   ECO:0000313|ZFIN:ZDB-GENE-040426-1931};
GN   Synonyms=wu:fa96b05 {ECO:0000313|RefSeq:NP_998163.1}, wu:fb02d07
GN   {ECO:0000313|RefSeq:NP_998163.1}, wu:fb18b10
GN   {ECO:0000313|RefSeq:NP_998163.1}, zgc:56177
GN   {ECO:0000313|RefSeq:NP_998163.1};
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955 {ECO:0000313|EMBL:AAH45971.1};
RN   [1] {ECO:0000313|EMBL:AAH45971.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=PCR rescue {ECO:0000313|EMBL:AAI64332.1}, and Whole body
RC   {ECO:0000313|EMBL:AAH45971.1};
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|RefSeq:NP_998163.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=16109975;
RA   Woods I.G., Wilson C., Friedlander B., Chang P., Reyes D.K., Nix R.,
RA   Kelly P.D., Chu F., Postlethwait J.H., Talbot W.S.;
RT   "The zebrafish gene map defines ancestral vertebrate chromosomes.";
RL   Genome Res. 15:1307-1314(2005).
RN   [3] {ECO:0000313|Proteomes:UP000000437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23594743; DOI=10.1038/nature12111;
RG   Genome Reference Consortium Zebrafish;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., 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., Eliott D.,
RA   Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA   Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA   Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA   Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA   Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA   Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA   Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA   Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA   Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA   Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA   Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA   Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA   Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA   Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA   Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA   Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA   Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA   Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA   Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA   Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA   Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA   Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [4] {ECO:0000313|RefSeq:NP_998163.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=26469318;
RA   Elkon R., Milon B., Morrison L., Shah M., Vijayakumar S., Racherla M.,
RA   Leitch C.C., Silipino L., Hadi S., Weiss-Gayet M., Barras E., Schmid C.D.,
RA   Ait-Lounis A., Barnes A., Song Y., Eisenman D.J., Eliyahu E.,
RA   Frolenkov G.I., Strome S.E., Durand B., Zaghloul N.A., Jones S.M.,
RA   Reith W., Hertzano R.;
RT   "RFX transcription factors are essential for hearing in mice.";
RL   Nat. Commun. 6:8549-8549(2015).
RN   [5] {ECO:0000313|RefSeq:NP_998163.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=28252024;
RA   Bayes A., Collins M.O., Reig-Viader R., Gou G., Goulding D., Izquierdo A.,
RA   Choudhary J.S., Emes R.D., Grant S.G.;
RT   "Evolution of complexity in the zebrafish synapse proteome.";
RL   Nat. Commun. 8:14613-14613(2017).
RN   [6] {ECO:0000313|RefSeq:NP_998163.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: The electron transfer flavoprotein serves as a specific
CC       electron acceptor for several dehydrogenases, including five acyl-CoA
CC       dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase. It transfers
CC       the electrons to the main mitochondrial respiratory chain via ETF-
CC       ubiquinone oxidoreductase (ETF dehydrogenase).
CC       {ECO:0000256|PIRNR:PIRNR000090}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit.
CC       {ECO:0000256|PIRNR:PIRNR000090}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000256|PIRNR:PIRNR000090}.
CC   -!- SIMILARITY: Belongs to the ETF beta-subunit/FixA family.
CC       {ECO:0000256|ARBA:ARBA00007557, ECO:0000256|PIRNR:PIRNR000090}.
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DR   EMBL; BC045971; AAH45971.1; -; mRNA.
DR   EMBL; BC164332; AAI64332.1; -; mRNA.
DR   RefSeq; NP_998163.1; NM_212998.2.
DR   GeneID; 406271; -.
DR   KEGG; dre:406271; -.
DR   AGR; ZFIN:ZDB-GENE-040426-1931; -.
DR   CTD; 2109; -.
DR   ZFIN; ZDB-GENE-040426-1931; etfb.
DR   OrthoDB; 5476365at2759; -.
DR   Proteomes; UP000000437; Chromosome 16.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
DR   GO; GO:0009063; P:amino acid catabolic process; IBA:GO_Central.
DR   GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IBA:GO_Central.
DR   CDD; cd01714; ETF_beta; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   InterPro; IPR000049; ET-Flavoprotein_bsu_CS.
DR   InterPro; IPR014730; ETF_a/b_N.
DR   InterPro; IPR012255; ETF_b.
DR   InterPro; IPR033948; ETF_beta_N.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR21294; ELECTRON TRANSFER FLAVOPROTEIN BETA-SUBUNIT; 1.
DR   PANTHER; PTHR21294:SF8; ELECTRON TRANSFER FLAVOPROTEIN SUBUNIT BETA; 1.
DR   Pfam; PF01012; ETF; 1.
DR   PIRSF; PIRSF000090; Beta-ETF; 1.
DR   SMART; SM00893; ETF; 1.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR   PROSITE; PS01065; ETF_BETA; 1.
PE   1: Evidence at protein level;
KW   Electron transport {ECO:0000256|PIRNR:PIRNR000090};
KW   Mitochondrion {ECO:0000256|PIRNR:PIRNR000090};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:Q7ZV76};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW   Transport {ECO:0000256|PIRNR:PIRNR000090}.
FT   DOMAIN          25..217
FT                   /note="Electron transfer flavoprotein alpha/beta-subunit N-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00893"
SQ   SEQUENCE   254 AA;  27525 MW;  A7C0DAB23291E8CD CRC64;
     MSARVLVGVK RVIDYAVKIR VKPDHTGVVT DGVKHSMNPF CEIAVEEAVK LKEKKLIKEV
     VAVSCGPQQV QETIRTALAM GADRGIHVEV SGKDYETLGP LQVSKILAAL AKKEEASLII
     LGKQAIDDDC NQTGQMTAAL LDWPQGTFAS ELAFEADKLK VVREIDGGLE TIKIKLPAVV
     TADLRLNTPR YATLPNIMKA KKKKIAMVKP ADLGVDVSSR LEVLKVDEPP TRQAGVKVET
     VEDLVGKLKE AGRV
//
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