NB5R2_DANRE
ID NB5R2_DANRE Reviewed; 309 AA.
AC Q0P487; A2CET6;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=NADH-cytochrome b5 reductase 2;
DE Short=b5R.2;
DE EC=1.6.2.2;
GN Name=cyb5r2; ORFNames=si:dkey-80c24.9, zgc:153291;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
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., 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., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., 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., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB; TISSUE=Skin;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: NADH-cytochrome b5 reductases are involved in desaturation
CC and elongation of fatty acids, cholesterol biosynthesis and drug
CC metabolism. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(III)-[cytochrome b5] + NADH = 2 Fe(II)-[cytochrome b5] +
CC H(+) + NAD(+); Xref=Rhea:RHEA:46680, Rhea:RHEA-COMP:10438, Rhea:RHEA-
CC COMP:10439, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.6.2.2;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the flavoprotein pyridine nucleotide cytochrome
CC reductase family. {ECO:0000305}.
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DR EMBL; CR759887; CAM16402.1; -; Genomic_DNA.
DR EMBL; BC122221; AAI22222.1; -; mRNA.
DR RefSeq; NP_001038825.1; NM_001045360.1.
DR AlphaFoldDB; Q0P487; -.
DR SMR; Q0P487; -.
DR STRING; 7955.ENSDARP00000084821; -.
DR PaxDb; Q0P487; -.
DR Ensembl; ENSDART00000090388; ENSDARP00000084821; ENSDARG00000051925.
DR GeneID; 751641; -.
DR KEGG; dre:751641; -.
DR CTD; 51700; -.
DR ZFIN; ZDB-GENE-060825-83; cyb5r2.
DR eggNOG; KOG0534; Eukaryota.
DR GeneTree; ENSGT00940000153962; -.
DR HOGENOM; CLU_003827_9_2_1; -.
DR InParanoid; Q0P487; -.
DR OMA; NKHDHIA; -.
DR OrthoDB; 1311668at2759; -.
DR PhylomeDB; Q0P487; -.
DR TreeFam; TF314333; -.
DR Reactome; R-DRE-1237044; Erythrocytes take up carbon dioxide and release oxygen.
DR PRO; PR:Q0P487; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 25.
DR Bgee; ENSDARG00000051925; Expressed in intestine and 15 other tissues.
DR ExpressionAtlas; Q0P487; baseline.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004128; F:cytochrome-b5 reductase activity, acting on NAD(P)H; IEA:UniProtKB-EC.
DR GO; GO:0071949; F:FAD binding; IBA:GO_Central.
DR GO; GO:0001878; P:response to yeast; IDA:ZFIN.
DR GO; GO:0016126; P:sterol biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR001834; CBR-like.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR19370; PTHR19370; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 2: Evidence at transcript level;
KW FAD; Flavoprotein; Lipid biosynthesis; Lipid metabolism; Membrane; NAD;
KW Oxidoreductase; Reference proteome; Steroid biosynthesis;
KW Steroid metabolism; Sterol biosynthesis; Sterol metabolism; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..309
FT /note="NADH-cytochrome b5 reductase 2"
FT /id="PRO_0000287552"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 48..160
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 140..170
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 179..214
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT CONFLICT 199
FT /note="I -> V (in Ref. 2; AAI22222)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="F -> S (in Ref. 2; AAI22222)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 309 AA; 34388 MW; 9EE4889EE66784F9 CRC64;
MDILTAPVLI GVSIVVITVL YLFLKPAGSN STPPKPQNKI PKALQDPSVK YPLPLIEKEE
INHDTKRFRF GLPSSSHVLG LPIGQHIYLS AKVNGSLVVR AYTPVSSDQD QGYVDLVVKV
YYKNTHPSYP DGGKMSQYLD NMKIGDTIDF RGPNGLLVYN GKGKFAIRPD KKSEAEVRKF
KHVAMIAGGT GITPMLQLIR SITADSFDET VCSLIFANQT EKDILLRNEL DEVHRNHPSK
LKLWYTLDRP SEGWKYSEGF VNAAMMKDHL PPADSDVLVV MCGPPAMIEK ACLPNLLKLG
YKKENIFAY
