NB5R4_DANRE
ID NB5R4_DANRE Reviewed; 527 AA.
AC Q502I6;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Cytochrome b5 reductase 4;
DE EC=1.6.2.2;
DE AltName: Full=Flavohemoprotein b5/b5R;
DE Short=b5+b5R;
DE AltName: Full=cb5/cb5R;
GN Name=cyb5r4; ORFNames=zgc:112177;
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 MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: NADH-cytochrome b5 reductase involved in endoplasmic
CC reticulum stress response pathway. {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: Endoplasmic reticulum. Note=Soluble protein.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the flavoprotein pyridine nucleotide cytochrome
CC reductase family. {ECO:0000305}.
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DR EMBL; BC095683; AAH95683.1; -; mRNA.
DR RefSeq; NP_001018496.1; NM_001020660.1.
DR AlphaFoldDB; Q502I6; -.
DR SMR; Q502I6; -.
DR STRING; 7955.ENSDARP00000003991; -.
DR PaxDb; Q502I6; -.
DR GeneID; 553685; -.
DR KEGG; dre:553685; -.
DR CTD; 51167; -.
DR ZFIN; ZDB-GENE-050522-225; cyb5r4.
DR eggNOG; KOG0534; Eukaryota.
DR eggNOG; KOG0536; Eukaryota.
DR InParanoid; Q502I6; -.
DR OrthoDB; 1311668at2759; -.
DR PhylomeDB; Q502I6; -.
DR Reactome; R-DRE-1237044; Erythrocytes take up carbon dioxide and release oxygen.
DR PRO; PR:Q502I6; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0004128; F:cytochrome-b5 reductase activity, acting on NAD(P)H; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006091; P:generation of precursor metabolites and energy; IBA:GO_Central.
DR GO; GO:0006801; P:superoxide metabolic process; IBA:GO_Central.
DR CDD; cd06490; p23_NCB5OR; 1.
DR Gene3D; 2.60.40.790; -; 1.
DR Gene3D; 3.10.120.10; -; 1.
DR Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR001834; CBR-like.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR007052; CS_dom.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR InterPro; IPR018506; Cyt_B5_heme-BS.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR037908; p23_NCB5OR.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR19370; PTHR19370; 1.
DR Pfam; PF00173; Cyt-b5; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00363; CYTOCHROMEB5.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF49764; SSF49764; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF55856; SSF55856; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS51203; CS; 1.
DR PROSITE; PS00191; CYTOCHROME_B5_1; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; FAD; Flavoprotein; Heme; Iron; Metal-binding; NAD;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..527
FT /note="Cytochrome b5 reductase 4"
FT /id="PRO_0000287559"
FT DOMAIN 56..132
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT DOMAIN 173..264
FT /note="CS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00547"
FT DOMAIN 281..392
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 138..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 91
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT BINDING 114
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT BINDING 372..387
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 399..431
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
SQ SEQUENCE 527 AA; 59452 MW; 0A58916CDCB39FD0 CRC64;
MLNVPSQAFP AAGSQQRVAP AGQSRNKVVL KPGHSLLDWI RLTKSGQDLT GLRGRLIEVT
EDELKKHNTK KDCWTCIRGM VYNLSAYMDF HPGGEEELMR AAGIDSTDLF DEVHRWVNYE
SMLKECLVGR MAVKPSPALQ AHTEKTESTH LNGLSAPPSL RPEPLSAPLP AKDHRPRYDW
FQTDGTVNIV VYTKRKIPSA GCAVVDLQDD NLRVEMLLGR MSYLLYWRLS SRVQDHVDVQ
TAHSVGKVQL CLRKSVKEKW TQLGQSLEHH DTFIQCKDRG LFYRECVLLS KTDVTHNTQL
LRLQLPRGSR MQVPVGRHVY LKTSVQGTDV VKPYTAVDQM LIPPSQSSAE VGSDIHLMIK
VYPDGVLTPH IANLPIGASL SVGGPEGSFT LRVLRDVTHL YMLAAGTGFT PMARLIRLAL
QDFTVIRKMK LMFFNRQERD ILWQSQLDEL CTKEERFEVQ HVLSEPADSW TGRRGRIDAC
MLQNFLERPE NSKCLVCVCG PAGFTESAVQ LVRQLDFSEE ELHVFQA
