ID I3MY26_ICTTR Unreviewed; 510 AA.
AC I3MY26;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Cytochrome b5 reductase 4 {ECO:0000256|ARBA:ARBA00022339};
DE EC=1.6.2.2 {ECO:0000256|ARBA:ARBA00012011};
DE AltName: Full=Flavohemoprotein b5/b5R {ECO:0000256|ARBA:ARBA00031842};
DE AltName: Full=cb5/cb5R {ECO:0000256|ARBA:ARBA00030883};
GN Name=CYB5R4 {ECO:0000313|Ensembl:ENSSTOP00000017021.2};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000017021.2, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000017021.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 Evidence={ECO:0000256|ARBA:ARBA00029341};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000256|ARBA:ARBA00004240}.
CC -!- SIMILARITY: Belongs to the flavoprotein pyridine nucleotide cytochrome
CC reductase family. {ECO:0000256|ARBA:ARBA00006105}.
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DR EMBL; AGTP01036093; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01036094; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; I3MY26; -.
DR Ensembl; ENSSTOT00000025292.2; ENSSTOP00000017021.2; ENSSTOG00000009367.3.
DR GeneTree; ENSGT00940000155536; -.
DR TreeFam; TF313874; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0004128; F:cytochrome-b5 reductase activity, acting on NAD(P)H; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd06183; cyt_b5_reduct_like; 1.
DR CDD; cd06490; p23_NCB5OR; 1.
DR Gene3D; 2.60.40.790; -; 1.
DR Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
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; PTHR46237:SF1; CYTOCHROME B5 REDUCTASE 4; 1.
DR PANTHER; PTHR46237; CYTOCHROME B5 REDUCTASE 4 FAMILY MEMBER; 1.
DR Pfam; PF04969; CS; 1.
DR Pfam; PF00173; Cyt-b5; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00406; CYTB5RDTASE.
DR PRINTS; PR00363; CYTOCHROMEB5.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF49764; HSP20-like chaperones; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 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 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000005215}.
FT DOMAIN 54..130
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT DOMAIN 154..245
FT /note="CS"
FT /evidence="ECO:0000259|PROSITE:PS51203"
FT DOMAIN 262..374
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 510 AA; 57888 MW; E7A0DF72FEDEB733 CRC64;
MLNVPSQSFP APSSQQRVAS GGRSKVPLKQ GRSLMDWIRL SKSGKDLTGL KGRLIDVTEE
ELKKHNKKED CWICIRGFVY NVSSYMEFHP GGEDELMRAA GSDGTDLFDQ VHRWVNYESM
LKECLVGRMA VKPAIPKGLL PKSQMTDIST KGGPSSPSYD WFQTDSLVTL VIYTKQKDIH
LDSIIIDHQN DSFRAETIIK DYSYLIHIGL SHEVQEDFSV RVVENVGKIE IVLKKTENIS
WKCLGRPLEK HNSLIPKKDT GLYYRKCQLI SKEDVTHDTK LFCLMLPPST HLQVPIGQHV
YLKLTITGTE IVKPYTPVFD SLLSEFKEPV LPNNKYIYFL IKIYPAGLFT PELDHLQIGD
FVPVSNPEGN FKISKLQEVE DLFLLAAGTG FTPMVKILKY ALINIPSLRK VKLMFFNKTE
DAIIWRSQLE KLAFEDKRFD VEYVLSAPTS EWKGKQGHIS PALLSEFLNK SSEKSKVLLC
ICGPTPFTEQ GIKLLHDLNF SKDEIHSFTA
//
