CYB5B_RAT
ID CYB5B_RAT Reviewed; 146 AA.
AC P04166; Q9QWG1;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Cytochrome b5 type B;
DE AltName: Full=Cytochrome b5 outer mitochondrial membrane isoform;
DE Flags: Precursor;
GN Name=Cyb5b; Synonyms=Cyb5m, Omb5;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kuroda R., Ikenoue T., Honsho M., Tujimoto S., Miroma J., Ito A.;
RT "Charged amino acids at the carboxy-terminal portions determine
RT intracellular locations of two isoforms of cytochrome b5.";
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 12-103, AND SUBCELLULAR LOCATION.
RX PubMed=6840088; DOI=10.1111/j.1432-1033.1983.tb07330.x;
RA Lederer F., Ghrir R., Guiard B., Cortial S., Ito A.;
RT "Two homologous cytochromes b5 in a single cell.";
RL Eur. J. Biochem. 132:95-102(1983).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RX PubMed=8973214; DOI=10.1021/bi961895o;
RA Rodriguez-Maranon M.J., Qiu F., Stark R.E., White S.P., Zhang X.,
RA Foundling S.I., Rodriguez V., Schilling C.L. III, Bunce R.A., Rivera M.;
RT "13C NMR spectroscopic and X-ray crystallographic study of the role played
RT by mitochondrial cytochrome b5 heme propionates in the electrostatic
RT binding to cytochrome c.";
RL Biochemistry 35:16378-16390(1996).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=9484218; DOI=10.1021/bi972390g;
RA Rivera M., Seetharaman R., Girdhar D., Wirtz M., Zhang X., Wang X.,
RA White S.;
RT "The reduction potential of cytochrome b5 is modulated by its exposed heme
RT edge.";
RL Biochemistry 37:1485-1494(1998).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 17-102.
RX PubMed=11197480; DOI=10.1039/b001520m;
RA Wirtz M., Oganesyan V., Zhang X., Studer J., Rivera M.;
RT "Modulation of redox potential in electron transfer proteins: effects of
RT complex formation on the active site microenvironment of cytochrome b5.";
RL Faraday Discuss. 116:221-234(2000).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 17-103.
RX PubMed=11583146; DOI=10.1021/bi010636i;
RA Altuve A., Silchenko S., Lee K.-H., Kuczera K., Terzyan S., Zhang X.,
RA Benson D.R., Rivera M.;
RT "Probing the differences between rat liver outer mitochondrial membrane
RT cytochrome b5 and microsomal cytochromes b5.";
RL Biochemistry 40:9469-9483(2001).
CC -!- FUNCTION: Cytochrome b5 is a membrane-bound hemoprotein functioning as
CC an electron carrier for several membrane-bound oxygenases.
CC -!- SUBUNIT: Component of a complex composed of cytochrome b5, NADH-
CC cytochrome b5 reductase (CYB5R3) and MTARC2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:6840088}.
CC -!- SIMILARITY: Belongs to the cytochrome b5 family. {ECO:0000305}.
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DR EMBL; Y12517; CAA73117.1; -; mRNA.
DR EMBL; BC072535; AAH72535.1; -; mRNA.
DR RefSeq; NP_085075.1; NM_030586.2.
DR PDB; 1AWP; X-ray; 2.00 A; A/B=13-103.
DR PDB; 1B5M; X-ray; 2.70 A; A=19-102.
DR PDB; 1EUE; X-ray; 1.80 A; A/B=17-102.
DR PDB; 1ICC; X-ray; 2.00 A; A/B/C/D=17-103.
DR PDB; 1LJ0; X-ray; 2.00 A; A/B/C/D=12-103.
DR PDB; 2I89; X-ray; 2.10 A; A/B/C/D=12-103.
DR PDB; 3MUS; X-ray; 2.00 A; A/B=17-102.
DR PDB; 4HIL; X-ray; 1.25 A; A/B=17-102.
DR PDBsum; 1AWP; -.
DR PDBsum; 1B5M; -.
DR PDBsum; 1EUE; -.
DR PDBsum; 1ICC; -.
DR PDBsum; 1LJ0; -.
DR PDBsum; 2I89; -.
DR PDBsum; 3MUS; -.
DR PDBsum; 4HIL; -.
DR AlphaFoldDB; P04166; -.
DR BMRB; P04166; -.
DR SMR; P04166; -.
DR STRING; 10116.ENSRNOP00000015006; -.
DR iPTMnet; P04166; -.
DR PhosphoSitePlus; P04166; -.
DR SwissPalm; P04166; -.
DR jPOST; P04166; -.
DR PaxDb; P04166; -.
DR PRIDE; P04166; -.
DR Ensembl; ENSRNOT00000099870; ENSRNOP00000093641; ENSRNOG00000011142.
DR GeneID; 80773; -.
DR KEGG; rno:80773; -.
DR UCSC; RGD:621551; rat.
DR CTD; 80777; -.
DR RGD; 621551; Cyb5b.
DR eggNOG; KOG0537; Eukaryota.
DR GeneTree; ENSGT00940000155584; -.
DR InParanoid; P04166; -.
DR OMA; KNNTCKS; -.
DR OrthoDB; 1566561at2759; -.
DR PhylomeDB; P04166; -.
DR TreeFam; TF314537; -.
DR Reactome; R-RNO-211945; Phase I - Functionalization of compounds.
DR EvolutionaryTrace; P04166; -.
DR PRO; PR:P04166; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Bgee; ENSRNOG00000011142; Expressed in duodenum and 20 other tissues.
DR Genevisible; P04166; RN.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
DR GO; GO:1903958; C:nitric-oxide synthase complex; ISO:RGD.
DR GO; GO:0008047; F:enzyme activator activity; IDA:RGD.
DR GO; GO:0020037; F:heme binding; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050421; F:nitrite reductase (NO-forming) activity; IEA:Ensembl.
DR GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; TAS:RGD.
DR GO; GO:0006809; P:nitric oxide biosynthetic process; ISO:RGD.
DR Gene3D; 3.10.120.10; -; 1.
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 Pfam; PF00173; Cyt-b5; 1.
DR PRINTS; PR00363; CYTOCHROMEB5.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF55856; SSF55856; 1.
DR PROSITE; PS00191; CYTOCHROME_B5_1; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Electron transport;
KW Heme; Iron; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion outer membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT PROPEP 1..11
FT /evidence="ECO:0000269|PubMed:6840088"
FT /id="PRO_0000006477"
FT CHAIN 12..146
FT /note="Cytochrome b5 type B"
FT /id="PRO_0000006478"
FT TRANSMEM 119..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 20..96
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT BINDING 55
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 BINDING 79
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 MOD_RES 30
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O43169"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CQX2"
FT CONFLICT 12
FT /note="N -> D (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 25..28
FT /evidence="ECO:0007829|PDB:4HIL"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:4HIL"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:4HIL"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:4HIL"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:4HIL"
FT HELIX 60..63
FT /evidence="ECO:0007829|PDB:4HIL"
FT TURN 64..67
FT /evidence="ECO:0007829|PDB:4HIL"
FT HELIX 71..77
FT /evidence="ECO:0007829|PDB:4HIL"
FT HELIX 81..85
FT /evidence="ECO:0007829|PDB:4HIL"
FT HELIX 86..89
FT /evidence="ECO:0007829|PDB:4HIL"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:4HIL"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:4HIL"
SQ SEQUENCE 146 AA; 16265 MW; 1CA90DD3C81C412E CRC64;
MATPEASGSG RNGQGSDPAV TYYRLEEVAK RNTAEETWMV IHGRVYDITR FLSEHPGGEE
VLLEQAGADA TESFEDVGHS PDAREMLKQY YIGDVHPNDL KPKDGDKDPS KNNSCQSSWA
YWIVPIVGAI LIGFLYRHFW ADSKSS
