CYB5_BOVIN
ID CYB5_BOVIN Reviewed; 134 AA.
AC P00171; Q27947; Q28837; Q32PH5;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Cytochrome b5;
GN Name=CYB5A; Synonyms=CYB5;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2915932; DOI=10.1093/nar/17.2.799;
RA Cristiano R.J., Steggles A.W.;
RT "The complete nucleotide sequence of bovine liver cytochrome b5 mRNA.";
RL Nucleic Acids Res. 17:799-799(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
RX PubMed=8406485; DOI=10.1006/geno.1993.1331;
RA Cristiano R.J., Giordano S.J., Steggles A.W.;
RT "The isolation and characterization of the bovine cytochrome b5 gene, and a
RT transcribed pseudogene.";
RL Genomics 17:348-354(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 2-98, AND ACETYLATION AT ALA-2.
RC TISSUE=Erythrocyte;
RX PubMed=4030743; DOI=10.1093/oxfordjournals.jbchem.a135224;
RA Abe K., Kimura S., Kizawa R., Anan F.K., Sugita Y.;
RT "Amino acid sequences of cytochrome b5 from human, porcine, and bovine
RT erythrocytes and comparison with liver microsomal cytochrome b5.";
RL J. Biochem. 97:1659-1668(1985).
RN [5]
RP PROTEIN SEQUENCE OF 2-11 AND 131-134.
RX PubMed=4810060; DOI=10.1021/bi00700a005;
RA Ozols J.;
RT "Cytochrome b5 from microsomal membranes of equine, bovine, and porcine
RT livers. Isolation and properties of preparations containing the membranous
RT segment.";
RL Biochemistry 13:426-434(1974).
RN [6]
RP PROTEIN SEQUENCE OF 2-6 AND 15-18, AND ACETYLATION AT ALA-2.
RX PubMed=2752049; DOI=10.1016/0167-4838(89)90143-x;
RA Ozols J.;
RT "Structure of cytochrome b5 and its topology in the microsomal membrane.";
RL Biochim. Biophys. Acta 997:121-130(1989).
RN [7]
RP PROTEIN SEQUENCE OF 6-98.
RX PubMed=5391285; DOI=10.1016/s0021-9258(18)63450-7;
RA Ozols J., Strittmatter P.;
RT "Correction of the amino acid sequence of calf liver microsomal cytochrome
RT b5.";
RL J. Biol. Chem. 244:6617-6618(1969).
RN [8]
RP PROTEIN SEQUENCE OF 6-96.
RX PubMed=5272324; DOI=10.1073/pnas.67.1.442;
RA Tsugita A., Kobayashi M., Tani S., Kyo S., Rashid M.A., Yoshida Y.,
RA Kajihara T., Hagihara B.;
RT "Comparative study of the primary structures of cytochrome b5 from four
RT species.";
RL Proc. Natl. Acad. Sci. U.S.A. 67:442-447(1970).
RN [9]
RP PROTEIN SEQUENCE OF 92-134.
RX PubMed=670203; DOI=10.1016/s0021-9258(17)30380-0;
RA Fleming P.J., Dailey H.A., Corcoran D., Strittmatter P.;
RT "The primary structure of the nonpolar segment of bovine cytochrome b5.";
RL J. Biol. Chem. 253:5369-5372(1978).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF OXIDIZED FORM.
RA Mathews F.S., Argos P., Levine M.;
RT "The structure of cytochrome b-5 at 2.0-A resolution.";
RL Cold Spring Harb. Symp. Quant. Biol. 37:387-395(1971).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF REDUCED FORM.
RX PubMed=1167544; DOI=10.1016/s0021-9258(19)41959-5;
RA Argos P., Mathews F.S.;
RT "The structure of ferrocytochrome b5 at 2.8-A resolution.";
RL J. Biol. Chem. 250:747-751(1975).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
RX PubMed=15299727; DOI=10.1107/s0907444995007827;
RA Durley R.C.E., Mathews F.S.;
RT "Refinement and structural analysis of bovine cytochrome b5 at 1.5-A
RT resolution.";
RL Acta Crystallogr. D 52:65-76(1996).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 8-89, AND MUTAGENESIS.
RX PubMed=10842340;
RX DOI=10.1002/(sici)1097-0134(20000801)40:2<249::aid-prot70>3.0.co;2-h;
RA Wu J., Gan J.-H., Xia Z.-X., Wang Y.-H., Wang W.-H., Xue L.-L., Xie Y.,
RA Huang Z.-X.;
RT "Crystal structure of recombinant trypsin-solubilized fragment of
RT cytochrome b5 and the structural comparison with Val61His mutant.";
RL Proteins 40:249-257(2000).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 8-89, AND MUTAGENESIS.
RX PubMed=12136141; DOI=10.1107/s0907444902010016;
RA Gan J.-H., Wu J., Wang Z.-Q., Wang Y.-H., Huang Z.-X., Xia Z.-X.;
RT "Structures of V45E and V45Y mutants and structure comparison of a variety
RT of cytochrome b5 mutants.";
RL Acta Crystallogr. D 58:1298-1306(2002).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 8-89, CIRCULAR DICHROISM ANALYSIS,
RP AND MUTAGENESIS.
RX PubMed=12199707; DOI=10.1046/j.1432-1033.2002.03120.x;
RA Yao P., Wu J., Wang Y.-H., Sun B.-Y., Xia Z.-X., Huang Z.-X.;
RT "X-ray crystallography, CD and kinetic studies revealed the essence of the
RT abnormal behaviors of the cytochrome b5 Phe35->Tyr mutant.";
RL Eur. J. Biochem. 269:4287-4296(2002).
RN [16]
RP STRUCTURE BY NMR.
RX PubMed=8613986; DOI=10.1006/jmbi.1996.0241;
RA Muskett F.W., Kelly G.P., Whitford D.;
RT "The solution structure of bovine ferricytochrome b5 determined using
RT heteronuclear NMR methods.";
RL J. Mol. Biol. 258:172-189(1996).
RN [17]
RP STRUCTURE BY NMR OF 8-89, AND MUTAGENESIS.
RX PubMed=11248680; DOI=10.1046/j.1432-1033.2001.02033.x;
RA Wu Y., Wang Y., Qian C., Lu J., Li E., Wang W., Lu J., Xie Y., Wang J.,
RA Zhu D., Huang Z., Tang W.;
RT "Solution structure of cytochrome b5 mutant (E44/48/56A/D60A) and its
RT interaction with cytochrome c.";
RL Eur. J. Biochem. 268:1620-1630(2001).
RN [18]
RP STRUCTURE BY NMR OF 8-89, AND MUTAGENESIS.
RX PubMed=11714912; DOI=10.1110/ps.12401;
RA Qian C., Yao Y., Ye K., Wang J., Tang W., Wang Y., Wang W., Lu J., Xie Y.,
RA Huang Z.;
RT "Effects of charged amino-acid mutation on the solution structure of
RT cytochrome b5 and binding between cytochrome b5 and cytochrome c.";
RL Protein Sci. 10:2451-2459(2001).
RN [19]
RP STRUCTURE BY NMR OF 8-89, AND MUTAGENESIS.
RX PubMed=12893266; DOI=10.1016/s0006-291x(03)01225-7;
RA Cao C., Zhang Q., Xue L.-L., Ma J., Wang Y.-H., Wu H., Huang Z.-X.;
RT "The solution structure of the oxidized bovine microsomal cytochrome b5
RT mutant V61H.";
RL Biochem. Biophys. Res. Commun. 307:600-609(2003).
CC -!- FUNCTION: Cytochrome b5 is a membrane-bound hemoprotein functioning as
CC an electron carrier for several membrane-bound oxygenases.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC membrane protein; Cytoplasmic side. Microsome membrane; Single-pass
CC membrane protein; Cytoplasmic side.
CC -!- SIMILARITY: Belongs to the cytochrome b5 family. {ECO:0000305}.
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DR EMBL; X13617; CAA31949.1; -; mRNA.
DR EMBL; M63328; AAC14455.1; ALT_SEQ; Genomic_DNA.
DR EMBL; M63326; AAC14455.1; JOINED; Genomic_DNA.
DR EMBL; M63327; AAC14455.1; JOINED; Genomic_DNA.
DR EMBL; L22966; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC108113; AAI08114.1; -; mRNA.
DR PIR; A47215; CBBO5.
DR RefSeq; NP_776458.1; NM_174033.3.
DR PDB; 1CYO; X-ray; 1.50 A; A=6-98.
DR PDB; 1EHB; X-ray; 1.90 A; A=8-89.
DR PDB; 1ES1; X-ray; 2.10 A; A=8-89.
DR PDB; 1F03; NMR; -; A=8-89.
DR PDB; 1F04; NMR; -; A=8-89.
DR PDB; 1HKO; NMR; -; A=2-105.
DR PDB; 1I5U; NMR; -; A=8-89.
DR PDB; 1J0Q; NMR; -; A=8-89.
DR PDB; 1LQX; X-ray; 1.80 A; A=8-89.
DR PDB; 1LR6; X-ray; 1.90 A; A=8-89.
DR PDB; 1M20; X-ray; 1.80 A; A=8-89.
DR PDB; 1M2I; X-ray; 1.80 A; A=8-89.
DR PDB; 1M2M; X-ray; 1.80 A; A=8-89.
DR PDB; 1M59; X-ray; 1.90 A; A=8-89.
DR PDB; 1NX7; NMR; -; A=8-89.
DR PDB; 1SH4; NMR; -; A=8-89.
DR PDB; 1U9M; X-ray; 2.00 A; A/B/C/D/E/F=8-89.
DR PDB; 1U9U; X-ray; 1.86 A; A=8-89.
DR PDB; 3OZZ; X-ray; 1.70 A; B=8-89.
DR PDB; 4HIN; X-ray; 2.40 A; A/B/C/D=8-89.
DR PDBsum; 1CYO; -.
DR PDBsum; 1EHB; -.
DR PDBsum; 1ES1; -.
DR PDBsum; 1F03; -.
DR PDBsum; 1F04; -.
DR PDBsum; 1HKO; -.
DR PDBsum; 1I5U; -.
DR PDBsum; 1J0Q; -.
DR PDBsum; 1LQX; -.
DR PDBsum; 1LR6; -.
DR PDBsum; 1M20; -.
DR PDBsum; 1M2I; -.
DR PDBsum; 1M2M; -.
DR PDBsum; 1M59; -.
DR PDBsum; 1NX7; -.
DR PDBsum; 1SH4; -.
DR PDBsum; 1U9M; -.
DR PDBsum; 1U9U; -.
DR PDBsum; 3OZZ; -.
DR PDBsum; 4HIN; -.
DR AlphaFoldDB; P00171; -.
DR BMRB; P00171; -.
DR SMR; P00171; -.
DR STRING; 9913.ENSBTAP00000015944; -.
DR iPTMnet; P00171; -.
DR PaxDb; P00171; -.
DR PeptideAtlas; P00171; -.
DR PRIDE; P00171; -.
DR Ensembl; ENSBTAT00000072295; ENSBTAP00000067864; ENSBTAG00000012012.
DR GeneID; 281110; -.
DR KEGG; bta:281110; -.
DR CTD; 1528; -.
DR VEuPathDB; HostDB:ENSBTAG00000012012; -.
DR VGNC; VGNC:50260; CYB5A.
DR eggNOG; KOG0537; Eukaryota.
DR GeneTree; ENSGT00940000156770; -.
DR HOGENOM; CLU_102602_3_3_1; -.
DR InParanoid; P00171; -.
DR OMA; YRFYFTQ; -.
DR OrthoDB; 1566561at2759; -.
DR TreeFam; TF314537; -.
DR SABIO-RK; P00171; -.
DR EvolutionaryTrace; P00171; -.
DR Proteomes; UP000009136; Chromosome 24.
DR Bgee; ENSBTAG00000012012; Expressed in liver and 103 other tissues.
DR ExpressionAtlas; P00171; baseline and differential.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2752049,
FT ECO:0000269|PubMed:4030743, ECO:0000269|PubMed:4810060"
FT CHAIN 2..134
FT /note="Cytochrome b5"
FT /id="PRO_0000166008"
FT TRANSMEM 109..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 9..85
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT BINDING 44
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 ECO:0000269|PubMed:15299727"
FT BINDING 68
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 ECO:0000269|PubMed:15299727"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:2752049,
FT ECO:0000269|PubMed:4030743"
FT MOD_RES 7
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P56395"
FT MOD_RES 10
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P56395"
FT MOD_RES 19
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P56395"
FT CONFLICT 2..5
FT /note="AEES -> ZSZZBA (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 16..18
FT /note="EIQ -> QIE (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 18
FT /note="Q -> E (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 62
FT /note="N -> D (in Ref. 7; AA sequence and 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="N -> D (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 9..12
FT /evidence="ECO:0007829|PDB:1U9M"
FT HELIX 14..17
FT /evidence="ECO:0007829|PDB:1CYO"
FT STRAND 21..24
FT /evidence="ECO:0007829|PDB:1M20"
FT STRAND 25..30
FT /evidence="ECO:0007829|PDB:1CYO"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:1CYO"
FT TURN 38..43
FT /evidence="ECO:0007829|PDB:1CYO"
FT HELIX 49..54
FT /evidence="ECO:0007829|PDB:1CYO"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:1HKO"
FT HELIX 60..65
FT /evidence="ECO:0007829|PDB:1CYO"
FT HELIX 70..76
FT /evidence="ECO:0007829|PDB:1CYO"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:1CYO"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:1CYO"
FT HELIX 86..91
FT /evidence="ECO:0007829|PDB:1CYO"
SQ SEQUENCE 134 AA; 15329 MW; 7B7B605158D97525 CRC64;
MAEESSKAVK YYTLEEIQKH NNSKSTWLIL HYKVYDLTKF LEEHPGGEEV LREQAGGDAT
ENFEDVGHST DARELSKTFI IGELHPDDRS KITKPSESII TTIDSNPSWW TNWLIPAISA
LFVALIYHLY TSEN
