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-APR-2013, entry version 129.
DE RecName: Full=Cytochrome b5;
GN Name=CYB5A; Synonyms=CYB5;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC Pecora; Bovidae; 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
RT 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,
RT and a 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.
RC TISSUE=Erythrocyte;
RX PubMed=4030743;
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
RT porcine livers. Isolation and properties of preparations containing
RT the membranous segment.";
RL Biochemistry 13:426-434(1974).
RN [6]
RP PROTEIN SEQUENCE OF 2-6 AND 15-18.
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
RT membrane.";
RL Biochim. Biophys. Acta 997:121-130(1989).
RN [7]
RP PROTEIN SEQUENCE OF 6-98.
RX PubMed=5391285;
RA Ozols J., Strittmatter P.;
RT "Correction of the amino acid sequence of calf liver microsomal
RT cytochrome 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
RT four species.";
RL Proc. Natl. Acad. Sci. U.S.A. 67:442-447(1970).
RN [9]
RP PROTEIN SEQUENCE OF 92-134.
RX PubMed=670203;
RA Fleming P.J., Dailey H.A., Corcoran D., Strittmatter P.;
RT "The primary structure of the nonpolar segment of bovine cytochrome
RT 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;
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.,
RA Xie Y., 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
RT variety 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
RP ANALYSIS, 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
RT the 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.1432-1327.2001.02033.x;
RA Wu Y., Wang Y., Qian C., Lu J., Li E., Wang W., Lu J., Xie Y.,
RA Wang J., 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.ps.12401;
RA Qian C., Yao Y., Ye K., Wang J., Tang W., Wang Y., Wang W., Lu J.,
RA Xie Y., 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
RT b5 mutant V61H.";
RL Biochem. Biophys. Res. Commun. 307:600-609(2003).
CC -!- FUNCTION: Cytochrome b5 is a membrane bound hemoprotein which
CC function as an electron carrier for several membrane bound
CC oxygenases.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC membrane protein; Cytoplasmic side. Microsome membrane; Single-
CC pass membrane protein; Cytoplasmic side.
CC -!- SIMILARITY: Belongs to the cytochrome b5 family.
CC -!- SIMILARITY: Contains 1 cytochrome b5 heme-binding domain.
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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 IPI; IPI00714055; -.
DR PIR; A47215; CBBO5.
DR RefSeq; NP_776458.1; NM_174033.3.
DR UniGene; Bt.65097; -.
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=8-88.
DR PDB; 1SH4; NMR; -; A=8-88.
DR PDB; 1U9M; X-ray; 2.00 A; A/B/C/D/E/F=8-88.
DR PDB; 1U9U; X-ray; 1.86 A; A=8-88.
DR PDB; 3OZZ; X-ray; 1.70 A; B=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 ProteinModelPortal; P00171; -.
DR SMR; P00171; 2-105.
DR PaxDb; P00171; -.
DR PRIDE; P00171; -.
DR Ensembl; ENSBTAT00000015944; ENSBTAP00000015944; ENSBTAG00000012012.
DR GeneID; 281110; -.
DR KEGG; bta:281110; -.
DR CTD; 1528; -.
DR eggNOG; COG5274; -.
DR GeneTree; ENSGT00510000046507; -.
DR HOGENOM; HOG000039853; -.
DR HOVERGEN; HBG002653; -.
DR InParanoid; P00171; -.
DR OMA; MAEQSDK; -.
DR OrthoDB; EOG4S7JRC; -.
DR EvolutionaryTrace; P00171; -.
DR NextBio; 20805181; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; IEA:Compara.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR Gene3D; 3.10.120.10; -; 1.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR018506; Cyt_B5_heme-BS.
DR Pfam; PF00173; Cyt-b5; 1.
DR PRINTS; PR00363; CYTOCHROMEB5.
DR SUPFAM; SSF55856; Cyt_B5; 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; Complete proteome;
KW Direct protein sequencing; Electron transport; Endoplasmic reticulum;
KW Heme; Iron; Membrane; Metal-binding; Microsome; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 134 Cytochrome b5.
FT /FTId=PRO_0000166008.
FT TRANSMEM 109 131 Helical; (Potential).
FT DOMAIN 9 85 Cytochrome b5 heme-binding.
FT METAL 44 44 Iron (heme axial ligand).
FT METAL 68 68 Iron (heme axial ligand).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 19 19 N6-acetyllysine (By similarity).
FT CONFLICT 2 5 AEES -> ZSZZBA (in Ref. 5; AA sequence).
FT CONFLICT 16 18 EIQ -> QIE (in Ref. 7; AA sequence).
FT CONFLICT 18 18 Q -> E (in Ref. 8; AA sequence).
FT CONFLICT 62 62 N -> D (in Ref. 7; AA sequence and 8; AA
FT sequence).
FT CONFLICT 134 134 N -> D (in Ref. 5; AA sequence).
FT STRAND 9 12
FT HELIX 14 17
FT STRAND 21 24
FT STRAND 25 30
FT STRAND 33 36
FT TURN 38 43
FT HELIX 49 54
FT STRAND 56 58
FT HELIX 60 65
FT HELIX 70 76
FT TURN 77 79
FT STRAND 80 84
FT HELIX 86 91
SQ SEQUENCE 134 AA; 15329 MW; 7B7B605158D97525 CRC64;
MAEESSKAVK YYTLEEIQKH NNSKSTWLIL HYKVYDLTKF LEEHPGGEEV LREQAGGDAT
ENFEDVGHST DARELSKTFI IGELHPDDRS KITKPSESII TTIDSNPSWW TNWLIPAISA
LFVALIYHLY TSEN
//
