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Entry: P00171
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Original site: P00171 
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   26-NOV-2014, entry version 141.
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.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. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 cytochrome b5 heme-binding domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00279}.
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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   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=8-89.
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   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; EOG78H3W2; -.
DR   TreeFam; TF314537; -.
DR   Reactome; REACT_223568; Vitamin C (ascorbate) metabolism.
DR   EvolutionaryTrace; P00171; -.
DR   NextBio; 20805181; -.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR   GO; GO:0070062; C:extracellular vesicular exosome; IEA:Ensembl.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation-reduction process; 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; 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; 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. {ECO:0000269|PubMed:2752049,
FT                                ECO:0000269|PubMed:4030743,
FT                                ECO:0000269|PubMed:4810060}.
FT   CHAIN         2    134       Cytochrome b5.
FT                                /FTId=PRO_0000166008.
FT   TRANSMEM    109    131       Helical. {ECO:0000255}.
FT   DOMAIN        9     85       Cytochrome b5 heme-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00279}.
FT   METAL        44     44       Iron (heme axial ligand).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00279,
FT                                ECO:0000269|PubMed:15299727}.
FT   METAL        68     68       Iron (heme axial ligand).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00279,
FT                                ECO:0000269|PubMed:15299727}.
FT   MOD_RES       2      2       N-acetylalanine.
FT                                {ECO:0000269|PubMed:2752049,
FT                                ECO:0000269|PubMed:4030743}.
FT   MOD_RES       7      7       N6-acetyllysine. {ECO:0000250}.
FT   MOD_RES      10     10       N6-acetyllysine. {ECO:0000250}.
FT   MOD_RES      19     19       N6-acetyllysine. {ECO:0000250}.
FT   CONFLICT      2      5       AEES -> ZSZZBA (in Ref. 5; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     16     18       EIQ -> QIE (in Ref. 7; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     18     18       Q -> E (in Ref. 8; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     62     62       N -> D (in Ref. 7; AA sequence and 8; AA
FT                                sequence). {ECO:0000305}.
FT   CONFLICT    134    134       N -> D (in Ref. 5; AA sequence).
FT                                {ECO:0000305}.
FT   STRAND        9     12       {ECO:0000244|PDB:1U9M}.
FT   HELIX        14     17       {ECO:0000244|PDB:1CYO}.
FT   STRAND       21     24       {ECO:0000244|PDB:1M20}.
FT   STRAND       25     30       {ECO:0000244|PDB:1CYO}.
FT   STRAND       33     36       {ECO:0000244|PDB:1CYO}.
FT   TURN         38     43       {ECO:0000244|PDB:1CYO}.
FT   HELIX        49     54       {ECO:0000244|PDB:1CYO}.
FT   STRAND       56     58       {ECO:0000244|PDB:1HKO}.
FT   HELIX        60     65       {ECO:0000244|PDB:1CYO}.
FT   HELIX        70     76       {ECO:0000244|PDB:1CYO}.
FT   TURN         77     79       {ECO:0000244|PDB:1CYO}.
FT   STRAND       80     84       {ECO:0000244|PDB:1CYO}.
FT   HELIX        86     91       {ECO:0000244|PDB:1CYO}.
SQ   SEQUENCE   134 AA;  15329 MW;  7B7B605158D97525 CRC64;
     MAEESSKAVK YYTLEEIQKH NNSKSTWLIL HYKVYDLTKF LEEHPGGEEV LREQAGGDAT
     ENFEDVGHST DARELSKTFI IGELHPDDRS KITKPSESII TTIDSNPSWW TNWLIPAISA
     LFVALIYHLY TSEN
//
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