CYB5_RABIT
ID CYB5_RABIT Reviewed; 134 AA.
AC P00169; Q28726;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Cytochrome b5;
GN Name=CYB5A; Synonyms=CYB5;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=3222252;
RA Dariush N., Fisher C.W., Steggles A.W.;
RT "The nucleotide sequence of rabbit liver cytochrome b5 mRNA.";
RL Protein Seq. Data Anal. 1:351-353(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=New Zealand white;
RX PubMed=1627141; DOI=10.1016/0006-291x(92)91704-t;
RA Takamatsu H., Kozutsumi Y., Suzuki A., Kawasaki T.;
RT "Molecular cloning of rabbit cytochrome b5 genes: evidence for the
RT occurrence of two separate genes encoding the soluble and microsomal
RT forms.";
RL Biochem. Biophys. Res. Commun. 185:845-851(1992).
RN [3]
RP PROTEIN SEQUENCE OF 9-46 AND 50-91.
RX PubMed=5709273; DOI=10.1093/oxfordjournals.jbchem.a128954;
RA Tsugita A., Kobayashi M., Kajihara T., Hagihara B.;
RT "Primary structure of rabbit liver cytochrome b5.";
RL J. Biochem. 64:727-730(1968).
RN [4]
RP PROTEIN SEQUENCE OF 7-8 AND 47-49.
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 [5]
RP PROTEIN SEQUENCE OF 5-98.
RX PubMed=5506260; DOI=10.1016/s0021-9258(18)62788-7;
RA Ozols J.;
RT "Amino acid sequence of rabbit liver microsomal cytochrome b5.";
RL J. Biol. Chem. 245:4863-4874(1970).
RN [6]
RP PROTEIN SEQUENCE OF 92-134.
RX PubMed=500581; DOI=10.1093/oxfordjournals.jbchem.a132606;
RA Kondo K., Tajima S., Sato R., Narita K.;
RT "Primary structure of the membrane-binding segment of rabbit cytochrome
RT b5.";
RL J. Biochem. 86:1119-1128(1979).
RN [7]
RP PROTEIN SEQUENCE OF 99-134.
RX PubMed=7354043; DOI=10.1016/s0021-9258(19)86065-9;
RA Takagaki Y., Gerber G.E., Nihei K., Khorana H.G.;
RT "Amino acid sequence of the membranous segment of rabbit liver cytochrome
RT b5. Methodology for separation of hydrophobic peptides.";
RL J. Biol. Chem. 255:1536-1541(1980).
RN [8]
RP PROTEIN SEQUENCE OF 2-11, 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 [9]
RP STRUCTURE BY NMR OF 7-100.
RX PubMed=10651812; DOI=10.1046/j.1432-1327.2000.01054.x;
RA Banci L., Bertini I., Rosato A., Scacchieri S.;
RT "Solution structure of oxidized microsomal rabbit cytochrome b5 factors
RT determining the heterogeneous binding of the heme.";
RL Eur. J. Biochem. 267:755-766(2000).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Liver, Membrane-bound;
CC IsoId=P00169-1; Sequence=Displayed;
CC Name=2; Synonyms=Erythrocyte, Cytoplasmic;
CC IsoId=P00169-2; Sequence=VSP_001244, VSP_001245;
CC -!- SIMILARITY: Belongs to the cytochrome b5 family. {ECO:0000305}.
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DR EMBL; M24844; AAB03878.1; -; mRNA.
DR EMBL; D10901; BAA01712.1; -; mRNA.
DR PIR; JN0316; JN0316.
DR PIR; S03373; CBRB5.
DR RefSeq; NP_001164734.1; NM_001171263.1. [P00169-2]
DR RefSeq; NP_001164735.1; NM_001171264.1. [P00169-1]
DR RefSeq; XP_017199148.1; XM_017343659.1. [P00169-1]
DR PDB; 1DO9; NMR; -; A=6-99.
DR PDB; 2M33; NMR; -; A=1-134.
DR PDBsum; 1DO9; -.
DR PDBsum; 2M33; -.
DR AlphaFoldDB; P00169; -.
DR BMRB; P00169; -.
DR SMR; P00169; -.
DR STRING; 9986.ENSOCUP00000013951; -.
DR iPTMnet; P00169; -.
DR Ensembl; ENSOCUT00000016229; ENSOCUP00000013951; ENSOCUG00000016235. [P00169-1]
DR Ensembl; ENSOCUT00000045010; ENSOCUP00000028877; ENSOCUG00000016235. [P00169-2]
DR GeneID; 100328912; -.
DR GeneID; 100328915; -.
DR KEGG; ocu:100328912; -.
DR KEGG; ocu:100328915; -.
DR eggNOG; KOG0537; Eukaryota.
DR GeneTree; ENSGT00940000156770; -.
DR HOGENOM; CLU_102602_3_3_1; -.
DR InParanoid; P00169; -.
DR OMA; YRFYFTQ; -.
DR OrthoDB; 1566561at2759; -.
DR TreeFam; TF314537; -.
DR EvolutionaryTrace; P00169; -.
DR Proteomes; UP000001811; Chromosome 9.
DR Bgee; ENSOCUG00000016235; Expressed in liver and 17 other tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
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; Alternative splicing; Direct protein sequencing;
KW Electron transport; Endoplasmic reticulum; Heme; Iron; Membrane;
KW Metal-binding; Microsome; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2752049"
FT CHAIN 2..134
FT /note="Cytochrome b5"
FT /id="PRO_0000166013"
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 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 MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:2752049"
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 VAR_SEQ 98
FT /note="T -> P (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1627141"
FT /id="VSP_001244"
FT VAR_SEQ 99..134
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1627141"
FT /id="VSP_001245"
FT CONFLICT 62
FT /note="N -> D (in Ref. 3; AA sequence and 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="D -> N (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:2M33"
FT HELIX 14..17
FT /evidence="ECO:0007829|PDB:1DO9"
FT TURN 18..20
FT /evidence="ECO:0007829|PDB:2M33"
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:2M33"
FT STRAND 27..36
FT /evidence="ECO:0007829|PDB:1DO9"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:1DO9"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:1DO9"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:1DO9"
FT HELIX 49..53
FT /evidence="ECO:0007829|PDB:1DO9"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:1DO9"
FT HELIX 60..66
FT /evidence="ECO:0007829|PDB:1DO9"
FT HELIX 70..79
FT /evidence="ECO:0007829|PDB:1DO9"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:1DO9"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:1DO9"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:1DO9"
SQ SEQUENCE 134 AA; 15349 MW; B748AE9D32FA5E46 CRC64;
MAAQSDKDVK YYTLEEIKKH NHSKSTWLIL HHKVYDLTKF LEEHPGGEEV LREQAGGDAT
ENFEDVGHST DARELSKTFI IGELHPDDRS KLSKPMETLI TTVDSNSSWW TNWVIPAISA
LIVALMYRLY MADD
