CYB5_HORSE
ID CYB5_HORSE Reviewed; 134 AA.
AC P00170;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Cytochrome b5;
GN Name=CYB5A; Synonyms=CYB5;
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP PROTEIN SEQUENCE OF 2-99.
RX PubMed=977596; DOI=10.1016/s0021-9258(17)33011-9;
RA Ozols J., Gerard C., Nobrega F.G.;
RT "Proteolytic cleavage of horse liver cytochrome b5. Primary structure of
RT the heme-containing moiety.";
RL J. Biol. Chem. 251:6767-6774(1976).
RN [2]
RP PROTEIN SEQUENCE OF 90-134.
RX PubMed=562879; DOI=10.1016/s0021-9258(19)75255-7;
RA Ozols J., Gerard C.;
RT "Covalent structure of the membranous segment of horse cytochrome b5.
RT Chemical cleavage of the native hemoprotein.";
RL J. Biol. Chem. 252:8549-8553(1977).
RN [3]
RP PROTEIN SEQUENCE OF 2-11.
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).
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 PIR; S07964; CBHO5.
DR AlphaFoldDB; P00170; -.
DR SMR; P00170; -.
DR PeptideAtlas; P00170; -.
DR InParanoid; P00170; -.
DR Proteomes; UP000002281; Unplaced.
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: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 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:0000250|UniProtKB:P00171,
FT ECO:0000269|PubMed:2752049, ECO:0000269|PubMed:977596"
FT CHAIN 2..134
FT /note="Cytochrome b5"
FT /id="PRO_0000166009"
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:0000250|UniProtKB:P00171"
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..6
FT /note="AEQSD -> ZEDAS (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 134 AA; 15271 MW; 1CE50847E1F68B21 CRC64;
MAEQSDKAVK YYTLEEIKKH NHSKSTWLIL HHKVYDLTKF LEDHPGGEEV LREQAGGDAT
ENFEDIGHST DARELSKTFI IGELHPDDRS KIAKPVETLI TTVDSNSSWW TNWVIPAISA
VVVALMYRIY TAED
