CYB5_ALOSE
ID CYB5_ALOSE Reviewed; 87 AA.
AC P00168;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Cytochrome b5;
DE Flags: Fragment;
GN Name=CYB5A; Synonyms=CYB5;
OS Alouatta seniculus (Red howler monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Atelidae;
OC Alouattinae; Alouatta.
OX NCBI_TaxID=9503;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=4993957; DOI=10.1016/s0021-9258(18)62368-3;
RA Nobrega F.G., Ozols J.;
RT "Amino acid sequences of tryptic peptides of cytochromes b5 from microsomes
RT of human, monkey, porcine, and chicken liver.";
RL J. Biol. Chem. 246:1706-1717(1971).
RN [2]
RP SEQUENCE REVISION TO 11; 14; 85 AND 87.
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 {ECO:0000250};
CC Single-pass membrane protein {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}. Microsome membrane {ECO:0000250}; Single-pass membrane
CC protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cytochrome b5 family. {ECO:0000305}.
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DR PIR; S07959; S07959.
DR AlphaFoldDB; P00168; -.
DR SMR; P00168; -.
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: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 Acetylation; Direct protein sequencing; Electron transport;
KW Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW Transmembrane; Transport.
FT CHAIN 1..>87
FT /note="Cytochrome b5"
FT /id="PRO_0000166007"
FT DOMAIN 5..81
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT BINDING 40
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 64
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 6
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P56395"
FT MOD_RES 15
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P56395"
FT CONFLICT 11..14
FT /note="EEIQ -> QEIE (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 85..87
FT /note="RPK -> KPR (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT NON_TER 87
SQ SEQUENCE 87 AA; 10032 MW; 5B3552315D1A0F5C CRC64;
SDEAVKYYTL EEIQKHNHSK STWLILHHKV YDLTKFLEEH PGGEEVLREQ AGGDATEDFE
DVGHSTDARE LSKTYIIGEL HPDDRPK