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CYB5_CHICK
ID   CYB5_CHICK              Reviewed;         138 AA.
AC   P00174;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 4.
DT   03-AUG-2022, entry version 159.
DE   RecName: Full=Cytochrome b5;
GN   Name=CYB5A; Synonyms=CYB5;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2369133; DOI=10.1016/0003-9861(90)90350-8;
RA   Zhang H., Somerville C.;
RT   "Soluble and membrane-bound forms of cytochrome b5 are the products of a
RT   single gene in chicken.";
RL   Arch. Biochem. Biophys. 280:412-415(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3395128; DOI=10.1016/0003-9861(88)90603-0;
RA   Zhang H., Somerville C.;
RT   "The primary structure of chicken liver cytochrome b5 deduced from the DNA
RT   sequence of a cDNA clone.";
RL   Arch. Biochem. Biophys. 264:343-347(1988).
RN   [3]
RP   PROTEIN SEQUENCE OF 14-97.
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   [4]
RP   PROTEIN SEQUENCE OF 4-16 AND 89-138.
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   EMBL; M32293; AAA48740.1; -; mRNA.
DR   EMBL; M18539; AAA48733.1; -; mRNA.
DR   PIR; A28811; CBCH5.
DR   RefSeq; NP_001001748.1; NM_001001748.2.
DR   AlphaFoldDB; P00174; -.
DR   SMR; P00174; -.
DR   STRING; 9031.ENSGALP00000022250; -.
DR   PaxDb; P00174; -.
DR   Ensembl; ENSGALT00000022289; ENSGALP00000022250; ENSGALG00000013708.
DR   GeneID; 414798; -.
DR   KEGG; gga:414798; -.
DR   CTD; 1528; -.
DR   VEuPathDB; HostDB:geneid_414798; -.
DR   eggNOG; KOG0537; Eukaryota.
DR   GeneTree; ENSGT00940000156770; -.
DR   HOGENOM; CLU_102602_3_3_1; -.
DR   InParanoid; P00174; -.
DR   OMA; RHKIAKP; -.
DR   OrthoDB; 1566561at2759; -.
DR   PhylomeDB; P00174; -.
DR   TreeFam; TF314537; -.
DR   Reactome; R-GGA-196836; Vitamin C (ascorbate) metabolism.
DR   Reactome; R-GGA-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
DR   PRO; PR:P00174; -.
DR   Proteomes; UP000000539; Chromosome 2.
DR   Bgee; ENSGALG00000013708; Expressed in kidney and 14 other tissues.
DR   ExpressionAtlas; P00174; baseline and differential.
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   Direct protein sequencing; Electron transport; Endoplasmic reticulum; Heme;
KW   Iron; Membrane; Metal-binding; Microsome; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..138
FT                   /note="Cytochrome b5"
FT                   /id="PRO_0000166015"
FT   TRANSMEM        114..136
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          14..90
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT   BINDING         49
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         73
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   CONFLICT        12
FT                   /note="W -> E (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        27..29
FT                   /note="NSQ -> ZSB (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        67
FT                   /note="N -> D (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        124
FT                   /note="A -> T (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        138
FT                   /note="E -> EE (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   138 AA;  15545 MW;  168F0B87251557A8 CRC64;
     MVGSSEAGGE AWRGRYYRLE EVQKHNNSQS TWIIVHHRIY DITKFLDEHP GGEEVLREQA
     GGDATENFED VGHSTDARAL SETFIIGELH PDDRPKLQKP AETLITTVQS NSSSWSNWVI
     PAIAAIIVAL MYRSYMSE
 
 
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