位置:首页 > 蛋白库 > CP2C3_RABIT
CP2C3_RABIT
ID   CP2C3_RABIT             Reviewed;         489 AA.
AC   P00182; Q29509; Q29525;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Cytochrome P450 2C3;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIIC3;
DE   AltName: Full=Cytochrome P450 PBc3;
DE   AltName: Full=Cytochrome P450 form 3B;
GN   Name=CYP2C3;
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   PROTEIN SEQUENCE.
RX   PubMed=3988762; DOI=10.1016/s0021-9258(18)89040-8;
RA   Ozols J., Heinemann F.S., Johnson E.F.;
RT   "The complete amino acid sequence of a constitutive form of liver
RT   microsomal cytochrome P-450.";
RL   J. Biol. Chem. 260:5427-5434(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=6546520; DOI=10.1021/bi00297a005;
RA   Leighton J.K., Debrunner-Vossbrinck B.A., Kemper B.;
RT   "Isolation and sequence analysis of three cloned cDNAs for rabbit liver
RT   proteins that are related to rabbit cytochrome P-450 (form 2), the major
RT   phenobarbital-inducible form.";
RL   Biochemistry 23:204-210(1984).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2340269; DOI=10.1021/bi00467a021;
RA   Chan G.;
RT   "Structure of the rabbit cytochrome P450IIC3 gene, a constitutive member of
RT   the P450IIC subfamily.";
RL   Biochemistry 29:3743-3750(1990).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=New Zealand white; TISSUE=Liver;
RA   Noshiro M., Ishida H., Okuda K.;
RT   "A member of cytochrome P450 2C family which is identical to rabbit
RT   P450pc3.";
RL   Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases.
CC       In liver microsomes, this enzyme is involved in an NADPH-dependent
CC       electron transport pathway. It oxidizes a variety of structurally
CC       unrelated compounds, including steroids, fatty acids, and xenobiotics.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein
CC         reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:30879, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:142491; EC=1.14.14.1;
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
CC       membrane protein. Microsome membrane; Peripheral membrane protein.
CC   -!- INDUCTION: Constitutively expressed.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; K01523; AAA31212.1; -; mRNA.
DR   EMBL; M31254; AAA31175.1; -; Genomic_DNA.
DR   EMBL; M31245; AAA31175.1; JOINED; Genomic_DNA.
DR   EMBL; M31247; AAA31175.1; JOINED; Genomic_DNA.
DR   EMBL; M31248; AAA31175.1; JOINED; Genomic_DNA.
DR   EMBL; M31249; AAA31175.1; JOINED; Genomic_DNA.
DR   EMBL; M31250; AAA31175.1; JOINED; Genomic_DNA.
DR   EMBL; M31251; AAA31175.1; JOINED; Genomic_DNA.
DR   EMBL; M31252; AAA31175.1; JOINED; Genomic_DNA.
DR   EMBL; M31253; AAA31175.1; JOINED; Genomic_DNA.
DR   EMBL; D26152; BAA05139.1; -; mRNA.
DR   PIR; A00183; O4RBP3.
DR   RefSeq; NP_001164736.1; NM_001171265.1.
DR   AlphaFoldDB; P00182; -.
DR   SMR; P00182; -.
DR   STRING; 9986.ENSOCUP00000023608; -.
DR   PRIDE; P00182; -.
DR   GeneID; 100328933; -.
DR   KEGG; ocu:100328933; -.
DR   CTD; 100328933; -.
DR   eggNOG; KOG0156; Eukaryota.
DR   InParanoid; P00182; -.
DR   OrthoDB; 702827at2759; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Endoplasmic reticulum; Heme; Iron; Membrane;
KW   Metal-binding; Microsome; Monooxygenase; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..489
FT                   /note="Cytochrome P450 2C3"
FT                   /id="PRO_0000051694"
FT   BINDING         434
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        49
FT                   /note="D -> N (in Ref. 3; AAA31175 and 4; BAA05139)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        82..84
FT                   /note="GVI -> TVK (in Ref. 3; AAA31175 and 4; BAA05139)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        89
FT                   /note="D -> Y (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        178
FT                   /note="I -> M (in Ref. 4; BAA05139)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        222
FT                   /note="L -> LG (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        256
FT                   /note="S -> L (in Ref. 3; AAA31175)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        338
FT                   /note="M -> S (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        342
FT                   /note="T -> S (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        364
FT                   /note="S -> T (in Ref. 4; BAA05139)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        429
FT                   /note="A -> T (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        471
FT                   /note="V -> L (in Ref. 4; BAA05139)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   489 AA;  55794 MW;  860D36E42D554C75 CRC64;
     MDLLIILGIC LSCVVLLSLW KKTHGKGKLP PGPTPLPVVG NLLQLETKDI NKSLSMLAKE
     YGSIFTLYFG MKPAVVLYGY EGVIEALIDR GEEFSGRGIF PVFDRVTKGL GIVFSSGEKW
     KETRRFSLTV LRNLGMGKKT IEERIQEEAL CLIQALRKTN ASPCDPTFLL FCVPCNVICS
     VIFQNRFDYD DEKFKTLIKY FHENFELLGT PWIQLYNIFP ILHYLPGSHR QLFKNIDGQI
     KFILEKVQEH QESLDSNNPR DFVDHFLIKM EKEKHKKQSE FTMDNLITTI WDVFSAGTDT
     TSNTLKFALL LLLKHPEITA KVQEEIEHVI GRHRSPCMQD RTRMPYTDAV MHEIQRYVDL
     VPTSLPHAVT QDIEFNGYLI PKGTDIIPSL TSVLYDDKEF PNPEKFDPGH FLDESGNFKK
     SDYFMPFSAG KRACVGEGLA RMELFLLLTT ILQHFTLKPL VDPKDIDPTP VENGFVSVPP
     SYELCFVPV
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024