CP2J1_RABIT
ID CP2J1_RABIT Reviewed; 501 AA.
AC P52786;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Cytochrome P450 2J1;
DE EC=1.14.14.1;
DE AltName: Full=CYPIIJ1;
DE AltName: Full=Cytochrome P-450IB;
GN Name=CYP2J1;
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], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=1717443; DOI=10.1016/s0021-9258(18)55201-7;
RA Kikuta Y., Sogawa K., Haniu M., Kinosaki M., Kusunose E., Nojima Y.,
RA Yamamoto S., Ichihara K., Kusunose M., Fujii-Kuriyama Y.;
RT "A novel species of cytochrome P-450 (P-450ib) specific for the small
RT intestine of rabbits. cDNA cloning and its expression in COS cells.";
RL J. Biol. Chem. 266:17821-17825(1991).
CC -!- FUNCTION: Catalyzes the N-demethylation of benzphetamine to
CC formaldehyde.
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 -!- TISSUE SPECIFICITY: Small intestine.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; D90405; BAA14401.1; -; mRNA.
DR PIR; A40938; A40938.
DR RefSeq; NP_001153760.1; NM_001160288.1.
DR AlphaFoldDB; P52786; -.
DR SMR; P52786; -.
DR STRING; 9986.ENSOCUP00000003635; -.
DR GeneID; 100301544; -.
DR KEGG; ocu:100301544; -.
DR CTD; 100301544; -.
DR eggNOG; KOG0156; Eukaryota.
DR InParanoid; P52786; -.
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; IPR008071; Cyt_P450_E_grp-I_CYP2J-like.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR01688; EP450ICYP2J.
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..501
FT /note="Cytochrome P450 2J1"
FT /id="PRO_0000051768"
FT BINDING 447
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 /evidence="ECO:0000250"
SQ SEQUENCE 501 AA; 57326 MW; 90EEE628F0538197 CRC64;
MVAALSSLAA ALGAGLHPKT LLLGAVAFLF FAYFLKTRRP KNYPPGPWRL PFLGNLFTLD
MEKSHLQLQQ FVKKYGNLFC LDLAGKSIVI VTGLPLIKEV LVHMDQNFIN RPVPPIRERS
FKKNGLIMSS GQLWKEQRRF ALMTLRNFGL GKKSLEERIQ EEARHLTEAM EKEGGQPFDA
HFKINNAVSN IICSITFGER FEYHDGQFQE LLKLFDEVMY LEASMLCQLY NIFPWIMKFL
PGAHQTLFSN WKKLELFVSR MLENHKKDWN PAETRDFIDA YLKEMSKYPG SATSSFNEEN
LICSTLDLFL AGTETTSDMR WGLLFMALYP EIQEKVHAEI DSVIGQWQQP SMASRESLPY
TNAVIHEVQR MGNILPLNVP REVTVDTTLA GYHLPKGTVV LTNLTALHKD PEEWATPDTF
NPEHFLENGQ FKKKEAFIPF SIGKRACLGE QLAKSELFIF FTSLMQKFTF KPPSDEKLTL
NFRMGITLSP VKHRICAIPR A