ID   CP2L1_PANAR             Reviewed;         492 AA.
AC   Q27712;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Cytochrome P450 2L1;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIIL1;
GN   Name=CYP2L1;
OS   Panulirus argus (Caribbean spiny lobster) (Palinurus argus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Achelata;
OC   Palinuroidea; Palinuridae; Panulirus.
OX   NCBI_TaxID=6737;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Hepatopancreas;
RX   PubMed=8619632; DOI=10.1006/abbi.1996.0188;
RA   James M.O., Boyle S.M., Trapido-Rosenthal H.G., Smith W.C., Greenberg R.M.,
RA   Shiverick K.T.;
RT   "cDNA and protein sequence of a major form of P450, CYP2L, in the
RT   hepatopancreas of the spiny lobster, Panulirus argus.";
RL   Arch. Biochem. Biophys. 329:31-38(1996).
CC   -!- FUNCTION: Efficient in catalyzing the monooxygenation of benzphetamine,
CC       aminopyrine, benzo(a)pyrene, progesterone, and testosterone.
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 {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}. Microsome membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; U44826; AAB03106.1; -; mRNA.
DR   PIR; S68856; S68856.
DR   AlphaFoldDB; Q27712; -.
DR   SMR; Q27712; -.
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.
FT   CHAIN           1..492
FT                   /note="Cytochrome P450 2L1"
FT                   /id="PRO_0000051776"
FT   BINDING         436
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   492 AA;  56767 MW;  F27EE702DD09D5EE CRC64;
     MLTGALLLLL LVVIVYLLDK KPSGLPPGIW GWPLVGRMPS RSKHLADQVK QLRKKYGDII
     TWRIGTRVNV FLCNFKLVKT ALSKFECSDR PDFYTFKLFG EGNDVGVVFS NGVMWQTHRR
     FILRQLRDLG MGKSRLEAAI QHEAACLVQE LKKHTDQPMP LPKSINLAVL NVIWKLVADH
     RYSLQDQEGQ YFTQLLTTTT DNMQGFALNL FNYLPWLLMI TPDFVKNWMG VRVLRDGVCE
     LKDYMKTFIK EHQATLDPSN PKDLLDAYLI DLQERKEDPL STMNIETVRA VIMDLFGAGT
     ETTSTMIRWT ILYLMKYPEV QAKIQREIDA AVPRGTLPSL EHKDKLAYFE ATIHEVHRIV
     SLVPLGVSHY TNQDTELAGY RLPKGTVVMS HLECCHRDPS YWEKPNEFYP EHFLDDQGKF
     VKREHLVNFS VGRRVCVGES LARMELFVFL SAILQNFTFS APKGEVLHTE KDPQQMLFSF
     PKPYQVIIRE RE