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 27-MAR-2024, entry version 100. 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}. 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; 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 CDD; cd20651; CYP15A1-like; 1. DR Gene3D; 1.10.630.10; Cytochrome P450; 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 PANTHER; PTHR24300:SF385; CYTOCHROME P450 306A1; 1. DR PANTHER; PTHR24300; CYTOCHROME P450 508A4-RELATED; 1. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; Cytochrome P450; 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 //