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Database: UniProt
Entry: Q9GQM9
LinkDB: Q9GQM9
Original site: Q9GQM9 
ID   CP6L1_BLAGE             Reviewed;         503 AA.
AC   Q9GQM9;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   13-SEP-2023, entry version 83.
DE   RecName: Full=Cytochrome P450 6l1;
DE            EC=1.14.-.-;
DE   AltName: Full=CYPVIL1;
GN   Name=CYP6L1;
OS   Blattella germanica (German cockroach) (Blatta germanica).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blaberoidea; Blattellidae;
OC   Blattella.
OX   NCBI_TaxID=6973;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=11164340; DOI=10.1016/s0965-1748(00)00116-8;
RA   Wen Z., Scott J.G.;
RT   "Cytochrome P450 CYP6L1 is specifically expressed in the reproductive
RT   tissues of adult male German cockroaches, Blattella germanica (L.).";
RL   Insect Biochem. Mol. Biol. 31:179-187(2001).
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC       Peripheral membrane protein {ECO:0000305}. Microsome membrane
CC       {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Detected only in testes and accessory glands of
CC       male adults. {ECO:0000269|PubMed:11164340}.
CC   -!- DEVELOPMENTAL STAGE: Detected only in male adults.
CC       {ECO:0000269|PubMed:11164340}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AF227531; AAG36792.1; -; mRNA.
DR   AlphaFoldDB; Q9GQM9; -.
DR   SMR; Q9GQM9; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   CDD; cd11056; CYP6-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; PTHR24292; CYTOCHROME P450; 1.
DR   PANTHER; PTHR24292:SF45; CYTOCHROME P450 6G1-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   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW   Monooxygenase; Oxidoreductase.
FT   CHAIN           1..503
FT                   /note="Cytochrome P450 6l1"
FT                   /id="PRO_0000051887"
FT   BINDING         438
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   503 AA;  57163 MW;  D02DD4986C1DB2A2 CRC64;
     MTLVDWFLDT IALLLGLLHI WIARHFQHWE EKGVHHVAPQ PLVGSMLRLL TFSVSPAVFI
     QGVHEAAGSH PYIGFYIFGR PALLVRDPSL LQHILVKDFS NFTDRLTSSN KHKDPVGAAN
     LFCIKGNRWR QIRACITHTF STARLKIMFS RVLNSASVTR DYILERGNQP INVKDLFVRT
     SLDSMCSTLF GIESSTLYNS EAQFLHYGHK MMRWTPYRAL EALAHFFSPE LLNVFDTRLF
     ECESTEFLIN AFSEAITERE KTGLYCSDLV DSLIQLKKQL IDVSEHEVLG QAMLFFAAGF
     ETTSSAMAFA MYELALHPEI QDRLRTEIQE VTACHGGQVT YEGVKKMSYL DMVVSEVLRK
     YPPMSFIDRV CLHDYHIPGT DVVIEKGTPI FVSLLGLHRD SIFYPDPEDF NPERFNKEKK
     SGVHPFSYIP FGDGPRNCIG LRLGLMSVKL VIIMLLQSLR VETHESTPVP LQLSPYVLFL
     KNLGRLPLMF VPIGEDNVET SLA
//
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