ID   CP4C1_BLADI             Reviewed;         511 AA.
AC   P29981;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Cytochrome P450 4C1;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIVC1;
GN   Name=CYP4C1;
OS   Blaberus discoidalis (Tropical cockroach).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blaberoidea; Blaberidae;
OC   Blaberinae; Blaberus.
OX   NCBI_TaxID=6981;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2034694; DOI=10.1073/pnas.88.10.4558;
RA   Bradfield J.Y., Lee Y.-H., Keeley L.L.;
RT   "Cytochrome P450 family 4 in a cockroach: molecular cloning and regulation
RT   by regulation by hypertrehalosemic hormone.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:4558-4562(1991).
CC   -!- FUNCTION: Involved in the metabolism of insect hormones and in the
CC       breakdown of synthetic insecticides.
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: By hypertrehalosemic hormone and starvation.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; M63798; AAA27819.1; -; mRNA.
DR   PIR; A39381; A39381.
DR   AlphaFoldDB; P29981; -.
DR   SMR; P29981; -.
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   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW   Monooxygenase; Oxidoreductase.
FT   CHAIN           1..511
FT                   /note="Cytochrome P450 4C1"
FT                   /id="PRO_0000051823"
FT   BINDING         314
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /note="covalent"
FT                   /evidence="ECO:0000250"
FT   BINDING         452
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   511 AA;  58754 MW;  E857E9404C30F9AD CRC64;
     MEFITILLST ALFIVTFLFL FRQGAKRARF VYLVNKLPGP TAYPVVGNAI EAIVPRNKLF
     QVFDRRAKLY GPLYRIWAGP IAQVGLTRPE HVELILRDTK HIDKSLVYSF IRPWLGEGLL
     TGTGAKWHSH RKMITPTFHF KILDIFVDVF VEKSEILVKK LQSKVGGKDF DIYPFITHCA
     LDIICETAMG IQMNAQEESE SEYVKAVYEI SELTMQRSVR PWLHPKVIFD LTTMGKRYAE
     CLRILHGFTN KVIQERKSLR QMTGMKPTIS NEEDELLGKK KRLAFLDLLL EASENGTKMS
     DTDIREEVDT FMFEGHDTTS AGICWALFLL GSHPEIQDKV YEELDHIFQG SDRSTTMRDL
     ADMKYLERVI KESLRLFPSV PFIGRVLKED TKIGDYLVPA GCMMNLQIYH VHRNQDQYPN
     PEAFNPDNFL PERVAKRHPY AYVPFSAGPR NCIGQKFATL EEKTVLSSIL RNFKVRSIEK
     REDLTLMNEL ILRPESGIKV ELIPRLPADA C