CP4CU_BLAGE
ID CP4CU_BLAGE Reviewed; 501 AA.
AC Q964T1;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Cytochrome P450 4c21;
DE EC=1.14.14.1;
DE AltName: Full=CYPIVC21;
GN Name=CYP4C21;
OS Blattella germanica (German cockroach) (Blatta germanica).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blaberoidea; Ectobiidae;
OC Blattellinae; Blattella.
OX NCBI_TaxID=6973;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RX PubMed=11470532; DOI=10.1016/s0378-1119(01)00529-7;
RA Wen Z., Horak C.E., Scott J.G.;
RT "CYP9E2, CYP4C21 and related pseudogenes from German cockroaches, Blattella
RT germanica: implications for molecular evolution, expression studies and
RT nomenclature of P450s.";
RL Gene 272:257-266(2001).
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:0000305};
CC Peripheral membrane protein {ECO:0000305}. Microsome membrane
CC {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
CC -!- INDUCTION: Expressed at all life stages. {ECO:0000269|PubMed:11470532}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AF275641; AAK69411.1; -; mRNA.
DR AlphaFoldDB; Q964T1; -.
DR SMR; Q964T1; -.
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..501
FT /note="Cytochrome P450 4c21"
FT /id="PRO_0000051824"
FT BINDING 309
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /note="covalent"
FT /evidence="ECO:0000250"
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; 58297 MW; 825F90FAA12AB22B CRC64;
MDITVFLSLT VVVFLAVIIF YGRNEERKRM LQKIPGAPSL PLIGTALPIL YRRKEDRMTW
IEEILEKYKP LILWYFGNRP FVNISSPELI EVVLRNTQLI DKAFLYDLFH SWLGTGLLTS
SGAKWHQHRK IITPTFHFSI LEGFITIFAE KSEILVRKLQ KEVGRGPFFI RQYVSNCALD
IICETAMGTS VNAQDEGFSE YVTAINKMTD VLSDRMANPL LYPEFIFKLT PYYWTHKKCL
KVLNGFVNKI IQERKEERKK SKVTQTSEDA DIGKKKRVPF LDTLLDASED DNKLTDTDIL
EEVHTFMFEG HDTVSAAMTW LLFELGHHPE IQEEAYKEVQ DIFQGSDRVP TMADLNNMNY
LERVIKESLR LHPSVIYFVR EAHQDFELGG YTIPAGTNID FSVPFIHRNP EIFPNPRCFN
PDNFLPDRVV NRHPYAYIPF SAGPRNCIGQ RFALLEEKVV LSYLLRHYRF RTVNKREDSK
FKLEMINTPV KPIQLIIEAR N