CP3AL_CALJA
ID CP3AL_CALJA Reviewed; 503 AA.
AC O18993;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Cytochrome P450 3A21;
DE EC=1.14.14.1;
DE AltName: Full=CYPIIIA21;
DE AltName: Full=Cytochrome P450 CM3A-10;
GN Name=CYP3A21;
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=9056237; DOI=10.1006/abbi.1996.9852;
RA Igarashi T., Sakuma T., Isogai M., Nagata R., Kamataki T.;
RT "Marmoset liver cytochrome P450s: study for expression and molecular
RT cloning of their cDNAs.";
RL Arch. Biochem. Biophys. 339:85-91(1997).
CC -!- FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases.
CC In liver microsomes, this enzyme is involved in an NADPH-dependent
CC electron transport pathway. It oxidizes a variety of structurally
CC unrelated compounds, including steroids, fatty acids, and xenobiotics.
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: P450 can be induced to high levels in liver and other
CC tissues by various foreign compounds, including drugs, pesticides, and
CC carcinogens.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; D31921; BAA22156.1; -; mRNA.
DR RefSeq; NP_001191369.1; NM_001204440.1.
DR AlphaFoldDB; O18993; -.
DR SMR; O18993; -.
DR STRING; 9483.ENSCJAP00000051348; -.
DR Ensembl; ENSCJAT00000030689; ENSCJAP00000029043; ENSCJAG00000015744.
DR GeneID; 100404344; -.
DR KEGG; cjc:100404344; -.
DR CTD; 1576; -.
DR eggNOG; KOG0158; Eukaryota.
DR GeneTree; ENSGT00950000182958; -.
DR HOGENOM; CLU_001570_5_2_1; -.
DR InParanoid; O18993; -.
DR OMA; TCLEYRK; -.
DR OrthoDB; 467733at2759; -.
DR TreeFam; TF105087; -.
DR Proteomes; UP000008225; Chromosome 2.
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 GO; GO:0004497; F:monooxygenase activity; ISS:UniProtKB.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR008072; Cyt_P450_E_CYP3A.
DR InterPro; IPR002402; Cyt_P450_E_grp-II.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00464; EP450II.
DR PRINTS; PR01689; EP450IICYP3A.
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; Reference proteome.
FT CHAIN 1..503
FT /note="Cytochrome P450 3A21"
FT /id="PRO_0000051803"
FT BINDING 442
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; 57564 MW; 9BFD421D72C76D6A CRC64;
MDFIPNLAVE TWLLLAVSLV LLYLYGTHSH GLFKKLGIPG PTPLPFLGTV LYYRQGFWKF
DMECYKKYGK MWGIYDGRQP VLAITDPNII KTVLVKECYS VFTNRRPFGP VGFMKSAISI
AQDDEWKRIR SLLSPTFTSG KLKEMVPIIA QYGEVLVRNL RREAEKGKPI NMKDIFGAYS
MDVITGTSFG VNIDSLNNPQ DPFVESTKKL LRFDFLDPFF LSITIFPFLT PILEALNISM
FPRDSTSFLR KSIKRIKESR LKDTHKHRVD FLQLMIDSQN SKETESDKAL SDLELVAQSI
IFIFAGYETT SSTLSFIMYE LATHPDVQQK LQEEIDAVLP NKAPATYDTV LQMEYLDMVV
NETLRLFPLA MRLERVCKKD VEINGVFIPK GVVVMIPSYA LHYDPKYWTE PEKFLPERFS
KNNKDNIDPY IYTPFGTGPR NCIGMRFALM NMKLALIRVL QNFSFKPCKE TQIPLKLRLG
GLLQTEKPIV LKVEPRDGTV SGA