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   27-MAR-2024, entry version 130.
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.ENSCJAP00000047441; -.
DR   Ensembl; ENSCJAT00000030689.5; ENSCJAP00000029043.4; ENSCJAG00000015744.6.
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   OrthoDB; 1611592at2759; -.
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   CDD; cd20650; CYP3A; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 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   PANTHER; PTHR24302:SF38; CYTOCHROME P450 3A7; 1.
DR   PANTHER; PTHR24302; CYTOCHROME P450 FAMILY 3; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00464; EP450II.
DR   PRINTS; PR01689; EP450IICYP3A.
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; 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
//