ID   CP3AT_PIG               Reviewed;         503 AA.
AC   P79401;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Cytochrome P450 3A29;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIIIA29;
GN   Name=CYP3A29;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Small intestine;
RX   PubMed=9682441; DOI=10.1046/j.1365-2052.1998.00225.x;
RA   Nissen P.H., Winteroe A.K., Fredholm M.;
RT   "Mapping of porcine genes belonging to two different cytochrome P450
RT   subfamilies.";
RL   Anim. Genet. 29:7-11(1998).
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; Z93099; CAB07513.1; -; mRNA.
DR   RefSeq; NP_999588.1; NM_214423.1.
DR   AlphaFoldDB; P79401; -.
DR   SMR; P79401; -.
DR   PeptideAtlas; P79401; -.
DR   PRIDE; P79401; -.
DR   GeneID; 403324; -.
DR   KEGG; ssc:403324; -.
DR   CTD; 403324; -.
DR   InParanoid; P79401; -.
DR   OrthoDB; 467733at2759; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
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   GO; GO:0071357; P:cellular response to type I interferon; IMP:AgBase.
DR   GO; GO:0070989; P:oxidative demethylation; IBA:GO_Central.
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 3A29"
FT                   /id="PRO_0000051808"
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;  57199 MW;  E3D411B2674FD17F CRC64;
     MDLIPGFSTE TWVLLATSLV LLYLYGTYSH GLFKKLGIPG PRPLPYFGNI LGYRKGVDHF
     DKKCFQQYGK MWGVYDGRQP LLAVTDPNMI KSVLVKECYS VFTNRRSFGP LGAMRNALSL
     AEDEEWKRIR TLLSPTFTSG KLKEMFPIIS HYGDLLVSNL RKEAEKGKPV TMKDIFGAYS
     MDVITSTAFG VNIDSLNNPQ DPFVENSKKL LKFSFFDPFL LSLIFFPFLT PIFEVLNITL
     FPKSSVNFFT KSVKRMKESR LTDQQKRRVD LLQLMINSQN SKEMDPHKSL SNEELVAQGI
     IFIFAGYETT SSALSLLAYE LATHPDVQQK LQEEIEATFP NKAPPTYDAL AQMEYLDMVV
     NETLRLYPIA ARLERACKKD VEIHGVFVPK GTVVVVPVFV LHRDPDLWPE PEEFRPERFS
     KKHKDTINPY TYLPFGTGPR NCIGMRFALM NMKLALVRVL QNFSFKPCKE TQIPLKLTTQ
     GLTQPEKPVV LKILPRDGTV SGA