CP17A_ICTPU
ID CP17A_ICTPU Reviewed; 514 AA.
AC O73853;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Steroid 17-alpha-hydroxylase/17,20 lyase;
DE EC=1.14.14.19 {ECO:0000250|UniProtKB:P05093};
DE EC=1.14.14.32 {ECO:0000250|UniProtKB:P05093};
DE AltName: Full=17-alpha-hydroxyprogesterone aldolase;
DE AltName: Full=CYPXVII;
DE AltName: Full=Cytochrome P450 17A1;
DE AltName: Full=Cytochrome P450-C17;
DE Short=Cytochrome P450c17;
GN Name=cyp17a1; Synonyms=cyp17;
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovary;
RA Trant J.M., Berard C., Byrne B.J., Wunder J.;
RT "Isolation and heterologous expression of the cDNA encoding the cytochrome
RT P450 17-hydroxylase from the channel catfish (Ictalurus punctatus).";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Conversion of pregnenolone and progesterone to their 17-
CC alpha-hydroxylated products and subsequently to dehydroepiandrosterone
CC (DHEA) and androstenedione. Catalyzes both the 17-alpha-hydroxylation
CC and the 17,20-lyase reaction.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a C21-steroid + O2 + reduced [NADPH--hemoprotein reductase] =
CC a 17alpha-hydroxy-C21-steroid + H(+) + H2O + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:65760, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:61313, ChEBI:CHEBI:138141; EC=1.14.14.19;
CC Evidence={ECO:0000250|UniProtKB:P05093};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=17alpha-hydroxyprogesterone + O2 + reduced [NADPH--hemoprotein
CC reductase] = acetate + androst-4-ene-3,17-dione + 2 H(+) + H2O +
CC oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:14753,
CC Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16422,
CC ChEBI:CHEBI:17252, ChEBI:CHEBI:30089, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210; EC=1.14.14.32;
CC Evidence={ECO:0000250|UniProtKB:P05093};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=17alpha-hydroxypregnenolone + O2 + reduced [NADPH--hemoprotein
CC reductase] = 3beta-hydroxyandrost-5-en-17-one + acetate + 2 H(+) +
CC H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:50244,
CC Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:28689,
CC ChEBI:CHEBI:28750, ChEBI:CHEBI:30089, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210; EC=1.14.14.32;
CC Evidence={ECO:0000250|UniProtKB:P05093};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- PATHWAY: Lipid metabolism; steroid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AF063837; AAC16551.1; -; mRNA.
DR RefSeq; NP_001187242.1; NM_001200313.1.
DR AlphaFoldDB; O73853; -.
DR SMR; O73853; -.
DR STRING; 7998.ENSIPUP00000036506; -.
DR GeneID; 100313515; -.
DR KEGG; ipu:100313515; -.
DR CTD; 100313515; -.
DR OrthoDB; 702827at2759; -.
DR UniPathway; UPA00062; -.
DR Proteomes; UP000221080; Chromosome 3.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0047442; F:17-alpha-hydroxyprogesterone aldolase activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004508; F:steroid 17-alpha-monooxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0007548; P:sex differentiation; IEA:InterPro.
DR GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR033282; CYP17A1.
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 PANTHER; PTHR24289:SF7; PTHR24289:SF7; 1.
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 Heme; Iron; Lipid metabolism; Lyase; Membrane; Metal-binding;
KW Monooxygenase; Oxidoreductase; Steroidogenesis.
FT CHAIN 1..514
FT /note="Steroid 17-alpha-hydroxylase/17,20 lyase"
FT /id="PRO_0000051945"
FT BINDING 445
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 514 AA; 58134 MW; 7CDF5CC0F6982053 CRC64;
MGWLICFCVF AAIIIVALYL RKIHGFLVDD RAPPNLPSLP IIGSLLSINS NSPPHIFFQQ
LQKKYGDIYS LDMGSNRVII VNNHHHAKEV LLRKGKIFAG RPRTVTTDIL TRDGKDIAFG
DYSATWKFHR KIVHGALCMF GEGTASIEKI ICREASSMCE ILTNLQSSAA DLAPELTRAV
TNVVCTLCFS SSYKRGDPEF EAMLKYSQGI VDTVAKDSLV DIFPWLQLFP NEDLRILRRC
VSIRDKLLQK KYEEHKADFS DNIQRDLFDA LLRAKNSSEN NNTSTQDVGL TDDHLLMTVG
DIFGAGVETT TTVLKWSILY LIHHPQVQRK IQEELDAKIG RDRHPQVNDR GNLPYLEATI
REVLRIRPVS PLLIPHVALS DANIGEYTVQ KGTRVIVNLW SLHHDEKEWK NPELFNPERF
LNEEGNSLCC PSLSYLPFGA GVRVCLGEAL AKLELFLFLS WILQRFTLEV PGGQPLPELQ
GKFRVVLQPQ KYKVIARLRT GWEKSLQSQE SESG
