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Database: UniProt
Entry: A0A151NV24_ALLMI
LinkDB: A0A151NV24_ALLMI
Original site: A0A151NV24_ALLMI 
ID   A0A151NV24_ALLMI        Unreviewed;       507 AA.
AC   A0A151NV24;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Steroid 17-alpha-hydroxylase/17,20 lyase {ECO:0000256|ARBA:ARBA00014119};
DE            EC=1.14.14.19 {ECO:0000256|ARBA:ARBA00012359};
DE            EC=1.14.14.32 {ECO:0000256|ARBA:ARBA00012354};
DE   AltName: Full=CYPXVII {ECO:0000256|ARBA:ARBA00032037};
DE   AltName: Full=Cytochrome P450 17A1 {ECO:0000256|ARBA:ARBA00030382};
DE   AltName: Full=Cytochrome P450-C17 {ECO:0000256|ARBA:ARBA00032167};
GN   Name=CYP17A1 {ECO:0000313|EMBL:KYO40638.1};
GN   ORFNames=Y1Q_0009640 {ECO:0000313|EMBL:KYO40638.1};
OS   Alligator mississippiensis (American alligator).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC   Alligator.
OX   NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO40638.1};
RN   [1] {ECO:0000313|EMBL:KYO40638.1, ECO:0000313|Proteomes:UP000050525}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO40638.1};
RX   PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA   St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA   Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA   Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA   Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA   Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA   McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA   Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA   Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA   Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA   Ray D.A.;
RT   "Sequencing three crocodilian genomes to illuminate the evolution of
RT   archosaurs and amniotes.";
RL   Genome Biol. 13:415-415(2012).
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC       {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KYO40638.1}.
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DR   EMBL; AKHW03001922; KYO40638.1; -; Genomic_DNA.
DR   RefSeq; XP_006278769.1; XM_006278707.3.
DR   AlphaFoldDB; A0A151NV24; -.
DR   STRING; 8496.A0A151NV24; -.
DR   GeneID; 102567971; -.
DR   KEGG; amj:102567971; -.
DR   eggNOG; KOG0156; Eukaryota.
DR   OrthoDB; 2900138at2759; -.
DR   UniPathway; UPA00062; -.
DR   Proteomes; UP000050525; Unassembled WGS sequence.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004508; F:steroid 17-alpha-monooxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd20673; CYP17A1; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 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   PANTHER; PTHR24289; STEROID 17-ALPHA-HYDROXYLASE/17,20 LYASE; 1.
DR   PANTHER; PTHR24289:SF13; STEROID 17-ALPHA-HYDROXYLASE_17,20 LYASE; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   3: Inferred from homology;
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|RuleBase:RU000461};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU000461};
KW   Lyase {ECO:0000313|EMBL:KYO40638.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU000461};
KW   Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050525};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Steroidogenesis {ECO:0000256|ARBA:ARBA00023250}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..507
FT                   /note="Steroid 17-alpha-hydroxylase/17,20 lyase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007586385"
SQ   SEQUENCE   507 AA;  56664 MW;  11D546E09E312924 CRC64;
     MVSLVLGALL LALALLALRR LSRDKADPGH RAPPCLPSLP VLGSLLQLAG HSELHTCFTG
     LQARYGCLYA LRLGSEYLVV VNNHLHAREV LFKKGKEFAG RPHSVTSDLM SRGGKDIAFA
     SYSPLWRFLR KLVHTALSMF GEGSVALQKI ICREAEGLCE VLAATQGAPL AMAPELTRAV
     TNVVCSLCFN SSYRRGDPEF EAMLQYSQGI VDTVGKESLV DIFPWLQYFP NKDLAWLRQC
     VKARDELLQK KFTEHKEAFC SDSVSDLMDA LLRAKLNMEN NNSRLEPGLE LTDDHLLMTV
     GDIFGAGVET TTTALKWAII YMLHYPEVQR KIQEELDQQL GLERRPQLSD RQRLPYLEAT
     ISEVLRIRPV APLLIPHVAL VDSSIGDYVI PKGTHVIVNI WAIHHDQDEW DKPEEFNPGR
     FLDEKGQRIY SPTPSYMPFG SGIRTCLGEV LAKMELFLLL SWILQRFTLE LPAHHPLPSL
     AGKFGIVLQA TGFEVKAVPR EPERAGP
//
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