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Database: UniProt
Entry: A0A452G7D3_CAPHI
LinkDB: A0A452G7D3_CAPHI
Original site: A0A452G7D3_CAPHI 
ID   A0A452G7D3_CAPHI        Unreviewed;       399 AA.
AC   A0A452G7D3;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=hypoxia-inducible factor-proline dioxygenase {ECO:0000256|ARBA:ARBA00039004};
DE            EC=1.14.11.29 {ECO:0000256|ARBA:ARBA00039004};
GN   Name=EGLN2 {ECO:0000313|Ensembl:ENSCHIP00000032382.1};
OS   Capra hircus (Goat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Capra.
OX   NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000032382.1, ECO:0000313|Proteomes:UP000291000};
RN   [1] {ECO:0000313|Ensembl:ENSCHIP00000032382.1, ECO:0000313|Proteomes:UP000291000}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA   Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA   Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA   Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA   Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT   "Polished mammalian reference genomes with single-molecule sequencing and
RT   chromosome conformation capture applied to the Capra hircus genome.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCHIP00000032382.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-prolyl-[hypoxia-inducible factor alpha
CC         subunit] + O2 = CO2 + succinate + trans-4-hydroxy-L-prolyl-[hypoxia-
CC         inducible factor alpha subunit]; Xref=Rhea:RHEA:48400, Rhea:RHEA-
CC         COMP:12093, Rhea:RHEA-COMP:12094, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC         ChEBI:CHEBI:50342, ChEBI:CHEBI:61965; EC=1.14.11.29;
CC         Evidence={ECO:0000256|ARBA:ARBA00035981};
CC   -!- COFACTOR:
CC       Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC         Evidence={ECO:0000256|ARBA:ARBA00001961};
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DR   EMBL; LWLT01000020; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_017917937.1; XM_018062448.1.
DR   RefSeq; XP_017917938.1; XM_018062449.1.
DR   AlphaFoldDB; A0A452G7D3; -.
DR   STRING; 9925.ENSCHIP00000032382; -.
DR   Ensembl; ENSCHIT00000040257.1; ENSCHIP00000032382.1; ENSCHIG00000026382.1.
DR   GeneID; 102191264; -.
DR   KEGG; chx:102191264; -.
DR   CTD; 112398; -.
DR   GeneTree; ENSGT00940000160655; -.
DR   OMA; HCPGAPG; -.
DR   OrthoDB; 5358684at2759; -.
DR   Proteomes; UP000291000; Chromosome 18.
DR   Bgee; ENSCHIG00000026382; Expressed in cerebellum and 18 other cell types or tissues.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0008198; F:ferrous iron binding; IEA:Ensembl.
DR   GO; GO:0031418; F:L-ascorbic acid binding; IEA:InterPro.
DR   GO; GO:0019826; F:oxygen sensor activity; IEA:Ensembl.
DR   GO; GO:0031545; F:peptidyl-proline 4-dioxygenase activity; IEA:Ensembl.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:Ensembl.
DR   GO; GO:0045732; P:positive regulation of protein catabolic process; IEA:Ensembl.
DR   GO; GO:0043523; P:regulation of neuron apoptotic process; IEA:Ensembl.
DR   GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR   Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1.
DR   InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR   InterPro; IPR006620; Pro_4_hyd_alph.
DR   InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY.
DR   PANTHER; PTHR12907; EGL NINE HOMOLOG-RELATED; 1.
DR   PANTHER; PTHR12907:SF6; PROLYL HYDROXYLASE EGLN2; 1.
DR   Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR   SMART; SM00702; P4Hc; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
PE   4: Predicted;
KW   Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000291000}.
FT   DOMAIN          270..368
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
FT   REGION          1..86
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          105..154
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        57..73
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   399 AA;  42812 MW;  94B2A4856E121349 CRC64;
     MDSPCQPQPL SQALPQLPGS VSEPLEPSRA RMGVESYLPC PLLSYHRPGA PTEASAGSGT
     PRATATSATG SPLREGFGGQ DGGELRPLQS EGAAALVTKG CQRLAAQGAR PEAPKRKWAE
     DGGDAPAPSK RPWARQENQE AEGEGCSSGS SEASAGLREE VLPAAPERLA LDYIVPCMRY
     YGICVKDSFL GAALGGQVLA EVEALKRGGR LRDGQLVSQR AIPPRSIRGD QIAWVEGHEP
     GCQSIGALMA HVDAVIRHCA GRLGSYVING RTKAMVACYP GNGLGYVRHV DNPHGDGRCI
     TCIYYLNQNW DVKVHGGLLQ IFPEGRPVVA NIEPLFDRLL IFWSDRRNPH EVKPAYATRY
     AITVWYFDAK ERAAAKDKYQ LASGQKGVQV PVSQPTTPT
//
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