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Database: UniProt
Entry: A0A0D9S0N1_CHLSB
LinkDB: A0A0D9S0N1_CHLSB
Original site: A0A0D9S0N1_CHLSB 
ID   A0A0D9S0N1_CHLSB        Unreviewed;       405 AA.
AC   A0A0D9S0N1;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 39.
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:ENSCSAP00000014420.1};
OS   Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Chlorocebus.
OX   NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000014420.1, ECO:0000313|Proteomes:UP000029965};
RN   [1] {ECO:0000313|Ensembl:ENSCSAP00000014420.1, ECO:0000313|Proteomes:UP000029965}
RP   NUCLEOTIDE SEQUENCE.
RA   Warren W., Wilson R.K.;
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCSAP00000014420.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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; AQIB01134722; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_007995067.1; XM_007996876.1.
DR   AlphaFoldDB; A0A0D9S0N1; -.
DR   STRING; 60711.ENSCSAP00000014420; -.
DR   Ensembl; ENSCSAT00000001664.1; ENSCSAP00000014420.1; ENSCSAG00000003635.1.
DR   GeneID; 103234719; -.
DR   KEGG; csab:103234719; -.
DR   CTD; 112398; -.
DR   eggNOG; KOG3710; Eukaryota.
DR   GeneTree; ENSGT00940000160655; -.
DR   OMA; HCPGAPG; -.
DR   OrthoDB; 5358684at2759; -.
DR   BioGRID-ORCS; 103234719; 0 hits in 9 CRISPR screens.
DR   Proteomes; UP000029965; Chromosome 6.
DR   Bgee; ENSCSAG00000003635; Expressed in blood and 7 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:UP000029965}.
FT   DOMAIN          276..374
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          48..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          106..155
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        58..75
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   405 AA;  43386 MW;  9819377DC1E005C0 CRC64;
     MDSPCQSQPL SQALPQLPGS SSEPLEPGRA RMGVESYLPC PLLPSYHCPG VPSEASAGSG
     TPRATATSTT ASPLRDGFGG QDGGELRPLQ SEGAAALVTK GCQRLAAQGA RPEAPKRKWA
     EDGGDAPSPS KRPWARQENQ EAEREGGMSC GCSSGSGEAS AGLMEEVLPS APERLALDYI
     VPCMRYYGIC VKDSFLGAAL GGRVLAEVEA LKRGGRLRDG QLVSQRAIPP RSIRGDQIAW
     VEGHEAGCRS IGALMAHVDA VIRHCAGRLG SYVINGRTKA MVACYPGNGL GYVRHVDNPH
     GDGRCITCIY YLNQNWDVKV HGGLLQIFPE GRPVVANIEP LFDRLLIFWS DRRNPHEVKP
     AYATRYAITV WYFDAKERAA AKDKYQLASG QKGVQVPVSQ PPTPT
//
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