ID G2HG38_PANTR Unreviewed; 407 AA. AC G2HG38; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAR-2024, entry version 90. 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|EMBL:JAA02544.1, GN ECO:0000313|Ensembl:ENSPTRP00000044177.4, GN ECO:0000313|VGNC:VGNC:14743}; OS Pan troglodytes (Chimpanzee). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Pan. OX NCBI_TaxID=9598 {ECO:0000313|EMBL:BAK62696.1}; RN [1] {ECO:0000313|Ensembl:ENSPTRP00000044177.4, ECO:0000313|Proteomes:UP000002277} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16136131; DOI=10.1038/nature04072; RG Chimpanzee sequencing and analysis consortium; RT "Initial sequence of the chimpanzee genome and comparison with the human RT genome."; RL Nature 437:69-87(2005). RN [2] {ECO:0000313|EMBL:BAK62696.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Testis {ECO:0000313|EMBL:BAK62696.1}; RX PubMed=21484476; DOI=10.1007/s10142-011-0220-9; RA Kim R.N., Kim D.W., Choi S.H., Chae S.H., Nam S.H., Kim D.W., Kim A., RA Kang A., Park K.H., Lee Y.S., Hirai M., Suzuki Y., Sugano S., Hashimoto K., RA Kim D.S., Park H.S.; RT "Major chimpanzee-specific structural changes in sperm development- RT associated genes."; RL Funct. Integr. Genomics 11:507-517(2011). RN [3] {ECO:0000313|EMBL:JAA02544.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Adipose stromal {ECO:0000313|EMBL:JAA02544.1}, and Skeletal RC muscle {ECO:0000313|EMBL:JAA39975.1}; RA Maudhoo M.D., Meehan D.T., Norgren R.B.Jr.; RT "De novo assembly of the reference chimpanzee transcriptome from NextGen RT mRNA sequences."; RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|Ensembl:ENSPTRP00000044177.4} 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AC194534; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AK305702; BAK62696.1; -; mRNA. DR EMBL; GABC01008794; JAA02544.1; -; mRNA. DR EMBL; GABE01004764; JAA39975.1; -; mRNA. DR RefSeq; NP_001233442.1; NM_001246513.1. DR RefSeq; XP_016789548.1; XM_016934059.1. DR RefSeq; XP_016789549.1; XM_016934060.1. DR RefSeq; XP_016789550.1; XM_016934061.1. DR RefSeq; XP_016802410.1; XM_016946921.1. DR RefSeq; XP_016802411.1; XM_016946922.1. DR RefSeq; XP_016802412.1; XM_016946923.1. DR PaxDb; 9598-ENSPTRP00000044177; -. DR Ensembl; ENSPTRT00000020431.6; ENSPTRP00000044177.4; ENSPTRG00000011010.6. DR Ensembl; ENSPTRT00000092346.1; ENSPTRP00000092229.1; ENSPTRG00000043786.1. DR GeneID; 456049; -. DR KEGG; ptr:456049; -. DR CTD; 112398; -. DR VGNC; VGNC:14743; EGLN2. DR eggNOG; KOG3710; Eukaryota. DR GeneTree; ENSGT00940000160655; -. DR HOGENOM; CLU_063064_0_0_1; -. DR OrthoDB; 5358684at2759; -. DR TreeFam; TF314595; -. DR Proteomes; UP000002277; Chromosome 19. DR Bgee; ENSPTRG00000011010; Expressed in testis and 11 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0008198; F:ferrous iron binding; IBA:GO_Central. DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:InterPro. DR GO; GO:0031545; F:peptidyl-proline 4-dioxygenase activity; IBA:GO_Central. DR GO; GO:0071456; P:cellular response to hypoxia; IBA:GO_Central. 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 2: Evidence at transcript level; 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:UP000002277}. FT DOMAIN 278..376 FT /note="Fe2OG dioxygenase" FT /evidence="ECO:0000259|PROSITE:PS51471" FT REGION 1..34 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 50..89 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 108..157 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 60..77 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 407 AA; 43650 MW; F172E9B0482C9CF3 CRC64; MDSPCQPQPL SQALPQLPGS SSEPLEPEPG RARMGVESYL PCPLLPSYHC PGVPSEASAG SGTPRATATS TTASPLRDGF GGQDGGELRP LQSEGAAALV TKGCQRLAAQ GARPEAPKRK WAEDGGDAPS PSKRPWARQE NQEAEREGGM SCSCSSGSGE ASAGLMEEAL PSAPERLALD YIVPCMRYYG ICVKDSFLGA ALGGRVLAEV EALKRGGRLR DGQLVSQRAI PPRSIRGDQI AWVEGHEPGC RSIGALMAHV DAVIRHCAGR LGSYVINGRT KAMVACYPGN GLGYVRHVDN PHGDGRCITC IYYLNQNWDV KVHGGLLQIF PEGRPVVANI EPLFDRLLIF WSDRRNPHEV KPAYATRYAI TVWYFDAKER AAAKDKYQLA SGQKGVQVPV SQPPTPT //