OGFD1_PONAB
ID OGFD1_PONAB Reviewed; 542 AA.
AC Q5R4R3;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Prolyl 3-hydroxylase OGFOD1;
DE EC=1.14.11.-;
DE AltName: Full=2-oxoglutarate and iron-dependent oxygenase domain-containing protein 1;
DE AltName: Full=uS12 prolyl 3-hydroxylase;
GN Name=OGFOD1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Prolyl 3-hydroxylase that catalyzes 3-hydroxylation of 'Pro-
CC 62' of small ribosomal subunit uS12 (RPS23), thereby regulating protein
CC translation termination efficiency. Involved in stress granule
CC formation. {ECO:0000250|UniProtKB:Q8N543}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + [ribosomal protein uS12]-L-proline + O2 =
CC [ribosomal protein uS12]-(3S)-3-hydroxy-L-proline + CO2 + succinate;
CC Xref=Rhea:RHEA:54156, Rhea:RHEA-COMP:13816, Rhea:RHEA-COMP:13818,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:50342, ChEBI:CHEBI:85428;
CC Evidence={ECO:0000250|UniProtKB:Q8N543};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00805};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00805};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000250|UniProtKB:Q8N543};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q8N543}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8N543}. Nucleus
CC {ECO:0000250|UniProtKB:Q8N543}.
CC -!- SIMILARITY: Belongs to the TPA1 family. {ECO:0000305}.
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DR EMBL; CR861181; CAH93253.1; -; mRNA.
DR RefSeq; NP_001128994.1; NM_001135522.1.
DR AlphaFoldDB; Q5R4R3; -.
DR SMR; Q5R4R3; -.
DR STRING; 9601.ENSPPYP00000008320; -.
DR GeneID; 100190834; -.
DR KEGG; pon:100190834; -.
DR CTD; 55239; -.
DR eggNOG; KOG3844; Eukaryota.
DR InParanoid; Q5R4R3; -.
DR OrthoDB; 623539at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0031544; F:peptidyl-proline 3-dioxygenase activity; ISS:UniProtKB.
DR GO; GO:0031543; F:peptidyl-proline dioxygenase activity; ISS:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; ISS:UniProtKB.
DR GO; GO:0018126; P:protein hydroxylation; ISS:UniProtKB.
DR GO; GO:0006449; P:regulation of translational termination; ISS:UniProtKB.
DR GO; GO:0034063; P:stress granule assembly; ISS:UniProtKB.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR019601; Oxoglutarate/Fe-dep_Oase_C.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR InterPro; IPR039558; TPA1/OFD1_N.
DR Pfam; PF13661; 2OG-FeII_Oxy_4; 1.
DR Pfam; PF10637; Ofd1_CTDD; 1.
DR SMART; SM00702; P4Hc; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Dioxygenase; Iron; Metal-binding; Nucleus; Oxidoreductase;
KW Reference proteome; Vitamin C.
FT CHAIN 1..542
FT /note="Prolyl 3-hydroxylase OGFOD1"
FT /id="PRO_0000288976"
FT DOMAIN 134..239
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT REGION 373..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..388
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 155
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P40032,
FT ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 157
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 169
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:P40032"
FT BINDING 218
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P40032,
FT ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 230
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:P40032,
FT ECO:0000255|PROSITE-ProRule:PRU00805"
SQ SEQUENCE 542 AA; 63159 MW; 9AE3DE1060611694 CRC64;
MNGKRPAEPG PARVGKKRKK EVMAEFSDAV TEETLKKQVA EAWSRRTPFS HEVIVMDMDP
FLHCVIPNFI QSQDFLEGLQ KELMNLDFHE KYNDLYKFQQ SDDLKKRREP HISALRKILF
EDFRSWLSDI SKIDLESTID MSCAKYEFTD ALLCHDDELE GRRIAFILYL VPPWDRSLGG
TLDLYSIDEH FQPKQIVKSL IPSWNKLVFF EVSPVSFHQV SEVLSEEKSR LSISGWFHGP
SLTRPPNHFE PPIPRSPHIP QDHEILYDWI NPTYLDMDYQ VQIQEEFEES SEILLKEFLK
PEKFMKVCEA LEHGDVEWSS RGPPNKRFYE KAEESKLPEI LKECMKLFHS EALFLLLSNF
TGLKLHFLAP SEEDEMNDKK EAEAADITEE GTSHSPPEPE NNQTAISNNS QQSNEQTDPE
PEENETKKES SVPTCQGELR RWKTGHYTLI HDHSKAEFAL DLILYCGCEG WEPEYGGFTS
YIAKGEDEEL LTVNPESNSL ALVYRDRETL KFVKHINHRS LEQKKTFPNR TGFWDFSFIY
YE
