OGFD1_XENLA
ID OGFD1_XENLA Reviewed; 511 AA.
AC Q6DE73;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 64.
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 Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-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; BC077268; AAH77268.1; -; mRNA.
DR RefSeq; NP_001086660.1; NM_001093191.1.
DR AlphaFoldDB; Q6DE73; -.
DR SMR; Q6DE73; -.
DR MaxQB; Q6DE73; -.
DR PRIDE; Q6DE73; -.
DR DNASU; 446495; -.
DR GeneID; 446495; -.
DR KEGG; xla:446495; -.
DR CTD; 446495; -.
DR Xenbase; XB-GENE-923206; ogfod1.L.
DR OrthoDB; 623539at2759; -.
DR Proteomes; UP000186698; Chromosome 4L.
DR Bgee; 446495; Expressed in pancreas and 19 other tissues.
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..511
FT /note="Prolyl 3-hydroxylase OGFOD1"
FT /id="PRO_0000288977"
FT DOMAIN 138..240
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 156
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P40032,
FT ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 158
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 170
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:P40032"
FT BINDING 219
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P40032,
FT ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 231
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:P40032,
FT ECO:0000255|PROSITE-ProRule:PRU00805"
SQ SEQUENCE 511 AA; 58296 MW; 60D4E385EC4D5E3B CRC64;
MTGKRGTAAG TDGSGNKKGK REFKAKLSGL LAEQTCRDSV KEAWEGNQGG QFGSVALDSV
PFPHGVIHPF IHNSDFLEEL KEELLNLNFQ PKSNDLYQFK QSEDLKNRKE SHIKALRHVL
FEDFRQWLSN ITNVELEKTV DISCAQYGYT DTLLCHDDEL EGRRFAFILY LVPEWSKSDG
GSLDLYGMDD NGQPGPIVKS LVPRWNSLVF FEVSPVSFHQ VSEVLSDGKC RLSVSGWFHG
CSLERPPRGL DHPPVRSPHI PHDDQILYEW INPSYLSLES QAQIQEEFEE RSEILLKDFL
KADKFQAICA ALETQSITLE KCGPPNKRCY DRAHGDFPGV IGSCMELLRS EAFFLFLSNF
TGLKLHFLAS NNEESDEGEG PSEPNTVSQQ GASSEDDKVP SCSGELRHWQ HSYYTMIHDL
DPERHEFALD LLLFCGCDDW EAEYGGFTSY IAKEEDEELL TVYPENNCLA LVYRDKETMR
FVKHINHKSQ QRDAKNTKHK GFWDFAFVYY E
