OGFD1_BOVIN
ID OGFD1_BOVIN Reviewed; 542 AA.
AC Q3MI03;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 89.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) 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; BC104499; AAI04500.1; -; mRNA.
DR EMBL; EE245591; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_001160085.1; NM_001166613.1.
DR AlphaFoldDB; Q3MI03; -.
DR SMR; Q3MI03; -.
DR STRING; 9913.ENSBTAP00000032330; -.
DR PaxDb; Q3MI03; -.
DR PRIDE; Q3MI03; -.
DR Ensembl; ENSBTAT00000032397; ENSBTAP00000032330; ENSBTAG00000001171.
DR GeneID; 514141; -.
DR KEGG; bta:514141; -.
DR CTD; 55239; -.
DR VEuPathDB; HostDB:ENSBTAG00000001171; -.
DR VGNC; VGNC:32408; OGFOD1.
DR eggNOG; KOG3844; Eukaryota.
DR GeneTree; ENSGT00390000002349; -.
DR HOGENOM; CLU_027679_0_0_1; -.
DR InParanoid; Q3MI03; -.
DR OMA; YTDALLC; -.
DR OrthoDB; 623539at2759; -.
DR TreeFam; TF105920; -.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000001171; Expressed in oocyte and 106 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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:0019511; P:peptidyl-proline hydroxylation; IBA:GO_Central.
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_0000288973"
FT DOMAIN 134..239
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT REGION 371..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..387
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..416
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"
FT CONFLICT 269
FT /note="W -> G (in Ref. 1; EE245591)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 542 AA; 62747 MW; 4DF77573AA12B953 CRC64;
MNGKRPAEPG SDRAGKKVKK EVMAKFSDAV TEETLKKQVA EAWSRRTPFR HEAIVMDMDP
FLHCVIPNFI QSQNFLEGLQ KELLNLDFHE KYNDLYKFQQ SDDLKKRREP HICALRKILF
EHFRSWISDI SKIDLESTID MSCAKYEFSD ALLCHDDELE GRRIAFILYL VPPWDASLGG
TLDLFSVDEH FQPKQIVKSL IPSWNTLVFF EVSPVSFHQV SEVLSEEKSR LSISGWFHGP
SLTRPPTYFE PLIARSPHIP QDHEILYDWI NPTYLDMEYQ AQIQEEFEES SEILLKEFLQ
PEKFAEVCEA LERGRVEWSS RGPPNKRFYE KAEESQLPDI LRDCMALFRS EAMFLLLSNF
TGLKLHFLAP SEDEPEDKKE RDAVSAAENT EEGTSHSSSE PENSWAATSD SSLQSEGPTD
PEEDEAKKES SVPTCQGELR HWKTGHYTLI HDNSKTEFAL DLLLYCGCEG WEPEYGGFTS
YIAKGEDEEL LTVNPENNSL ALVYRDRETL KFVKHINHRS LEQKKSFPNR TGFWDFSFVY
YE
