OGFD1_MOUSE
ID OGFD1_MOUSE Reviewed; 545 AA.
AC Q3U0K8; Q3TLS5; Q3TPR4; Q80TB3; Q8CFR6;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
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; Synonyms=Kiaa1612;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 9-545 (ISOFORM 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Hippocampus, Mammary gland, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-545 (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q3U0K8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3U0K8-2; Sequence=VSP_025854;
CC Name=3;
CC IsoId=Q3U0K8-3; Sequence=VSP_025853;
CC -!- SIMILARITY: Belongs to the TPA1 family. {ECO:0000305}.
CC -!- CAUTION: Contains Thr-228 instead of the expected predicted active site
CC Lys. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH40267.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK156765; BAE33844.1; -; mRNA.
DR EMBL; AK164189; BAE37671.1; -; mRNA.
DR EMBL; AK166343; BAE38717.1; -; mRNA.
DR EMBL; BC040267; AAH40267.1; ALT_INIT; mRNA.
DR EMBL; AK122532; BAC65814.1; -; mRNA.
DR CCDS; CCDS22535.2; -. [Q3U0K8-1]
DR CCDS; CCDS52636.1; -. [Q3U0K8-2]
DR RefSeq; NP_001087226.1; NM_001093757.1. [Q3U0K8-2]
DR RefSeq; NP_808435.3; NM_177767.4. [Q3U0K8-1]
DR AlphaFoldDB; Q3U0K8; -.
DR SMR; Q3U0K8; -.
DR BioGRID; 234757; 14.
DR STRING; 10090.ENSMUSP00000105183; -.
DR iPTMnet; Q3U0K8; -.
DR PhosphoSitePlus; Q3U0K8; -.
DR EPD; Q3U0K8; -.
DR MaxQB; Q3U0K8; -.
DR PaxDb; Q3U0K8; -.
DR PeptideAtlas; Q3U0K8; -.
DR PRIDE; Q3U0K8; -.
DR ProteomicsDB; 293927; -. [Q3U0K8-1]
DR ProteomicsDB; 293928; -. [Q3U0K8-2]
DR ProteomicsDB; 293929; -. [Q3U0K8-3]
DR Antibodypedia; 756; 208 antibodies from 26 providers.
DR DNASU; 270086; -.
DR Ensembl; ENSMUST00000093301; ENSMUSP00000090991; ENSMUSG00000033009. [Q3U0K8-2]
DR Ensembl; ENSMUST00000109556; ENSMUSP00000105183; ENSMUSG00000033009. [Q3U0K8-1]
DR GeneID; 270086; -.
DR KEGG; mmu:270086; -.
DR UCSC; uc009mvq.1; mouse. [Q3U0K8-1]
DR UCSC; uc009mvr.1; mouse. [Q3U0K8-2]
DR UCSC; uc012gim.1; mouse. [Q3U0K8-3]
DR CTD; 55239; -.
DR MGI; MGI:2442978; Ogfod1.
DR VEuPathDB; HostDB:ENSMUSG00000033009; -.
DR eggNOG; KOG3844; Eukaryota.
DR GeneTree; ENSGT00390000002349; -.
DR InParanoid; Q3U0K8; -.
DR OMA; YTDALLC; -.
DR OrthoDB; 623539at2759; -.
DR PhylomeDB; Q3U0K8; -.
DR TreeFam; TF105920; -.
DR BioGRID-ORCS; 270086; 7 hits in 72 CRISPR screens.
DR ChiTaRS; Ogfod1; mouse.
DR PRO; PR:Q3U0K8; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q3U0K8; protein.
DR Bgee; ENSMUSG00000033009; Expressed in ventromedial nucleus of hypothalamus and 225 other tissues.
DR ExpressionAtlas; Q3U0K8; baseline and differential.
DR Genevisible; Q3U0K8; MM.
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; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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; ISO:MGI.
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 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Dioxygenase; Iron; Metal-binding; Nucleus;
KW Oxidoreductase; Reference proteome; Vitamin C.
FT CHAIN 1..545
FT /note="Prolyl 3-hydroxylase OGFOD1"
FT /id="PRO_0000288975"
FT DOMAIN 137..239
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..418
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 VAR_SEQ 52
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12693553"
FT /id="VSP_025853"
FT VAR_SEQ 220..262
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_025854"
FT CONFLICT 12
FT /note="A -> V (in Ref. 1; BAE38717)"
FT /evidence="ECO:0000305"
FT CONFLICT 48
FT /note="P -> S (in Ref. 1; BAE38717)"
FT /evidence="ECO:0000305"
FT CONFLICT 58
FT /note="M -> V (in Ref. 1; BAE38717)"
FT /evidence="ECO:0000305"
FT CONFLICT 80
FT /note="H -> Q (in Ref. 1; BAE38717)"
FT /evidence="ECO:0000305"
FT CONFLICT 397
FT /note="R -> Q (in Ref. 1; BAE38717)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 545 AA; 62734 MW; 92F376ABC86CB410 CRC64;
MNGKRPADPG PARPMKKGKK QVSAEFSDAV TEEILRKQVA EAWSCRTPFS HEAIALDMDP
FLHCVIPNFI QSQDFLEGLH KELLSLDFHE KYNDLYKFQQ SDDLKNRKEP HISALRKLMF
EDFRAWLSKV SGIDLEPTID MSCAKYEFTD ALLCHDDELE GRRIAFILYL VPSWDRDLGG
TLDLYDTDEH LQPKQIVKSL IPSWNKLVFF EVSPVSFHQV SEVLSEETSR LSISGWFYGP
SLTRPPTYFE PPIPRNPHIP QDHEILYEWI NPAYLEMDYQ MQIQEEFEER SEILLKEFLK
PEKFAEVCEA LEKGDVEWKS HGPPNKRFYE KAEENNLPDV LKECMGLFRS EALFLLLSNL
TGLKLHFLAP SEDDETEEKG EGETASAAAG TEEGTSRRPS GPENNQVAAG SHSQENGEQA
DPEAQEEEAK KESSVPMCQG ELRRWKTGHY TLVHDNTKTE FALDLFLYCG CEGWEPEYGG
FTSYIAKGED EELLIVNPEN NSLALVYRDR ETLRFVKHIN HRSLEQSKAF PSRSGFWDFA
FIYYE
