OGFD2_MOUSE
ID OGFD2_MOUSE Reviewed; 349 AA.
AC Q9CQ04; Q78IV7; Q8BMW3;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=2-oxoglutarate and iron-dependent oxygenase domain-containing protein 2;
DE EC=1.14.11.-;
GN Name=Ogfod2;
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].
RC STRAIN=C57BL/6J; TISSUE=Colon, Embryo, and Liver;
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].
RC STRAIN=FVB/N; TISSUE=Colon, and Salivary gland;
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).
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; Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the OGFOD2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH22762.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC25517.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK004943; BAB23687.1; -; mRNA.
DR EMBL; AK017497; BAC25517.1; ALT_FRAME; mRNA.
DR EMBL; AK018534; BAB31259.1; -; mRNA.
DR EMBL; BC022762; AAH22762.1; ALT_INIT; mRNA.
DR EMBL; BC069872; AAH69872.1; -; mRNA.
DR CCDS; CCDS19672.1; -.
DR RefSeq; NP_079947.1; NM_025671.2.
DR AlphaFoldDB; Q9CQ04; -.
DR SMR; Q9CQ04; -.
DR STRING; 10090.ENSMUSP00000024470; -.
DR PhosphoSitePlus; Q9CQ04; -.
DR EPD; Q9CQ04; -.
DR MaxQB; Q9CQ04; -.
DR PaxDb; Q9CQ04; -.
DR PRIDE; Q9CQ04; -.
DR ProteomicsDB; 294166; -.
DR Antibodypedia; 31731; 132 antibodies from 26 providers.
DR Ensembl; ENSMUST00000024470; ENSMUSP00000024470; ENSMUSG00000023707.
DR GeneID; 66627; -.
DR KEGG; mmu:66627; -.
DR UCSC; uc008zox.1; mouse.
DR CTD; 79676; -.
DR MGI; MGI:1913877; Ogfod2.
DR VEuPathDB; HostDB:ENSMUSG00000023707; -.
DR eggNOG; KOG1971; Eukaryota.
DR GeneTree; ENSGT00940000153974; -.
DR HOGENOM; CLU_045835_1_0_1; -.
DR InParanoid; Q9CQ04; -.
DR OMA; FYTCSCF; -.
DR OrthoDB; 756511at2759; -.
DR PhylomeDB; Q9CQ04; -.
DR TreeFam; TF329650; -.
DR BioGRID-ORCS; 66627; 4 hits in 73 CRISPR screens.
DR PRO; PR:Q9CQ04; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9CQ04; protein.
DR Bgee; ENSMUSG00000023707; Expressed in spermatocyte and 222 other tissues.
DR ExpressionAtlas; Q9CQ04; baseline and differential.
DR Genevisible; Q9CQ04; MM.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
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:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR SMART; SM00702; P4Hc; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 2: Evidence at transcript level;
KW Dioxygenase; Iron; Metal-binding; Oxidoreductase; Reference proteome;
KW Vitamin C.
FT CHAIN 1..349
FT /note="2-oxoglutarate and iron-dependent oxygenase domain-
FT containing protein 2"
FT /id="PRO_0000288979"
FT DOMAIN 214..308
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 234
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 236
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 289
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 299
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT CONFLICT 8
FT /note="R -> G (in Ref. 1; BAC25517)"
FT /evidence="ECO:0000305"
FT CONFLICT 47
FT /note="S -> T (in Ref. 1; BAC25517)"
FT /evidence="ECO:0000305"
FT CONFLICT 72..73
FT /note="RL -> SV (in Ref. 1; BAC25517)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 349 AA; 39270 MW; E03BA81E019BB194 CRC64;
MATAAQRRFC RCACFCSQNL YVARYGLHLR FRDEHQLRRD YGQLLRSRGC VTSKDFQQLL
EELEQEVGRR RRLGQESAVR KALIASSYHP ARPEVYSSLQ DAALAPEFMA AAEYSTSPGA
DLEGLLQRLE TVSEEKRIYR VPVFSAKFCQ TLLEELEHFE QSDMPKGRPN TMNNHGVLMY
ELGLDDPLVT PLRERFLLPL MALLYPDYGG GYLDSHRAFV VKYALGQDLD LGCHYDNAEL
TLNVALGKDF TGGALYFGGL FQAPAALKET LEVEHVVGSG ILHRGGQLHG ARPLCKGERW
NLVVWLRASA VRNRLCPMCC QKPELVDDEG FGDGFTREEP TTVDVCVLT
