OGFD3_MOUSE
ID OGFD3_MOUSE Reviewed; 315 AA.
AC Q9D136;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=2-oxoglutarate and iron-dependent oxygenase domain-containing protein 3;
DE EC=1.14.11.-;
GN Name=Ogfod3;
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=BALB/cJ, and C57BL/6J; TISSUE=Embryo, and Placenta;
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=Kidney;
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the OGFOD3 family. {ECO:0000305}.
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DR EMBL; AK004005; BAB23119.1; -; mRNA.
DR EMBL; AK145938; BAE26768.1; -; mRNA.
DR EMBL; AK168300; BAE40241.1; -; mRNA.
DR EMBL; BC024349; AAH24349.1; -; mRNA.
DR CCDS; CCDS25770.1; -.
DR RefSeq; NP_079678.1; NM_025402.2.
DR AlphaFoldDB; Q9D136; -.
DR SMR; Q9D136; -.
DR STRING; 10090.ENSMUSP00000026169; -.
DR GlyConnect; 2097; 1 N-Linked glycan (1 site).
DR GlyGen; Q9D136; 2 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q9D136; -.
DR PhosphoSitePlus; Q9D136; -.
DR EPD; Q9D136; -.
DR MaxQB; Q9D136; -.
DR PaxDb; Q9D136; -.
DR PeptideAtlas; Q9D136; -.
DR PRIDE; Q9D136; -.
DR ProteomicsDB; 293930; -.
DR Antibodypedia; 63655; 15 antibodies from 8 providers.
DR DNASU; 66179; -.
DR Ensembl; ENSMUST00000026169; ENSMUSP00000026169; ENSMUSG00000025169.
DR GeneID; 66179; -.
DR KEGG; mmu:66179; -.
DR UCSC; uc007mvk.1; mouse.
DR CTD; 79701; -.
DR MGI; MGI:1913429; Ogfod3.
DR VEuPathDB; HostDB:ENSMUSG00000025169; -.
DR eggNOG; ENOG502QR2P; Eukaryota.
DR GeneTree; ENSGT00390000005895; -.
DR HOGENOM; CLU_042482_0_0_1; -.
DR InParanoid; Q9D136; -.
DR OMA; RVEKVLW; -.
DR OrthoDB; 674380at2759; -.
DR PhylomeDB; Q9D136; -.
DR TreeFam; TF329031; -.
DR BioGRID-ORCS; 66179; 1 hit in 71 CRISPR screens.
DR PRO; PR:Q9D136; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9D136; protein.
DR Bgee; ENSMUSG00000025169; Expressed in epithelium of lens and 227 other tissues.
DR Genevisible; Q9D136; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IPR039210; OGFOD3.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY.
DR PANTHER; PTHR14650; PTHR14650; 1.
DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR SMART; SM00702; P4Hc; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 2: Evidence at transcript level;
KW Dioxygenase; Glycoprotein; Iron; Membrane; Metal-binding; Oxidoreductase;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix;
KW Vitamin C.
FT CHAIN 1..315
FT /note="2-oxoglutarate and iron-dependent oxygenase domain-
FT containing protein 3"
FT /id="PRO_0000325886"
FT TOPO_DOM 1..41
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..62
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..315
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 203..305
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 294
FT /evidence="ECO:0000255"
FT BINDING 226
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 228
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 284
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 294
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 315 AA; 35385 MW; 7D4C5CD55F55EA36 CRC64;
MAPQRRGPPR IPEGSSAAER RRATSTKKDR LPREAQRTWL RIVAFGVGLA LVTCLLWSSV
GIDDDVAEVV ARRGEVLEGR FIEVPCSEDY DGHRRFEGCT PRKCGRGVTD IVITREEAEQ
IRRIAEKGLS LGGSDGGASI LDLHSGALSV GKHFVNLYRY FGDKIQNIFS EEDFQLYRDI
RQKVQLTIAE AFGISASLLY LTKPTFFSRI NSTEARTAHD EYWHAHVDKV TYGSFDYTSL
LYLSDYLEDF GGGRFVFMEE GSNKTVEPRA GRVSFFTSGS ENLHRVEKVL WGTRYAITIA
FTCNPDHGIE DPVLT
