ID   OGFD3_RAT               Reviewed;         315 AA.
AC   Q5M843;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=2-oxoglutarate and iron-dependent oxygenase domain-containing protein 3;
DE            EC=1.14.11.-;
GN   Name=Ogfod3;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
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; BC088238; AAH88238.1; -; mRNA.
DR   RefSeq; NP_001013998.1; NM_001013976.1.
DR   AlphaFoldDB; Q5M843; -.
DR   SMR; Q5M843; -.
DR   IntAct; Q5M843; 1.
DR   STRING; 10116.ENSRNOP00000051808; -.
DR   GlyGen; Q5M843; 2 sites.
DR   PhosphoSitePlus; Q5M843; -.
DR   PaxDb; Q5M843; -.
DR   PRIDE; Q5M843; -.
DR   Ensembl; ENSRNOT00000054925; ENSRNOP00000051808; ENSRNOG00000036668.
DR   GeneID; 303749; -.
DR   KEGG; rno:303749; -.
DR   CTD; 79701; -.
DR   RGD; 1305007; Ogfod3.
DR   eggNOG; ENOG502QR2P; Eukaryota.
DR   GeneTree; ENSGT00390000005895; -.
DR   HOGENOM; CLU_042482_0_0_1; -.
DR   InParanoid; Q5M843; -.
DR   OMA; RVEKVLW; -.
DR   OrthoDB; 674380at2759; -.
DR   PhylomeDB; Q5M843; -.
DR   TreeFam; TF329031; -.
DR   PRO; PR:Q5M843; -.
DR   Proteomes; UP000002494; Chromosome 10.
DR   Bgee; ENSRNOG00000036668; Expressed in ovary and 19 other tissues.
DR   Genevisible; Q5M843; RN.
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_0000325887"
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..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..32
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;  7589FB5F286CD89D CRC64;
     MAPQRRGPPR VPEGNSAAER RHANSTKKDR LPQEAQRTWL RIVALGVSLA LVTFLLWSSA
     GIDDDVAEVV AHRGEVLEGR FIEVPCSEDY DGHRRFEGCT PRKCGRGVTD IVITREEAEQ
     IRRIAEKGLS LGGSDGGASI LDLHSGALSV GKHFVNLYRY FGDKIQTIFS EEDFQLYRDI
     RQKVQLTIAE AFGIRASLLY LTKPTFFSRI NSTEAQTAHD EYWHAHVDKV TYGSFDYTSL
     LYLSDYLEDF GGGRFVFMEE GSNKTVEPRA GRVSFFTSGS ENLHRVEKVL WGTRYAITIA
     FTCNPDHGIE DPVLT