OGFD1_DROME
ID OGFD1_DROME Reviewed; 536 AA.
AC Q9I7H9;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Prolyl 3-hydroxylase sudestada1;
DE EC=1.14.11.-;
DE AltName: Full=2-oxoglutarate and iron-dependent oxygenase domain-containing protein 1 homolog;
DE AltName: Full=uS12 prolyl 3-hydroxylase;
GN Name=sud1; ORFNames=CG18761, CG31120, CG44254;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=24550463; DOI=10.1073/pnas.1314485111;
RA Katz M.J., Acevedo J.M., Loenarz C., Galagovsky D., Liu-Yi P.,
RA Perez-Pepe M., Thalhammer A., Sekirnik R., Ge W., Melani M., Thomas M.G.,
RA Simonetta S., Boccaccio G.L., Schofield C.J., Cockman M.E., Ratcliffe P.J.,
RA Wappner P.;
RT "Sudestada1, a Drosophila ribosomal prolyl-hydroxylase required for mRNA
RT translation, cell homeostasis, and organ growth.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:4025-4030(2014).
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. {ECO:0000269|PubMed:24550463}.
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: Nucleus {ECO:0000269|PubMed:24550463}. Cytoplasm
CC {ECO:0000269|PubMed:24550463}. Note=Localizes predominantly to the
CC nucleus. Present at lower levels are also detected in the cytoplasm.
CC -!- TISSUE SPECIFICITY: In third-instar larval tissues,highly expressed in
CC the fat body, with significant expression in other organs including the
CC brain, salivary glands, imaginal disks and gut.
CC {ECO:0000269|PubMed:24550463}.
CC -!- DEVELOPMENTAL STAGE: Expressed at all developmental stages, with the
CC highest levels at the first larval instar.
CC {ECO:0000269|PubMed:24550463}.
CC -!- SIMILARITY: Belongs to the TPA1 family. {ECO:0000305}.
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DR EMBL; AE014297; AAG22170.1; -; Genomic_DNA.
DR EMBL; AY058522; AAL13751.1; -; mRNA.
DR RefSeq; NP_733061.1; NM_170182.3.
DR AlphaFoldDB; Q9I7H9; -.
DR SMR; Q9I7H9; -.
DR BioGRID; 2593515; 2.
DR IntAct; Q9I7H9; 28.
DR PRIDE; Q9I7H9; -.
DR DNASU; 19834718; -.
DR EnsemblMetazoa; FBtr0339113; FBpp0308258; FBgn0265189.
DR GeneID; 19834718; -.
DR KEGG; dme:Dmel_CG44254; -.
DR UCSC; CG31120-RA; d. melanogaster.
DR CTD; 19834718; -.
DR FlyBase; FBgn0265189; sud1.
DR VEuPathDB; VectorBase:FBgn0265189; -.
DR GeneTree; ENSGT00390000002349; -.
DR HOGENOM; CLU_027679_0_0_1; -.
DR InParanoid; Q9I7H9; -.
DR OMA; SCYARTD; -.
DR OrthoDB; 623539at2759; -.
DR BioGRID-ORCS; 19834718; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 19834718; -.
DR PRO; PR:Q9I7H9; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0265189; Expressed in oocyte and 27 other tissues.
DR Genevisible; Q9I7H9; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0031418; F:L-ascorbic acid binding; ISM:FlyBase.
DR GO; GO:0031543; F:peptidyl-proline dioxygenase activity; IDA:UniProtKB.
DR GO; GO:0019511; P:peptidyl-proline hydroxylation; IMP:FlyBase.
DR GO; GO:0018126; P:protein hydroxylation; IDA:UniProtKB.
DR GO; GO:0006417; P:regulation of translation; IMP:UniProtKB.
DR GO; GO:0006449; P:regulation of translational termination; IBA:GO_Central.
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..536
FT /note="Prolyl 3-hydroxylase sudestada1"
FT /id="PRO_0000429171"
FT DOMAIN 165..275
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 185
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P40032,
FT ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 187
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 199
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:P40032"
FT BINDING 254
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P40032,
FT ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 266
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ SEQUENCE 536 AA; 61193 MW; 93ADAD52DAED3DCC CRC64;
METSSSSPVK PRRKDKDEDG RAEQEDSADQ VGEPHRKLLR LGDILETNEV LLNEAYQQPE
LTKWLQTAWT EEKSQGTKET QTGAQVFSDP FQICLLPGML EKGQSQALVA EIIQKVQWSR
KQMDLYEFYQ SADLSNMPAC RLLTNFLQVL RKQVRPWLEK VTNLKLDYVS ASCSMYTCGD
YLLVHDDLLK DRQVAFIYYL SPWEGAEEWT DEQGGCLEIF GSDDQCFPQF PVQRKIAPKD
NQFAFFKVGS RSFHQVGEVT TFDYPRLTIN GWFHGDTNEA FVADSLRAFP RLNYLQPDGL
NRPPLGLFLN NVYLKGATRR SIQKRIEENS EICLYEFFKR EKFELARSQL LADSDTLKWR
RQGPANAHNY EVLDLTTARG TILELLQLFR SHAMFDLLRD FTDLDLAGTD AESPTCSVEL
QRWSHGNYTV LGDGLTSEEN TLDLVYYLNA AEGAAVITYL APDAEMPTAK APTDGRRSDY
DDEEEDDSVL LTITPVDNAL NIVYRCEGTT KFTKYVSRNT PLEKGPVFVI SCSYKE
