OFD1_SCHPO
ID OFD1_SCHPO Reviewed; 515 AA.
AC Q11120;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Prolyl 3,4-dihydroxylase ofd1;
DE EC=1.14.11.- {ECO:0000269|PubMed:24550462};
DE AltName: Full=2-oxoglutarate and Fe(II) dioxygenase domain-containing protein 1;
DE AltName: Full=PKHD-type hydroxylase ofd1;
DE AltName: Full=uS12 prolyl 3,4-dihydroxylase;
GN Name=ofd1 {ECO:0000312|EMBL:CAA17051.1}; ORFNames=SPBC6B1.08c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1] {ECO:0000312|EMBL:BAA12034.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Okazaki K., Okayama H.;
RT "Fission yeast TPR gene involved in G0 transition.";
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:CAA17051.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3] {ECO:0000305}
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [4]
RP FUNCTION, INTERACTION WITH NRO1, AND MUTAGENESIS OF HIS-142 AND HIS-210.
RX PubMed=19158663; DOI=10.1038/emboj.2008.271;
RA Lee C.Y., Stewart E.V., Hughes B.T., Espenshade P.J.;
RT "Oxygen-dependent binding of Nro1 to the prolyl hydroxylase Ofd1 regulates
RT SREBP degradation in yeast.";
RL EMBO J. 28:135-143(2009).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=24550462; DOI=10.1073/pnas.1311750111;
RA Loenarz C., Sekirnik R., Thalhammer A., Ge W., Spivakovsky E.,
RA Mackeen M.M., McDonough M.A., Cockman M.E., Kessler B.M., Ratcliffe P.J.,
RA Wolf A., Schofield C.J.;
RT "Hydroxylation of the eukaryotic ribosomal decoding center affects
RT translational accuracy.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:4019-4024(2014).
CC -!- FUNCTION: Prolyl 3,4-dihydroxylase that catalyzes 3,4-dihydroxylation
CC of 'Pro-62' of small ribosomal subunit uS12 (rps23 and rps2302),
CC thereby regulating protein translation termination efficiency. Negative
CC regulator of the stability of the N-terminal transcription factor
CC domain (Sre1N) of sre1 which is released from the membrane and enters
CC the nucleus to activate hypoxic gene expression.
CC {ECO:0000269|PubMed:19158663, ECO:0000269|PubMed:24550462}.
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:0000269|PubMed:24550462};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + [ribosomal protein uS12]-(3S)-3-hydroxy-L-
CC proline + O2 = [ribosomal protein uS12]-(3S)-3,4-dihydroxy-L-proline
CC + CO2 + succinate; Xref=Rhea:RHEA:54160, Rhea:RHEA-COMP:13817,
CC Rhea:RHEA-COMP:13818, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:85428,
CC ChEBI:CHEBI:138052; Evidence={ECO:0000269|PubMed:24550462};
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:P40032, ECO:0000305};
CC -!- SUBUNIT: Monomer and homodimer (By similarity). Interacts with nro1
CC (PubMed:19158663). {ECO:0000250|UniProtKB:P40032,
CC ECO:0000269|PubMed:19158663}.
CC -!- INTERACTION:
CC Q11120; Q9USJ7: nro1; NbExp=11; IntAct=EBI-8549003, EBI-8549032;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the TPA1 family. {ECO:0000255}.
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DR EMBL; D83659; BAA12034.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA17051.1; -; Genomic_DNA.
DR PIR; T40649; T40649.
DR RefSeq; NP_596087.1; NM_001022001.2.
DR PDB; 6E0T; X-ray; 2.02 A; X=255-515.
DR PDBsum; 6E0T; -.
DR AlphaFoldDB; Q11120; -.
DR SMR; Q11120; -.
DR BioGRID; 277693; 16.
DR DIP; DIP-57179N; -.
DR IntAct; Q11120; 1.
DR MINT; Q11120; -.
DR STRING; 4896.SPBC6B1.08c.1; -.
DR MaxQB; Q11120; -.
DR PaxDb; Q11120; -.
DR EnsemblFungi; SPBC6B1.08c.1; SPBC6B1.08c.1:pep; SPBC6B1.08c.
DR GeneID; 2541179; -.
DR KEGG; spo:SPBC6B1.08c; -.
DR PomBase; SPBC6B1.08c; ofd1.
DR VEuPathDB; FungiDB:SPBC6B1.08c; -.
DR eggNOG; KOG3844; Eukaryota.
DR HOGENOM; CLU_017005_0_0_1; -.
DR InParanoid; Q11120; -.
DR OMA; YMAGDDD; -.
DR PhylomeDB; Q11120; -.
DR PRO; PR:Q11120; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
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:0019826; F:oxygen sensor activity; IDA:PomBase.
DR GO; GO:0031543; F:peptidyl-proline dioxygenase activity; IDA:UniProtKB.
DR GO; GO:0140311; F:protein sequestering activity; IPI:PomBase.
DR GO; GO:0071456; P:cellular response to hypoxia; IEP:PomBase.
DR GO; GO:2000639; P:negative regulation of SREBP signaling pathway; IMP:PomBase.
DR GO; GO:0018188; P:peptidyl-proline di-hydroxylation; IDA:UniProtKB.
DR GO; GO:0019511; P:peptidyl-proline hydroxylation; IBA:GO_Central.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:PomBase.
DR GO; GO:0006449; P:regulation of translational termination; IBA:GO_Central.
DR Gene3D; 3.60.130.20; -; 1.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR019601; Oxoglutarate/Fe-dep_Oase_C.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR InterPro; IPR043044; TPA1/Ofd1_C.
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 3D-structure; Cytoplasm; Dioxygenase; Iron; Metal-binding; Nucleus;
KW Oxidoreductase; Reference proteome; Transcription;
KW Transcription regulation; Vitamin C.
FT CHAIN 1..515
FT /note="Prolyl 3,4-dihydroxylase ofd1"
FT /id="PRO_0000315938"
FT DOMAIN 119..230
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 142
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P40032,
FT ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 144
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P40032,
FT ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 156
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:P40032"
FT BINDING 210
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P40032,
FT ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 221
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:P40032,
FT ECO:0000255|PROSITE-ProRule:PRU00805"
FT MUTAGEN 142
FT /note="H->A: Reduces nro1-binding and leads to constitutive
FT activity for sre1N degradation."
FT /evidence="ECO:0000269|PubMed:19158663"
FT MUTAGEN 210
FT /note="H->A: Reduces nro1-binding and leads to constitutive
FT activity for sre1N degradation."
FT /evidence="ECO:0000269|PubMed:19158663"
FT HELIX 278..284
FT /evidence="ECO:0007829|PDB:6E0T"
FT TURN 285..287
FT /evidence="ECO:0007829|PDB:6E0T"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:6E0T"
FT HELIX 295..308
FT /evidence="ECO:0007829|PDB:6E0T"
FT STRAND 309..315
FT /evidence="ECO:0007829|PDB:6E0T"
FT HELIX 319..334
FT /evidence="ECO:0007829|PDB:6E0T"
FT HELIX 341..343
FT /evidence="ECO:0007829|PDB:6E0T"
FT TURN 354..356
FT /evidence="ECO:0007829|PDB:6E0T"
FT STRAND 360..362
FT /evidence="ECO:0007829|PDB:6E0T"
FT HELIX 377..379
FT /evidence="ECO:0007829|PDB:6E0T"
FT HELIX 381..391
FT /evidence="ECO:0007829|PDB:6E0T"
FT STRAND 395..405
FT /evidence="ECO:0007829|PDB:6E0T"
FT TURN 407..409
FT /evidence="ECO:0007829|PDB:6E0T"
FT STRAND 421..428
FT /evidence="ECO:0007829|PDB:6E0T"
FT TURN 432..435
FT /evidence="ECO:0007829|PDB:6E0T"
FT HELIX 437..439
FT /evidence="ECO:0007829|PDB:6E0T"
FT STRAND 443..447
FT /evidence="ECO:0007829|PDB:6E0T"
FT STRAND 468..472
FT /evidence="ECO:0007829|PDB:6E0T"
FT STRAND 476..484
FT /evidence="ECO:0007829|PDB:6E0T"
FT STRAND 488..492
FT /evidence="ECO:0007829|PDB:6E0T"
FT HELIX 497..499
FT /evidence="ECO:0007829|PDB:6E0T"
FT STRAND 503..512
FT /evidence="ECO:0007829|PDB:6E0T"
SQ SEQUENCE 515 AA; 59178 MW; 4A6EBD870424EE0B CRC64;
MGDTQQPTVL DRFAPHALDT SEAERLSREY HKNGPYNHVV IRPLINDTLL RNVRKELMEN
IHFTEKVTDI YRVWQTGDLA NLDGLDKKEQ NMLKYLRQVR DALYSEEFRS HVQKITGCGP
LSASKKDLSV NVYSKGCHLM NHDDVIGTRC ISYILYLVEP DEGWKPEYGG ALRLFPTLQP
SFPAADFCHS IPPQWNQLSF FRVKPGHSFH DVEEVYVDKP RMAISGWFHY PQPGEPGYDA
NYCDNTVSTL QSLTMKQMDL ELPRFSYYPV VKPEPLSKQD TDILSNYINP LYLTPDGIEK
LSKRFFQDSV IVLVEFLNQE FANTLLKRII DAERQPTPMH SSEVSFPWKT AIPPHKHRYL
YLDHEEFGPD IILPMDLQRL PAFQRWIQLV SGLPLRSFHQ VGRRFRPGSD FTLATTNDTA
LLEATLCLSP GTGIANTDNG AYDIYMIGDE DPDVDAAVYR GDQQDDSILL SLPAAWNVFS
LVYRDEGVLQ FVKYVSRQAE SSRWDIYSQW NPVAE
