OSGEP_DANRE
ID OSGEP_DANRE Reviewed; 335 AA.
AC Q5RHZ6; Q561S3;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=tRNA N6-adenosine threonylcarbamoyltransferase {ECO:0000255|HAMAP-Rule:MF_03180};
DE EC=2.3.1.234 {ECO:0000255|HAMAP-Rule:MF_03180};
DE AltName: Full=O-sialoglycoprotein endopeptidase {ECO:0000255|HAMAP-Rule:MF_03180};
DE AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein osgep {ECO:0000255|HAMAP-Rule:MF_03180};
DE AltName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein osgep {ECO:0000255|HAMAP-Rule:MF_03180};
GN Name=osgep {ECO:0000255|HAMAP-Rule:MF_03180,
GN ECO:0000312|ZFIN:ZDB-GENE-030131-7880};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP DISRUPTION PHENOTYPE.
RX PubMed=29346415; DOI=10.1371/journal.pone.0191503;
RA Jobst-Schwan T., Schmidt J.M., Schneider R., Hoogstraten C.A.,
RA Ullmann J.F.P., Schapiro D., Majmundar A.J., Kolb A., Eddy K., Shril S.,
RA Braun D.A., Poduri A., Hildebrandt F.;
RT "Acute multi-sgRNA knockdown of KEOPS complex genes reproduces the
RT microcephaly phenotype of the stable knockout zebrafish model.";
RL PLoS ONE 13:E0191503-E0191503(2018).
RN [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=28805828; DOI=10.1038/ng.3933;
RA Braun D.A., Rao J., Mollet G., Schapiro D., Daugeron M.C., Tan W.,
RA Gribouval O., Boyer O., Revy P., Jobst-Schwan T., Schmidt J.M.,
RA Lawson J.A., Schanze D., Ashraf S., Ullmann J.F.P., Hoogstraten C.A.,
RA Boddaert N., Collinet B., Martin G., Liger D., Lovric S., Furlano M.,
RA Guerrera I.C., Sanchez-Ferras O., Hu J.F., Boschat A.C., Sanquer S.,
RA Menten B., Vergult S., De Rocker N., Airik M., Hermle T., Shril S.,
RA Widmeier E., Gee H.Y., Choi W.I., Sadowski C.E., Pabst W.L., Warejko J.K.,
RA Daga A., Basta T., Matejas V., Scharmann K., Kienast S.D., Behnam B.,
RA Beeson B., Begtrup A., Bruce M., Ch'ng G.S., Lin S.P., Chang J.H.,
RA Chen C.H., Cho M.T., Gaffney P.M., Gipson P.E., Hsu C.H., Kari J.A.,
RA Ke Y.Y., Kiraly-Borri C., Lai W.M., Lemyre E., Littlejohn R.O., Masri A.,
RA Moghtaderi M., Nakamura K., Ozaltin F., Praet M., Prasad C., Prytula A.,
RA Roeder E.R., Rump P., Schnur R.E., Shiihara T., Sinha M.D., Soliman N.A.,
RA Soulami K., Sweetser D.A., Tsai W.H., Tsai J.D., Topaloglu R., Vester U.,
RA Viskochil D.H., Vatanavicharn N., Waxler J.L., Wierenga K.J., Wolf M.T.F.,
RA Wong S.N., Leidel S.A., Truglio G., Dedon P.C., Poduri A., Mane S.,
RA Lifton R.P., Bouchard M., Kannu P., Chitayat D., Magen D., Callewaert B.,
RA van Tilbeurgh H., Zenker M., Antignac C., Hildebrandt F.;
RT "Mutations in KEOPS-complex genes cause nephrotic syndrome with primary
RT microcephaly.";
RL Nat. Genet. 49:1529-1538(2017).
CC -!- FUNCTION: Component of the EKC/KEOPS complex that is required for the
CC formation of a threonylcarbamoyl group on adenosine at position 37
CC (t(6)A37) in tRNAs that read codons beginning with adenine. The complex
CC is probably involved in the transfer of the threonylcarbamoyl moiety of
CC threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. OSGEP likely
CC plays a direct catalytic role in this reaction, but requires other
CC protein(s) of the complex to fulfill this activity. {ECO:0000255|HAMAP-
CC Rule:MF_03180}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP +
CC H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA;
CC Xref=Rhea:RHEA:37059, Rhea:RHEA-COMP:10162, Rhea:RHEA-COMP:10163,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:73682, ChEBI:CHEBI:74411,
CC ChEBI:CHEBI:74418, ChEBI:CHEBI:456215; EC=2.3.1.234;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03180};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03180};
CC Note=Binds 1 divalent metal cation per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_03180};
CC -!- SUBUNIT: Component of the EKC/KEOPS complex composed of at least
CC tp53rk, tprkb, osgep and lage3; the whole complex dimerizes.
CC {ECO:0000255|HAMAP-Rule:MF_03180}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03180}.
CC Nucleus {ECO:0000255|HAMAP-Rule:MF_03180}.
CC -!- DISRUPTION PHENOTYPE: Embryos display primary microcephaly, leading to
CC early lethality (PubMed:29346415, PubMed:28805828). Marked apoptosis is
CC observed in the brain (telencephalon) (PubMed:28805828). Fishes do not
CC show a renal phenotype, possibly as a result of early lethality
CC (PubMed:28805828). {ECO:0000269|PubMed:28805828,
CC ECO:0000269|PubMed:29346415}.
CC -!- SIMILARITY: Belongs to the KAE1 / TsaD family. {ECO:0000255|HAMAP-
CC Rule:MF_03180}.
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DR EMBL; BX323558; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC093366; AAH93366.1; -; mRNA.
DR EMBL; BC164136; AAI64136.1; -; mRNA.
DR RefSeq; NP_001017751.2; NM_001017751.2.
DR AlphaFoldDB; Q5RHZ6; -.
DR SMR; Q5RHZ6; -.
DR STRING; 7955.ENSDARP00000118646; -.
DR PaxDb; Q5RHZ6; -.
DR PRIDE; Q5RHZ6; -.
DR DNASU; 550447; -.
DR Ensembl; ENSDART00000067375; ENSDARP00000067374; ENSDARG00000045846.
DR Ensembl; ENSDART00000144225; ENSDARP00000118646; ENSDARG00000045846.
DR GeneID; 550447; -.
DR KEGG; dre:550447; -.
DR CTD; 55644; -.
DR ZFIN; ZDB-GENE-030131-7880; osgep.
DR eggNOG; KOG2708; Eukaryota.
DR GeneTree; ENSGT00940000153744; -.
DR HOGENOM; CLU_023208_2_2_1; -.
DR InParanoid; Q5RHZ6; -.
DR OMA; MRIMCEE; -.
DR OrthoDB; 829465at2759; -.
DR PhylomeDB; Q5RHZ6; -.
DR TreeFam; TF313621; -.
DR PRO; PR:Q5RHZ6; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 4.
DR Bgee; ENSDARG00000045846; Expressed in presomitic mesoderm and 24 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0000408; C:EKC/KEOPS complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061711; F:N(6)-L-threonylcarbamoyladenine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; ISS:UniProtKB.
DR HAMAP; MF_01446; Kae1; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR000905; Gcp-like_dom.
DR InterPro; IPR017861; KAE1/TsaD.
DR InterPro; IPR034680; Kae1_archaea_euk.
DR InterPro; IPR017860; Peptidase_M22_CS.
DR PANTHER; PTHR11735; PTHR11735; 1.
DR PANTHER; PTHR11735:SF14; PTHR11735:SF14; 1.
DR Pfam; PF00814; TsaD; 1.
DR PRINTS; PR00789; OSIALOPTASE.
DR SUPFAM; SSF53067; SSF53067; 1.
DR TIGRFAMs; TIGR00329; gcp_kae1; 1.
DR PROSITE; PS01016; GLYCOPROTEASE; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Cytoplasm; Metal-binding; Nucleus; Reference proteome;
KW Transferase; tRNA processing.
FT CHAIN 1..335
FT /note="tRNA N6-adenosine threonylcarbamoyltransferase"
FT /id="PRO_0000444043"
FT BINDING 109
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT BINDING 113
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT BINDING 130..134
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT BINDING 130
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT BINDING 162
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT BINDING 181
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT BINDING 266
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT BINDING 294
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT CONFLICT 284
FT /note="I -> L (in Ref. 2; AAH93366/AAI64136)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 335 AA; 36728 MW; D7D36716D9DA69A2 CRC64;
MTIVIGFEGS ANKIGIGIIK DGEVLSNPRR TYITPPGQGF LPGETAKHHR SVILTVLQEA
LDEAGLKAAD IDCVAYTKGP GMGAPLVTVA IVARTVAQLW GKPLLGVNHC IGHIEMGRLI
TNAQNPTVLY VSGGNTQVIA YSERRYRIFG ETIDIAVGNC LDRFARVIKI SNDPSPGYNI
EQMAKKGNKY IELPYTVKGM DVSFSGILSY IEDAAHKMLS TDQCTPEDLC FSLQETVFAM
LVEITERAMA HCGSQEVLIV GGVGCNLRLQ EMMGVMCKER GARIFATDES FCIDNGAMIA
QAGWEMFRSG HVTELPDSWI TQRYRTDEVE VTWRD
