OSGL1_MOUSE
ID OSGL1_MOUSE Reviewed; 414 AA.
AC Q6PEB4; Q3UVG1; Q8BLB6; Q9D0N0;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=tRNA N6-adenosine threonylcarbamoyltransferase, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03179};
DE EC=2.3.1.234 {ECO:0000255|HAMAP-Rule:MF_03179};
DE AltName: Full=N6-L-threonylcarbamoyladenine synthase {ECO:0000255|HAMAP-Rule:MF_03179};
DE Short=t(6)A synthase {ECO:0000255|HAMAP-Rule:MF_03179};
DE AltName: Full=O-sialoglycoprotein endopeptidase-like protein 1 {ECO:0000255|HAMAP-Rule:MF_03179};
DE AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein Osgepl1 {ECO:0000255|HAMAP-Rule:MF_03179};
DE AltName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein Osgepl1 {ECO:0000255|HAMAP-Rule:MF_03179};
DE Flags: Precursor;
GN Name=Osgepl1 {ECO:0000255|HAMAP-Rule:MF_03179};
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Corpora quadrigemina, and Embryo;
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] (ISOFORM 1).
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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).
RN [3]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-299, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC -!- FUNCTION: Required for the formation of a threonylcarbamoyl group on
CC adenosine at position 37 (t(6)A37) in mitochondrial tRNAs that read
CC codons beginning with adenine. Probably involved in the transfer of the
CC threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6
CC group of A37. Involved in mitochondrial genome maintenance.
CC {ECO:0000255|HAMAP-Rule:MF_03179}.
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_03179};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03179};
CC Note=Binds 1 divalent metal cation per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_03179};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_03179}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03179}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6PEB4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6PEB4-2; Sequence=VSP_028831, VSP_028832;
CC -!- SIMILARITY: Belongs to the KAE1 / TsaD family. {ECO:0000255|HAMAP-
CC Rule:MF_03179}.
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DR EMBL; AK011265; BAB27506.1; -; mRNA.
DR EMBL; AK045669; BAC32450.1; -; mRNA.
DR EMBL; AK137332; BAE23308.1; -; mRNA.
DR EMBL; BC058172; AAH58172.1; -; mRNA.
DR CCDS; CCDS14953.1; -. [Q6PEB4-1]
DR RefSeq; NP_001272768.1; NM_001285839.1. [Q6PEB4-1]
DR AlphaFoldDB; Q6PEB4; -.
DR SMR; Q6PEB4; -.
DR STRING; 10090.ENSMUSP00000110128; -.
DR iPTMnet; Q6PEB4; -.
DR PhosphoSitePlus; Q6PEB4; -.
DR MaxQB; Q6PEB4; -.
DR PaxDb; Q6PEB4; -.
DR PRIDE; Q6PEB4; -.
DR ProteomicsDB; 294226; -. [Q6PEB4-1]
DR ProteomicsDB; 294227; -. [Q6PEB4-2]
DR Antibodypedia; 34028; 76 antibodies from 21 providers.
DR DNASU; 72085; -.
DR Ensembl; ENSMUST00000027265; ENSMUSP00000027265; ENSMUSG00000026096. [Q6PEB4-1]
DR Ensembl; ENSMUST00000114484; ENSMUSP00000110128; ENSMUSG00000026096. [Q6PEB4-1]
DR Ensembl; ENSMUST00000135614; ENSMUSP00000137994; ENSMUSG00000026096. [Q6PEB4-2]
DR GeneID; 72085; -.
DR KEGG; mmu:72085; -.
DR UCSC; uc007aza.2; mouse. [Q6PEB4-1]
DR CTD; 64172; -.
DR MGI; MGI:1919335; Osgepl1.
DR VEuPathDB; HostDB:ENSMUSG00000026096; -.
DR eggNOG; KOG2707; Eukaryota.
DR GeneTree; ENSGT00940000153744; -.
DR HOGENOM; CLU_023208_1_2_1; -.
DR InParanoid; Q6PEB4; -.
DR OMA; HLEGHIY; -.
DR OrthoDB; 656684at2759; -.
DR PhylomeDB; Q6PEB4; -.
DR TreeFam; TF314600; -.
DR BioGRID-ORCS; 72085; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Osgepl1; mouse.
DR PRO; PR:Q6PEB4; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q6PEB4; protein.
DR Bgee; ENSMUSG00000026096; Expressed in interventricular septum and 220 other tissues.
DR ExpressionAtlas; Q6PEB4; baseline and differential.
DR Genevisible; Q6PEB4; MM.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061711; F:N(6)-L-threonylcarbamoyladenine synthase activity; ISS:UniProtKB.
DR GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; ISS:UniProtKB.
DR HAMAP; MF_01445; TsaD; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR000905; Gcp-like_dom.
DR InterPro; IPR017861; KAE1/TsaD.
DR InterPro; IPR022450; TsaD.
DR PANTHER; PTHR11735; PTHR11735; 1.
DR PANTHER; PTHR11735:SF6; PTHR11735:SF6; 1.
DR Pfam; PF00814; TsaD; 1.
DR PRINTS; PR00789; OSIALOPTASE.
DR SUPFAM; SSF53067; SSF53067; 1.
DR TIGRFAMs; TIGR00329; gcp_kae1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Acyltransferase; Alternative splicing; Metal-binding;
KW Mitochondrion; Reference proteome; Transferase; Transit peptide;
KW tRNA processing.
FT TRANSIT 1..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
FT CHAIN 30..414
FT /note="tRNA N6-adenosine threonylcarbamoyltransferase,
FT mitochondrial"
FT /id="PRO_0000307779"
FT BINDING 147
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
FT BINDING 151
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
FT BINDING 169..173
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
FT BINDING 202
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
FT BINDING 222
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
FT BINDING 226
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
FT BINDING 329..330
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
FT BINDING 357
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
FT BINDING 358
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
FT MOD_RES 74
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4B0"
FT MOD_RES 140
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4B0"
FT MOD_RES 203
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4B0"
FT MOD_RES 230
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4B0"
FT MOD_RES 299
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT VAR_SEQ 366..371
FT /note="NGIERL -> HGGARL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_028831"
FT VAR_SEQ 372..414
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_028832"
FT CONFLICT 102
FT /note="C -> S (in Ref. 2; AAH58172)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="Q -> R (in Ref. 2; AAH58172)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="Q -> H (in Ref. 2; AAH58172)"
FT /evidence="ECO:0000305"
FT CONFLICT 276
FT /note="G -> E (in Ref. 1; BAB27506)"
FT /evidence="ECO:0000305"
FT CONFLICT 394
FT /note="V -> I (in Ref. 2; AAH58172)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 414 AA; 44928 MW; 9A2D27B576C7DB24 CRC64;
MLMLRRTAGA IPKPPKSKVY GFLRRFSVHP RTLSCHKLVL GIETSCDDTG AAVVDETGNV
LGEALHSQTQ VHLKTGGIVP PVAQQLHREN IQRIVEETLS ACRITPSDLS AIATTIKPGL
ALSLGVGLSF SLQLVNQFKK PFIPIHHMEA HALTIRLTNK VEFPFLVLLI SGGHCLLALV
QGVSDFLLLG KSLDIAPGDM LDKVARRLSL IKHPECSTMS GGKAIEQLAK DGNRFHFTIN
PPMQNAKNCD FSFTGLQHIT DKLITHKEKE EGIEKGQILS SAADIAAAVQ HATACHLAKR
THRAILFCKQ KNLLSPANAV LVVSGGVASN LYIRKALEIV ANATQCTLLC PPPRLCTDNG
IMIAWNGIER LRAGLGVLHD VEDIRYEPKC PLGVDISREV AEAAIKVPRL KMAL
