TSR3_MOUSE
ID TSR3_MOUSE Reviewed; 323 AA.
AC Q5HZH2; Q9DD00;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=18S rRNA aminocarboxypropyltransferase {ECO:0000305};
DE EC=2.5.1.- {ECO:0000250|UniProtKB:Q9UJK0};
DE AltName: Full=20S S rRNA accumulation protein 3 homolog {ECO:0000250|UniProtKB:Q9UJK0};
GN Name=Tsr3 {ECO:0000312|MGI:MGI:1915577};
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].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Kidney, and Visual cortex;
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].
RC STRAIN=C57BL/6J; TISSUE=Eye;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Aminocarboxypropyltransferase that catalyzes the
CC aminocarboxypropyl transfer on pseudouridine at position 1248 (Psi1248)
CC in 18S rRNA. It constitutes the last step in biosynthesis of the
CC hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine
CC (m1acp3-Psi) conserved in eukaryotic 18S rRNA.
CC {ECO:0000250|UniProtKB:Q9UJK0}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(1)-methylpseudouridine(1248) in human 18S rRNA + S-adenosyl-
CC L-methionine = H(+) + N(1)-methyl-N(3)-[(3S)-3-amino-3-
CC carboxypropyl]pseudouridine(1248) in human 18S rRNA + S-methyl-5'-
CC thioadenosine; Xref=Rhea:RHEA:63292, Rhea:RHEA-COMP:11639, Rhea:RHEA-
CC COMP:16308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74890, ChEBI:CHEBI:146234;
CC Evidence={ECO:0000250|UniProtKB:Q9UJK0, ECO:0000255|HAMAP-
CC Rule:MF_03146};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63293;
CC Evidence={ECO:0000250|UniProtKB:Q9UJK0, ECO:0000255|HAMAP-
CC Rule:MF_03146};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q12094,
CC ECO:0000255|HAMAP-Rule:MF_03146}.
CC -!- SIMILARITY: Belongs to the TDD superfamily. TSR3 family.
CC {ECO:0000255|HAMAP-Rule:MF_03146}.
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DR EMBL; AK002309; BAB22003.1; -; mRNA.
DR EMBL; AK158743; BAE34637.1; -; mRNA.
DR EMBL; AK170074; BAE41547.1; -; mRNA.
DR EMBL; BC089019; AAH89019.1; -; mRNA.
DR CCDS; CCDS28512.1; -.
DR RefSeq; NP_001157190.1; NM_001163718.1.
DR RefSeq; NP_080952.2; NM_026676.3.
DR AlphaFoldDB; Q5HZH2; -.
DR SMR; Q5HZH2; -.
DR STRING; 10090.ENSMUSP00000068511; -.
DR iPTMnet; Q5HZH2; -.
DR PhosphoSitePlus; Q5HZH2; -.
DR EPD; Q5HZH2; -.
DR MaxQB; Q5HZH2; -.
DR PaxDb; Q5HZH2; -.
DR PeptideAtlas; Q5HZH2; -.
DR PRIDE; Q5HZH2; -.
DR ProteomicsDB; 298148; -.
DR Antibodypedia; 52454; 22 antibodies from 11 providers.
DR DNASU; 68327; -.
DR Ensembl; ENSMUST00000063574; ENSMUSP00000068511; ENSMUSG00000015126.
DR GeneID; 68327; -.
DR KEGG; mmu:68327; -.
DR UCSC; uc008baf.2; mouse.
DR CTD; 115939; -.
DR MGI; MGI:1915577; Tsr3.
DR VEuPathDB; HostDB:ENSMUSG00000015126; -.
DR eggNOG; KOG3154; Eukaryota.
DR GeneTree; ENSGT00390000014665; -.
DR HOGENOM; CLU_035060_2_0_1; -.
DR InParanoid; Q5HZH2; -.
DR OMA; GRECMNL; -.
DR OrthoDB; 1222562at2759; -.
DR PhylomeDB; Q5HZH2; -.
DR TreeFam; TF105862; -.
DR BioGRID-ORCS; 68327; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Tsr3; mouse.
DR PRO; PR:Q5HZH2; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q5HZH2; protein.
DR Bgee; ENSMUSG00000015126; Expressed in floor plate of midbrain and 242 other tissues.
DR Genevisible; Q5HZH2; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0106388; F:18S rRNA aminocarboxypropyltransferase activity; ISO:MGI.
DR GO; GO:1904047; F:S-adenosyl-L-methionine binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016740; F:transferase activity; ISO:MGI.
DR GO; GO:0000455; P:enzyme-directed rRNA pseudouridine synthesis; ISO:MGI.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IBA:GO_Central.
DR HAMAP; MF_01116; TSR3; 1.
DR InterPro; IPR007209; RNaseL-inhib-like_metal-bd_dom.
DR InterPro; IPR022968; Tsr3-like.
DR InterPro; IPR007177; Tsr3_C.
DR PANTHER; PTHR20426; PTHR20426; 1.
DR Pfam; PF04034; Ribo_biogen_C; 1.
DR Pfam; PF04068; RLI; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Phosphoprotein; Reference proteome; Ribosome biogenesis;
KW rRNA processing; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..323
FT /note="18S rRNA aminocarboxypropyltransferase"
FT /id="PRO_0000278670"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..282
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..323
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 74
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:E1QU22"
FT BINDING 122
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:E1QU22"
FT BINDING 145
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:E1QU22"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 245
FT /note="V -> E (in Ref. 1; BAB22003)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 323 AA; 35334 MW; CCBE907B0F811EBB CRC64;
MGRKKVARGS RKESGRVRRP SGRSLDAFAE EVGAALRASV QPEEAEDQGG PGPAALPCAL
AMWELGHCDP KRCTGRKLAR LGLVRCLRLS QRFGGLVLSP VGTEYVSPAD RQLVAQSGVA
VIDCSWAKLD DTPFQKMRGS HLRLLPYLVA ANPVNYGRPC KLSCVEAFAA AFCIVGFSDL
AVILLRKFKW GKGFLDLNRE LLDKYAACRG PEEVLQAEQG YLASTRDTPE EDIDPFDVDS
GREFVNLNRP VASTRLPEDM DDTDGSEEHS EDSEEDSDEC EEPGPGANGG DSNYSGAEET
PEQEAQARDS TEIWKGIKKR QRD
