SEN2_MOUSE
ID SEN2_MOUSE Reviewed; 460 AA.
AC Q6P7W5; Q3UYG6;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=tRNA-splicing endonuclease subunit Sen2;
DE EC=4.6.1.16;
DE AltName: Full=tRNA-intron endonuclease Sen2;
GN Name=Tsen2; Synonyms=Sen2;
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; TISSUE=Medulla oblongata;
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=Brain;
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-403; SER-406 AND SER-410, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
CC -!- FUNCTION: Constitutes one of the two catalytic subunit of the tRNA-
CC splicing endonuclease complex, a complex responsible for identification
CC and cleavage of the splice sites in pre-tRNA. It cleaves pre-tRNA at
CC the 5'- and 3'-splice sites to release the intron. The products are an
CC intron and two tRNA half-molecules bearing 2',3'-cyclic phosphate and
CC 5'-OH termini. There are no conserved sequences at the splice sites,
CC but the intron is invariably located at the same site in the gene,
CC placing the splice sites an invariant distance from the constant
CC structural features of the tRNA body. Probably carries the active site
CC for 5'-splice site cleavage. The tRNA splicing endonuclease is also
CC involved in mRNA processing via its association with pre-mRNA 3'-end
CC processing factors, establishing a link between pre-tRNA splicing and
CC pre-mRNA 3'-end formation, suggesting that the endonuclease subunits
CC function in multiple RNA-processing events (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=pretRNA = a 3'-half-tRNA molecule with a 5'-OH end + a 5'-
CC half-tRNA molecule with a 2',3'-cyclic phosphate end + an intron with
CC a 2',3'-cyclic phosphate and a 5'-hydroxyl terminus.; EC=4.6.1.16;
CC -!- SUBUNIT: tRNA splicing endonuclease is a heterotetramer composed of
CC TSEN2, TSEN15, TSEN34/LENG5 and TSEN54. tRNA splicing endonuclease
CC complex also contains proteins of the pre-mRNA 3'-end processing
CC machinery such as CLP1, CPSF1, CPSF4 and CSTF2 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus, nucleolus
CC {ECO:0000250}. Note=May be transiently localized in the nucleolus.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the tRNA-intron endonuclease family.
CC {ECO:0000305}.
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DR EMBL; AK134697; BAE22246.1; -; mRNA.
DR EMBL; BC061473; AAH61473.1; -; mRNA.
DR CCDS; CCDS20440.1; -.
DR RefSeq; NP_950198.1; NM_199033.1.
DR AlphaFoldDB; Q6P7W5; -.
DR SMR; Q6P7W5; -.
DR STRING; 10090.ENSMUSP00000038211; -.
DR iPTMnet; Q6P7W5; -.
DR PhosphoSitePlus; Q6P7W5; -.
DR EPD; Q6P7W5; -.
DR MaxQB; Q6P7W5; -.
DR PaxDb; Q6P7W5; -.
DR PeptideAtlas; Q6P7W5; -.
DR PRIDE; Q6P7W5; -.
DR ProteomicsDB; 256955; -.
DR Antibodypedia; 26210; 203 antibodies from 25 providers.
DR DNASU; 381802; -.
DR Ensembl; ENSMUST00000040234; ENSMUSP00000038211; ENSMUSG00000042389.
DR GeneID; 381802; -.
DR KEGG; mmu:381802; -.
DR UCSC; uc009diu.1; mouse.
DR CTD; 80746; -.
DR MGI; MGI:2141599; Tsen2.
DR VEuPathDB; HostDB:ENSMUSG00000042389; -.
DR eggNOG; KOG4685; Eukaryota.
DR GeneTree; ENSGT00390000013266; -.
DR HOGENOM; CLU_046429_1_0_1; -.
DR InParanoid; Q6P7W5; -.
DR OMA; TFEETFF; -.
DR OrthoDB; 1219366at2759; -.
DR PhylomeDB; Q6P7W5; -.
DR TreeFam; TF314679; -.
DR BioGRID-ORCS; 381802; 21 hits in 75 CRISPR screens.
DR ChiTaRS; Tsen2; mouse.
DR PRO; PR:Q6P7W5; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q6P7W5; protein.
DR Bgee; ENSMUSG00000042389; Expressed in dorsal pancreas and 227 other tissues.
DR ExpressionAtlas; Q6P7W5; baseline and differential.
DR Genevisible; Q6P7W5; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0000214; C:tRNA-intron endonuclease complex; IBA:GO_Central.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0000213; F:tRNA-intron endonuclease activity; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0006388; P:tRNA splicing, via endonucleolytic cleavage and ligation; ISO:MGI.
DR GO; GO:0000379; P:tRNA-type intron splice site recognition and cleavage; IBA:GO_Central.
DR Gene3D; 3.40.1350.10; -; 1.
DR InterPro; IPR011856; tRNA_endonuc-like_dom_sf.
DR InterPro; IPR036167; tRNA_intron_Endo_cat-like_sf.
DR InterPro; IPR006677; tRNA_intron_Endonuc_cat-like.
DR InterPro; IPR006678; tRNA_intron_Endonuc_N.
DR InterPro; IPR006676; tRNA_splic.
DR InterPro; IPR016589; tRNA_splic_SEN2.
DR PANTHER; PTHR21227; PTHR21227; 1.
DR Pfam; PF01974; tRNA_int_endo; 1.
DR Pfam; PF02778; tRNA_int_endo_N; 1.
DR PIRSF; PIRSF011789; tRNA_splic_SEN2; 1.
DR SUPFAM; SSF53032; SSF53032; 1.
PE 1: Evidence at protein level;
KW Lyase; mRNA processing; Nucleus; Phosphoprotein; Reference proteome;
KW tRNA processing.
FT CHAIN 1..460
FT /note="tRNA-splicing endonuclease subunit Sen2"
FT /id="PRO_0000109453"
FT REGION 143..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 364
FT /evidence="ECO:0000250"
FT ACT_SITE 372
FT /evidence="ECO:0000250"
FT ACT_SITE 411
FT /evidence="ECO:0000250"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747"
FT MOD_RES 406
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747"
FT MOD_RES 410
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747"
SQ SEQUENCE 460 AA; 52214 MW; 1FC32E811F488184 CRC64;
MAEAVFRAPK RKRRVYESYE SPLPIPFGQD QGPRKEFRIF QAEMISNNVV VRGTEDMEQL
YGKGYFGKGI LSRSRPNFTI ANPTLAARWK GVQTDMPIIT SEKYQHRVEW ARDFLRRQGH
DESTVQKILT DYTEPLELPC REEKEETPQH EPLSSKADSS LEGRVEKDEL PVTPGGAGQS
DDLPGLGTHS DCLQEGPGHA TLAAASPSSH NGHVAEDPEV LPQETLVPQG GLWPEASSQA
AGEKRAAHEY VLIEEELCGA QEEEAAAASD EKLLKRKKLV CRRNPYRIFE YLQLSLEEAF
FLAYALGCLS IYYEKEPLTI VKLWQAFTAV QPTFRTTYMA YHYFRSKGWV PKVGLKYGTD
LLLYRKGPPF YHASYSVIIE LLDDNYEGSL RRPFSWKSLA ALSRVSGNVS KELMLCYLIK
PSTMTAEDME TPECMKRIQV QEVILSRWVS SRERSDQDEL
