SEN15_MOUSE
ID SEN15_MOUSE Reviewed; 168 AA.
AC Q8R3W5; A6H601; Q9CQW8; Q9CYI5;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=tRNA-splicing endonuclease subunit Sen15;
DE AltName: Full=tRNA-intron endonuclease Sen15;
GN Name=Tsen15; Synonyms=Sen15;
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=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].
RC STRAIN=FVB/N-3; TISSUE=Brain, and Mammary gland;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, 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: Non-catalytic subunit of the tRNA-splicing endonuclease
CC complex, a complex responsible for identification and cleavage of the
CC splice sites in pre-tRNA. It cleaves pre-tRNA at the 5' and 3' splice
CC sites to release the intron. The products are an intron and two tRNA
CC half-molecules bearing 2',3' cyclic phosphate and 5'-OH termini. There
CC are no conserved sequences at the splice sites, but the intron is
CC invariably located at the same site in the gene, placing the splice
CC sites an invariant distance from the constant structural features of
CC the tRNA body. The tRNA splicing endonuclease is also involved in mRNA
CC processing via its association with pre-mRNA 3'-end processing factors,
CC establishing a link between pre-tRNA splicing and pre-mRNA 3'-end
CC formation, suggesting that the endonuclease subunits function in
CC multiple RNA-processing events (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. tRNA splicing endonuclease is a heterotetramer
CC composed of TSEN2, TSEN15, TSEN34/LENG5 and TSEN54. tRNA splicing
CC endonuclease complex also contains proteins of the pre-mRNA 3' end
CC processing machinery such as CLP1, CPSF1, CPSF4 and CSTF2 (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q8WW01}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Nucleus, nucleolus
CC {ECO:0000305}. Note=May be transiently localized in the nucleolus.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the SEN15 family. {ECO:0000305}.
CC -!- CAUTION: Although only weakly related to the S.cerevisiae SEN15
CC protein, it probably displays the same function within the tRNA
CC splicing endonuclease complex. {ECO:0000305}.
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DR EMBL; AK017650; BAB30855.1; -; mRNA.
DR EMBL; BC024342; AAH24342.1; -; mRNA.
DR EMBL; BC145701; AAI45702.1; -; mRNA.
DR CCDS; CCDS15363.1; -.
DR RefSeq; NP_079953.2; NM_025677.3.
DR AlphaFoldDB; Q8R3W5; -.
DR SMR; Q8R3W5; -.
DR BioGRID; 211612; 1.
DR STRING; 10090.ENSMUSP00000015124; -.
DR PhosphoSitePlus; Q8R3W5; -.
DR MaxQB; Q8R3W5; -.
DR PaxDb; Q8R3W5; -.
DR PeptideAtlas; Q8R3W5; -.
DR PRIDE; Q8R3W5; -.
DR ProteomicsDB; 256777; -.
DR GeneID; 66637; -.
DR KEGG; mmu:66637; -.
DR CTD; 116461; -.
DR MGI; MGI:1913887; Tsen15.
DR eggNOG; ENOG502S21U; Eukaryota.
DR InParanoid; Q8R3W5; -.
DR OrthoDB; 1522443at2759; -.
DR PhylomeDB; Q8R3W5; -.
DR BioGRID-ORCS; 66637; 20 hits in 72 CRISPR screens.
DR ChiTaRS; Tsen15; mouse.
DR PRO; PR:Q8R3W5; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8R3W5; protein.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0006388; P:tRNA splicing, via endonucleolytic cleavage and ligation; IEA:InterPro.
DR Gene3D; 3.40.1350.10; -; 1.
DR InterPro; IPR018593; tRNA-endonuc_su_Sen15.
DR InterPro; IPR011856; tRNA_endonuc-like_dom_sf.
DR InterPro; IPR036167; tRNA_intron_Endo_cat-like_sf.
DR Pfam; PF09631; Sen15; 1.
DR SUPFAM; SSF53032; SSF53032; 1.
PE 1: Evidence at protein level;
KW mRNA processing; Nucleus; Phosphoprotein; Reference proteome;
KW tRNA processing.
FT CHAIN 1..168
FT /note="tRNA-splicing endonuclease subunit Sen15"
FT /id="PRO_0000194024"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WW01"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WW01"
FT CONFLICT 5..8
FT /note="SDSE -> TSSK (in Ref. 1; BAB30855)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 168 AA; 18530 MW; 99D8E6E14C2FCAA0 CRC64;
MEERSDSEPT PGCSGPGPAP VRDGGGAHTW APEDAWMGTH PKYLEMMELD IGDATQVYIA
FLVYLDLMES KSWHEVNCVG IPELQLICLL GTEIEGEGLQ TVVPTPISAS LSHNRIREIL
KASRKLQGDP ELPMSFTLAI VESDSTIVYY KLTDGFMLPD PQNISLRR
