SEN54_MOUSE
ID SEN54_MOUSE Reviewed; 525 AA.
AC Q8C2A2; B1ATA4; B1ATA5; Q9DCI5;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=tRNA-splicing endonuclease subunit Sen54;
DE AltName: Full=tRNA-intron endonuclease Sen54;
GN Name=Tsen54; Synonyms=Sen54;
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] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 4-525 (ISOFORM 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Kidney, and Thymus;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
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: 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:0000305}. Nucleus, nucleolus
CC {ECO:0000305}. Note=May be transiently localized in the nucleolus.
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8C2A2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8C2A2-2; Sequence=VSP_010990;
CC -!- SIMILARITY: Belongs to the SEN54 family. {ECO:0000305}.
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DR EMBL; AK002758; BAB22335.1; -; mRNA.
DR EMBL; AK089005; BAC40696.1; -; mRNA.
DR EMBL; AL645852; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS25648.1; -. [Q8C2A2-1]
DR RefSeq; NP_083833.1; NM_029557.1. [Q8C2A2-1]
DR AlphaFoldDB; Q8C2A2; -.
DR STRING; 10090.ENSMUSP00000021134; -.
DR iPTMnet; Q8C2A2; -.
DR PhosphoSitePlus; Q8C2A2; -.
DR EPD; Q8C2A2; -.
DR MaxQB; Q8C2A2; -.
DR PaxDb; Q8C2A2; -.
DR PRIDE; Q8C2A2; -.
DR ProteomicsDB; 256958; -. [Q8C2A2-1]
DR ProteomicsDB; 256959; -. [Q8C2A2-2]
DR Antibodypedia; 32191; 58 antibodies from 19 providers.
DR Ensembl; ENSMUST00000021134; ENSMUSP00000021134; ENSMUSG00000020781. [Q8C2A2-1]
DR Ensembl; ENSMUST00000106481; ENSMUSP00000102090; ENSMUSG00000020781. [Q8C2A2-2]
DR GeneID; 76265; -.
DR KEGG; mmu:76265; -.
DR UCSC; uc007miq.1; mouse. [Q8C2A2-1]
DR UCSC; uc011yhp.1; mouse. [Q8C2A2-2]
DR CTD; 283989; -.
DR MGI; MGI:1923515; Tsen54.
DR VEuPathDB; HostDB:ENSMUSG00000020781; -.
DR eggNOG; KOG4772; Eukaryota.
DR GeneTree; ENSGT00390000004214; -.
DR HOGENOM; CLU_033069_1_0_1; -.
DR InParanoid; Q8C2A2; -.
DR OMA; AMVLQHI; -.
DR OrthoDB; 1617156at2759; -.
DR PhylomeDB; Q8C2A2; -.
DR TreeFam; TF314691; -.
DR BioGRID-ORCS; 76265; 26 hits in 75 CRISPR screens.
DR ChiTaRS; Tsen54; mouse.
DR PRO; PR:Q8C2A2; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8C2A2; protein.
DR Bgee; ENSMUSG00000020781; Expressed in yolk sac and 165 other tissues.
DR ExpressionAtlas; Q8C2A2; baseline and differential.
DR Genevisible; Q8C2A2; MM.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0000214; C:tRNA-intron endonuclease complex; 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 InterPro; IPR024337; tRNA_splic_suSen54.
DR InterPro; IPR024336; tRNA_splic_suSen54_N.
DR PANTHER; PTHR21027; PTHR21027; 1.
DR Pfam; PF12928; tRNA_int_end_N2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Alternative splicing; mRNA processing; Nucleus;
KW Phosphoprotein; Reference proteome; tRNA processing.
FT CHAIN 1..525
FT /note="tRNA-splicing endonuclease subunit Sen54"
FT /id="PRO_0000194030"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z6J9"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z6J9"
FT MOD_RES 180
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z6J9"
FT VAR_SEQ 438..476
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_010990"
FT CONFLICT 244
FT /note="S -> P (in Ref. 1; BAC40696)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 525 AA; 59083 MW; EBC3D92CFA647BF7 CRC64;
MEPEPEPGSV EVPAGRVLSA SELRAARSRS QKLPQRSHGP KDFLPDGSEA QAERLRLCRQ
ELWQLLAEER VERLGSLVAA EWKPEEGFVE LTSPAGKFWQ TMGYSEEGRQ RLHPEEALYL
LECGSIQLFY QDLPLSIQEA YQLLLTEDTL SFLQYQVFSH LKRLGYVVRR FQLSSVVSPY
ERQLNLDGYA QCLEDGSGKR KRSSSCRSVN KKPKVLQNSL PPVSLAASSS PACDQSSQYP
EEKSQDSSPR QGSELPLQFL GSSEPCSDLA REDVGCDRES HKIENGAKGT PKLRWNFEQI
SFPNMASDSR HTFLPAPAPE LLPANVIGRG TDAESWCQKL NQRREKLSRR DREQQAVVQQ
FREDVNADPE VRGCSSWQEY KELLQRRQTQ KSQPRPPHLW GQSVTPLLDP DKADCPAAVL
QHISVLQTTH LADGGYRLLE KSGGLQISFD VYQADAVATF RKNSPGKPYV RMCISGFDDP
VPDLCSLKCL TYQSGDVPLI FALVDHGDIS FYSFRDFTLP RDLGH
