ID SEN2_RAT Reviewed; 463 AA. AC Q5M954; DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-2005, sequence version 1. DT 24-JAN-2024, entry version 125. DE RecName: Full=tRNA-splicing endonuclease subunit Sen2; DE EC=4.6.1.16; DE AltName: Full=tRNA-intron endonuclease Sen2; GN Name=Tsen2; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC 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 [2] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32 AND SER-147, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22673903; DOI=10.1038/ncomms1871; RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., RA Olsen J.V.; RT "Quantitative maps of protein phosphorylation sites across 14 different rat RT organs and tissues."; RL Nat. Commun. 3:876-876(2012). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC087631; AAH87631.1; -; mRNA. DR RefSeq; NP_001014079.1; NM_001014057.1. DR RefSeq; XP_008761462.1; XM_008763240.2. DR RefSeq; XP_008761463.1; XM_008763241.1. DR RefSeq; XP_008761464.1; XM_008763242.2. DR AlphaFoldDB; Q5M954; -. DR SMR; Q5M954; -. DR STRING; 10116.ENSRNOP00000073692; -. DR iPTMnet; Q5M954; -. DR PhosphoSitePlus; Q5M954; -. DR PaxDb; 10116-ENSRNOP00000053267; -. DR Ensembl; ENSRNOT00000081957.2; ENSRNOP00000073692.1; ENSRNOG00000060175.2. DR Ensembl; ENSRNOT00055015518; ENSRNOP00055012433; ENSRNOG00055009167. DR Ensembl; ENSRNOT00060045077; ENSRNOP00060037398; ENSRNOG00060025995. DR Ensembl; ENSRNOT00065050259; ENSRNOP00065041281; ENSRNOG00065029073. DR GeneID; 312649; -. DR KEGG; rno:312649; -. DR UCSC; RGD:1309946; rat. DR AGR; RGD:1309946; -. DR CTD; 80746; -. DR RGD; 1309946; Tsen2. DR eggNOG; KOG4685; Eukaryota. DR GeneTree; ENSGT00390000013266; -. DR HOGENOM; CLU_046429_1_0_1; -. DR InParanoid; Q5M954; -. DR OMA; RRPFTWK; -. DR OrthoDB; 35871at2759; -. DR PhylomeDB; Q5M954; -. DR PRO; PR:Q5M954; -. DR Proteomes; UP000002494; Chromosome 4. DR Bgee; ENSRNOG00000060175; Expressed in stomach and 19 other cell types or tissues. DR GO; GO:0005813; C:centrosome; IEA:Ensembl. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell. DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl. 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:RGD. DR GO; GO:0000379; P:tRNA-type intron splice site recognition and cleavage; IBA:GO_Central. DR CDD; cd22363; tRNA-intron_lyase_C; 1. 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; TRNA-SPLICING ENDONUCLEASE SUBUNIT SEN2; 1. DR PANTHER; PTHR21227:SF0; TRNA-SPLICING ENDONUCLEASE SUBUNIT SEN2; 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; tRNA-intron endonuclease catalytic domain-like; 1. DR Genevisible; Q5M954; RN. PE 1: Evidence at protein level; KW Lyase; mRNA processing; Nucleus; Phosphoprotein; Reference proteome; KW tRNA processing. FT CHAIN 1..463 FT /note="tRNA-splicing endonuclease subunit Sen2" FT /id="PRO_0000109454" FT REGION 120..213 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 136..169 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 173..191 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 367 FT /evidence="ECO:0000250" FT ACT_SITE 375 FT /evidence="ECO:0000250" FT ACT_SITE 414 FT /evidence="ECO:0000250" FT MOD_RES 32 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 147 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 406 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q6P7W5" FT MOD_RES 409 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q6P7W5" FT MOD_RES 413 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q6P7W5" SQ SEQUENCE 463 AA; 52952 MW; F66CD72240AB7229 CRC64; MAEAVFRAPK RKRRVYESYE SPLPIPFSQD QSPRKEFRIF QAEMISNNVV VRGTEDMEQL YGKGYFGKGI LSRSRPNFTI SNPKLAARWK GVQTDMPIIT SEKYQHRVEW ARDFMRRQGH DESTVQKILT DYTEPLEPPY RERKGESPQH EPLSSKADSS LEGREGKDEL SVTTGGAGQS DDLQGLNTHS DCRQEGPGHA TLTVASPSSL NGHAIEDPEA LSQIPCCSQE ALGQQDDLWP EASSQIAGES RAAHEYVLIE EELCDVQEGA APHDELLKRK RLVCRRNPYR IFEYLQLSLE EAFFLAYALG CLSIYYEKEP LTIVKLWQAF TAVQPTFRTT YMAYHYFRSK GWVPKVGLKY GTDLLLYRKG PPFYHASYSV IIELVDDNFE GSLRRPFSWK SLAALSRVSG NVSKELMLCY LIKPSTMTNE DMETPECMRR IQVQEVILSR WVSSRERSDQ DEL //