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   03-AUG-2022, entry version 119.
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}.
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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.ENSRNOP00000053267; -.
DR   iPTMnet; Q5M954; -.
DR   PhosphoSitePlus; Q5M954; -.
DR   PaxDb; Q5M954; -.
DR   PRIDE; Q5M954; -.
DR   Ensembl; ENSRNOT00000081957; ENSRNOP00000073692; ENSRNOG00000060175.
DR   GeneID; 312649; -.
DR   KEGG; rno:312649; -.
DR   UCSC; RGD:1309946; rat.
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; TFEETFF; -.
DR   OrthoDB; 1219366at2759; -.
DR   PhylomeDB; Q5M954; -.
DR   PRO; PR:Q5M954; -.
DR   Proteomes; UP000002494; Chromosome 4.
DR   Bgee; ENSRNOG00000060175; Expressed in stomach and 19 other tissues.
DR   Genevisible; Q5M954; RN.
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   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..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