ID   SEN34_MOUSE             Reviewed;         316 AA.
AC   Q8BMZ5; Q58EU2; Q99LV6; Q9CYW1;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 2.
DT   24-JAN-2024, entry version 149.
DE   RecName: Full=tRNA-splicing endonuclease subunit Sen34;
DE            EC=4.6.1.16;
DE   AltName: Full=Leukocyte receptor cluster member 5 homolog;
DE   AltName: Full=tRNA-intron endonuclease Sen34;
GN   Name=Tsen34; Synonyms=Leng5, Sen34;
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] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Oviduct;
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] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Salivary 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).
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. The tRNA splicing endonuclease is
CC       also involved in mRNA processing via its association with pre-mRNA 3'-
CC       end processing factors, establishing a link between pre-tRNA splicing
CC       and pre-mRNA 3'-end formation, suggesting that the endonuclease
CC       subunits 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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BMZ5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BMZ5-2; Sequence=VSP_010987;
CC   -!- SIMILARITY: Belongs to the tRNA-intron endonuclease family.
CC       {ECO:0000305}.
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DR   EMBL; AK003757; BAC25051.1; -; mRNA.
DR   EMBL; AK013253; BAB28747.1; -; mRNA.
DR   EMBL; AK053916; BAC35591.1; -; mRNA.
DR   EMBL; BC002205; AAH02205.1; -; mRNA.
DR   EMBL; BC091756; AAH91756.1; -; mRNA.
DR   CCDS; CCDS20725.1; -. [Q8BMZ5-1]
DR   CCDS; CCDS51966.1; -. [Q8BMZ5-2]
DR   RefSeq; NP_001157676.1; NM_001164204.1. [Q8BMZ5-1]
DR   RefSeq; NP_001157677.1; NM_001164205.1. [Q8BMZ5-2]
DR   RefSeq; NP_077130.1; NM_024168.2. [Q8BMZ5-1]
DR   RefSeq; XP_017167711.1; XM_017312222.1.
DR   RefSeq; XP_017167712.1; XM_017312223.1.
DR   RefSeq; XP_017167713.1; XM_017312224.1. [Q8BMZ5-1]
DR   RefSeq; XP_017167714.1; XM_017312225.1. [Q8BMZ5-1]
DR   RefSeq; XP_017167715.1; XM_017312226.1. [Q8BMZ5-1]
DR   AlphaFoldDB; Q8BMZ5; -.
DR   SMR; Q8BMZ5; -.
DR   BioGRID; 211199; 1.
DR   IntAct; Q8BMZ5; 1.
DR   MINT; Q8BMZ5; -.
DR   STRING; 10090.ENSMUSP00000104270; -.
DR   iPTMnet; Q8BMZ5; -.
DR   PhosphoSitePlus; Q8BMZ5; -.
DR   EPD; Q8BMZ5; -.
DR   MaxQB; Q8BMZ5; -.
DR   PaxDb; 10090-ENSMUSP00000104270; -.
DR   PeptideAtlas; Q8BMZ5; -.
DR   ProteomicsDB; 256956; -. [Q8BMZ5-1]
DR   ProteomicsDB; 256957; -. [Q8BMZ5-2]
DR   Pumba; Q8BMZ5; -.
DR   Antibodypedia; 32835; 43 antibodies from 12 providers.
DR   DNASU; 66078; -.
DR   Ensembl; ENSMUST00000108627.4; ENSMUSP00000104267.4; ENSMUSG00000035585.17. [Q8BMZ5-1]
DR   Ensembl; ENSMUST00000108629.8; ENSMUSP00000104269.2; ENSMUSG00000035585.17. [Q8BMZ5-2]
DR   Ensembl; ENSMUST00000108630.8; ENSMUSP00000104270.2; ENSMUSG00000035585.17. [Q8BMZ5-1]
DR   GeneID; 66078; -.
DR   KEGG; mmu:66078; -.
DR   UCSC; uc009evu.2; mouse. [Q8BMZ5-2]
DR   UCSC; uc009evv.2; mouse. [Q8BMZ5-1]
DR   AGR; MGI:1913328; -.
DR   CTD; 79042; -.
DR   MGI; MGI:1913328; Tsen34.
DR   VEuPathDB; HostDB:ENSMUSG00000035585; -.
DR   eggNOG; KOG4133; Eukaryota.
DR   GeneTree; ENSGT00390000003912; -.
DR   InParanoid; Q8BMZ5; -.
DR   OrthoDB; 35871at2759; -.
DR   PhylomeDB; Q8BMZ5; -.
DR   TreeFam; TF314631; -.
DR   BioGRID-ORCS; 66078; 22 hits in 80 CRISPR screens.
DR   ChiTaRS; Tsen34; mouse.
DR   PRO; PR:Q8BMZ5; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; Q8BMZ5; Protein.
DR   Bgee; ENSMUSG00000035585; Expressed in embryonic facial prominence and 65 other cell types or tissues.
DR   ExpressionAtlas; Q8BMZ5; baseline and differential.
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; IEA:InterPro.
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: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; IPR006676; tRNA_splic.
DR   InterPro; IPR016690; tRNA_splic_SEN34.
DR   NCBIfam; TIGR00324; endA; 1.
DR   PANTHER; PTHR13070:SF0; TRNA-SPLICING ENDONUCLEASE SUBUNIT SEN34; 1.
DR   PANTHER; PTHR13070; TRNA-SPLICING ENDONUCLEASE SUBUNIT SEN34-RELATED; 1.
DR   Pfam; PF01974; tRNA_int_endo; 1.
DR   PIRSF; PIRSF017250; tRNA_splic_SEN34; 1.
DR   SUPFAM; SSF53032; tRNA-intron endonuclease catalytic domain-like; 1.
DR   Genevisible; Q8BMZ5; MM.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Lyase; mRNA processing; Nucleus; Reference proteome;
KW   tRNA processing.
FT   CHAIN           1..316
FT                   /note="tRNA-splicing endonuclease subunit Sen34"
FT                   /id="PRO_0000109464"
FT   REGION          120..184
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        142..177
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        253
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        261
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        292
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         255..283
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_010987"
FT   CONFLICT        20
FT                   /note="Q -> L (in Ref. 1; BAB28747)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        280
FT                   /note="L -> Q (in Ref. 1; BAB28747)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   316 AA;  34196 MW;  86A169BC119F7AC3 CRC64;
     MLVVEVANGR SLVWGAEAVQ ALRERLGVGG RTVGALPRGP RQNSRLGLPL LLLPEEARLL
     AEIGAVTLVS APRPDPRNHG LALASFKRQQ EQSFQDQNTL AAEARETRRQ ELLEKIVEGQ
     AAKKQKLEQD SGADEGGQEA GGSEATQGSE TSDDGQPSAE QEGAAPSLDS SSPQPGPSNG
     VTPLPRSALL IQLATARPRP VKAKPLDWRV QSKDWPHAGR PAHELRYSIY RDLWERGFFL
     SAAGKFGGDF LVYPGDPLRF HAHYIAQCWS AEDPIPLQDL VSAGRLGTSV RKTLLLCSPQ
     PDGKVVYTSL QWASLQ
//