SEN34_MOUSE
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 03-AUG-2022, entry version 142.
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}.
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; 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. [Q8BMZ5-1]
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; Q8BMZ5; -.
DR PeptideAtlas; Q8BMZ5; -.
DR PRIDE; Q8BMZ5; -.
DR ProteomicsDB; 256956; -. [Q8BMZ5-1]
DR ProteomicsDB; 256957; -. [Q8BMZ5-2]
DR Antibodypedia; 32835; 38 antibodies from 12 providers.
DR DNASU; 66078; -.
DR Ensembl; ENSMUST00000108627; ENSMUSP00000104267; ENSMUSG00000035585. [Q8BMZ5-1]
DR Ensembl; ENSMUST00000108629; ENSMUSP00000104269; ENSMUSG00000035585. [Q8BMZ5-2]
DR Ensembl; ENSMUST00000108630; ENSMUSP00000104270; ENSMUSG00000035585. [Q8BMZ5-1]
DR GeneID; 66078; -.
DR KEGG; mmu:66078; -.
DR UCSC; uc009evu.2; mouse. [Q8BMZ5-2]
DR UCSC; uc009evv.2; mouse. [Q8BMZ5-1]
DR CTD; 79042; -.
DR MGI; MGI:1913328; Tsen34.
DR VEuPathDB; HostDB:ENSMUSG00000035585; -.
DR eggNOG; KOG4133; Eukaryota.
DR GeneTree; ENSGT00390000003912; -.
DR InParanoid; Q8BMZ5; -.
DR OrthoDB; 1621103at2759; -.
DR PhylomeDB; Q8BMZ5; -.
DR TreeFam; TF314631; -.
DR BioGRID-ORCS; 66078; 22 hits in 75 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 62 other tissues.
DR ExpressionAtlas; Q8BMZ5; baseline and differential.
DR Genevisible; Q8BMZ5; MM.
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 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 Pfam; PF01974; tRNA_int_endo; 1.
DR PIRSF; PIRSF017250; tRNA_splic_SEN34; 1.
DR SUPFAM; SSF53032; SSF53032; 1.
DR TIGRFAMs; TIGR00324; endA; 1.
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