SEN2_YEAST
ID SEN2_YEAST Reviewed; 377 AA.
AC P16658; D6VYA5;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=tRNA-splicing endonuclease subunit SEN2;
DE EC=4.6.1.16;
DE AltName: Full=Splicing endonuclease protein 2;
DE AltName: Full=tRNA-intron endonuclease SEN2;
GN Name=SEN2; OrderedLocusNames=YLR105C; ORFNames=L8004.12;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION, SUBUNIT, AND MUTANT
RP SEN2-3.
RX PubMed=9200603; DOI=10.1016/s0092-8674(00)80270-6;
RA Trotta C.R., Miao F., Arn E.A., Stevens S.W., Ho C.K., Rauhut R.,
RA Abelson J.N.;
RT "The yeast tRNA splicing endonuclease: a tetrameric enzyme with two active
RT site subunits homologous to the archaeal tRNA endonucleases.";
RL Cell 89:849-858(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP SUBUNIT.
RX PubMed=2211694; DOI=10.1016/s0021-9258(17)44735-1;
RA Rauhut R., Green P.R., Abelson J.N.;
RT "Yeast tRNA-splicing endonuclease is a heterotrimeric enzyme.";
RL J. Biol. Chem. 265:18180-18184(1990).
RN [5]
RP FUNCTION.
RX PubMed=2182322; DOI=10.1002/j.1460-2075.1990.tb08232.x;
RA Ho C.K., Rauhut R., Vijayraghavan U., Abelson J.;
RT "Accumulation of pre-tRNA splicing '2/3' intermediates in a Saccharomyces
RT cerevisiae mutant.";
RL EMBO J. 9:1245-1252(1990).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=12925762; DOI=10.1091/mbc.e02-11-0757;
RA Yoshihisa T., Yunoki-Esaki K., Ohshima C., Tanaka N., Endo T.;
RT "Possibility of cytoplasmic pre-tRNA splicing: the yeast tRNA splicing
RT endonuclease mainly localizes on the mitochondria.";
RL Mol. Biol. Cell 14:3266-3279(2003).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16823961; DOI=10.1021/pr050477f;
RA Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.;
RT "Toward the complete yeast mitochondrial proteome: multidimensional
RT separation techniques for mitochondrial proteomics.";
RL J. Proteome Res. 5:1543-1554(2006).
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. This subunit may anchor the
CC endonuclease complex to the nuclear membrane. Probably carries the
CC active site for 5'-splice site cleavage. {ECO:0000269|PubMed:2182322}.
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: Heterotetramer composed of SEN2, SEN15, SEN34 and SEN54.
CC Interacts directly with SEN54. {ECO:0000269|PubMed:2211694,
CC ECO:0000269|PubMed:9200603}.
CC -!- INTERACTION:
CC P16658; Q02825: SEN54; NbExp=4; IntAct=EBI-16953, EBI-16829;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12925762}.
CC Endomembrane system {ECO:0000269|PubMed:12925762}; Peripheral membrane
CC protein {ECO:0000269|PubMed:12925762}. Mitochondrion outer membrane
CC {ECO:0000269|PubMed:12925762, ECO:0000269|PubMed:16823961}; Peripheral
CC membrane protein {ECO:0000269|PubMed:12925762,
CC ECO:0000269|PubMed:16823961}; Cytoplasmic side
CC {ECO:0000269|PubMed:12925762, ECO:0000269|PubMed:16823961}. Note=The
CC tRNA splicing endonuclease complex is predominantly associated with the
CC outer membrane of mitochondria, suggesting that tRNA splicing mainly
CC takes place on the mitochondrial surface.
CC -!- MISCELLANEOUS: The tRNA splicing endonuclease complex is present with
CC 100 molecules/cell. {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: Present with 319 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the tRNA-intron endonuclease family.
CC {ECO:0000305}.
CC -!- CAUTION: According to PubMed:9200603, it contains a transmembrane
CC domain and may be responsible to anchor the complex into membranes,
CC however, PubMed:12925762 showed that it is peripherically associated
CC with membranes, and is probably not a transmembrane protein.
CC {ECO:0000305}.
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DR EMBL; M32336; AAB65811.1; -; Genomic_DNA.
DR EMBL; Z73277; CAA97670.1; -; Genomic_DNA.
DR EMBL; U53876; AAB67547.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09421.1; -; Genomic_DNA.
DR PIR; A38862; A38862.
DR RefSeq; NP_013206.1; NM_001181992.1.
DR AlphaFoldDB; P16658; -.
DR SMR; P16658; -.
DR BioGRID; 31378; 80.
DR ComplexPortal; CPX-1832; tRNA-intron endonuclease complex.
DR DIP; DIP-4821N; -.
DR IntAct; P16658; 7.
DR MINT; P16658; -.
DR STRING; 4932.YLR105C; -.
DR iPTMnet; P16658; -.
DR MaxQB; P16658; -.
DR PaxDb; P16658; -.
DR PRIDE; P16658; -.
DR EnsemblFungi; YLR105C_mRNA; YLR105C; YLR105C.
DR GeneID; 850795; -.
DR KEGG; sce:YLR105C; -.
DR SGD; S000004095; SEN2.
DR VEuPathDB; FungiDB:YLR105C; -.
DR eggNOG; KOG4685; Eukaryota.
DR GeneTree; ENSGT00390000013266; -.
DR HOGENOM; CLU_012847_2_0_1; -.
DR InParanoid; P16658; -.
DR OMA; LPAFYPN; -.
DR BioCyc; MetaCyc:G3O-32253-MON; -.
DR BioCyc; YEAST:G3O-32253-MON; -.
DR BRENDA; 4.6.1.16; 984.
DR PRO; PR:P16658; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P16658; protein.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0000214; C:tRNA-intron endonuclease complex; IDA:SGD.
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; IDA:SGD.
DR GO; GO:0098787; P:mRNA cleavage involved in mRNA processing; IMP:SGD.
DR GO; GO:0000379; P:tRNA-type intron splice site recognition and cleavage; IDA:SGD.
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; IPR016589; tRNA_splic_SEN2.
DR PANTHER; PTHR21227; PTHR21227; 1.
DR Pfam; PF01974; tRNA_int_endo; 1.
DR PIRSF; PIRSF011789; tRNA_splic_SEN2; 1.
DR SUPFAM; SSF53032; SSF53032; 1.
DR TIGRFAMs; TIGR00324; endA; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Lyase; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW Nucleus; Reference proteome; tRNA processing.
FT CHAIN 1..377
FT /note="tRNA-splicing endonuclease subunit SEN2"
FT /id="PRO_0000109462"
FT COILED 119..174
FT /evidence="ECO:0000255"
FT ACT_SITE 289
FT /evidence="ECO:0000250"
FT ACT_SITE 297
FT /evidence="ECO:0000250"
FT ACT_SITE 328
FT /evidence="ECO:0000250"
FT VARIANT 292
FT /note="G -> E (in the cold-sensitive allele sen2-3;
FT defective in cleavage only at the 5'-splice site of tRNA
FT precursors)"
SQ SEQUENCE 377 AA; 44109 MW; B5A9C7F865538F5C CRC64;
MSKGRVNQKR YKYPLPIHPV DDLPELILHN PLSWLYWAYR YYKSTNALND KVHVDFIGDT
TLHITVQDDK QMLYLWNNGF FGTGQFSRSE PTWKARTEAR LGLNDTPLHN RGGTKSNTET
EMTLEKVTQQ RRLQRLEFKK ERAKLERELL ELRKKGGHID EENILLEKQR ESLRKFKLKQ
TEDVGIVAQQ QDISESNLRD EDNNLLDENG DLLPLESLEL MPVEAMFLTF ALPVLDISPA
CLAGKLFQFD AKYKDIHSFV RSYVIYHHYR SHGWCVRSGI KFGCDYLLYK RGPPFQHAEF
CVMGLDHDVS KDYTWYSSIA RVVGGAKKTF VLCYVERLIS EQEAIALWKS NNFTKLFNSF
QVGEVLYKRW VPGRNRD
