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Q8BMZ5 (SEN34_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
tRNA-splicing endonuclease subunit Sen34

EC=4.6.1.16
Alternative name(s):
Leukocyte receptor cluster member 5 homolog
tRNA-intron endonuclease Sen34
Gene names
Name:Tsen34
Synonyms:Leng5, Sen34
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length316 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Constitutes one of the two catalytic subunit of the tRNA-splicing endonuclease complex, a complex responsible for identification and cleavage of the splice sites in pre-tRNA. It cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3'-cyclic phosphate and 5'-OH termini. There are no conserved sequences at the splice sites, but the intron is invariably located at the same site in the gene, placing the splice sites an invariant distance from the constant structural features of the tRNA body. The tRNA splicing endonuclease is also involved in mRNA processing via its association with pre-mRNA 3'-end processing factors, establishing a link between pre-tRNA splicing and pre-mRNA 3'-end formation, suggesting that the endonuclease subunits function in multiple RNA-processing events By similarity.

Catalytic activity

PretRNA = a 3'-half-tRNA molecule with a 5'-OH end + a 5'-half-tRNA molecule with a 2',3'-cyclic phosphate end + an intron with a 2',3'-cyclic phosphate and a 5'-hydroxyl terminus.

Subunit structure

tRNA splicing endonuclease is a heterotetramer composed of SEN2, SEN15, SEN34/LENG5 and SEN54. tRNA splicing endonuclease complex also contains proteins of the pre-mRNA 3'-end processing machinery such as CLP1, CPSF1, CPSF4 and CSTF2 By similarity.

Subcellular location

Nucleus By similarity. Nucleusnucleolus By similarity. Note: May be transiently localized in the nucleolus By similarity.

Sequence similarities

Belongs to the tRNA-intron endonuclease family.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8BMZ5-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8BMZ5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     255-283: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 316316tRNA-splicing endonuclease subunit Sen34
PRO_0000109464

Sites

Active site2531 By similarity
Active site2611 By similarity
Active site2921 By similarity

Natural variations

Alternative sequence255 – 28329Missing in isoform 2.
VSP_010987

Experimental info

Sequence conflict201Q → L in BAB28747. Ref.1
Sequence conflict2801L → Q in BAB28747. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 19, 2004. Version 2.
Checksum: 86A169BC119F7AC3

FASTA31634,196
        10         20         30         40         50         60 
MLVVEVANGR SLVWGAEAVQ ALRERLGVGG RTVGALPRGP RQNSRLGLPL LLLPEEARLL 

        70         80         90        100        110        120 
AEIGAVTLVS APRPDPRNHG LALASFKRQQ EQSFQDQNTL AAEARETRRQ ELLEKIVEGQ 

       130        140        150        160        170        180 
AAKKQKLEQD SGADEGGQEA GGSEATQGSE TSDDGQPSAE QEGAAPSLDS SSPQPGPSNG 

       190        200        210        220        230        240 
VTPLPRSALL IQLATARPRP VKAKPLDWRV QSKDWPHAGR PAHELRYSIY RDLWERGFFL 

       250        260        270        280        290        300 
SAAGKFGGDF LVYPGDPLRF HAHYIAQCWS AEDPIPLQDL VSAGRLGTSV RKTLLLCSPQ 

       310 
PDGKVVYTSL QWASLQ 

« Hide

Isoform 2 [UniParc].

Checksum: 0692A1E911014158
Show »

FASTA28730,964

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Strain: C57BL/6J.
Tissue: Embryo and Oviduct.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: FVB/N.
Tissue: Salivary gland.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK003757 mRNA. Translation: BAC25051.1.
AK013253 mRNA. Translation: BAB28747.1.
AK053916 mRNA. Translation: BAC35591.1.
BC002205 mRNA. Translation: AAH02205.1.
BC091756 mRNA. Translation: AAH91756.1.
CCDSCCDS20725.1. [Q8BMZ5-1]
CCDS51966.1. [Q8BMZ5-2]
RefSeqNP_001157676.1. NM_001164204.1. [Q8BMZ5-1]
NP_001157677.1. NM_001164205.1. [Q8BMZ5-2]
NP_077130.1. NM_024168.2. [Q8BMZ5-1]
XP_006540345.1. XM_006540282.1. [Q8BMZ5-1]
XP_006540346.1. XM_006540283.1. [Q8BMZ5-1]
XP_006540347.1. XM_006540284.1. [Q8BMZ5-1]
XP_006540348.1. XM_006540285.1. [Q8BMZ5-1]
UniGeneMm.379100.

3D structure databases

ProteinModelPortalQ8BMZ5.
SMRQ8BMZ5. Positions 203-312.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ8BMZ5. 1 interaction.

PTM databases

PhosphoSiteQ8BMZ5.

Proteomic databases

PaxDbQ8BMZ5.
PRIDEQ8BMZ5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000108627; ENSMUSP00000104267; ENSMUSG00000035585. [Q8BMZ5-1]
ENSMUST00000108629; ENSMUSP00000104269; ENSMUSG00000035585. [Q8BMZ5-2]
ENSMUST00000108630; ENSMUSP00000104270; ENSMUSG00000035585. [Q8BMZ5-1]
GeneID66078.
KEGGmmu:66078.
UCSCuc009evu.2. mouse. [Q8BMZ5-2]
uc009evv.2. mouse. [Q8BMZ5-1]

Organism-specific databases

CTD79042.
MGIMGI:1913328. Tsen34.

Phylogenomic databases

eggNOGCOG1676.
GeneTreeENSGT00390000003912.
HOGENOMHOG000232197.
HOVERGENHBG054846.
InParanoidQ8BMZ5.
KOK15323.
OMARTFSIEW.
OrthoDBEOG75XGMQ.
PhylomeDBQ8BMZ5.
TreeFamTF314631.

Gene expression databases

BgeeQ8BMZ5.
GenevestigatorQ8BMZ5.

Family and domain databases

Gene3D3.40.1350.10. 1 hit.
InterProIPR011856. tRNA_endonuc-like_dom.
IPR006677. tRNA_intron_Endonuc_cat-like.
IPR006676. tRNA_splic.
IPR016690. tRNA_splic_SEN34.
[Graphical view]
PfamPF01974. tRNA_int_endo. 1 hit.
[Graphical view]
PIRSFPIRSF017250. tRNA_splic_SEN34. 1 hit.
SUPFAMSSF53032. SSF53032. 1 hit.
TIGRFAMsTIGR00324. endA. 1 hit.
ProtoNetSearch...

Other

NextBio320564.
PROQ8BMZ5.
SOURCESearch...

Entry information

Entry nameSEN34_MOUSE
AccessionPrimary (citable) accession number: Q8BMZ5
Secondary accession number(s): Q58EU2, Q99LV6, Q9CYW1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: July 19, 2004
Last modified: July 9, 2014
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot