SLU7_MOUSE
ID SLU7_MOUSE Reviewed; 585 AA.
AC Q8BHJ9; Q3KQQ3; Q5SRU1; Q63ZX3; Q6P923; Q8BL59; Q8BXD5; Q8R5C1; Q91YV6;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Pre-mRNA-splicing factor SLU7;
GN Name=Slu7; Synonyms=D11Ertd730e;
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].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Corpora quadrigemina, and Skin;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Heart, Kidney, Lung, and Mammary tumor;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215 AND SER-235, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Required for pre-mRNA splicing as component of the
CC spliceosome. Participates in the second catalytic step of pre-mRNA
CC splicing, when the free hydroxyl group of exon I attacks the 3'-splice
CC site to generate spliced mRNA and the excised lariat intron. Required
CC for holding exon 1 properly in the spliceosome and for correct AG
CC identification when more than one possible AG exists in 3'-splicing
CC site region. May be involved in the activation of proximal AG. Probably
CC also involved in alternative splicing regulation.
CC {ECO:0000250|UniProtKB:O95391}.
CC -!- SUBUNIT: Component of pre-catalytic, catalytic and post-catalytic
CC spliceosomes. Associates with the spliceosome prior to recognition of
CC the 3'-splice site for step II, probably during catalysis of step I.
CC {ECO:0000250|UniProtKB:O95391}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O95391}. Nucleus
CC speckle {ECO:0000250|UniProtKB:O95391}. Cytoplasm
CC {ECO:0000250|UniProtKB:O95391}. Note=Predominantly nuclear. Shuttling
CC between the nucleus and the cytoplasm is regulated by the CCHC-type
CC zinc finger. Upon UV-C stress stimulus, the nuclear concentration of
CC the protein decreases, affecting alternative splicing. Translocates
CC from the nucleus to the cytoplasm after heat shock cell treatment.
CC Accumulates in cytoplasmic vesicle-like organelles after heat shock
CC treatment, which may represent stress granules.
CC {ECO:0000250|UniProtKB:O95391}.
CC -!- DOMAIN: The CCHC-type zinc finger is required to retain the protein
CC within the nucleus and prevent its shuttle back to the cytoplasm via
CC the CRM1 pathway. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SLU7 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH13810.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAI24831.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AK029117; BAC26306.1; -; mRNA.
DR EMBL; AK046262; BAC32662.1; -; mRNA.
DR EMBL; AK047597; BAC33093.1; -; mRNA.
DR EMBL; AK049178; BAC33589.1; -; mRNA.
DR EMBL; AL670472; CAI24830.1; -; Genomic_DNA.
DR EMBL; AL670472; CAI24831.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC013810; AAH13810.1; ALT_INIT; mRNA.
DR EMBL; BC023057; AAH23057.1; -; mRNA.
DR EMBL; BC060954; AAH60954.1; -; mRNA.
DR EMBL; BC082780; AAH82780.1; ALT_TERM; mRNA.
DR EMBL; BC106099; AAI06100.1; -; mRNA.
DR CCDS; CCDS24557.1; -.
DR RefSeq; NP_683514.2; NM_148673.3.
DR RefSeq; NP_945174.1; NM_198936.1.
DR RefSeq; XP_011247125.1; XM_011248823.1.
DR AlphaFoldDB; Q8BHJ9; -.
DR SMR; Q8BHJ9; -.
DR BioGRID; 228728; 20.
DR STRING; 10090.ENSMUSP00000020681; -.
DR iPTMnet; Q8BHJ9; -.
DR PhosphoSitePlus; Q8BHJ9; -.
DR EPD; Q8BHJ9; -.
DR jPOST; Q8BHJ9; -.
DR MaxQB; Q8BHJ9; -.
DR PaxDb; Q8BHJ9; -.
DR PeptideAtlas; Q8BHJ9; -.
DR PRIDE; Q8BHJ9; -.
DR ProteomicsDB; 261083; -.
DR Antibodypedia; 28531; 339 antibodies from 29 providers.
DR DNASU; 193116; -.
DR Ensembl; ENSMUST00000020681; ENSMUSP00000020681; ENSMUSG00000020409.
DR Ensembl; ENSMUST00000178622; ENSMUSP00000137281; ENSMUSG00000020409.
DR GeneID; 193116; -.
DR KEGG; mmu:193116; -.
DR UCSC; uc007imp.1; mouse.
DR CTD; 10569; -.
DR MGI; MGI:2385598; Slu7.
DR VEuPathDB; HostDB:ENSMUSG00000020409; -.
DR eggNOG; KOG2560; Eukaryota.
DR GeneTree; ENSGT00390000002292; -.
DR HOGENOM; CLU_019317_2_0_1; -.
DR InParanoid; Q8BHJ9; -.
DR OMA; KKPFYVD; -.
DR OrthoDB; 816947at2759; -.
DR PhylomeDB; Q8BHJ9; -.
DR TreeFam; TF105691; -.
DR Reactome; R-MMU-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-MMU-72187; mRNA 3'-end processing.
DR Reactome; R-MMU-73856; RNA Polymerase II Transcription Termination.
DR BioGRID-ORCS; 193116; 24 hits in 72 CRISPR screens.
DR ChiTaRS; Slu7; mouse.
DR PRO; PR:Q8BHJ9; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8BHJ9; protein.
DR Bgee; ENSMUSG00000020409; Expressed in saccule of membranous labyrinth and 275 other tissues.
DR ExpressionAtlas; Q8BHJ9; baseline and differential.
DR Genevisible; Q8BHJ9; MM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISS:HGNC-UCL.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0030532; C:small nuclear ribonucleoprotein complex; ISS:HGNC-UCL.
DR GO; GO:0005681; C:spliceosomal complex; ISS:HGNC-UCL.
DR GO; GO:0030628; F:pre-mRNA 3'-splice site binding; ISS:HGNC-UCL.
DR GO; GO:0000386; F:second spliceosomal transesterification activity; ISS:HGNC-UCL.
DR GO; GO:0008270; F:zinc ion binding; ISS:HGNC-UCL.
DR GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; ISS:HGNC-UCL.
DR GO; GO:0034605; P:cellular response to heat; ISS:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; ISS:UniProtKB.
DR GO; GO:0000389; P:mRNA 3'-splice site recognition; ISS:HGNC-UCL.
DR GO; GO:0008380; P:RNA splicing; IBA:GO_Central.
DR GO; GO:0000375; P:RNA splicing, via transesterification reactions; ISS:HGNC-UCL.
DR InterPro; IPR021715; Slu7_dom.
DR InterPro; IPR039974; Splicing_factor_SLU7.
DR PANTHER; PTHR12942; PTHR12942; 1.
DR Pfam; PF11708; Slu7; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Isopeptide bond; Metal-binding; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Spliceosome;
KW Ubl conjugation; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O95391"
FT CHAIN 2..585
FT /note="Pre-mRNA-splicing factor SLU7"
FT /id="PRO_0000289196"
FT ZN_FING 118..135
FT /note="CCHC-type"
FT REGION 1..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 129..169
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 20..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..529
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..576
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:O95391"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95391"
FT MOD_RES 235
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT CROSSLNK 349
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O95391"
FT CROSSLNK 408
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O95391"
FT CONFLICT 43
FT /note="R -> K (in Ref. 1; BAC32662)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="Y -> H (in Ref. 1; BAC33093)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 585 AA; 68080 MW; 1020FE4B6D65668B CRC64;
MSAAAVDPVS ATPMTGSKEM SLEEPKKMTR EDWRKKKELE EQRKLGNAPA EVDEEGKDIN
PHIPQYISSV PWYIDPSKRP TLKHQRPQPE KQKQFSSSGE WYKRGVKENS ITTKYRKGAC
ENCGAMTHKR KDCFERPRRV GAKFTGTNIA PDEHVQPQLM FDYDGKRDRW NGYNPEEHMK
IVEEYAKVDL AKRTLKAQKL QEELASGKLV EQANSPKHQW GEEEPNSQME KDHNSEDEDE
DKYADDIDMP GQNFDSKRRI TVRNLRIRED IAKYLRNLDP NSAYYDPKTR AMRENPYANA
GKNPDEVSYA GDNFVRYTGD TISMAQTQLF AWEAYDKGSE VHLQADPTKL ELLYKSFKVK
KEDFKEQQKE SILEKYGGQE HLDAPPAELL LAQTEDYVEY SRHGTVIKGQ ERAVACSKYE
EDVKINNHTH IWGSYWKEGR WGYKCCHSFF KYSYCTGEAG KESVNSEECI ITGATAEESV
KKPQALLELH QEKLKEEKKK KKKKKKHRKS SSDSDDEERK QEKLKKALNA EEARLLHVKE
IMQIDERKRP YNSIYETREP TEEEMEAYRM KRQRPDDPMA SFLGQ
