SLU7_RAT
ID SLU7_RAT Reviewed; 586 AA.
AC Q80ZG5; Q6P6G1;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Pre-mRNA-splicing factor SLU7;
GN Name=Slu7;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15181151; DOI=10.1091/mbc.e04-02-0152;
RA Shomron N., Reznik M., Ast G.;
RT "Splicing factor hSlu7 contains a unique functional domain required to
RT retain the protein within the nucleus.";
RL Mol. Biol. Cell 15:3782-3795(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-493.
RC TISSUE=Pituitary;
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-215 AND SER-235, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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=AAO17154.2; Type=Miscellaneous discrepancy; Note=Many sequencing errors.; Evidence={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; AY207315; AAO17154.2; ALT_SEQ; mRNA.
DR EMBL; AABR03074285; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03076495; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC062243; AAH62243.1; ALT_TERM; mRNA.
DR RefSeq; NP_001094020.1; NM_001100550.1.
DR RefSeq; XP_008765864.1; XM_008767642.2.
DR AlphaFoldDB; Q80ZG5; -.
DR SMR; Q80ZG5; -.
DR STRING; 10116.ENSRNOP00000005132; -.
DR iPTMnet; Q80ZG5; -.
DR PhosphoSitePlus; Q80ZG5; -.
DR PaxDb; Q80ZG5; -.
DR PRIDE; Q80ZG5; -.
DR Ensembl; ENSRNOT00000005132; ENSRNOP00000005132; ENSRNOG00000003822.
DR GeneID; 303057; -.
DR KEGG; rno:303057; -.
DR UCSC; RGD:631432; rat.
DR CTD; 10569; -.
DR RGD; 631432; Slu7.
DR eggNOG; KOG2560; Eukaryota.
DR GeneTree; ENSGT00390000002292; -.
DR HOGENOM; CLU_019317_2_0_1; -.
DR InParanoid; Q80ZG5; -.
DR OMA; KKPFYVD; -.
DR OrthoDB; 816947at2759; -.
DR PhylomeDB; Q80ZG5; -.
DR TreeFam; TF105691; -.
DR Reactome; R-RNO-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-RNO-72187; mRNA 3'-end processing.
DR Reactome; R-RNO-73856; RNA Polymerase II Transcription Termination.
DR PRO; PR:Q80ZG5; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000003822; Expressed in lung and 20 other tissues.
DR ExpressionAtlas; Q80ZG5; baseline and differential.
DR Genevisible; Q80ZG5; RN.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0016607; C:nuclear speck; ISS:HGNC-UCL.
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..586
FT /note="Pre-mRNA-splicing factor SLU7"
FT /id="PRO_0000289197"
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..586
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..577
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:22673903"
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:22673903"
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"
SQ SEQUENCE 586 AA; 68337 MW; DBDBFBCDE5DC571A CRC64;
MSAAAVDPVS ATPMTGSKEM NLEEPKKMTR EDWRKKKELE EQRKLGNAPA EVDEEGKDIN
PHIPQYISSV PWYIDPSKRP TLKHQRPQPE KQKQFSSSGE WYKRGVKENS ITTKYRKGAC
ENCGAMTHKR KDCFERPRRV GAKFTGTNIA PDEHIQPQLM 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 INDATGEEPV
KKPQTLMELH QEKLKEEKKK KKKKKKHRKS SSDSDDDEER KQEKLKKALN AEEARLLHVK
EIMQVDERKR PYNSIYETRE PTEEEMEAYR MKRQRPDDPM ASFLGQ
