SRSF5_MOUSE
ID SRSF5_MOUSE Reviewed; 269 AA.
AC O35326; Q640L9;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Serine/arginine-rich splicing factor 5;
DE AltName: Full=Delayed-early protein HRS;
DE AltName: Full=Pre-mRNA-splicing factor SRP40;
DE AltName: Full=Splicing factor, arginine/serine-rich 5;
GN Name=Srsf5; Synonyms=Hrs, Sfrs5;
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 [GENOMIC DNA].
RC TISSUE=Liver;
RX PubMed=9434190; DOI=10.1016/s0378-1119(97)00552-0;
RA Du K., Taub R.;
RT "Alternative splicing and structure of the human and mouse SFRS5/HRS/SRp40
RT genes.";
RL Gene 204:243-249(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Amnion;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [6]
RP INTERACTION WITH PHF5A.
RX PubMed=18758164; DOI=10.1159/000138890;
RA Rzymski T., Grzmil P., Meinhardt A., Wolf S., Burfeind P.;
RT "PHF5A represents a bridge protein between splicing proteins and ATP-
RT dependent helicases and is differentially expressed during mouse
RT spermatogenesis.";
RL Cytogenet. Genome Res. 121:232-244(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-167, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: May be required for progression through G1 and entry into S
CC phase of cell growth. May play a regulatory role in pre-mRNA splicing.
CC Autoregulates its own expression. Plays a role in constitutive splicing
CC and can modulate the selection of alternative splice sites (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Found in a pre-mRNA splicing complex with SRSF4/SFRS4,
CC SRSF5/SFRS5, SNRNP70, SNRPA1, SRRM1 and SRRM2 (By similarity).
CC Interacts (via RS domain) with PHF5A (via N-terminus). {ECO:0000250,
CC ECO:0000269|PubMed:18758164}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- PTM: Extensively phosphorylated on serine residues in the RS domain.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
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DR EMBL; AF020308; AAC39946.1; -; Genomic_DNA.
DR EMBL; AK146624; BAE27313.1; -; mRNA.
DR EMBL; AC125092; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466590; EDL02685.1; -; Genomic_DNA.
DR EMBL; CH466590; EDL02687.1; -; Genomic_DNA.
DR EMBL; CH466590; EDL02690.1; -; Genomic_DNA.
DR EMBL; CH466590; EDL02692.1; -; Genomic_DNA.
DR EMBL; CH466590; EDL02693.1; -; Genomic_DNA.
DR EMBL; BC082593; AAH82593.1; -; mRNA.
DR CCDS; CCDS36484.1; -.
DR RefSeq; NP_001073162.1; NM_001079694.2.
DR RefSeq; NP_001073163.1; NM_001079695.2.
DR RefSeq; NP_001334345.1; NM_001347416.1.
DR RefSeq; NP_033185.2; NM_009159.3.
DR AlphaFoldDB; O35326; -.
DR SMR; O35326; -.
DR BioGRID; 203190; 16.
DR DIP; DIP-48724N; -.
DR IntAct; O35326; 2.
DR MINT; O35326; -.
DR STRING; 10090.ENSMUSP00000105985; -.
DR iPTMnet; O35326; -.
DR PhosphoSitePlus; O35326; -.
DR EPD; O35326; -.
DR jPOST; O35326; -.
DR PaxDb; O35326; -.
DR PeptideAtlas; O35326; -.
DR PRIDE; O35326; -.
DR ProteomicsDB; 257414; -.
DR Antibodypedia; 25065; 117 antibodies from 26 providers.
DR DNASU; 20384; -.
DR Ensembl; ENSMUST00000094693; ENSMUSP00000131323; ENSMUSG00000021134.
DR Ensembl; ENSMUST00000110352; ENSMUSP00000105981; ENSMUSG00000021134.
DR Ensembl; ENSMUST00000110356; ENSMUSP00000105985; ENSMUSG00000021134.
DR GeneID; 20384; -.
DR KEGG; mmu:20384; -.
DR UCSC; uc007obo.1; mouse.
DR CTD; 6430; -.
DR MGI; MGI:98287; Srsf5.
DR VEuPathDB; HostDB:ENSMUSG00000021134; -.
DR eggNOG; KOG0106; Eukaryota.
DR GeneTree; ENSGT00940000158275; -.
DR HOGENOM; CLU_012062_34_2_1; -.
DR InParanoid; O35326; -.
DR OMA; WETXARE; -.
DR TreeFam; TF351335; -.
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; 20384; 12 hits in 72 CRISPR screens.
DR ChiTaRS; Srsf5; mouse.
DR PRO; PR:O35326; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; O35326; protein.
DR Bgee; ENSMUSG00000021134; Expressed in retinal neural layer and 74 other tissues.
DR ExpressionAtlas; O35326; baseline and differential.
DR Genevisible; O35326; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0043422; F:protein kinase B binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; ISO:MGI.
DR GO; GO:0050733; F:RS domain binding; IPI:MGI.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0033120; P:positive regulation of RNA splicing; ISO:MGI.
DR GO; GO:0032868; P:response to insulin; ISO:MGI.
DR GO; GO:0009611; P:response to wounding; IDA:MGI.
DR CDD; cd12337; RRM1_SRSF4_like; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR035585; RRM1_SRSF4-like.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW Acetylation; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding; Transcription;
KW Transcription regulation.
FT CHAIN 1..269
FT /note="Serine/arginine-rich splicing factor 5"
FT /id="PRO_0000081928"
FT DOMAIN 4..74
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 108..189
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 73..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..224
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13243"
FT MOD_RES 167
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13243"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13243"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13243"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13243"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13243"
SQ SEQUENCE 269 AA; 30891 MW; 0FC90628B64DE845 CRC64;
MSGCRVFIGR LNPAAREKDV ERFFKGYGRI RDIDLKRGFG FVEFEDPRDA DDAVYELDGK
ELCSERVTIE HARARSRGGR GRGRYSDRFS SRRPRNDRRN APPVRTENRL IVENLSSRVS
WQDLKDFMRQ AGEVTFADAH RPKLNEGVVE FASYGDLKNA IEKLSGKEIN GRKIKLIEGS
KRHRSRSRSR SRTRSSSRSR SRSRSRRSKS YSRSRSRSRS RSKSRSGSRS PVPEKSQKRG
SSSRSKSPAS VDRQRSRSRS RSRSVDSGN
