SRSF6_RAT
ID SRSF6_RAT Reviewed; 339 AA.
AC G3V6S8; Q5PQM1;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Serine/arginine-rich splicing factor 6;
DE AltName: Full=Pre-mRNA-splicing factor SRP55;
DE AltName: Full=Splicing factor, arginine/serine-rich 6;
GN Name=Srsf6; Synonyms=Sfrs6, Srp55;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=12549914; DOI=10.1021/bi026753a;
RA Tran Q., Roesser J.R.;
RT "SRp55 is a regulator of calcitonin/CGRP alternative RNA splicing.";
RL Biochemistry 42:951-957(2003).
RN [5]
RP INTERACTION WITH DYRK1A, AND TISSUE SPECIFICITY.
RX PubMed=22767602; DOI=10.1074/jbc.m112.355412;
RA Yin X., Jin N., Gu J., Shi J., Zhou J., Gong C.X., Iqbal K.,
RA Grundke-Iqbal I., Liu F.;
RT "Dual-specificity tyrosine phosphorylation-regulated kinase 1A (Dyrk1A)
RT modulates serine/arginine-rich protein 55 (SRp55)-promoted Tau exon 10
RT inclusion.";
RL J. Biol. Chem. 287:30497-30506(2012).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45 AND SER-303, 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: Plays a role in constitutive splicing and modulates the
CC selection of alternative splice sites. Plays a role in the alternative
CC splicing of MAPT/Tau exon 10. Binds to alternative exons of TNC pre-
CC mRNA and promotes the expression of alternatively spliced TNC. Plays a
CC role in wound healing and in the regulation of keratinocyte
CC differentiation and proliferation via its role in alternative splicing
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binds SREK1/SFRS12 (By similarity). Interacts with DYRK1A.
CC {ECO:0000250, ECO:0000269|PubMed:22767602}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12549914}. Nucleus
CC speckle {ECO:0000250|UniProtKB:Q13247}.
CC -!- TISSUE SPECIFICITY: Detected in liver and brain (at protein level).
CC {ECO:0000269|PubMed:12549914, ECO:0000269|PubMed:22767602}.
CC -!- PTM: Extensively phosphorylated on serine residues in the RS domain.
CC Phosphorylated by DYRK1A, probably in the RS domain. Phosphorylation by
CC DYRK1A modulates alternative splice site selection and inhibits the
CC expression of MAPT/Tau exon 10 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
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DR EMBL; AABR06027490; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH474005; EDL96600.1; -; Genomic_DNA.
DR EMBL; BC087121; AAH87121.1; -; mRNA.
DR RefSeq; NP_001014207.2; NM_001014185.2.
DR AlphaFoldDB; G3V6S8; -.
DR SMR; G3V6S8; -.
DR BioGRID; 263314; 3.
DR IntAct; G3V6S8; 2.
DR MINT; G3V6S8; -.
DR STRING; 10116.ENSRNOP00000008427; -.
DR iPTMnet; G3V6S8; -.
DR PhosphoSitePlus; G3V6S8; -.
DR jPOST; G3V6S8; -.
DR PaxDb; G3V6S8; -.
DR PRIDE; G3V6S8; -.
DR Ensembl; ENSRNOT00000008427; ENSRNOP00000008427; ENSRNOG00000006380.
DR GeneID; 362264; -.
DR KEGG; rno:362264; -.
DR UCSC; RGD:1359241; rat.
DR CTD; 6431; -.
DR RGD; 1359241; Srsf6.
DR eggNOG; KOG0106; Eukaryota.
DR GeneTree; ENSGT00940000155448; -.
DR HOGENOM; CLU_012062_34_2_1; -.
DR InParanoid; G3V6S8; -.
DR OMA; DRVSHSH; -.
DR OrthoDB; 1315388at2759; -.
DR PhylomeDB; G3V6S8; -.
DR TreeFam; TF351335; -.
DR Reactome; R-RNO-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-RNO-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-RNO-72165; mRNA Splicing - Minor Pathway.
DR Reactome; R-RNO-72187; mRNA 3'-end processing.
DR Reactome; R-RNO-73856; RNA Polymerase II Transcription Termination.
DR PRO; PR:G3V6S8; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Proteomes; UP000234681; Chromosome 3.
DR Bgee; ENSRNOG00000006380; Expressed in thymus and 20 other tissues.
DR Genevisible; G3V6S8; RN.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0036002; F:pre-mRNA binding; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0006376; P:mRNA splice site selection; ISS:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0060548; P:negative regulation of cell death; ISO:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:RGD.
DR GO; GO:0045617; P:negative regulation of keratinocyte differentiation; ISS:UniProtKB.
DR GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; ISO:RGD.
DR GO; GO:2000675; P:negative regulation of type B pancreatic cell apoptotic process; IMP:RGD.
DR GO; GO:0060501; P:positive regulation of epithelial cell proliferation involved in lung morphogenesis; ISO:RGD.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0010837; P:regulation of keratinocyte proliferation; ISS:UniProtKB.
DR GO; GO:0061041; P:regulation of wound healing; ISS:UniProtKB.
DR GO; GO:0032868; P:response to insulin; IEP:RGD.
DR CDD; cd12596; RRM1_SRSF6; 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; IPR000504; RRM_dom.
DR InterPro; IPR029541; SRSF6.
DR InterPro; IPR034511; SRSF6_RRM1.
DR PANTHER; PTHR23147:SF82; PTHR23147:SF82; 1.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW Acetylation; Isopeptide bond; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; RNA-binding;
KW Ubl conjugation.
FT CHAIN 1..339
FT /note="Serine/arginine-rich splicing factor 6"
FT /id="PRO_0000426096"
FT DOMAIN 2..72
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 110..183
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 75..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..249
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..295
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13247"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13247"
FT MOD_RES 165
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q3TWW8"
FT MOD_RES 297
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13247"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13247"
FT MOD_RES 303
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13247"
FT MOD_RES 316
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13247"
FT CROSSLNK 182
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13247"
FT CONFLICT 181
FT /note="D -> Y (in Ref. 3; AAH87121)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 339 AA; 39025 MW; AE8B6650D7294A0D CRC64;
MPRVYIGRLS YNVREKDIQR FFSGYGRLLE IDLKNGYGFV EFEDSRDADD AVYELNSKEL
CGERVIVEHA RGPRRDRDGY SYGSRSGGGG YSSRRTSGRD KYGPPVRTEY RLIVENLSSR
CSWQDLKDFM RQAGEVTYAD AHKERTNEGV IEFRSYSDMK RALDKLDGTE INGRNIRLIE
DKPRTSHRRS YSGSRSRSRS RRRSRSRSRR SSRSRSRSIS KSRSRSRSRS KGRSRSRSKG
RKSRSKSKSK PKSDRGSHSH SRSRSKDKYG KSRSRSRSRS PKENGKGDIK SKSRSRSQSR
SHSPLPAPPS KARSMSPPPK RASRSRSRSR SRSRSSSRD
