SREK1_RAT
ID SREK1_RAT Reviewed; 494 AA.
AC Q9JKL7;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Splicing regulatory glutamine/lysine-rich protein 1;
DE AltName: Full=SR-related protein of 86 kDa;
DE AltName: Full=Serine/arginine-rich-splicing regulatory protein 86;
DE Short=SRrp86;
DE AltName: Full=Splicing factor, arginine/serine-rich 12;
GN Name=Srek1; Synonyms=Sfrs12, Srrp86;
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], FUNCTION, HOMODIMERIZATION, AND INTERACTION
RP WITH SFRS1; SFRS2; SFRS3 AND SFRS6.
RC TISSUE=Brain;
RX PubMed=10757789; DOI=10.1128/mcb.20.9.3049-3057.2000;
RA Barnard D.C., Patton J.G.;
RT "Identification and characterization of a novel serine-arginine-rich
RT splicing regulatory protein.";
RL Mol. Cell. Biol. 20:3049-3057(2000).
RN [2]
RP FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH SFRS2 AND SFRS3.
RX PubMed=11991645; DOI=10.1017/s1355838202029928;
RA Barnard D.C., Li J., Peng R., Patton J.G.;
RT "Regulation of alternative splicing by SRrp86 through coactivation and
RT repression of specific SR proteins.";
RL RNA 8:526-533(2002).
CC -!- FUNCTION: Participates in the regulation of alternative splicing by
CC modulating the activity of other splice facors. Inhibits the splicing
CC activity of SFRS1, SFRS2 and SFRS6. Augments the splicing activity of
CC SFRS3. {ECO:0000269|PubMed:10757789, ECO:0000269|PubMed:11991645}.
CC -!- SUBUNIT: Interacts with SREK1IP1 (By similarity). Homodimer. Binds
CC SFRS1, SFRS2, SFRS3 and SFRS6. Interacts with the spliceosome.
CC {ECO:0000250, ECO:0000269|PubMed:10757789,
CC ECO:0000269|PubMed:11991645}.
CC -!- INTERACTION:
CC Q9JKL7; Q92841: DDX17; Xeno; NbExp=3; IntAct=EBI-6452221, EBI-746012;
CC Q9JKL7; P38159: RBMX; Xeno; NbExp=3; IntAct=EBI-6452221, EBI-743526;
CC Q9JKL7; Q15424: SAFB; Xeno; NbExp=3; IntAct=EBI-6452221, EBI-348298;
CC Q9JKL7; P84103: SRSF3; Xeno; NbExp=3; IntAct=EBI-6452221, EBI-372557;
CC Q9JKL7; Q16629: SRSF7; Xeno; NbExp=3; IntAct=EBI-6452221, EBI-398885;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Detected in liver, brain, lung, spleen,
CC testis and pancreas. {ECO:0000269|PubMed:11991645}.
CC -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
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DR EMBL; AF234765; AAF37578.1; -; mRNA.
DR RefSeq; NP_064477.1; NM_020092.1.
DR AlphaFoldDB; Q9JKL7; -.
DR SMR; Q9JKL7; -.
DR IntAct; Q9JKL7; 53.
DR STRING; 10116.ENSRNOP00000049050; -.
DR PhosphoSitePlus; Q9JKL7; -.
DR PaxDb; Q9JKL7; -.
DR PRIDE; Q9JKL7; -.
DR GeneID; 56763; -.
DR KEGG; rno:56763; -.
DR UCSC; RGD:621696; rat.
DR CTD; 140890; -.
DR RGD; 621696; Srek1.
DR eggNOG; KOG4676; Eukaryota.
DR InParanoid; Q9JKL7; -.
DR PRO; PR:Q9JKL7; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR CDD; cd12260; RRM2_SREK1; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR034192; SREK1_RRM2.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Spliceosome.
FT CHAIN 1..494
FT /note="Splicing regulatory glutamine/lysine-rich protein 1"
FT /id="PRO_0000081942"
FT DOMAIN 69..145
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 176..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..261
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..350
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..393
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..480
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WXA9"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WXA9"
FT MOD_RES 348
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8WXA9"
SQ SEQUENCE 494 AA; 56849 MW; 1BD81112FAD6132E CRC64;
MTSLVPGAGL LPIPTSSPLT AVSSLGVSLS SLGAIPAAAL DPNITALGEI PQPPLMGNVD
PSKIDEIRRT VYVGNLNSQT TTADQLLEFF KQVGEVKFVR MAGDETQPTR FAFVEFADQN
SVPRALAFNG VMFGDRPLKI NHSNNAIVKP PEMTPQAAAK ELEEVMKRVR EAQSFISAAI
EPESGKSNER KGGRSRSHTR SKSRSSSKSH SRRKRSQSKH RSRSHNRSRS RQKDRARSKS
PHKKRSKSRE RRKSRSRSRS RDKRKDTREK VKERVKERER EKEKEREKER EKDKERGKNK
DKDREKEKDH EKERDKEKEK EQDKDKEREK DRSKEADEKR KKEKKSRTPP RSYNSSRRSR
SASRERRRRR SRSSSRSPRT SKTIKRKSSR SPSPRGRNKK EKKREKERDH ISDRRERERS
TSTKKSSSDR DGKEKVEKTN TPVKEKEHSK EADSTVSTDA DEKDTARTEE ESKAQHNGNC
QPHEERLCST ADAV
