SRSF5_RAT
ID SRSF5_RAT Reviewed; 269 AA.
AC Q09167; O35335;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Serine/arginine-rich splicing factor 5;
DE AltName: Full=Delayed-early protein HRS;
DE AltName: Full=Insulin-induced growth response protein CL-4;
DE AltName: Full=Pre-mRNA-splicing factor SRP40;
DE AltName: Full=Splicing factor, arginine/serine-rich 5;
GN Name=Srsf5; Synonyms=Cl-4, Hrs, Sfrs5;
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].
RC TISSUE=Liver;
RX PubMed=7686911; DOI=10.1016/s0021-9258(18)82454-1;
RA Diamond R.H., Du K., Lee V.M., Mohn K.L., Haber B.A., Tewari D.S., Taub R.;
RT "Novel delayed-early and highly insulin-induced growth response genes.
RT Identification of HRS, a potential regulator of alternative pre-mRNA
RT splicing.";
RL J. Biol. Chem. 268:15185-15192(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Thymus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 NUCLEOTIDE SEQUENCE [MRNA] OF 185-269.
RC STRAIN=Sprague-Dawley; TISSUE=Testis;
RX PubMed=8161377; DOI=10.1210/endo.134.3.8161377;
RA Hamil K.G., Hall S.H.;
RT "Cloning of rat Sertoli cell follicle-stimulating hormone primary response
RT complementary deoxyribonucleic acid: regulation of TSC-22 gene
RT expression.";
RL Endocrinology 134:1205-1212(1994).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND IDENTIFICATION BY
RP 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: 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). Could play an important role in development and
CC differentiation in the spleen and thymus. {ECO:0000250}.
CC -!- SUBUNIT: Found in a pre-mRNA splicing complex with SRSF4/SFRS4,
CC SRSF5/SFRS5, SNRNP70, SNRPA1, SRRM1 and SRRM2. Interacts (via RS
CC domain) with PHF5A (via N-terminus) (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q09167-1; Sequence=Displayed;
CC Name=2; Synonyms=HRR-LF;
CC IsoId=Q09167-2; Sequence=VSP_005867, VSP_005868;
CC -!- TISSUE SPECIFICITY: Highly expressed in spleen and thymus.
CC -!- INDUCTION: By insulin and hepatectomy.
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; L13635; AAA62266.1; -; mRNA.
DR EMBL; AF020683; AAB71864.1; -; mRNA.
DR EMBL; BC058479; AAH58479.1; -; mRNA.
DR EMBL; L33267; AAA42316.1; -; mRNA.
DR PIR; B47112; B47112.
DR RefSeq; NP_001182434.1; NM_001195505.1. [Q09167-1]
DR RefSeq; NP_001182435.1; NM_001195506.1. [Q09167-1]
DR RefSeq; NP_062130.2; NM_019257.3. [Q09167-1]
DR AlphaFoldDB; Q09167; -.
DR SMR; Q09167; -.
DR BioGRID; 248288; 2.
DR STRING; 10116.ENSRNOP00000007583; -.
DR iPTMnet; Q09167; -.
DR PhosphoSitePlus; Q09167; -.
DR jPOST; Q09167; -.
DR PaxDb; Q09167; -.
DR PRIDE; Q09167; -.
DR DNASU; 29667; -.
DR Ensembl; ENSRNOT00000107441; ENSRNOP00000087250; ENSRNOG00000005513. [Q09167-1]
DR GeneID; 29667; -.
DR KEGG; rno:29667; -.
DR UCSC; RGD:3664; rat. [Q09167-1]
DR CTD; 6430; -.
DR RGD; 3664; Srsf5.
DR eggNOG; KOG0106; Eukaryota.
DR GeneTree; ENSGT00940000158275; -.
DR HOGENOM; CLU_012062_34_2_1; -.
DR InParanoid; Q09167; -.
DR OMA; WETXARE; -.
DR OrthoDB; 1315388at2759; -.
DR PhylomeDB; Q09167; -.
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-72187; mRNA 3'-end processing.
DR Reactome; R-RNO-73856; RNA Polymerase II Transcription Termination.
DR PRO; PR:Q09167; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000005513; Expressed in thymus and 19 other tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0043422; F:protein kinase B binding; IPI:RGD.
DR GO; GO:0003723; F:RNA binding; IDA:RGD.
DR GO; GO:0050733; F:RS domain binding; ISO:RGD.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IEP:RGD.
DR GO; GO:0001889; P:liver development; IEP:RGD.
DR GO; GO:0097421; P:liver regeneration; IEP:RGD.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0033120; P:positive regulation of RNA splicing; IMP:RGD.
DR GO; GO:0051726; P:regulation of cell cycle; IEP:RGD.
DR GO; GO:0032868; P:response to insulin; IDA:RGD.
DR GO; GO:0009611; P:response to wounding; ISO:RGD.
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; Alternative splicing; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; RNA-binding; Transcription;
KW Transcription regulation.
FT CHAIN 1..269
FT /note="Serine/arginine-rich splicing factor 5"
FT /id="PRO_0000081929"
FT DOMAIN 4..74
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 108..181
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:0000250|UniProtKB:Q13243"
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:0007744|PubMed:22673903"
FT VAR_SEQ 123..124
FT /note="DL -> VC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9434190"
FT /id="VSP_005867"
FT VAR_SEQ 125..269
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9434190"
FT /id="VSP_005868"
FT CONFLICT 69
FT /note="I -> M (in Ref. 2; AAB71864)"
FT /evidence="ECO:0000305"
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
