KHDR3_RAT
ID KHDR3_RAT Reviewed; 346 AA.
AC Q9JLP1;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=KH domain-containing, RNA-binding, signal transduction-associated protein 3;
DE AltName: Full=Sam68-like mammalian protein 2;
DE Short=SLM-2;
DE Short=rSLM-2;
GN Name=Khdrbs3; Synonyms=Slm2;
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, AND INTERACTION WITH HNRPL; SFRS9;
RP SAFB AND YTHDC1.
RC TISSUE=Brain;
RX PubMed=11118435; DOI=10.1074/jbc.m006851200;
RA Stoss O., Olbrich M., Hartmann A.M., Koenig H., Memmott J., Andreadis A.,
RA Stamm S.;
RT "The STAR/GSG family protein rSLM-2 regulates the selection of alternative
RT splice sites.";
RL J. Biol. Chem. 276:8665-8673(2001).
RN [2]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC TISSUE=Testis;
RX PubMed=10332027; DOI=10.1093/hmg/8.6.959;
RA Venables J.P., Vernet C., Chew S.L., Elliott D.J., Cowmeadow R.B., Wu J.,
RA Cooke H.J., Artzt K., Eperon I.C.;
RT "T-STAR/ETOILE: a novel relative of SAM68 that interacts with an RNA-
RT binding protein implicated in spermatogenesis.";
RL Hum. Mol. Genet. 8:959-969(1999).
RN [3]
RP INTERACTION WITH KHDRBS2, AND TISSUE SPECIFICITY.
RX PubMed=15345239; DOI=10.1016/j.mcn.2004.04.011;
RA Stoss O., Novoyatleva T., Gencheva M., Olbrich M., Benderska N., Stamm S.;
RT "p59(fyn)-mediated phosphorylation regulates the activity of the tissue-
RT specific splicing factor rSLM-1.";
RL Mol. Cell. Neurosci. 27:8-21(2004).
CC -!- FUNCTION: RNA-binding protein that plays a role in the regulation of
CC alternative splicing and influences mRNA splice site selection and exon
CC inclusion (PubMed:11118435). Binds preferentially to the 5'-[AU]UAAA-3'
CC motif in vitro. Binds optimally to RNA containing 5'-[AU]UAA-3' as a
CC bipartite motif spaced by more than 15 nucleotides. Binds poly(A). RNA-
CC binding abilities are down-regulated by tyrosine kinase PTK6 (By
CC similarity). Involved in splice site selection of vascular endothelial
CC growth factor. In vitro regulates CD44 alternative splicing by direct
CC binding to purine-rich exonic enhancer (PubMed:11118435). Can regulate
CC alternative splicing of neurexins NRXN1-3 in the laminin G-like domain
CC 6 containing the evolutionary conserved neurexin alternative spliced
CC segment 4 (AS4) involved in neurexin selective targeting to
CC postsynaptic partners such as neuroligins and LRRTM family members.
CC Targeted, cell-type specific splicing regulation of NRXN1 at AS4 is
CC involved in neuronal glutamatergic synapse function and plasticity. May
CC regulate expression of KHDRBS2/SLIM-1 in defined brain neuron
CC populations by modifying its alternative splicing. Can bind FABP9 mRNA
CC (By similarity). May play a role as a negative regulator of cell
CC growth. Inhibits cell proliferation (By similarity).
CC {ECO:0000250|UniProtKB:O75525, ECO:0000250|UniProtKB:Q9R226,
CC ECO:0000269|PubMed:11118435}.
CC -!- SUBUNIT: Self-associates to form homooligomers; dimerization increases
CC RNA affinity (By similarity). Interacts with KHDRBS1/SAM68 and
CC KHDRBS2/SLM-1; heterooligomer formation of KHDRBS family proteins may
CC modulate RNA substrate specificity (PubMed:15345239). Interacts with
CC the splicing regulatory proteins SFRS9, SAFB and YTHDC1. Interacts with
CC HNRPL (PubMed:11118435). Interacts with RBMX, RBMY1A1, p85 subunit of
CC PI3-kinase, SERPINB5 (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:11118435, ECO:0000269|PubMed:15345239}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10332027}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in brain, heart,
CC testis and in Sertoli cells at all stages of spermatogenesis. Expressed
CC in neurons. Detected in cortical layers of the forebrain and in the CA1
CC to CA4 regions of the hippocampus. {ECO:0000269|PubMed:10332027,
CC ECO:0000269|PubMed:15345239}.
CC -!- DOMAIN: The proline-rich site binds the SH3 domain of the p85 subunit
CC of PI3-kinase. {ECO:0000250|UniProtKB:O75525}.
CC -!- PTM: Phosphorylated on tyrosine residues.
CC {ECO:0000250|UniProtKB:O75525, ECO:0000250|UniProtKB:Q9R226}.
CC -!- SIMILARITY: Belongs to the KHDRBS family. {ECO:0000305}.
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DR EMBL; AF152547; AAF73222.1; -; mRNA.
DR RefSeq; NP_071585.1; NM_022249.1.
DR AlphaFoldDB; Q9JLP1; -.
DR SMR; Q9JLP1; -.
DR BioGRID; 248934; 10.
DR STRING; 10116.ENSRNOP00000012753; -.
DR iPTMnet; Q9JLP1; -.
DR PhosphoSitePlus; Q9JLP1; -.
DR jPOST; Q9JLP1; -.
DR PaxDb; Q9JLP1; -.
DR PRIDE; Q9JLP1; -.
DR GeneID; 64015; -.
DR KEGG; rno:64015; -.
DR UCSC; RGD:620921; rat.
DR CTD; 10656; -.
DR RGD; 620921; Khdrbs3.
DR eggNOG; KOG1588; Eukaryota.
DR InParanoid; Q9JLP1; -.
DR OrthoDB; 1012406at2759; -.
DR PhylomeDB; Q9JLP1; -.
DR Reactome; R-RNO-8849468; PTK6 Regulates Proteins Involved in RNA Processing.
DR PRO; PR:Q9JLP1; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005654; C:nucleoplasm; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0003727; F:single-stranded RNA binding; IDA:RGD.
DR GO; GO:0006397; P:mRNA processing; IDA:RGD.
DR GO; GO:0033120; P:positive regulation of RNA splicing; IMP:RGD.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; ISO:RGD.
DR GO; GO:0007283; P:spermatogenesis; IEP:UniProtKB.
DR Gene3D; 3.30.1370.10; -; 1.
DR InterPro; IPR045071; BBP-like.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR InterPro; IPR032571; Qua1_dom.
DR InterPro; IPR032335; Sam68-YY.
DR PANTHER; PTHR11208; PTHR11208; 1.
DR Pfam; PF00013; KH_1; 1.
DR Pfam; PF16274; Qua1; 1.
DR Pfam; PF16568; Sam68-YY; 1.
DR SMART; SM00322; KH; 1.
DR SUPFAM; SSF54791; SSF54791; 1.
PE 1: Evidence at protein level;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; RNA-binding;
KW SH3-binding; Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..346
FT /note="KH domain-containing, RNA-binding, signal
FT transduction-associated protein 3"
FT /id="PRO_0000232524"
FT DOMAIN 61..127
FT /note="KH"
FT REGION 1..160
FT /note="Involved in homodimerization"
FT /evidence="ECO:0000250|UniProtKB:O75525"
FT REGION 212..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 320..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..264
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 4
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75525"
SQ SEQUENCE 346 AA; 38779 MW; E218071BE6615544 CRC64;
MEEKYLPELM AEKDSLDPSF THALRLVNRE IEKFQKGEAK DEEKYIDVVI NKNMKLGQKV
LIPVKQFPKF NFVGKLLGPR GNSLKRLQEE TLTKMSILGK GSMRDKAKEE ELRKSGEAKY
FHLNDDLHVL IEVFAPPAEA YARMGHALED IKKFLIPDYN DEIRQAQLQE LTYLNGGSEN
ADVPVVRGKS TLRTRGVTTP AITRGRGGVT ARPVAVGVPR GTPTPRGVLS TRGPVSRGRG
LLTPRARGVP PTGYRPPPPP PTQETYGEYD YDDGYSTAYD DQSYDSYDNS YSTPAQSGAD
YYDYGHGLGE EAYDSYGQED WTNSRHKAPS ARTAKGVYRE QPYGRY
