RSP3_CAEEL
ID RSP3_CAEEL Reviewed; 258 AA.
AC Q9NEW6; Q9GQI7;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Probable splicing factor, arginine/serine-rich 3;
DE AltName: Full=CeSF2;
DE AltName: Full=CeSF2/ASF;
GN Name=rsp-3; ORFNames=Y111B2A.18;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAG36874.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, PHOSPHORYLATION OF RS DOMAIN, AND
RP TISSUE SPECIFICITY.
RX PubMed=11091073; DOI=10.1016/s0925-4773(00)00477-9;
RA Kuroyanagi H., Kimura T., Wada K., Hisamoto N., Matsumoto K., Hagiwara M.;
RT "SPK-1, a C. elegans SR protein kinase homologue, is essential for
RT embryogenesis and required for germline development.";
RL Mech. Dev. 99:51-64(2000).
RN [2] {ECO:0000312|EMBL:CAC35847.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CAC35847.2};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3] {ECO:0000305}
RP IDENTIFICATION, AND FUNCTION.
RX PubMed=10747030; DOI=10.1093/emboj/19.7.1625;
RA Longman D., Johnstone I.L., Caceres J.F.;
RT "Functional characterization of SR and SR-related genes in Caenorhabditis
RT elegans.";
RL EMBO J. 19:1625-1637(2000).
CC -!- FUNCTION: Plays an essential role in embryogenesis.
CC {ECO:0000269|PubMed:10747030, ECO:0000269|PubMed:11091073}.
CC -!- SUBUNIT: Interacts with spk-1. {ECO:0000269|PubMed:11091073}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Predominantly coexpressed with spk-1 in adult
CC hermaphrodite germlines. {ECO:0000269|PubMed:11091073}.
CC -!- PTM: Directly phosphorylated by spk-1 in vitro on serine residues of
CC the RS domain. {ECO:0000269|PubMed:11091073}.
CC -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000255}.
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DR EMBL; AF242767; AAG36874.1; -; mRNA.
DR EMBL; AL132904; CAC35847.2; -; Genomic_DNA.
DR RefSeq; NP_499649.2; NM_067248.4.
DR AlphaFoldDB; Q9NEW6; -.
DR SMR; Q9NEW6; -.
DR BioGRID; 41865; 39.
DR STRING; 6239.Y111B2A.18.1; -.
DR iPTMnet; Q9NEW6; -.
DR EPD; Q9NEW6; -.
DR PaxDb; Q9NEW6; -.
DR PeptideAtlas; Q9NEW6; -.
DR EnsemblMetazoa; Y111B2A.18.1; Y111B2A.18.1; WBGene00004700.
DR EnsemblMetazoa; Y111B2A.18.2; Y111B2A.18.2; WBGene00004700.
DR GeneID; 176688; -.
DR UCSC; Y111B2A.18.1; c. elegans.
DR CTD; 176688; -.
DR WormBase; Y111B2A.18; CE31089; WBGene00004700; rsp-3.
DR eggNOG; KOG0105; Eukaryota.
DR GeneTree; ENSGT00940000164330; -.
DR HOGENOM; CLU_012062_34_0_1; -.
DR InParanoid; Q9NEW6; -.
DR OMA; KMDGNRS; -.
DR OrthoDB; 1321443at2759; -.
DR PhylomeDB; Q9NEW6; -.
DR Reactome; R-CEL-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-CEL-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-CEL-72165; mRNA Splicing - Minor Pathway.
DR Reactome; R-CEL-72187; mRNA 3'-end processing.
DR Reactome; R-CEL-73856; RNA Polymerase II Transcription Termination.
DR PRO; PR:Q9NEW6; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00004700; Expressed in embryo and 5 other tissues.
DR GO; GO:0016607; C:nuclear speck; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; ISS:WormBase.
DR GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:UniProtKB.
DR GO; GO:0006376; P:mRNA splice site selection; ISS:WormBase.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0008380; P:RNA splicing; NAS:UniProtKB.
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 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 Developmental protein; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..258
FT /note="Probable splicing factor, arginine/serine-rich 3"
FT /id="PRO_0000081950"
FT DOMAIN 9..83
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 123..197
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 81..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..246
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 90
FT /note="G -> S (in Ref. 1; AAG36874)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 258 AA; 28680 MW; 35ABA5DA89AEF315 CRC64;
MPRGGSEDQK VYVGNLPGDV REKEVEDIFH KYGRIKYVDI KSGRGPAFAF VEFEDHRDAE
DAVRARDGYE FDGRRIRVEF TRGVGPRGPG GRPLQDGGDH RGGDFRGGRG GGRGGGPQRR
TGYRVIVEGL PPTGSWQDLK DHMRDAGDVC YADVARDGTG VVEFTRYEDV KYAVRKLDDT
KFRSHEGETA YIRVREDNSS GGGSGGGGRD RSRSRSPRAE RRASPKYSPR RSRSRSRSRS
RSRSRSASRS PSRSPSPQ
