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RSP2_CAEEL
ID   RSP2_CAEEL              Reviewed;         281 AA.
AC   Q23120;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Probable splicing factor, arginine/serine-rich 2;
DE   AltName: Full=CeSRp40;
DE   AltName: Full=RNA-binding protein srp-4;
GN   Name=rsp-2; Synonyms=srp-4 {ECO:0000303|PubMed:10906451};
GN   ORFNames=W02B12.2;
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:0000312|EMBL:CAA91394.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000312|EMBL:CAA91394.1};
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   [2] {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).
RN   [3] {ECO:0000305}
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=10906451; DOI=10.1016/s0925-4773(00)00339-7;
RA   Kawano T., Fujita M., Sakamoto H.;
RT   "Unique and redundant functions of SR proteins, a conserved family of
RT   splicing factors, in Caenorhabditis elegans development.";
RL   Mech. Dev. 95:67-76(2000).
CC   -!- FUNCTION: Plays a functionally redundant role in spermatogenesis and
CC       growth rate control. Required for the development of somatic gonad
CC       structures and for progression from larval stage to adulthood.
CC       {ECO:0000269|PubMed:10747030, ECO:0000269|PubMed:10906451}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10906451}.
CC   -!- PTM: Extensively phosphorylated on serine residues in the RS domain.
CC       {ECO:0000250|UniProtKB:Q9NEW6}.
CC   -!- MISCELLANEOUS: RNA-mediated interference (RNAi) of rsp-1 and rsp-2
CC       result in reduced brood sizes and abnormal egg-laying behavior, and the
CC       presence of unusual vacuolated structures in some of the secondary
CC       spermatocytes, spermatids and spermatozoa. Rsp-2/rsp-6 RNAi caused
CC       severe abnormalities in somatic gonad structures and in some cases
CC       animals were arrested or dead at the larval stage.
CC   -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000255}.
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DR   EMBL; Z66521; CAA91394.1; -; Genomic_DNA.
DR   PIR; T26084; T26084.
DR   RefSeq; NP_496441.1; NM_064040.6.
DR   AlphaFoldDB; Q23120; -.
DR   SMR; Q23120; -.
DR   BioGRID; 40054; 2.
DR   DIP; DIP-26059N; -.
DR   STRING; 6239.W02B12.2; -.
DR   iPTMnet; Q23120; -.
DR   EPD; Q23120; -.
DR   PaxDb; Q23120; -.
DR   PeptideAtlas; Q23120; -.
DR   EnsemblMetazoa; W02B12.2.1; W02B12.2.1; WBGene00004699.
DR   GeneID; 174747; -.
DR   KEGG; cel:CELE_W02B12.2; -.
DR   UCSC; W02B12.2; c. elegans.
DR   CTD; 174747; -.
DR   WormBase; W02B12.2; CE03762; WBGene00004699; rsp-2.
DR   eggNOG; KOG0106; Eukaryota.
DR   HOGENOM; CLU_012062_34_2_1; -.
DR   InParanoid; Q23120; -.
DR   OMA; CFSTHDD; -.
DR   OrthoDB; 1315388at2759; -.
DR   PhylomeDB; Q23120; -.
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:Q23120; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00004699; Expressed in embryo and 4 other tissues.
DR   GO; GO:0016607; C:nuclear speck; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; ISS:WormBase.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0008406; P:gonad development; IGI:UniProtKB.
DR   GO; GO:0007506; P:gonadal mesoderm development; IEA:UniProtKB-KW.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:WormBase.
DR   GO; GO:0002119; P:nematode larval development; IGI:UniProtKB.
DR   GO; GO:0040009; P:regulation of growth rate; IGI:UniProtKB.
DR   GO; GO:0008380; P:RNA splicing; NAS:UniProtKB.
DR   GO; GO:0007283; P:spermatogenesis; IGI:UniProtKB.
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   3: Inferred from homology;
KW   Developmental protein; Differentiation; Gonadal differentiation;
KW   Growth regulation; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; RNA-binding; Spermatogenesis.
FT   CHAIN           1..281
FT                   /note="Probable splicing factor, arginine/serine-rich 2"
FT                   /id="PRO_0000081949"
FT   DOMAIN          2..72
FT                   /note="RRM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          112..186
FT                   /note="RRM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          78..100
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          168..281
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        168..191
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        192..208
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        212..248
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   281 AA;  32421 MW;  06B467776DBDA061 CRC64;
     MVRVYIGRLP NRASDRDVEH FFRGYGKLSD VIMKNGFGFV DFQDQRDADD AVHDLNGKEL
     CGERVILEFP RRKVGYNEER SGSGFRGREP TFRKGGERQF SNRYSRPCST RFRLVIDNLS
     TRYSWQDIKD HIRKLGIEPT YSEAHKRNVN QAIVCFTSHD DLRDAMNKLQ GEDLNGRKLK
     CTDETRDRSR SRSPRRRSRS RSPTRSRSPP ARRRSPGSDR SDRKSRSASP KKRSDKRARS
     ESKSRSRSGG RRSRSNSPPN RSPSPKKRRD NSSPRSGSAS P
 
 
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