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RSP1_CAEEL
ID   RSP1_CAEEL              Reviewed;         312 AA.
AC   Q23121; Q8I106; Q8I107;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 145.
DE   RecName: Full=Probable splicing factor, arginine/serine-rich 1;
DE   AltName: Full=CeSRp75;
DE   AltName: Full=RNA-binding protein srp-5;
GN   Name=rsp-1; Synonyms=srp-5 {ECO:0000303|PubMed:10906451};
GN   ORFNames=W02B12.3;
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:CAA91395.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC   STRAIN=Bristol N2 {ECO:0000312|EMBL:CAA91395.1};
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. {ECO:0000269|PubMed:10747030,
CC       ECO:0000269|PubMed:10906451}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10906451}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=a {ECO:0000303|PubMed:9851916};
CC         IsoId=Q23121-1; Sequence=Displayed;
CC       Name=b {ECO:0000303|PubMed:9851916};
CC         IsoId=Q23121-2; Sequence=VSP_051626, VSP_051627;
CC       Name=c {ECO:0000303|PubMed:9851916};
CC         IsoId=Q23121-3; Sequence=VSP_051628, VSP_051629;
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.
CC   -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000255}.
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DR   EMBL; Z66521; CAA91395.1; -; Genomic_DNA.
DR   EMBL; Z66521; CAD59159.1; -; Genomic_DNA.
DR   EMBL; Z66521; CAD59160.1; -; Genomic_DNA.
DR   PIR; T26085; T26085.
DR   RefSeq; NP_001317731.1; NM_001330960.1.
DR   RefSeq; NP_496442.1; NM_064041.4. [Q23121-1]
DR   RefSeq; NP_871913.1; NM_182113.6.
DR   AlphaFoldDB; Q23121; -.
DR   SMR; Q23121; -.
DR   BioGRID; 40055; 3.
DR   STRING; 6239.W02B12.3a; -.
DR   iPTMnet; Q23121; -.
DR   EPD; Q23121; -.
DR   PaxDb; Q23121; -.
DR   PeptideAtlas; Q23121; -.
DR   EnsemblMetazoa; W02B12.3a.1; W02B12.3a.1; WBGene00004698. [Q23121-1]
DR   EnsemblMetazoa; W02B12.3b.1; W02B12.3b.1; WBGene00004698. [Q23121-2]
DR   EnsemblMetazoa; W02B12.3b.2; W02B12.3b.2; WBGene00004698. [Q23121-2]
DR   EnsemblMetazoa; W02B12.3b.3; W02B12.3b.3; WBGene00004698. [Q23121-2]
DR   EnsemblMetazoa; W02B12.3c.1; W02B12.3c.1; WBGene00004698.
DR   GeneID; 174748; -.
DR   KEGG; cel:CELE_W02B12.3; -.
DR   UCSC; W02B12.3a; c. elegans. [Q23121-1]
DR   CTD; 174748; -.
DR   WormBase; W02B12.3a; CE03763; WBGene00004698; rsp-1. [Q23121-1]
DR   WormBase; W02B12.3b; CE32944; WBGene00004698; rsp-1. [Q23121-2]
DR   WormBase; W02B12.3c; CE51629; WBGene00004698; rsp-1.
DR   eggNOG; KOG0106; Eukaryota.
DR   GeneTree; ENSGT00940000156213; -.
DR   HOGENOM; CLU_012062_34_2_1; -.
DR   InParanoid; Q23121; -.
DR   OMA; RKIKMID; -.
DR   OrthoDB; 1315388at2759; -.
DR   PhylomeDB; Q23121; -.
DR   PRO; PR:Q23121; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00004698; Expressed in embryo and 4 other tissues.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
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:0000398; P:mRNA splicing, via spliceosome; ISS:WormBase.
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; 1.
PE   3: Inferred from homology;
KW   Alternative splicing; Developmental protein; Differentiation;
KW   Growth regulation; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; RNA-binding; Spermatogenesis.
FT   CHAIN           1..312
FT                   /note="Probable splicing factor, arginine/serine-rich 1"
FT                   /id="PRO_0000081948"
FT   DOMAIN          3..73
FT                   /note="RRM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          129..202
FT                   /note="RRM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          69..125
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          196..312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..125
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        210..254
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        255..282
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         144..150
FT                   /note="DLKDQVR -> VCKTKRR (in isoform c)"
FT                   /evidence="ECO:0000303|PubMed:9851916"
FT                   /id="VSP_051628"
FT   VAR_SEQ         144..148
FT                   /note="DLKDQ -> QEKIV (in isoform b)"
FT                   /evidence="ECO:0000303|PubMed:9851916"
FT                   /id="VSP_051626"
FT   VAR_SEQ         149..312
FT                   /note="Missing (in isoform b)"
FT                   /evidence="ECO:0000303|PubMed:9851916"
FT                   /id="VSP_051627"
FT   VAR_SEQ         151..312
FT                   /note="Missing (in isoform c)"
FT                   /evidence="ECO:0000303|PubMed:9851916"
FT                   /id="VSP_051629"
SQ   SEQUENCE   312 AA;  35042 MW;  457C9DB8537F1514 CRC64;
     MAARIYIGRL TSRVSEKDIE HFFRGYGQIR DVLLKNGFGF VEFDDKRDAE DAVHDLNGKE
     LGGERVILDY SKPRGGGGDR GGFGGGGRGG ARVSSYSGGG GGGRDRFDRY DRGPPRRESR
     YGRPYSTRHR VVVENLSSRI SWQDLKDQVR RQGVEPTYAE AHKRPNEALL CFATPSDLKR
     CIEKCDGMDL NGRKIKMIDD SQAGRSRSRS NSRSRSRSRS RDRRRSRSRS SSRSKSRSRS
     PPKRSRRESK SKSRSRSRSR SADNRKSRSP SRSPKKVDRS PSPPRGSRSP SEKGSPRRSR
     SASPMDNGDG DN
 
 
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