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SYM2_CAEEL
ID   SYM2_CAEEL              Reviewed;         618 AA.
AC   Q22708; Q23391; Q86GJ8;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 3.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=RNA-binding protein sym-2;
DE   AltName: Full=Synthetic lethal with mec-8 protein 2;
GN   Name=sym-2; ORFNames=ZK1067.6;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND DISRUPTION PHENOTYPE.
RX   PubMed=15579686; DOI=10.1534/genetics.104.029827;
RA   Yochem J., Bell L.R., Herman R.K.;
RT   "The identities of sym-2, sym-3 and sym-4, three genes that are
RT   synthetically lethal with mec-8 in Caenorhabditis elegans.";
RL   Genetics 168:1293-1306(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
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]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=18454200; DOI=10.1371/journal.pgen.1000001;
RA   Barberan-Soler S., Zahler A.M.;
RT   "Alternative splicing regulation during C. elegans development: splicing
RT   factors as regulated targets.";
RL   PLoS Genet. 4:E1000001-E1000001(2008).
CC   -!- FUNCTION: mRNA splicing factor that regulates alternative splicing of
CC       many genes in embryo. Probably plays a role in the formation of embryo-
CC       specific isoforms. {ECO:0000269|PubMed:18454200}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- DEVELOPMENTAL STAGE: Expressed at higher level in embryos than in L1
CC       larvae.
CC   -!- DISRUPTION PHENOTYPE: Worms lacking both symn-2 and mec-8 die during
CC       late embryogenesis. Lethality is probably due to defects in alternative
CC       splicing regulation. {ECO:0000269|PubMed:15579686,
CC       ECO:0000269|PubMed:18454200}.
CC   -!- SIMILARITY: Belongs to the ESRP family. {ECO:0000305}.
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DR   EMBL; AY220985; AAO65265.1; -; mRNA.
DR   EMBL; Z70038; CAA93887.2; -; Genomic_DNA.
DR   EMBL; Z68319; CAA93887.2; JOINED; Genomic_DNA.
DR   PIR; T25208; T25208.
DR   RefSeq; NP_495960.2; NM_063559.6.
DR   AlphaFoldDB; Q22708; -.
DR   SMR; Q22708; -.
DR   BioGRID; 39786; 6.
DR   IntAct; Q22708; 5.
DR   STRING; 6239.ZK1067.6; -.
DR   EPD; Q22708; -.
DR   PaxDb; Q22708; -.
DR   PeptideAtlas; Q22708; -.
DR   EnsemblMetazoa; ZK1067.6a.1; ZK1067.6a.1; WBGene00006367.
DR   GeneID; 174461; -.
DR   KEGG; cel:CELE_ZK1067.6; -.
DR   UCSC; ZK1067.6; c. elegans.
DR   CTD; 174461; -.
DR   WormBase; ZK1067.6a; CE35148; WBGene00006367; sym-2.
DR   eggNOG; KOG1365; Eukaryota.
DR   GeneTree; ENSGT00940000169473; -.
DR   HOGENOM; CLU_008009_2_2_1; -.
DR   InParanoid; Q22708; -.
DR   OMA; HRQVIGQ; -.
DR   OrthoDB; 863041at2759; -.
DR   PhylomeDB; Q22708; -.
DR   PRO; PR:Q22708; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00006367; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR   ExpressionAtlas; Q22708; baseline and differential.
DR   GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR   GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; ISS:WormBase.
DR   GO; GO:0009792; P:embryo development ending in birth or egg hatching; IGI:WormBase.
DR   GO; GO:0010172; P:embryonic body morphogenesis; IGI:WormBase.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0050879; P:multicellular organismal movement; IGI:WormBase.
DR   GO; GO:0043484; P:regulation of RNA splicing; ISS:WormBase.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.330; -; 3.
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; 1.
DR   SMART; SM00360; RRM; 3.
DR   SUPFAM; SSF54928; SSF54928; 3.
DR   PROSITE; PS50102; RRM; 1.
PE   2: Evidence at transcript level;
KW   mRNA processing; mRNA splicing; Nucleus; Reference proteome; Repeat;
KW   RNA-binding.
FT   CHAIN           1..618
FT                   /note="RNA-binding protein sym-2"
FT                   /id="PRO_0000370635"
FT   DOMAIN          281..357
FT                   /note="RRM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          389..473
FT                   /note="RRM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          33..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   618 AA;  69176 MW;  18A75818C63A1EF5 CRC64;
     MNRQTSHPEQ RLLLIRVSDG NYDENTKLVV TSFYPRRQED ANNNSTSPSS ASSSGSEIST
     RLVNITPEDV VKFFDEHPTS SYIFTKGPEP IRHVLIPLFA RNELCVPHPL HHYYDIKHLY
     YGNQEEDGME QEEIEDDVAI ARAILDMDDE LLEKTHQFVN IEYQPAPILE DQEVGADGDN
     VVCRARGLPW QASDHHVAQF FAGLDIVPGG IALCLSSEGR RNGEVLVQFS SQESRDLALK
     RHRNFLLSRY IEVYKAGLDE FMHVATGSST EAMEFVSANA IIVRMRGLPY DCTDAQIRTF
     FEPLKLTDKI LFITRTDGRP TGDAFVQFET EEDAQQGLLK HRQVIGQRYI ELFKSTAAEV
     QQVVKRCNLI NSSPAVANAV EAPEEKKKDC VRLRGLPYEA TVQHIVTFLG DFATMVKFQG
     VHMVYNNQGH PSGEAFIQMI NEQAASACAA GVHNNFMSVG KKKRYIEVFQ ASAEELNLHH
     LVGQQHQVPP PAPLGFMGQL PPQAPQPQQF WSSYPSPPIS PIVPGQVTQL IIYGIHMSIG
     VPELVANFTT PEHTVDNVLF TRWPTHLCPG EAILTLRNRG APPPQTSPLS QISQLSAPNF
     AAYSHHPQNF PLQPILME
 
 
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