ASD2_CAEEL
ID ASD2_CAEEL Reviewed; 445 AA.
AC G5EFF1; G5EFG9; O02065;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=RNA-binding protein asd-2 {ECO:0000305};
DE AltName: Full=Alternative splicing defective protein 2 {ECO:0000303|PubMed:18230701};
GN Name=asd-2 {ECO:0000303|PubMed:18230701, ECO:0000312|WormBase:T21G5.5c};
GN Synonyms=let-529 {ECO:0000312|WormBase:T21G5.5c},
GN star-2 {ECO:0000303|PubMed:20573244, ECO:0000312|WormBase:T21G5.5c},
GN tag-44 {ECO:0000312|WormBase:T21G5.5c};
GN ORFNames=T21G5.5 {ECO:0000312|WormBase:T21G5.5c};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|EMBL:ABU96120.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B AND C), FUNCTION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP GLU-244.
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:ABU96120.1};
RX PubMed=18230701; DOI=10.1101/gad.1620608;
RA Ohno G., Hagiwara M., Kuroyanagi H.;
RT "STAR family RNA-binding protein ASD-2 regulates developmental switching of
RT mutually exclusive alternative splicing in vivo.";
RL Genes Dev. 22:360-374(2008).
RN [2] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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 FUNCTION, AND DOMAIN.
RX PubMed=20573244; DOI=10.1186/1471-2199-11-48;
RA Carmel A.B., Wu J., Lehmann-Blount K.A., Williamson J.R.;
RT "High-affinity consensus binding of target RNAs by the STAR/GSG proteins
RT GLD-1, STAR-2 and Quaking.";
RL BMC Mol. Biol. 11:48-48(2010).
RN [4] {ECO:0000305}
RP FUNCTION, INTERACTION WITH SUP-12, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=23071450; DOI=10.1371/journal.pgen.1002991;
RA Ohno G., Ono K., Togo M., Watanabe Y., Ono S., Hagiwara M., Kuroyanagi H.;
RT "Muscle-specific splicing factors ASD-2 and SUP-12 cooperatively switch
RT alternative pre-mRNA processing patterns of the ADF/cofilin gene in
RT Caenorhabditis elegans.";
RL PLoS Genet. 8:E1002991-E1002991(2012).
CC -!- FUNCTION: RNA-binding protein that binds to the 5'-NACUAAY-N(1,20)-
CC UAAY-3' consensus sequence in pre-mRNA introns to promote alternative
CC splicing (PubMed:18230701, PubMed:20573244, PubMed:23071450). Required
CC for mutually exclusive alternative splicing where it modulates the
CC switch between mutually exclusive exons during pre-mRNA maturation
CC (PubMed:18230701, PubMed:23071450). Involved in muscle-specific gene
CC expression regulating the alternative splicing of genes such as let-2
CC and unc-60 to ensure that their respective isoforms are expressed in
CC muscle (PubMed:18230701, PubMed:23071450). Promotes the removal of
CC intron 10 from let-2 pre-mRNA to allow for the exclusive expression of
CC the muscle-specific let-2 isoform (as opposed to the non-muscle-
CC specific isoform expressed in embryos) in body wall muscles during late
CC larval and adult stages of development (PubMed:18230701). Binds
CC cooperatively with RNA-binding protein sup-12 to intron 1A of the unc-
CC 60 pre-mRNA to promote alternative splicing and expression of the
CC muscle specific isoform of unc-60 (PubMed:23071450).
CC {ECO:0000269|PubMed:18230701, ECO:0000269|PubMed:20573244,
CC ECO:0000269|PubMed:23071450}.
CC -!- SUBUNIT: Interacts with sup-12; in the presence of RNA, but with weak
CC affinity in the absence of RNA. {ECO:0000269|PubMed:23071450}.
CC -!- INTERACTION:
CC G5EFF1; Q20084: exc-7; NbExp=3; IntAct=EBI-316859, EBI-321225;
CC G5EFF1; G5ECJ4: mec-8; NbExp=4; IntAct=EBI-316859, EBI-317668;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23071450}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=c {ECO:0000312|WormBase:T21G5.5c}; Synonyms=b
CC {ECO:0000303|PubMed:18230701, ECO:0000303|PubMed:23071450};
CC IsoId=G5EFF1-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:T21G5.5a};
CC IsoId=G5EFF1-2; Sequence=VSP_058956, VSP_058957, VSP_058958;
CC Name=b {ECO:0000312|WormBase:T21G5.5b}; Synonyms=a
CC {ECO:0000303|PubMed:18230701};
CC IsoId=G5EFF1-3; Sequence=VSP_058956;
CC -!- TISSUE SPECIFICITY: Isoform b: Expressed in the hypodermis and
CC pharyngeal muscles (PubMed:18230701). Isoform c: Expressed in body wall
CC muscles and phayngeal muscles (PubMed:18230701, PubMed:23071450).
CC {ECO:0000269|PubMed:18230701, ECO:0000269|PubMed:23071450}.
CC -!- DEVELOPMENTAL STAGE: Expressed during embryonic development.
CC {ECO:0000269|PubMed:18230701}.
CC -!- DOMAIN: The KH domain and the Qua2 region are involved in RNA binding.
CC {ECO:0000305|PubMed:20573244}.
CC -!- DISRUPTION PHENOTYPE: Defective alternative splicing of the unc-60 gene
CC which results in decreased expression of the muscle-specific isoform of
CC unc-60 (PubMed:23071450). Double knockout with isoform c of unc-60
CC rescues the motility and actin filament disorganization defects in the
CC single unc-60 isoform c mutant (PubMed:23071450). RNAi-mediated
CC knockdown results animals that are viable throughout embryonic and
CC larval development, and furthermore, results in defective alternative
CC splicing of the let-2 gene, whereby transcripts containing exon 10 are
CC not formed in larvae and so the muscle-specific isoform of let-2 is not
CC expressed in body wall muscles (PubMed:18230701). RNAi-mediated
CC knockdown results in abnormal ectopic expression of the non-muscle-
CC specific isoform b of unc-60 in body wall muscles (PubMed:23071450).
CC {ECO:0000269|PubMed:18230701, ECO:0000269|PubMed:23071450}.
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DR EMBL; EF630625; ABU96119.1; -; mRNA.
DR EMBL; EF630626; ABU96120.1; -; mRNA.
DR EMBL; BX284601; CCD67593.1; -; Genomic_DNA.
DR EMBL; BX284601; CCD67594.1; -; Genomic_DNA.
DR EMBL; BX284601; CCD67595.1; -; Genomic_DNA.
DR PIR; T15136; T15136.
DR RefSeq; NP_001021625.1; NM_001026454.3. [G5EFF1-2]
DR RefSeq; NP_001021626.1; NM_001026455.3. [G5EFF1-3]
DR RefSeq; NP_001021627.1; NM_001026456.2. [G5EFF1-1]
DR AlphaFoldDB; G5EFF1; -.
DR SMR; G5EFF1; -.
DR DIP; DIP-26760N; -.
DR IntAct; G5EFF1; 19.
DR STRING; 6239.T21G5.5d; -.
DR EnsemblMetazoa; T21G5.5a.1; T21G5.5a.1; WBGene00006423. [G5EFF1-2]
DR EnsemblMetazoa; T21G5.5b.1; T21G5.5b.1; WBGene00006423. [G5EFF1-3]
DR EnsemblMetazoa; T21G5.5b.2; T21G5.5b.2; WBGene00006423. [G5EFF1-3]
DR EnsemblMetazoa; T21G5.5c.1; T21G5.5c.1; WBGene00006423. [G5EFF1-1]
DR GeneID; 188703; -.
DR UCSC; T21G5.5c; c. elegans.
DR CTD; 188703; -.
DR WormBase; T21G5.5a; CE32731; WBGene00006423; asd-2. [G5EFF1-2]
DR WormBase; T21G5.5b; CE13896; WBGene00006423; asd-2. [G5EFF1-3]
DR WormBase; T21G5.5c; CE37411; WBGene00006423; asd-2. [G5EFF1-1]
DR eggNOG; KOG1588; Eukaryota.
DR GeneTree; ENSGT00940000167937; -.
DR OMA; ISHAGAM; -.
DR PhylomeDB; G5EFF1; -.
DR PRO; PR:G5EFF1; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00006423; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR ExpressionAtlas; G5EFF1; baseline and differential.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0043186; C:P granule; IDA:WormBase.
DR GO; GO:1990904; C:ribonucleoprotein complex; IPI:WormBase.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0097157; F:pre-mRNA intronic binding; IPI:WormBase.
DR GO; GO:0003727; F:single-stranded RNA binding; IDA:WormBase.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IMP:WormBase.
DR GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
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; IPR032377; STAR_dimer.
DR PANTHER; PTHR11208; PTHR11208; 1.
DR Pfam; PF00013; KH_1; 1.
DR Pfam; PF16544; STAR_dimer; 1.
DR SMART; SM00322; KH; 1.
DR SUPFAM; SSF54791; SSF54791; 1.
DR PROSITE; PS50084; KH_TYPE_1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; mRNA processing; mRNA splicing; Nucleus;
KW Reference proteome; RNA-binding.
FT CHAIN 1..445
FT /note="RNA-binding protein asd-2"
FT /evidence="ECO:0000305"
FT /id="PRO_0000440162"
FT DOMAIN 145..171
FT /note="KH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT REGION 22..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 71..128
FT /note="Qua1 domain"
FT /evidence="ECO:0000250|UniProtKB:Q17339"
FT REGION 230..253
FT /note="Qua2 domain; involved in RNA binding"
FT /evidence="ECO:0000250|UniProtKB:Q17339"
FT COMPBIAS 41..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 145
FT /note="Involved in RNA binding"
FT /evidence="ECO:0000250|UniProtKB:Q17339"
FT SITE 153
FT /note="Important for the interaction between KH and Qua2
FT domains"
FT /evidence="ECO:0000250|UniProtKB:Q17339"
FT SITE 168
FT /note="Involved in RNA binding"
FT /evidence="ECO:0000250|UniProtKB:Q17339"
FT SITE 172
FT /note="Involved in RNA binding"
FT /evidence="ECO:0000250|UniProtKB:Q17339"
FT SITE 178
FT /note="Important for RNA binding"
FT /evidence="ECO:0000250|UniProtKB:Q17339"
FT SITE 238
FT /note="Involved in RNA binding"
FT /evidence="ECO:0000250|UniProtKB:Q17339"
FT SITE 241
FT /note="Involved in RNA binding"
FT /evidence="ECO:0000250|UniProtKB:Q17339"
FT SITE 245
FT /note="Important for the interaction between KH and Qua2
FT domains"
FT /evidence="ECO:0000250|UniProtKB:Q17339"
FT VAR_SEQ 1..54
FT /note="MDCDNGVVSEISDDKELLNLETVIPPPPNDSGHEFIGPSSGPPQVTITPSGV
FT QS -> MTHASTDLLTPN (in isoform a and isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_058956"
FT VAR_SEQ 370
FT /note="S -> R (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_058957"
FT VAR_SEQ 371..445
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_058958"
FT MUTAGEN 244
FT /note="E->K: In yb1423; defective alternative splicing of
FT the let-2 gene whereby intron 10 within the let-2 pre-mRNA
FT is not removed."
FT /evidence="ECO:0000269|PubMed:18230701"
SQ SEQUENCE 445 AA; 47789 MW; BBF0A250ED49EC52 CRC64;
MDCDNGVVSE ISDDKELLNL ETVIPPPPND SGHEFIGPSS GPPQVTITPS GVQSGSANGV
STSQQQQYSA EYLSQLLKDK KQLAAFPNVF HHLERLADEE INKVRVVLFQ CEFSKESAPL
PDAEGDSTVH TEKVFVPAKE HPDYNFVGRI LGPRGMTAKQ LEQETGCKIM VRGRGSMRDK
KKEELNRGKP NWEHLSEELH VLIQCEDTEN RAKVKLMRAV EEVRKLLVPA PEGEDDLKRK
QLMELAIING TYRSGTDQSA LAAAQLAAVK HQQQPFAAAL QAAALQRGVL PMMANGLSRS
PTMAVCGAPI VMSPSGRASS AGATATSQAA LIMQQQSQLH AANAGNAALQ QQAALLQQQQ
AAEYQQLLLS QAGLYDFSAM QQQYAAVGQN AAVAAAQAQA QAQYGALAAA AAANSAGNQQ
YADYAGVDLT SQQSAHGGYY VRRWA
