SMA3_CAEEL
ID SMA3_CAEEL Reviewed; 393 AA.
AC P45896;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Dwarfin sma-3;
DE AltName: Full=MAD protein homolog 2;
GN Name=sma-3 {ECO:0000312|WormBase:R13F6.9};
GN Synonyms=cem-2 {ECO:0000303|PubMed:7768443};
GN ORFNames=R13F6.9 {ECO:0000312|WormBase:R13F6.9};
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].
RC STRAIN=Bristol N2;
RX PubMed=8570636; DOI=10.1073/pnas.93.2.790;
RA Savage C., Das P., Finelli A.L., Townsend S.R., Sun C.-Y., Baird S.E.,
RA Padgett R.W.;
RT "Caenorhabditis elegans genes sma-2, sma-3, and sma-4 define a conserved
RT family of transforming growth factor beta pathway components.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:790-794(1996).
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 GENE NAME CEM-2.
RX PubMed=7768443; DOI=10.1093/genetics/139.3.1347;
RA Sekelsky J.J., Newfeld S.J., Raftery L.A., Chartoff E.H., Gelbart W.M.;
RT "Genetic characterization and cloning of mothers against dpp, a gene
RT required for decapentaplegic function in Drosophila melanogaster.";
RL Genetics 139:1347-1358(1995).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF GLY-348.
RX PubMed=21408209; DOI=10.1371/journal.pgen.1002010;
RA Nelson M.D., Zhou E., Kiontke K., Fradin H., Maldonado G., Martin D.,
RA Shah K., Fitch D.H.;
RT "A bow-tie genetic architecture for morphogenesis suggested by a genome-
RT wide RNAi screen in Caenorhabditis elegans.";
RL PLoS Genet. 7:E1002010-E1002010(2011).
CC -!- FUNCTION: Involved in TGF-beta pathway. Plays a role in male tail tip
CC morphogenesis (PubMed:21408209). {ECO:0000269|PubMed:21408209}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21408209}. Nucleus
CC {ECO:0000269|PubMed:21408209}. Note=In males localizes to the nuclei
CC and cytoplasm during tail tip morphogenesis (PubMed:21408209). In
CC hermaphrodites localizes only to the cytoplasm during tail tip
CC morphogenesis throughout the L4 stage (PubMed:21408209).
CC {ECO:0000269|PubMed:21408209}.
CC -!- DEVELOPMENTAL STAGE: Expressed at low levels in the tail tip in both
CC males and hermaphrodites from the L4 larval stage.
CC {ECO:0000269|PubMed:21408209}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown disrupts tail tip
CC morphogenesis resulting in retention of the pointed larval tail tip in
CC adult males (also known as the Lep phenotype).
CC {ECO:0000269|PubMed:21408209}.
CC -!- SIMILARITY: Belongs to the dwarfin/SMAD family. {ECO:0000305}.
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DR EMBL; U34902; AAA97607.1; -; mRNA.
DR EMBL; BX284603; CCD70180.1; -; Genomic_DNA.
DR PIR; T16750; T16750.
DR RefSeq; NP_498493.1; NM_066092.3.
DR AlphaFoldDB; P45896; -.
DR SMR; P45896; -.
DR BioGRID; 41170; 18.
DR IntAct; P45896; 9.
DR STRING; 6239.R13F6.9; -.
DR PaxDb; P45896; -.
DR PeptideAtlas; P45896; -.
DR EnsemblMetazoa; R13F6.9.1; R13F6.9.1; WBGene00004857.
DR GeneID; 175955; -.
DR KEGG; cel:CELE_R13F6.9; -.
DR UCSC; R13F6.9; c. elegans.
DR CTD; 175955; -.
DR WormBase; R13F6.9; CE25974; WBGene00004857; sma-3.
DR eggNOG; KOG3701; Eukaryota.
DR HOGENOM; CLU_026736_0_2_1; -.
DR InParanoid; P45896; -.
DR OMA; GSHSKCV; -.
DR OrthoDB; 608001at2759; -.
DR PhylomeDB; P45896; -.
DR Reactome; R-CEL-201451; Signaling by BMP.
DR Reactome; R-CEL-5689880; Ub-specific processing proteases.
DR Reactome; R-CEL-8941326; RUNX2 regulates bone development.
DR SignaLink; P45896; -.
DR PRO; PR:P45896; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00004857; Expressed in larva and 3 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0071144; C:heteromeric SMAD protein complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0070411; F:I-SMAD binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:WormBase.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
DR GO; GO:0030509; P:BMP signaling pathway; ISS:WormBase.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0050832; P:defense response to fungus; IMP:WormBase.
DR GO; GO:0045087; P:innate immune response; IMP:WormBase.
DR GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR GO; GO:0090597; P:nematode male tail mating organ morphogenesis; IMP:UniProtKB.
DR GO; GO:0045138; P:nematode male tail tip morphogenesis; IMP:WormBase.
DR GO; GO:0060465; P:pharynx development; IMP:UniProtKB.
DR GO; GO:0045793; P:positive regulation of cell size; IMP:WormBase.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:WormBase.
DR GO; GO:0110039; P:positive regulation of nematode male tail tip morphogenesis; IMP:UniProtKB.
DR GO; GO:0046622; P:positive regulation of organ growth; IMP:WormBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:WormBase.
DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IGI:UniProtKB.
DR GO; GO:0042661; P:regulation of mesodermal cell fate specification; IGI:UniProtKB.
DR GO; GO:0060395; P:SMAD protein signal transduction; IBA:GO_Central.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IBA:GO_Central.
DR GO; GO:1901048; P:transforming growth factor beta receptor signaling pathway involved in regulation of multicellular organism growth; IMP:UniProtKB.
DR Gene3D; 2.60.200.10; -; 1.
DR Gene3D; 3.90.520.10; -; 1.
DR InterPro; IPR013790; Dwarfin.
DR InterPro; IPR003619; MAD_homology1_Dwarfin-type.
DR InterPro; IPR013019; MAD_homology_MH1.
DR InterPro; IPR017855; SMAD-like_dom_sf.
DR InterPro; IPR001132; SMAD_dom_Dwarfin-type.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR InterPro; IPR036578; SMAD_MH1_sf.
DR PANTHER; PTHR13703; PTHR13703; 1.
DR Pfam; PF03165; MH1; 1.
DR Pfam; PF03166; MH2; 1.
DR SMART; SM00523; DWA; 1.
DR SMART; SM00524; DWB; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR SUPFAM; SSF56366; SSF56366; 1.
DR PROSITE; PS51075; MH1; 1.
DR PROSITE; PS51076; MH2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; DNA-binding; Metal-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; Zinc.
FT CHAIN 1..393
FT /note="Dwarfin sma-3"
FT /id="PRO_0000090880"
FT DOMAIN 10..139
FT /note="MH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00438"
FT DOMAIN 197..393
FT /note="MH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00439"
FT REGION 136..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT MUTAGEN 348
FT /note="G->R: In e491; low-penetrant disruption (57%) of
FT tail tip morphogenesis resulting in retention of the
FT pointed larval tail tip in adult males (also known as the
FT Lep phenotype). This phenotype is enhanced by RNAi against
FT sma-2."
FT /evidence="ECO:0000269|PubMed:21408209"
SQ SEQUENCE 393 AA; 44527 MW; D3C4601CA291D8C4 CRC64;
MNGLLHMHGP AVKKLLGWKI GEDEEKWCEK AVEALVKKLK KKNNGCGTLE DLECVLANPC
TNSRCITIAK SLDGRLQVSH KKGLPHVIYC RVWRWPDISS PHELRSIDTC SYPYESSSKT
MYICINPYHY QRLSRPQGLN SSMPSPQPIS SPNTIWQSSG SSTASCASSP SPSVFSEDGG
EVQVHQRPPP FRHPKSWAQI TYFELNSRVG EVFKLVNLSI TVDGYTNPSN SNTRICLGQL
TNVNRNGTIE NTRMHIGKGI QLDNKEDQMH IMITNNSDMP VFVQSKNTNL MMNMPLVKVC
RIPPHSQLCV FEFNLFFQML EQSCNDSDGL NELSKHCFIR ISFVKGWGED YPRQDVTSTP
CWLELRLNVP LAYIDQKMKQ TPRTNLMEPN SMT
