SMA2_CAEEL
ID SMA2_CAEEL Reviewed; 418 AA.
AC Q02330; Q02329;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Dwarfin sma-2;
DE AltName: Full=MAD protein homolog 1;
GN Name=sma-2 {ECO:0000312|WormBase:ZK370.2};
GN Synonyms=cem-1 {ECO:0000312|WormBase:ZK370.2};
GN ORFNames=ZK370.2 {ECO:0000312|WormBase:ZK370.2};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [4]
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 [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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. Nucleus {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown enhances tail tip
CC morphogenesis resulting in retention of the pointed larval tail tip in
CC adult males (also known as the Lep phenotype) of sma-3 e491 mutants.
CC {ECO:0000269|PubMed:21408209}.
CC -!- SIMILARITY: Belongs to the dwarfin/SMAD family. {ECO:0000305}.
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DR EMBL; U10327; AAC46583.1; -; mRNA.
DR EMBL; U34778; AAA97606.1; -; mRNA.
DR EMBL; BX284603; CCD61720.1; -; Genomic_DNA.
DR PIR; B88538; B88538.
DR PIR; S55018; S55018.
DR RefSeq; NP_498931.2; NM_066530.4.
DR AlphaFoldDB; Q02330; -.
DR SMR; Q02330; -.
DR BioGRID; 41432; 8.
DR DIP; DIP-27082N; -.
DR IntAct; Q02330; 2.
DR STRING; 6239.ZK370.2; -.
DR EPD; Q02330; -.
DR PaxDb; Q02330; -.
DR PeptideAtlas; Q02330; -.
DR EnsemblMetazoa; ZK370.2a.1; ZK370.2a.1; WBGene00004856.
DR EnsemblMetazoa; ZK370.2a.2; ZK370.2a.2; WBGene00004856.
DR GeneID; 176229; -.
DR UCSC; ZK370.2; c. elegans.
DR CTD; 176229; -.
DR WormBase; ZK370.2; CE33015; WBGene00004856; sma-2.
DR eggNOG; KOG3701; Eukaryota.
DR GeneTree; ENSGT00940000163092; -.
DR HOGENOM; CLU_026736_0_2_1; -.
DR InParanoid; Q02330; -.
DR OMA; TNNRADV; -.
DR OrthoDB; 608001at2759; -.
DR PhylomeDB; Q02330; -.
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 PRO; PR:Q02330; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00004856; Expressed in larva and 3 other tissues.
DR ExpressionAtlas; Q02330; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0071144; C:heteromeric SMAD protein complex; IBA:GO_Central.
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:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
DR GO; GO:0030509; P:BMP signaling pathway; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
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:0030307; P:positive regulation of cell growth; IMP:UniProtKB.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:UniProtKB.
DR GO; GO:0110039; P:positive regulation of nematode male tail tip morphogenesis; IMP:UniProtKB.
DR GO; GO:0009791; P:post-embryonic development; 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 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 2: Evidence at transcript level;
KW Cytoplasm; DNA-binding; Metal-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; Zinc.
FT CHAIN 1..418
FT /note="Dwarfin sma-2"
FT /id="PRO_0000090879"
FT DOMAIN 8..134
FT /note="MH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00438"
FT DOMAIN 222..418
FT /note="MH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00439"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 119
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"
SQ SEQUENCE 418 AA; 47926 MW; 5916C5B031FAA13F CRC64;
MINFDGIKKI TERLKWKQGD EDENWAKKAI DNLMKKLIKH NKQALENLEF ALRCQGQQKT
ECVTIPRSLD GRLQISHRKA LPHVIYCRVY RWPDLQSHHE LKAIEDCRFC YESGQKDICI
NPYHYKRVHA TGVLPPVLVP RYSEKPPQEV PPTLAKFQLM EMSGSRMPQN VNMANVNFTA
NQFHQYNPNG IEEMDTSQKF DIPPGVPTCL VPFDKVWEEQ FWATVSYYEL NTRVGEQVKV
SSTTITIDGF TDPCINGSKI SLGLFSNVNR NATIENTRRH IGNGVKLTYV RSNGSLFAQC
ESDSAIFVQS SNCNYINGFH STTVVKIANK CSLKIFDMEI FRQLLEDCSR RGFDASFDLQ
KMTFIRMSFV KGWGAEYQRQ DVTSTPCWIE IHLHAPLAWL DRVLSTMGPT PRPISSIS
