SMA4_CAEEL
ID SMA4_CAEEL Reviewed; 570 AA.
AC P45897;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Dwarfin sma-4;
DE AltName: Full=MAD protein homolog 3;
GN Name=sma-4; Synonyms=cem-3; ORFNames=R12B2.1;
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-3.
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).
CC -!- FUNCTION: Involved in TGF-beta pathway.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the dwarfin/SMAD family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CCD73313.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U34596; AAA97605.1; -; mRNA.
DR EMBL; FO081686; CCD73313.1; ALT_INIT; Genomic_DNA.
DR PIR; T16725; T16725.
DR RefSeq; NP_001040864.1; NM_001047399.2.
DR AlphaFoldDB; P45897; -.
DR SMR; P45897; -.
DR BioGRID; 41038; 41.
DR IntAct; P45897; 21.
DR STRING; 6239.R12B2.1a.3; -.
DR PaxDb; P45897; -.
DR EnsemblMetazoa; R12B2.1a.1; R12B2.1a.1; WBGene00004858.
DR EnsemblMetazoa; R12B2.1a.2; R12B2.1a.2; WBGene00004858.
DR GeneID; 175815; -.
DR KEGG; cel:CELE_R12B2.1; -.
DR UCSC; R12B2.1a.1; c. elegans.
DR CTD; 175815; -.
DR WormBase; R12B2.1a; CE25077; WBGene00004858; sma-4.
DR eggNOG; KOG3701; Eukaryota.
DR HOGENOM; CLU_026736_1_2_1; -.
DR InParanoid; P45897; -.
DR OrthoDB; 676553at2759; -.
DR PhylomeDB; P45897; -.
DR Reactome; R-CEL-1181150; Signaling by NODAL.
DR Reactome; R-CEL-1502540; Signaling by Activin.
DR Reactome; R-CEL-201451; Signaling by BMP.
DR Reactome; R-CEL-2173789; TGF-beta receptor signaling activates SMADs.
DR Reactome; R-CEL-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
DR Reactome; R-CEL-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
DR Reactome; R-CEL-8941326; RUNX2 regulates bone development.
DR Reactome; R-CEL-8941855; RUNX3 regulates CDKN1A transcription.
DR Reactome; R-CEL-9617828; FOXO-mediated transcription of cell cycle genes.
DR SignaLink; P45897; -.
DR PRO; PR:P45897; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00004858; Expressed in larva and 3 other tissues.
DR ExpressionAtlas; P45897; 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:0040024; P:dauer larval development; IGI:WormBase.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:UniProtKB.
DR GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR GO; GO:0045138; P:nematode male tail tip morphogenesis; IMP:WormBase.
DR GO; GO:0007567; P:parturition; IMP:UniProtKB.
DR GO; GO:0030307; P:positive regulation of cell growth; 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:UniProtKB.
DR GO; GO:0046622; P:positive regulation of organ growth; IMP:WormBase.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IMP:WormBase.
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..570
FT /note="Dwarfin sma-4"
FT /id="PRO_0000090881"
FT DOMAIN 150..273
FT /note="MH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00438"
FT DOMAIN 350..570
FT /note="MH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00439"
FT REGION 115..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..133
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 203
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 247
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 258
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 263
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 570 AA; 63369 MW; EFDC218B9FC336AD CRC64;
MFHPGMTSQP STSNQMYYDP LYGAEQIVQC NPMDYHQANI LCGMQYFNNS HNRYPLLPQM
PPQFTNDHPY DFPNVPTIST LDEASSFNGF LIPSQPSSYN NNNISCVFTP TPCTSSQASS
QPPPTPTVNP TPIPPNAGAV LTTAMDSCQQ ISHVLQCYQQ GGEDSDFVRK AIESLVKKLK
DKRIELDALI TAVTSNGKQP TGCVTIQRSL DGRLQVAGRK GVPHVVYARI WRWPKVSKNE
LVKLVQCQTS SDHPDNICIN PYHYERVVSN RITSADQSLH VENSPMKSEY LGDAGVIDSC
SDWPNTPPDN NFNGGFAPDQ PQLVTPIISD IPIDLNQIYV PTPPQLLDNW CSIIYYELDT
PIGETFKVSA RDHGKVIVDG GMDPHGENEG RLCLGALSNV HRTEASEKAR IHIGRGVELT
AHADGNISIT SNCKIFVRSG YLDYTHGSEY SSKAHRFTPN ESSFTVFDIR WAYMQMLRRS
RSSNEAVRAQ AAAVAGYAPM SVMPAIMPDS GVDRMRRDFC TIAISFVKAW GDVYQRKTIK
ETPCWIEVTL HRPLQILDQL LKNSSQFGSS
