LOCUS       NP_034884                467 aa            linear   ROD 11-MAR-2025
DEFINITION  mothers against decapentaplegic homolog 2 isoform 1 [Mus musculus].
ACCESSION   NP_034884
VERSION     NP_034884.2
DBSOURCE    REFSEQ: accession NM_010754.5
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 467)
  AUTHORS   Hrncir,H.R., Goodloe,B., Bombin,S., Hogan,C.B., Jadi,O. and
            Gracz,A.D.
  TITLE     Sox9 inhibits Activin A to promote biliary maturation and branching
            morphogenesis
  JOURNAL   Nat Commun 16 (1), 1667 (2025)
   PUBMED   39955269
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 467)
  AUTHORS   Song,C., Sawall,J.K., Ji,X., Song,F., Liao,X., Peng,R., Ren,H.,
            Koyama,E., Pacifici,M. and Long,F.
  TITLE     Tgfbeta signaling stimulates glycolysis to promote the genesis of
            synovial joint interzone in developing mouse embryonic limbs
  JOURNAL   Sci Adv 11 (2), eadq4991 (2025)
   PUBMED   39772668
REFERENCE   3  (residues 1 to 467)
  AUTHORS   Weberling,A., Siriwardena,D., Penfold,C., Christodoulou,N.,
            Boroviak,T.E. and Zernicka-Goetz,M.
  TITLE     Primitive to visceral endoderm maturation is essential for mouse
            epiblast survival beyond implantation
  JOURNAL   iScience 28 (1), 111671 (2024)
   PUBMED   39868030
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 467)
  AUTHORS   Hung,Y.S., Lin,W.M., Wang,Y.C., Kuo,W.C., Chen,Y.Y., Fann,M.J.,
            Yu,J.Y. and Wong,Y.H.
  TITLE     Protogenin facilitates trunk-to-tail HOX code transition via
            modulating GDF11/SMAD2 signaling in mammalian embryos
  JOURNAL   Commun Biol 7 (1), 1669 (2024)
   PUBMED   39702818
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 467)
  AUTHORS   Zhu,S., Huo,S., Wang,Z., Huang,C., Li,C., Song,H., Yang,X., He,R.,
            Ding,C., Qiu,M. and Zhu,X.J.
  TITLE     Follistatin controls the number of murine teeth by limiting
            TGF-beta signaling
  JOURNAL   iScience 27 (9), 110785 (2024)
   PUBMED   39286503
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 467)
  AUTHORS   Dick,A., Risau,W. and Drexler,H.
  TITLE     Expression of Smad1 and Smad2 during embryogenesis suggests a role
            in organ development
  JOURNAL   Dev Dyn 211 (4), 293-305 (1998)
   PUBMED   9566949
REFERENCE   7  (residues 1 to 467)
  AUTHORS   Waldrip,W.R., Bikoff,E.K., Hoodless,P.A., Wrana,J.L. and
            Robertson,E.J.
  TITLE     Smad2 signaling in extraembryonic tissues determines
            anterior-posterior polarity of the early mouse embryo
  JOURNAL   Cell 92 (6), 797-808 (1998)
   PUBMED   9529255
REFERENCE   8  (residues 1 to 467)
  AUTHORS   Devereux,T.R., Anna,C.H., Patel,A.C., White,C.M., Festing,M.F. and
            You,M.
  TITLE     Smad4 (homolog of human DPC4) and Smad2 (homolog of human JV18-1):
            candidates for murine lung tumor resistance and suppressor genes
  JOURNAL   Carcinogenesis 18 (9), 1751-1755 (1997)
   PUBMED   9328171
REFERENCE   9  (residues 1 to 467)
  AUTHORS   Chen,Y., Lebrun,J.J. and Vale,W.
  TITLE     Regulation of transforming growth factor beta- and activin-induced
            transcription by mammalian Mad proteins
  JOURNAL   Proc Natl Acad Sci U S A 93 (23), 12992-12997 (1996)
   PUBMED   8917532
REFERENCE   10 (residues 1 to 467)
  AUTHORS   Baker,J.C. and Harland,R.M.
  TITLE     A novel mesoderm inducer, Madr2, functions in the activin signal
            transduction pathway
  JOURNAL   Genes Dev 10 (15), 1880-1889 (1996)
   PUBMED   8756346
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BU058005.1, AK007817.1, AC164009.3, BC058713.1, CN456711.1 and
            BM248478.2.
            
            On Jun 10, 2003 this sequence version replaced NP_034884.1.
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1). Both variants 1 and 2 encode the same isoform.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK007817.1, BC021342.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..467
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="18"
                     /map="18 51.42 cM"
     Protein         1..467
                     /product="mothers against decapentaplegic homolog 2
                     isoform 1"
                     /note="mothers against decapentaplegic homolog 2;
                     mad-related protein 2; mothers against DPP homolog 2; Smad
                     2; MAD homolog 2"
                     /calculated_mol_wt=52135
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:Q15796; propagated from
                     UniProtKB/Swiss-Prot (Q62432.2)"
     Region          8..172
                     /region_name="MH1_SMAD_2_3"
                     /note="N-terminal Mad Homology 1 (MH1) domain in SMAD2 and
                     SMAD3; cd10491"
                     /db_xref="CDD:199815"
     Site            8
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q15796; propagated from
                     UniProtKB/Swiss-Prot (Q62432.2)"
     Site            19
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q15796; propagated from
                     UniProtKB/Swiss-Prot (Q62432.2)"
     Site            order(43,47,110,114..118,121,140..141)
                     /site_type="DNA binding"
                     /note="DNA binding site [nucleotide binding]"
                     /db_xref="CDD:199815"
     Site            order(74,149,161,166)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:199815"
     Region          207..251
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62432.2)"
     Site            220
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q15796; propagated from
                     UniProtKB/Swiss-Prot (Q62432.2)"
     Region          221..225
                     /region_name="PY-motif. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q62432.2)"
     Site            240
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CAMK2.
                     /evidence=ECO:0000250|UniProtKB:Q15796,
                     ECO:0000255|PROSITE-ProRule:PRU00439; propagated from
                     UniProtKB/Swiss-Prot (Q62432.2)"
     Site            245
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q15796; propagated from
                     UniProtKB/Swiss-Prot (Q62432.2)"
     Site            250
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q15796; propagated from
                     UniProtKB/Swiss-Prot (Q62432.2)"
     Site            255
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q15796; propagated from
                     UniProtKB/Swiss-Prot (Q62432.2)"
     Region          266..456
                     /region_name="MH2_SMAD_2_3"
                     /note="C-terminal Mad Homology 2 (MH2) domain in SMAD2 and
                     SMAD3; cd10985"
                     /db_xref="CDD:199826"
     Site            order(283,288..289,291,302..306,310,314,317,319..320,
                     326..327,329..331,334,403,406,409,413,415,419..421,426,
                     428,432,437,439,441,443,446..447,449..450,453..454)
                     /site_type="other"
                     /note="trimer interface [polypeptide binding]"
                     /db_xref="CDD:199826"
     Site            458
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q15796,
                     ECO:0000255|PROSITE-ProRule:PRU00439; propagated from
                     UniProtKB/Swiss-Prot (Q62432.2)"
     Site            460
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q15796,
                     ECO:0000255|PROSITE-ProRule:PRU00439; propagated from
                     UniProtKB/Swiss-Prot (Q62432.2)"
     Site            464
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q15796,
                     ECO:0000255|PROSITE-ProRule:PRU00439; propagated from
                     UniProtKB/Swiss-Prot (Q62432.2)"
     Site            465
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by TGFBR1.
                     /evidence=ECO:0000250|UniProtKB:Q15796,
                     ECO:0000255|PROSITE-ProRule:PRU00439; propagated from
                     UniProtKB/Swiss-Prot (Q62432.2)"
     Site            467
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by TGFBR1.
                     /evidence=ECO:0000250|UniProtKB:Q15796,
                     ECO:0000255|PROSITE-ProRule:PRU00439; propagated from
                     UniProtKB/Swiss-Prot (Q62432.2)"
     CDS             1..467
                     /gene="Smad2"
                     /gene_synonym="7120426M23Rik; Madh2; Madr2; mMad2; Smad-2"
                     /coded_by="NM_010754.5:332..1735"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS29350.1"
                     /db_xref="GeneID:17126"
                     /db_xref="MGI:MGI:108051"
ORIGIN      
        1 mssilpftpp vvkrllgwkk saggsggagg geqngqeekw cekavkslvk klkktgrlde
       61 lekaittqnc ntkcvtipst cseiwglsta ntvdqwdttg lysfseqtrs ldgrlqvshr
      121 kglphviycr lwrwpdlhsh helkaience yafnlkkdev cvnpyhyqrv etpvlppvlv
      181 prhteiltel pplddythsi pentnfpagi epqsnyipet pppgyisedg etsdqqlnqs
      241 mdtgspaels pttlspvnhs ldlqpvtyse pafwcsiayy elnqrvgetf hasqpsltvd
      301 gftdpsnser fclgllsnvn rnatvemtrr higrgvrlyy iggevfaecl sdsaifvqsp
      361 ncnqrygwhp atvckippgc nlkifnnqef aallaqsvnq gfeavyqltr mctirmsfvk
      421 gwgaeyrrqt vtstpcwiel hlngplqwld kvltqmgsps vrcssms
//
