ID K7FH52_PELSI Unreviewed; 496 AA.
AC K7FH52;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Mothers against decapentaplegic homolog {ECO:0000256|RuleBase:RU361195};
DE Short=MAD homolog {ECO:0000256|RuleBase:RU361195};
DE Short=Mothers against DPP homolog {ECO:0000256|RuleBase:RU361195};
DE AltName: Full=SMAD family member {ECO:0000256|RuleBase:RU361195};
GN Name=SMAD2 {ECO:0000313|Ensembl:ENSPSIP00000007362.1};
OS Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC Trionychidae; Pelodiscus.
OX NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000007362.1, ECO:0000313|Proteomes:UP000007267};
RN [1] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RG Soft-shell Turtle Genome Consortium;
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
RN [3] {ECO:0000313|Ensembl:ENSPSIP00000007362.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU361195}.
CC Nucleus {ECO:0000256|RuleBase:RU361195}.
CC -!- SIMILARITY: Belongs to the dwarfin/SMAD family.
CC {ECO:0000256|ARBA:ARBA00005545, ECO:0000256|RuleBase:RU361195}.
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DR EMBL; AGCU01175681; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01175682; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01175683; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01175684; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01175685; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01175686; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01175687; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01175688; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01175689; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01175690; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006136810.1; XM_006136748.2.
DR AlphaFoldDB; K7FH52; -.
DR STRING; 13735.ENSPSIP00000007362; -.
DR Ensembl; ENSPSIT00000007403.1; ENSPSIP00000007362.1; ENSPSIG00000006646.1.
DR GeneID; 102457921; -.
DR KEGG; pss:102457921; -.
DR CTD; 4087; -.
DR eggNOG; KOG3701; Eukaryota.
DR GeneTree; ENSGT00940000153499; -.
DR HOGENOM; CLU_026736_0_2_1; -.
DR OMA; RAIEHCE; -.
DR OrthoDB; 2891561at2759; -.
DR TreeFam; TF314923; -.
DR Proteomes; UP000007267; Unassembled WGS sequence.
DR GO; GO:0032444; C:activin responsive factor complex; IEA:Ensembl.
DR GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR GO; GO:0071144; C:heteromeric SMAD protein complex; IEA:Ensembl.
DR GO; GO:0071142; C:homomeric SMAD protein complex; IEA:Ensembl.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0070410; F:co-SMAD binding; IEA:Ensembl.
DR GO; GO:0097718; F:disordered domain specific binding; IEA:Ensembl.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0070411; F:I-SMAD binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019902; F:phosphatase binding; IEA:Ensembl.
DR GO; GO:0070412; F:R-SMAD binding; IEA:Ensembl.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IEA:Ensembl.
DR GO; GO:0048156; F:tau protein binding; IEA:Ensembl.
DR GO; GO:0034713; F:type I transforming growth factor beta receptor binding; IEA:Ensembl.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IEA:Ensembl.
DR GO; GO:0003180; P:aortic valve morphogenesis; IEA:Ensembl.
DR GO; GO:0045165; P:cell fate commitment; IEA:Ensembl.
DR GO; GO:0003140; P:determination of left/right asymmetry in lateral mesoderm; IEA:Ensembl.
DR GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IEA:Ensembl.
DR GO; GO:0048617; P:embryonic foregut morphogenesis; IEA:Ensembl.
DR GO; GO:0003203; P:endocardial cushion morphogenesis; IEA:Ensembl.
DR GO; GO:0001706; P:endoderm formation; IEA:Ensembl.
DR GO; GO:0030073; P:insulin secretion; IEA:Ensembl.
DR GO; GO:0030324; P:lung development; IEA:Ensembl.
DR GO; GO:0001707; P:mesoderm formation; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IEA:Ensembl.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR GO; GO:0038092; P:nodal signaling pathway; IEA:Ensembl.
DR GO; GO:0071895; P:odontoblast differentiation; IEA:Ensembl.
DR GO; GO:0035265; P:organ growth; IEA:Ensembl.
DR GO; GO:0031016; P:pancreas development; IEA:Ensembl.
DR GO; GO:0048340; P:paraxial mesoderm morphogenesis; IEA:Ensembl.
DR GO; GO:0060039; P:pericardium development; IEA:Ensembl.
DR GO; GO:0030513; P:positive regulation of BMP signaling pathway; IEA:Ensembl.
DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
DR GO; GO:0003184; P:pulmonary valve morphogenesis; IEA:Ensembl.
DR GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0070723; P:response to cholesterol; IEA:Ensembl.
DR GO; GO:0009749; P:response to glucose; IEA:Ensembl.
DR GO; GO:0062009; P:secondary palate development; IEA:Ensembl.
DR GO; GO:0060395; P:SMAD protein signal transduction; IEA:Ensembl.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0001657; P:ureteric bud development; IEA:Ensembl.
DR GO; GO:0007352; P:zygotic specification of dorsal/ventral axis; IEA:Ensembl.
DR CDD; cd10491; MH1_SMAD_2_3; 1.
DR CDD; cd10985; MH2_SMAD_2_3; 1.
DR Gene3D; 2.60.200.10; -; 1.
DR Gene3D; 3.90.520.10; SMAD MH1 domain; 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:SF42; MOTHERS AGAINST DECAPENTAPLEGIC HOMOLOG 2; 1.
DR PANTHER; PTHR13703; SMAD; 1.
DR Pfam; PF03165; MH1; 1.
DR Pfam; PF03166; MH2; 1.
DR SMART; SM00523; DWA; 1.
DR SMART; SM00524; DWB; 1.
DR SUPFAM; SSF56366; SMAD MH1 domain; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS51075; MH1; 1.
DR PROSITE; PS51076; MH2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|RuleBase:RU361195};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU361195};
KW Reference proteome {ECO:0000313|Proteomes:UP000007267};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU361195};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW ECO:0000256|RuleBase:RU361195}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 39..205
FT /note="MH1"
FT /evidence="ECO:0000259|PROSITE:PS51075"
FT DOMAIN 303..496
FT /note="MH2"
FT /evidence="ECO:0000259|PROSITE:PS51076"
FT REGION 236..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 496 AA; 55595 MW; 2C6F96EBC69073DE CRC64;
MGTHILNSCY CTDWTQQLTN WTQCAVSENM SSILPFTPPV VKRLLGWKKS AGGSGGAGGG
EQNGQEEKWC EKAVKSLVKK LKKTGQLDEL EKAITTQNCN TKCVTIPSTC SEIWGLSTPN
TIDQWDTTGL YSFSEQTRSL DGRLQVSHRK GLPHVIYCRL WRWPDLHSHH ELKAIENCEY
AFNLKKDEVC VNPYHYQRVE TPVLPPVLVP RHTEILTELP PLDDYTHSIP ENTNFPAGIE
PQSNYIPETP PPGYISEDGE TSDQQLNQSM DTGSPAELSP STLSPVNHSL DLQPVTYSEP
AFWCSIAYYE LNQRVGETFH ASQPSLTVDG FTDPSNSERF CLGLLSNVNR NATVEMTRRH
IGRGVRLYYI GGEVFAECLS DSAIFVQSPN CNQRYGWHPA TVCKIPPGCN LKIFNNQEFA
ALLAQSVNQG FEAVYQLTRM CTIRMSFVKG WGAEYRRQTV TSTPCWIELH LNGPLQWLDK
VLTQMGSPSV RCSSMS
//
