ID   SMAD2_RAT               Reviewed;         467 AA.
AC   O70436; A0JPM1;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   27-MAR-2024, entry version 198.
DE   RecName: Full=Mothers against decapentaplegic homolog 2;
DE            Short=MAD homolog 2;
DE            Short=Mothers against DPP homolog 2;
DE   AltName: Full=Mad-related protein 2;
DE   AltName: Full=SMAD family member 2;
DE            Short=SMAD 2;
DE            Short=Smad2;
GN   Name=Smad2; Synonyms=Madh2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RX   PubMed=10382592; DOI=10.1007/s001250051220;
RA   Zhang Y.-Q., Kanzaki M., Furukawa M., Shibata H., Ozeki M., Kojima I.;
RT   "Involvement of Smad proteins in the differentiation of pancreatic AR42J
RT   cells induced by activin A.";
RL   Diabetologia 42:719-727(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10670756; DOI=10.1507/endocrj.46.695;
RA   Osaki M., Tsukazaki T., Ono N., Yonekura A., Hirota Y., Miyazaki Y.,
RA   Shindo H., Sonta S., Yamashita S.;
RT   "cDNA cloning and chromosomal mapping of rat Smad2 and Smad4 and their
RT   expression in cultured rat articular chondrocytes.";
RL   Endocr. J. 46:695-701(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Testis;
RA   Miyakita A., Okuno S., Watanabe T.K., Oga K., Tsuji A., Hishigaki H.,
RA   Kato S., Sano A., Suto T., Nakagawa K., Nakahara Y., Haraguchi N.,
RA   Higashi K.;
RT   "Molecular cloning of rat Smad2 gene.";
RL   Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=21791611; DOI=10.1128/mcb.05448-11;
RA   Yan X., Zhang J., Pan L., Wang P., Xue H., Zhang L., Gao X., Zhao X.,
RA   Ning Y., Chen Y.G.;
RT   "TSC-22 promotes transforming growth factor beta-mediated cardiac
RT   myofibroblast differentiation by antagonizing Smad7 activity.";
RL   Mol. Cell. Biol. 31:3700-3709(2011).
CC   -!- FUNCTION: Receptor-regulated SMAD (R-SMAD) that is an intracellular
CC       signal transducer and transcriptional modulator activated by TGF-beta
CC       (transforming growth factor) and activin type 1 receptor kinases. Binds
CC       the TRE element in the promoter region of many genes that are regulated
CC       by TGF-beta and, on formation of the SMAD2/SMAD4 complex, activates
CC       transcription. Promotes TGFB1-mediated transcription of odontoblastic
CC       differentiation genes in dental papilla cells (By similarity).
CC       Positively regulates PDPK1 kinase activity by stimulating its
CC       dissociation from the 14-3-3 protein YWHAQ which acts as a negative
CC       regulator (By similarity). {ECO:0000250|UniProtKB:Q15796,
CC       ECO:0000250|UniProtKB:Q62432}.
CC   -!- SUBUNIT: Monomer; in the absence of TGF-beta (By similarity).
CC       Heterodimer; in the presence of TGF-beta (By similarity). Forms a
CC       heterodimer with co-SMAD, SMAD4, in the nucleus to form the
CC       transactivation complex SMAD2/SMAD4 (By similarity). Found in a complex
CC       with SMAD3 and TRIM33 upon addition of TGF-beta (By similarity).
CC       Identified in a complex that contains at least ZNF451, SMAD2, SMAD3 and
CC       SMAD4 (By similarity). Interacts (via the MH2 domain) with ZFYVE9; may
CC       form trimers with the SMAD4 co-SMAD (By similarity). Interacts with
CC       TAZ/WWRT1 (By similarity). Interacts with FOXH1 (By similarity).
CC       Interacts with SNW1 (By similarity). Interacts with CREB-binding
CC       protein (CBP) and EP300 (By similarity). Interacts with SNON (By
CC       similarity). Interacts with ALK4/ACVR1B (By similarity). Interacts with
CC       SKOR1 (By similarity). Interacts with SKOR2 (By similarity). Interacts
CC       with PRDM16 (By similarity). Interacts (via MH2 domain) with LEMD3 (By
CC       similarity). Interacts with RBPMS (By similarity). Interacts with WWP1.
CC       Interacts (dephosphorylated form, via the MH1 and MH2 domains) with
CC       RANBP3 (via its C-terminal R domain); the interaction results in the
CC       export of dephosphorylated SMAD3 out of the nucleus and termination of
CC       the TGF-beta signaling (By similarity). Interacts with PDPK1 (via PH
CC       domain) (By similarity). Interacts with DAB2; the interactions are
CC       enhanced upon TGF-beta stimulation (By similarity). Interacts with
CC       USP15 (By similarity). Interacts with PPP5C (By similarity). Interacts
CC       with LDLRAD4 (via the SMAD interaction motif) (By similarity).
CC       Interacts (via MH2 domain) with PMEPA1 (via the SMAD interaction motif)
CC       (By similarity). Interacts with ZFHX3 (By similarity). Interacts with
CC       ZNF451 (By similarity). Interacts with SMURF2 when phosphorylated on
CC       Ser-465/467 (By similarity). Interacts with PPM1A (By similarity).
CC       Interacts with TGF-beta (By similarity). Interacts with TGFBR1 (By
CC       similarity). Interacts with TGIF (By similarity). Interacts with SMAD3
CC       and TRIM33 (By similarity). Interacts with ZNF580 (By similarity).
CC       Interacts with NEDD4L in response to TGF-beta (By similarity).
CC       Interacts with HGS (By similarity). Interacts with AIP1 (By
CC       similarity). Interacts with WWP1 (By similarity). Interacts with PML
CC       (By similarity). Interacts weakly with ZNF8 (By similarity). Interacts
CC       (when phosphorylated) with RNF111; RNF111 acts as an enhancer of the
CC       transcriptional responses by mediating ubiquitination and degradation
CC       of SMAD2 inhibitors (By similarity). Interacts with YAP1 (when
CC       phosphorylated at 'Ser-112') (By similarity). Interacts when
CC       phosphorylated with IPO7; the interaction facilitates translocation of
CC       SMAD2 to the nucleus (By similarity). {ECO:0000250|UniProtKB:Q15796,
CC       ECO:0000250|UniProtKB:Q62432}.
CC   -!- INTERACTION:
CC       O70436; P47196: Akt1; NbExp=2; IntAct=EBI-7948047, EBI-7204362;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q15796}. Nucleus
CC       {ECO:0000250|UniProtKB:Q15796}. Note=Cytoplasmic and nuclear in the
CC       absence of TGF-beta (By similarity). On TGF-beta stimulation, migrates
CC       to the nucleus when complexed with SMAD4 or with IPO7 (By similarity).
CC       On dephosphorylation by phosphatase PPM1A, released from the
CC       SMAD2/SMAD4 complex, and exported out of the nucleus by interaction
CC       with RANBP1 (By similarity). Localized mainly to the nucleus in the
CC       early stages of embryo development with expression becoming evident in
CC       the cytoplasm at the blastocyst and epiblast stages (By similarity).
CC       {ECO:0000250|UniProtKB:Q15796, ECO:0000250|UniProtKB:Q62432}.
CC   -!- TISSUE SPECIFICITY: Expressed in cardiomyocytes.
CC       {ECO:0000269|PubMed:21791611}.
CC   -!- PTM: In response to TGF-beta, phosphorylated on the C-terminal SXS
CC       motif by TGF-beta and activin type 1 receptor kinases, phosphorylation
CC       declines progressively in a KMT5A-dependent manner. Phosphorylation in
CC       this motif is required for interaction with a number of proteins
CC       including SMURF2, SNON and SMAD4 in response to TGF-beta.
CC       Dephosphorylated in this motif by PPM1A leading to disruption of the
CC       SMAD2/3-SMAD4 complex, nuclear export and termination of the TGF-beta
CC       signaling. In response to decorin, the naturally occurring inhibitor of
CC       TGF-beta signaling, phosphorylated on Ser-240 by CaMK2. Phosphorylated
CC       by MAPK3 upon EGF stimulation; which increases transcriptional activity
CC       and stability, and is blocked by calmodulin. Phosphorylated by PDPK1
CC       (By similarity). {ECO:0000250|UniProtKB:Q15796}.
CC   -!- PTM: Acetylated on Lys-19 by coactivators in response to TGF-beta
CC       signaling, which increases transcriptional activity.
CC       {ECO:0000250|UniProtKB:Q15796}.
CC   -!- PTM: In response to TGF-beta, ubiquitinated by NEDD4L; which promotes
CC       its degradation. Monoubiquitinated, leading to prevent DNA-binding (By
CC       similarity). Deubiquitination by USP15 alleviates inhibition and
CC       promotes activation of TGF-beta target genes (By similarity).
CC       Ubiquitinated by RNF111, leading to its degradation: only SMAD2
CC       proteins that are 'in use' are targeted by RNF111, RNF111 playing a key
CC       role in activating SMAD2 and regulating its turnover (By similarity).
CC       {ECO:0000250|UniProtKB:Q15796, ECO:0000250|UniProtKB:Q62432}.
CC   -!- SIMILARITY: Belongs to the dwarfin/SMAD family. {ECO:0000305}.
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DR   EMBL; AB017912; BAA33453.1; -; mRNA.
DR   EMBL; AF056001; AAC12780.1; -; mRNA.
DR   EMBL; AB010147; BAA81909.1; -; mRNA.
DR   EMBL; BC127497; AAI27498.1; -; mRNA.
DR   RefSeq; NP_001264379.1; NM_001277450.1.
DR   RefSeq; NP_062064.1; NM_019191.2.
DR   AlphaFoldDB; O70436; -.
DR   SMR; O70436; -.
DR   BioGRID; 248011; 2.
DR   IntAct; O70436; 1.
DR   MINT; O70436; -.
DR   STRING; 10116.ENSRNOP00000075341; -.
DR   ChEMBL; CHEMBL3784912; -.
DR   iPTMnet; O70436; -.
DR   PhosphoSitePlus; O70436; -.
DR   jPOST; O70436; -.
DR   PaxDb; 10116-ENSRNOP00000048329; -.
DR   ABCD; O70436; 1 sequenced antibody.
DR   Ensembl; ENSRNOT00000092173.2; ENSRNOP00000075341.1; ENSRNOG00000018140.8.
DR   Ensembl; ENSRNOT00055023871; ENSRNOP00055019469; ENSRNOG00055013852.
DR   Ensembl; ENSRNOT00060017914; ENSRNOP00060013920; ENSRNOG00060010583.
DR   Ensembl; ENSRNOT00065039114; ENSRNOP00065031768; ENSRNOG00065022764.
DR   GeneID; 29357; -.
DR   KEGG; rno:29357; -.
DR   AGR; RGD:3031; -.
DR   CTD; 4087; -.
DR   RGD; 3031; Smad2.
DR   eggNOG; KOG3701; Eukaryota.
DR   GeneTree; ENSGT00940000153499; -.
DR   HOGENOM; CLU_026736_0_2_1; -.
DR   InParanoid; O70436; -.
DR   OMA; RAIEHCE; -.
DR   OrthoDB; 2891561at2759; -.
DR   PhylomeDB; O70436; -.
DR   TreeFam; TF314923; -.
DR   Reactome; R-RNO-1181150; Signaling by NODAL.
DR   Reactome; R-RNO-1502540; Signaling by Activin.
DR   Reactome; R-RNO-2173788; Downregulation of TGF-beta receptor signaling.
DR   Reactome; R-RNO-2173789; TGF-beta receptor signaling activates SMADs.
DR   Reactome; R-RNO-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
DR   Reactome; R-RNO-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
DR   Reactome; R-RNO-5689880; Ub-specific processing proteases.
DR   Reactome; R-RNO-9617828; FOXO-mediated transcription of cell cycle genes.
DR   PRO; PR:O70436; -.
DR   Proteomes; UP000002494; Chromosome 18.
DR   Bgee; ENSRNOG00000018140; Expressed in thymus and 19 other cell types or tissues.
DR   ExpressionAtlas; O70436; baseline and differential.
DR   GO; GO:0032444; C:activin responsive factor complex; ISO:RGD.
DR   GO; GO:0000785; C:chromatin; ISO:RGD.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0071144; C:heteromeric SMAD protein complex; ISO:RGD.
DR   GO; GO:0071142; C:homomeric SMAD protein complex; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR   GO; GO:0071141; C:SMAD protein complex; ISO:RGD.
DR   GO; GO:0005667; C:transcription regulator complex; ISS:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; ISO:RGD.
DR   GO; GO:0070410; F:co-SMAD binding; ISO:RGD.
DR   GO; GO:0097718; F:disordered domain specific binding; ISO:RGD.
DR   GO; GO:0003677; F:DNA binding; ISO:RGD.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:RGD.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:RGD.
DR   GO; GO:0003690; F:double-stranded DNA binding; ISS:UniProtKB.
DR   GO; GO:0070411; F:I-SMAD binding; ISO:RGD.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019902; F:phosphatase binding; ISO:RGD.
DR   GO; GO:0070412; F:R-SMAD binding; ISO:RGD.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR   GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISS:UniProtKB.
DR   GO; GO:0046332; F:SMAD binding; ISO:RGD.
DR   GO; GO:0048156; F:tau protein binding; ISO:RGD.
DR   GO; GO:0005160; F:transforming growth factor beta receptor binding; ISO:RGD.
DR   GO; GO:0034713; F:type I transforming growth factor beta receptor binding; ISO:RGD.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR   GO; GO:0032924; P:activin receptor signaling pathway; ISO:RGD.
DR   GO; GO:0030325; P:adrenal gland development; IDA:RGD.
DR   GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
DR   GO; GO:0009952; P:anterior/posterior pattern specification; ISS:UniProtKB.
DR   GO; GO:0003180; P:aortic valve morphogenesis; ISO:RGD.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0045165; P:cell fate commitment; ISS:UniProtKB.
DR   GO; GO:0071333; P:cellular response to glucose stimulus; IEP:RGD.
DR   GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEP:RGD.
DR   GO; GO:0003140; P:determination of left/right asymmetry in lateral mesoderm; ISO:RGD.
DR   GO; GO:0048589; P:developmental growth; ISO:RGD.
DR   GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; ISO:RGD.
DR   GO; GO:0048617; P:embryonic foregut morphogenesis; ISO:RGD.
DR   GO; GO:0009880; P:embryonic pattern specification; ISO:RGD.
DR   GO; GO:0003203; P:endocardial cushion morphogenesis; ISO:RGD.
DR   GO; GO:0007492; P:endoderm development; ISO:RGD.
DR   GO; GO:0001706; P:endoderm formation; ISO:RGD.
DR   GO; GO:0007369; P:gastrulation; ISO:RGD.
DR   GO; GO:0007507; P:heart development; ISO:RGD.
DR   GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR   GO; GO:0030073; P:insulin secretion; ISO:RGD.
DR   GO; GO:0035556; P:intracellular signal transduction; ISS:UniProtKB.
DR   GO; GO:0030324; P:lung development; ISO:RGD.
DR   GO; GO:0001707; P:mesoderm formation; ISS:UniProtKB.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:RGD.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISO:RGD.
DR   GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR   GO; GO:0038092; P:nodal signaling pathway; ISO:RGD.
DR   GO; GO:0071895; P:odontoblast differentiation; ISS:UniProtKB.
DR   GO; GO:0035265; P:organ growth; ISO:RGD.
DR   GO; GO:0031016; P:pancreas development; ISO:RGD.
DR   GO; GO:0048340; P:paraxial mesoderm morphogenesis; ISS:UniProtKB.
DR   GO; GO:0007389; P:pattern specification process; ISO:RGD.
DR   GO; GO:0060039; P:pericardium development; ISO:RGD.
DR   GO; GO:0030513; P:positive regulation of BMP signaling pathway; ISO:RGD.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISS:UniProtKB.
DR   GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; ISO:RGD.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR   GO; GO:0009791; P:post-embryonic development; ISO:RGD.
DR   GO; GO:0003184; P:pulmonary valve morphogenesis; ISO:RGD.
DR   GO; GO:0051098; P:regulation of binding; ISS:UniProtKB.
DR   GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; ISO:RGD.
DR   GO; GO:0070723; P:response to cholesterol; ISO:RGD.
DR   GO; GO:0009749; P:response to glucose; ISO:RGD.
DR   GO; GO:0062009; P:secondary palate development; ISO:RGD.
DR   GO; GO:0023019; P:signal transduction involved in regulation of gene expression; IMP:BHF-UCL.
DR   GO; GO:0060395; P:SMAD protein signal transduction; IMP:BHF-UCL.
DR   GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IMP:BHF-UCL.
DR   GO; GO:0001657; P:ureteric bud development; ISO:RGD.
DR   GO; GO:0007352; P:zygotic specification of dorsal/ventral axis; ISO:RGD.
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.
DR   Genevisible; O70436; RN.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; DNA-binding; Metal-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation; Ubl conjugation; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q15796"
FT   CHAIN           2..467
FT                   /note="Mothers against decapentaplegic homolog 2"
FT                   /id="PRO_0000090854"
FT   DOMAIN          10..176
FT                   /note="MH1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00438"
FT   DOMAIN          274..467
FT                   /note="MH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00439"
FT   REGION          207..251
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           221..225
FT                   /note="PY-motif"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        229..251
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         74
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         149
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         161
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         166
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15796"
FT   MOD_RES         8
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15796"
FT   MOD_RES         19
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15796"
FT   MOD_RES         220
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15796"
FT   MOD_RES         240
FT                   /note="Phosphoserine; by CAMK2"
FT                   /evidence="ECO:0000250|UniProtKB:Q15796,
FT                   ECO:0000255|PROSITE-ProRule:PRU00439"
FT   MOD_RES         245
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15796"
FT   MOD_RES         250
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15796"
FT   MOD_RES         255
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15796"
FT   MOD_RES         458
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15796,
FT                   ECO:0000255|PROSITE-ProRule:PRU00439"
FT   MOD_RES         460
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15796,
FT                   ECO:0000255|PROSITE-ProRule:PRU00439"
FT   MOD_RES         464
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15796,
FT                   ECO:0000255|PROSITE-ProRule:PRU00439"
FT   MOD_RES         465
FT                   /note="Phosphoserine; by TGFBR1"
FT                   /evidence="ECO:0000250|UniProtKB:Q15796,
FT                   ECO:0000255|PROSITE-ProRule:PRU00439"
FT   MOD_RES         467
FT                   /note="Phosphoserine; by TGFBR1"
FT                   /evidence="ECO:0000250|UniProtKB:Q15796,
FT                   ECO:0000255|PROSITE-ProRule:PRU00439"
SQ   SEQUENCE   467 AA;  52239 MW;  3A775444411F6619 CRC64;
     MSSILPFTPP VVKRLLGWKK SAGGSGGAGG GEQNGQEEKW CEKAVKSLVK KLKKTGRLDE
     LEKAITTQNC NTKCVTIPST CSEIWGLSTA NTVDQWDTTG LYSFSEQTRS LDGRLQVSHR
     KGLPHVIYCR LWRWPDLHSH HELKAIENCE YAFSLKKDEV CVNPYHYQRV ETPVLPPVLV
     PRHTEILTEL PPLDDYTHSI PENTNFPAGI EPQSNYIPET PPPGYISEDG ETSDQQLNQS
     MDTGSPAELS PTTLSPVNHS LDLQPVTYSE PAFWCSIAYY ELNQRVGETF HASQPSLTVD
     GFTDPSNSER FCLGLLSNVN RNATVEMTRR HIGRGVRLYY IGGEVFAECL SDSAIFVQSP
     NCNQRYGWHP ATVCKIPPGC NLKIFNNQEF AALLAQSVNQ GFEAVYQLTR MCTIRMSFVK
     GWGAEYRRQT VTSTPCWIEL HLNGPLQWLD KVLTQMGSPS VRCSSMS
//