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Database: UniProt
Entry: P51865
LinkDB: P51865
Original site: P51865 
ID   TDGF1_MOUSE             Reviewed;         171 AA.
AC   P51865;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   13-FEB-2019, entry version 146.
DE   RecName: Full=Teratocarcinoma-derived growth factor;
DE   AltName: Full=Cripto growth factor;
DE   AltName: Full=Epidermal growth factor-like Cripto protein;
DE   Flags: Precursor;
GN   Name=Tdgf1; Synonyms=Cripto;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=7916676;
RA   Dono R., Scalera L., Pacifico F., Acampora D., Persico M.G.,
RA   Simeone A.;
RT   "The murine cripto gene: expression during mesoderm induction and
RT   early heart morphogenesis.";
RL   Development 118:1157-1168(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 135-171.
RC   STRAIN=129/Sv;
RX   PubMed=8661720; DOI=10.1007/s003359900100;
RA   Liguori G., Tucci M., Montuori N., Dono R., Lago C.T., Pacifico A.F.,
RA   Persico M.G.;
RT   "Characterization of the mouse Tdgf1 gene and Tdgf pseudogenes.";
RL   Mamm. Genome 7:344-348(1996).
RN   [3]
RP   SUBCELLULAR LOCATION, AND GPI-ANCHOR.
RX   PubMed=10640699; DOI=10.1016/S0925-4773(99)00235-X;
RA   Minchiotti G., Parisi S., Liguori G., Signore M., Lania G.,
RA   Adamson E.D., Lago C.T., Persico M.G.;
RT   "Membrane-anchorage of Cripto protein by glycosylphosphatidylinositol
RT   and its distribution during early mouse development.";
RL   Mech. Dev. 90:133-142(2000).
RN   [4]
RP   STRUCTURE BY NMR OF 96-134, DISULFIDE BONDS, AND MUTAGENESIS OF
RP   TRP-107.
RX   PubMed=17125258; DOI=10.1021/jm060772r;
RA   Calvanese L., Saporito A., Marasco D., D'Auria G., Minchiotti G.,
RA   Pedone C., Paolillo L., Falcigno L., Ruvo M.;
RT   "Solution structure of mouse Cripto CFC domain and its inactive
RT   variant Trp107Ala.";
RL   J. Med. Chem. 49:7054-7062(2006).
CC   -!- FUNCTION: GPI-anchored cell membrane protein involved in Nodal
CC       signaling. Cell-associated Tdgf1 acts as a Nodal coreceptor in
CC       cis. Shedding of Tdgf1 by Tmem8a modulates Nodal signaling by
CC       allowing soluble Tdgf1 to act as a Nodal coreceptor on other
CC       cells. Could play a role in the determination of the epiblastic
CC       cells that subsequently give rise to the mesoderm.
CC       {ECO:0000250|UniProtKB:P13385}.
CC   -!- SUBUNIT: Interacts with the activin type-1 receptor ACVR1B.
CC       {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q9W6I6:lft1 (xeno); NbExp=2; IntAct=EBI-15529529, EBI-15529806;
CC       O13144:ndr1 (xeno); NbExp=2; IntAct=EBI-15529529, EBI-15529595;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10640699};
CC       Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:10640699}. Secreted
CC       {ECO:0000250|UniProtKB:P13385}. Note=Released from the cell
CC       membrane by GPI cleavage. {ECO:0000250|UniProtKB:P13385}.
CC   -!- TISSUE SPECIFICITY: Expressed at low level in specific organs of
CC       the adult animal such as spleen, heart, lung and brain. During
CC       gastrulation, expressed in the forming mesoderm. In later stages
CC       of the developing heart, expression is restricted to the truncus
CC       arteriosus.
CC   -!- DEVELOPMENTAL STAGE: First expressed prior to the onset of
CC       gastrulation (early streak stage), then continues throughout
CC       embryonic development.
CC   -!- PTM: The GPI-anchor is attached to the protein in the endoplasmic
CC       reticulum and serves to target the protein to the cell surface.
CC       There, it is processed by GPI processing phospholipase A2
CC       (Tmem8a), removing an acyl-chain at the sn-2 position of GPI and
CC       releasing Tdgf1 as a lysophosphatidylinositol-bearing form, which
CC       is further cleaved by phospholipase D (Gpld1) into a soluble form.
CC       {ECO:0000250|UniProtKB:P13385}.
CC   -!- SIMILARITY: Belongs to the EGF-CFC (Cripto-1/FRL1/Cryptic) family.
CC       {ECO:0000305}.
DR   EMBL; M87321; AAA37459.1; -; mRNA.
DR   EMBL; X94083; CAA63827.1; -; Genomic_DNA.
DR   CCDS; CCDS40783.1; -.
DR   PIR; I49612; I49612.
DR   UniGene; Mm.5090; -.
DR   PDB; 2J5H; NMR; -; A=96-134.
DR   PDBsum; 2J5H; -.
DR   ProteinModelPortal; P51865; -.
DR   SMR; P51865; -.
DR   DIP; DIP-46063N; -.
DR   IntAct; P51865; 4.
DR   STRING; 10090.ENSMUSP00000035075; -.
DR   PaxDb; P51865; -.
DR   PRIDE; P51865; -.
DR   MGI; MGI:98658; Tdgf1.
DR   eggNOG; KOG1217; Eukaryota.
DR   eggNOG; ENOG410XP6K; LUCA.
DR   HOGENOM; HOG000145523; -.
DR   HOVERGEN; HBG054705; -.
DR   InParanoid; P51865; -.
DR   PhylomeDB; P51865; -.
DR   EvolutionaryTrace; P51865; -.
DR   PRO; PR:P51865; -.
DR   Proteomes; UP000000589; Unplaced.
DR   GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR   GO; GO:0009986; C:cell surface; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IDA:MGI.
DR   GO; GO:0019897; C:extrinsic component of plasma membrane; IDA:MGI.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR   GO; GO:0045121; C:membrane raft; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0070697; F:activin receptor binding; IBA:GO_Central.
DR   GO; GO:0015026; F:coreceptor activity; IDA:UniProtKB.
DR   GO; GO:0008083; F:growth factor activity; ISO:MGI.
DR   GO; GO:0038100; F:nodal binding; IPI:UniProtKB.
DR   GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR   GO; GO:0070698; F:type I activin receptor binding; IPI:UniProtKB.
DR   GO; GO:0017147; F:Wnt-protein binding; IPI:UniProtKB.
DR   GO; GO:0000187; P:activation of MAPK activity; ISO:MGI.
DR   GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR   GO; GO:0009948; P:anterior/posterior axis specification; IGI:MGI.
DR   GO; GO:0008595; P:anterior/posterior axis specification, embryo; IMP:MGI.
DR   GO; GO:0009952; P:anterior/posterior pattern specification; IBA:GO_Central.
DR   GO; GO:0030509; P:BMP signaling pathway; IDA:MGI.
DR   GO; GO:0060070; P:canonical Wnt signaling pathway; IDA:MGI.
DR   GO; GO:0055007; P:cardiac muscle cell differentiation; IMP:MGI.
DR   GO; GO:0030154; P:cell differentiation; TAS:UniProtKB.
DR   GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; ISO:MGI.
DR   GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; ISO:MGI.
DR   GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; ISO:MGI.
DR   GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; ISO:MGI.
DR   GO; GO:0071346; P:cellular response to interferon-gamma; ISO:MGI.
DR   GO; GO:0071354; P:cellular response to interleukin-6; ISO:MGI.
DR   GO; GO:0071356; P:cellular response to tumor necrosis factor; ISO:MGI.
DR   GO; GO:0007368; P:determination of left/right symmetry; IBA:GO_Central.
DR   GO; GO:0007369; P:gastrulation; IGI:MGI.
DR   GO; GO:0007507; P:heart development; IDA:UniProtKB.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0001763; P:morphogenesis of a branching structure; IDA:UniProtKB.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR   GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IGI:MGI.
DR   GO; GO:0038092; P:nodal signaling pathway; IMP:UniProtKB.
DR   GO; GO:0018105; P:peptidyl-serine phosphorylation; ISO:MGI.
DR   GO; GO:0030335; P:positive regulation of cell migration; IDA:UniProtKB.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR   GO; GO:0001954; P:positive regulation of cell-matrix adhesion; IMP:MGI.
DR   GO; GO:0010595; P:positive regulation of endothelial cell migration; ISO:MGI.
DR   GO; GO:0048146; P:positive regulation of fibroblast proliferation; IMP:MGI.
DR   GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:MGI.
DR   GO; GO:0030334; P:regulation of cell migration; IMP:MGI.
DR   GO; GO:0009966; P:regulation of signal transduction; IDA:MGI.
DR   GO; GO:0001570; P:vasculogenesis; IMP:MGI.
DR   InterPro; IPR017047; Cripto_growth_factor.
DR   InterPro; IPR019011; Cryptic/Cripto_CFC-dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   PANTHER; PTHR14949:SF26; PTHR14949:SF26; 1.
DR   Pfam; PF09443; CFC; 1.
DR   PIRSF; PIRSF036301; Cripto_growth_factor; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS50026; EGF_3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Complete proteome; Disulfide bond;
KW   EGF-like domain; Glycoprotein; GPI-anchor; Growth factor; Lipoprotein;
KW   Membrane; Reference proteome; Secreted; Signal.
FT   SIGNAL        1     17       {ECO:0000255}.
FT   CHAIN        18    134       Teratocarcinoma-derived growth factor.
FT                                /FTId=PRO_0000007504.
FT   PROPEP      135    171       Removed in mature form. {ECO:0000250}.
FT                                /FTId=PRO_0000395411.
FT   DOMAIN       62     91       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   LIPID       134    134       GPI-anchor amidated aspartate.
FT                                {ECO:0000250}.
FT   CARBOHYD     63     63       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     66     73       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     67     79       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     81     90       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     99    117       {ECO:0000255|PROSITE-ProRule:PRU00076,
FT                                ECO:0000269|PubMed:17125258}.
FT   DISULFID    112    133       {ECO:0000255|PROSITE-ProRule:PRU00076,
FT                                ECO:0000269|PubMed:17125258}.
FT   DISULFID    115    124       {ECO:0000255|PROSITE-ProRule:PRU00076,
FT                                ECO:0000269|PubMed:17125258}.
FT   MUTAGEN     107    107       W->A: Unable to bind Cripto receptor.
FT                                {ECO:0000269|PubMed:17125258}.
FT   STRAND      119    121       {ECO:0000244|PDB:2J5H}.
FT   STRAND      127    130       {ECO:0000244|PDB:2J5H}.
SQ   SEQUENCE   171 AA;  18754 MW;  C52051AEACDB5380 CRC64;
     MGYFSSSVVL LVAISSAFEF GPVAGRDLAI RDNSIWDQKE PAVRDRSFQF VPSVGIQNSK
     SLNKTCCLNG GTCILGSFCA CPPSFYGRNC EHDVRKEHCG SILHGTWLPK KCSLCRCWHG
     QLHCLPQTFL PGCDGHVMDQ DLKASRTPCQ TPSVTTTFML AGACLFLDMK V
//
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