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Database: UniProt
Entry: P51864
LinkDB: P51864
Original site: P51864 
ID   TDGF3_HUMAN             Reviewed;         188 AA.
AC   P51864;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   16-JAN-2019, entry version 133.
DE   RecName: Full=Putative teratocarcinoma-derived growth factor 3;
DE   AltName: Full=Cripto-3 growth factor;
DE   AltName: Full=Epidermal growth factor-like cripto protein CR3;
DE   AltName: Full=Teratocarcinoma-derived growth factor 1 pseudogene 3;
GN   Name=TDGF1P3; Synonyms=CRIPTO3, TDGF2, TDGF3;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Lung fibroblast;
RX   PubMed=1882841;
RA   Dono R., Montuori N., Rocchi M., de Ponti-Zilli L., Ciccodicola A.,
RA   Persico M.G.;
RT   "Isolation and characterization of the CRIPTO autosomal gene and its
RT   X-linked related sequence.";
RL   Am. J. Hum. Genet. 49:555-565(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Kintner M.A., Kintner R.L., Hosick H.L.;
RT   "Cripto-3 and Cripto-1 have different effects on the growth
RT   characteristics of MCF-7 and Vero cells.";
RL   Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15772651; DOI=10.1038/nature03440;
RA   Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA   Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
RA   Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA   Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA   Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA   Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA   Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA   Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA   Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA   Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA   Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA   Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA   Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA   Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA   Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA   Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA   Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
RA   Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA   Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA   Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA   Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA   Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA   Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA   Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA   Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA   Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA   de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA   Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA   Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA   Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA   Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA   McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
RA   Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA   Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA   Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA   Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA   Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA   Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA   Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA   Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA   Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
RA   Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA   Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA   Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA   Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA   Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA   Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA   Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA   Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA   Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
RA   Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA   Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence of the human X chromosome.";
RL   Nature 434:325-337(2005).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=18835250; DOI=10.1016/j.bbrc.2008.09.113;
RA   Sun C., Orozco O., Olson D.L., Choi E., Garber E., Tizard R., Szak S.,
RA   Sanicola M., Carulli J.P.;
RT   "CRIPTO3, a presumed pseudogene, is expressed in cancer.";
RL   Biochem. Biophys. Res. Commun. 377:215-220(2008).
CC   -!- FUNCTION: Could play a role in the determination of the epiblastic
CC       cells that subsequently give rise to the mesoderm. Activates the
CC       Nodal-dependent signaling pathway. {ECO:0000269|PubMed:18835250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18835250}.
CC   -!- TISSUE SPECIFICITY: Expressed weakly in lung, colon and breast.
CC       Expressed also strongly in primary cancer tissues; lung and colon
CC       cancers. {ECO:0000269|PubMed:18835250}.
CC   -!- SIMILARITY: Belongs to the EGF-CFC (Cripto-1/FRL1/Cryptic) family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Could be the product of a pseudogene. The TDGF3 locus has
CC       characteristics of a retrotransposon, including lack of introns
CC       and a poly(A) sequence. {ECO:0000305}.
DR   EMBL; M96956; AAA61135.1; -; mRNA.
DR   EMBL; AF251549; AAG49538.1; -; Genomic_DNA.
DR   EMBL; AF251550; AAG49539.1; -; Genomic_DNA.
DR   EMBL; AC000113; AAB46353.1; -; Genomic_DNA.
DR   UniGene; Hs.592361; -.
DR   ProteinModelPortal; P51864; -.
DR   SMR; P51864; -.
DR   BioMuta; HGNC:11703; -.
DR   DMDM; 1706127; -.
DR   jPOST; P51864; -.
DR   PeptideAtlas; P51864; -.
DR   PRIDE; P51864; -.
DR   ProteomicsDB; 56441; -.
DR   DisGeNET; 6998; -.
DR   GeneCards; TDGF1P3; -.
DR   HGNC; HGNC:11703; TDGF1P3.
DR   MIM; 187395; gene+phenotype.
DR   neXtProt; NX_P51864; -.
DR   eggNOG; KOG1217; Eukaryota.
DR   eggNOG; ENOG410XP6K; LUCA.
DR   HOVERGEN; HBG054705; -.
DR   InParanoid; P51864; -.
DR   Reactome; R-HSA-1181150; Signaling by NODAL.
DR   Reactome; R-HSA-1433617; Regulation of signaling by NODAL.
DR   ChiTaRS; TDGF1P3; human.
DR   PRO; PR:P51864; -.
DR   Proteomes; UP000005640; Unplaced.
DR   GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0070697; F:activin receptor binding; IBA:GO_Central.
DR   GO; GO:0008083; F:growth factor activity; NAS:UniProtKB.
DR   GO; GO:0038100; F:nodal binding; IBA:GO_Central.
DR   GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR   GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR   GO; GO:0009952; P:anterior/posterior pattern specification; IBA:GO_Central.
DR   GO; GO:0030509; P:BMP signaling pathway; IBA:GO_Central.
DR   GO; GO:0007368; P:determination of left/right symmetry; IBA:GO_Central.
DR   GO; GO:0007507; P:heart development; IBA:GO_Central.
DR   GO; GO:0038092; P:nodal signaling pathway; IBA:GO_Central.
DR   GO; GO:0007165; P:signal transduction; IDA:UniProtKB.
DR   InterPro; IPR017047; Cripto_growth_factor.
DR   InterPro; IPR019011; Cryptic/Cripto_CFC-dom.
DR   InterPro; IPR013032; EGF-like_CS.
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.
PE   5: Uncertain;
KW   Cell membrane; Complete proteome; Disulfide bond; EGF-like domain;
KW   Glycoprotein; Growth factor; Membrane; Reference proteome.
FT   CHAIN         1    188       Putative teratocarcinoma-derived growth
FT                                factor 3.
FT                                /FTId=PRO_0000055627.
FT   DOMAIN       78    107       EGF-like.
FT   CARBOHYD     79     79       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     82     89       {ECO:0000250}.
FT   DISULFID     83     95       {ECO:0000250}.
FT   DISULFID     97    106       {ECO:0000250}.
FT   DISULFID    115    133       {ECO:0000250}.
FT   DISULFID    128    149       {ECO:0000250}.
FT   DISULFID    131    140       {ECO:0000250}.
SQ   SEQUENCE   188 AA;  21181 MW;  C07AC973E4D82B32 CRC64;
     MDCRKMVRFS YSVIWIMAIS KAFELGLVAG LGHQEFARPS RGDLAFRDDS IWPQEEPAIR
     PRSSQRVLPM GIQHSKELNR TCCLNGGTCM LESFCACPPS FYGRNCEHDV RKENCGSVPH
     DTWLPKKCSL CKCWHGQLRC FPQAFLPGCD GLVMDEHLVA SRTPELPPSA RTTTFMLAGI
     CLSIQSYY
//
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