TDGF3_HUMAN
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 03-AUG-2022, entry version 145.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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 X-
RT 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 characteristics
RT 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., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., 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., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., 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., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., 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., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., 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., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA 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 Nodal-
CC 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 and a
CC poly(A) sequence. {ECO:0000305}.
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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 AlphaFoldDB; P51864; -.
DR GlyGen; P51864; 1 site.
DR BioMuta; HGNC:11703; -.
DR DMDM; 1706127; -.
DR jPOST; P51864; -.
DR MassIVE; P51864; -.
DR PeptideAtlas; P51864; -.
DR PRIDE; P51864; -.
DR ProteomicsDB; 56441; -.
DR Ensembl; ENST00000602699.1; ENSP00000507999.1; ENSG00000225366.5.
DR MANE-Select; ENST00000602699.2; ENSP00000507999.1; NM_001397362.1; NP_001384291.1.
DR GeneCards; TDGF1P3; -.
DR HGNC; HGNC:11703; TDGF1P3.
DR MIM; 187395; gene+phenotype.
DR neXtProt; NX_P51864; -.
DR OpenTargets; ENSG00000225366; -.
DR GeneTree; ENSGT00940000159076; -.
DR InParanoid; P51864; -.
DR PathwayCommons; P51864; -.
DR Reactome; R-HSA-1181150; Signaling by NODAL.
DR Reactome; R-HSA-1433617; Regulation of signaling by NODAL.
DR SignaLink; P51864; -.
DR ChiTaRS; TDGF1P3; human.
DR Pharos; P51864; Tdark.
DR PRO; PR:P51864; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P51864; protein.
DR Bgee; ENSG00000225366; Expressed in adrenal tissue and 14 other tissues.
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:0001568; P:blood vessel development; 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; IPR000742; EGF-like_dom.
DR Pfam; PF09443; CFC; 1.
DR PIRSF; PIRSF036301; Cripto_growth_factor; 1.
DR PROSITE; PS00022; EGF_1; 1.
PE 5: Uncertain;
KW Cell membrane; Disulfide bond; EGF-like domain; Glycoprotein;
KW Growth factor; Membrane; Reference proteome.
FT CHAIN 1..188
FT /note="Putative teratocarcinoma-derived growth factor 3"
FT /id="PRO_0000055627"
FT DOMAIN 78..107
FT /note="EGF-like"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 82..89
FT /evidence="ECO:0000250"
FT DISULFID 83..95
FT /evidence="ECO:0000250"
FT DISULFID 97..106
FT /evidence="ECO:0000250"
FT DISULFID 115..133
FT /evidence="ECO:0000250"
FT DISULFID 128..149
FT /evidence="ECO:0000250"
FT DISULFID 131..140
FT /evidence="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