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Trophoblast glycoprotein (5T4 oncofetal trophoblast glycoprotein) (5T4 oncotrophoblast glycoprotein) (Wnt-activated inhibitory factor 1) (WAIF1)

 TPBG_MOUSE              Reviewed;         426 AA.
Q9Z0L0; Q3UPI2; Q6PE98; Q8BQA4;
16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 3.
23-MAY-2018, entry version 131.
RecName: Full=Trophoblast glycoprotein;
AltName: Full=5T4 oncofetal trophoblast glycoprotein;
Short=5T4 oncotrophoblast glycoprotein;
AltName: Full=Wnt-activated inhibitory factor 1;
Short=WAIF1;
Flags: Precursor;
Name=Tpbg; Synonyms=5t4;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
STRAIN=129/Sv;
PubMed=10366710; DOI=10.1016/S0167-4781(99)00055-X;
King K.W., Sheppard F.C., Westwater C., Stern P.L., Myers K.A.;
"Organisation of the mouse and human 5T4 oncofetal leucine-rich
glycoprotein gene and expression in foetal and adult murine tissues.";
Biochim. Biophys. Acta 1445:257-270(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-281.
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
-!- FUNCTION: May function as an inhibitor of Wnt/beta-catenin
signaling by indirectly interacting with LRP6 and blocking Wnt3a-
dependent LRP6 internalization. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass
type I membrane protein {ECO:0000250}.
-!- TISSUE SPECIFICITY: Highly expressed in embryo and placenta. In
adult, expressed only in brain and ovary. Not detected in kidney
small intestine, heart, spleen, testis, liver, lung, thymus and
stomach. {ECO:0000269|PubMed:10366710}.
-!- DOMAIN: The C-terminus of LRR N-terminal cap (LRRNT) and LRR 1 are
essential for the inhibition of the Wnt signaling pathway.
{ECO:0000250}.
-!- PTM: Highly glycosylated. {ECO:0000250}.
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EMBL; AJ012160; CAA09931.1; -; Genomic_DNA.
EMBL; AK051162; BAC34540.1; -; mRNA.
EMBL; AK143519; BAE25413.1; -; mRNA.
EMBL; BC058198; AAH58198.1; -; mRNA.
CCDS; CCDS23380.1; -.
RefSeq; NP_001158264.1; NM_001164792.1.
RefSeq; NP_035757.2; NM_011627.4.
RefSeq; XP_017168769.1; XM_017313280.1.
RefSeq; XP_017168770.1; XM_017313281.1.
RefSeq; XP_017168771.1; XM_017313282.1.
UniGene; Mm.20864; -.
UniGene; Mm.484180; -.
ProteinModelPortal; Q9Z0L0; -.
SMR; Q9Z0L0; -.
STRING; 10090.ENSMUSP00000006559; -.
iPTMnet; Q9Z0L0; -.
PhosphoSitePlus; Q9Z0L0; -.
SwissPalm; Q9Z0L0; -.
MaxQB; Q9Z0L0; -.
PaxDb; Q9Z0L0; -.
PeptideAtlas; Q9Z0L0; -.
PRIDE; Q9Z0L0; -.
Ensembl; ENSMUST00000006559; ENSMUSP00000006559; ENSMUSG00000035274.
Ensembl; ENSMUST00000098500; ENSMUSP00000096101; ENSMUSG00000035274.
GeneID; 21983; -.
KEGG; mmu:21983; -.
UCSC; uc009qwz.2; mouse.
CTD; 7162; -.
MGI; MGI:1341264; Tpbg.
eggNOG; KOG0619; Eukaryota.
eggNOG; COG4886; LUCA.
GeneTree; ENSGT00880000138002; -.
HOGENOM; HOG000013090; -.
HOVERGEN; HBG053843; -.
InParanoid; Q9Z0L0; -.
OMA; TYVSFRN; -.
OrthoDB; EOG091G0BIH; -.
TreeFam; TF351115; -.
PRO; PR:Q9Z0L0; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000035274; -.
CleanEx; MM_TPBG; -.
Genevisible; Q9Z0L0; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0051965; P:positive regulation of synapse assembly; IDA:MGI.
Gene3D; 3.80.10.10; -; 1.
InterPro; IPR000483; Cys-rich_flank_reg_C.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
InterPro; IPR032675; LRR_dom_sf.
InterPro; IPR000372; LRRNT.
Pfam; PF13855; LRR_8; 2.
Pfam; PF01462; LRRNT; 1.
SMART; SM00369; LRR_TYP; 6.
SMART; SM00082; LRRCT; 1.
SMART; SM00013; LRRNT; 1.
PROSITE; PS51450; LRR; 4.
1: Evidence at protein level;
Cell membrane; Complete proteome; Disulfide bond; Glycoprotein;
Leucine-rich repeat; Membrane; Phosphoprotein; Reference proteome;
Repeat; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 31 {ECO:0000255}.
CHAIN 32 426 Trophoblast glycoprotein.
/FTId=PRO_0000019593.
TOPO_DOM 32 361 Extracellular. {ECO:0000255}.
TRANSMEM 362 382 Helical. {ECO:0000255}.
TOPO_DOM 383 426 Cytoplasmic. {ECO:0000255}.
DOMAIN 53 91 LRRNT.
REPEAT 92 113 LRR 1.
REPEAT 116 139 LRR 2.
REPEAT 141 163 LRR 3.
REPEAT 172 210 LRR 4.
REPEAT 215 238 LRR 5.
REPEAT 239 261 LRR 6.
REPEAT 262 281 LRR 7.
DOMAIN 289 352 LRRCT.
COMPBIAS 32 53 Ser-rich.
MOD_RES 424 424 Phosphoserine.
{ECO:0000250|UniProtKB:Q5PQV5}.
CARBOHYD 124 124 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 281 281 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
DISULFID 62 68 {ECO:0000250}.
DISULFID 66 77 {ECO:0000250}.
DISULFID 304 329 {ECO:0000250}.
DISULFID 306 350 {ECO:0000250}.
CONFLICT 47 47 A -> D (in Ref. 1; CAA09931).
{ECO:0000305}.
CONFLICT 161 161 A -> V (in Ref. 1; CAA09931).
{ECO:0000305}.
CONFLICT 220 220 R -> C (in Ref. 3; AAH58198).
{ECO:0000305}.
CONFLICT 288 288 H -> Q (in Ref. 1; CAA09931 and 3;
AAH58198). {ECO:0000305}.
SEQUENCE 426 AA; 46451 MW; A03A76377F68D2A4 CRC64;
MPGAGSRGPS AGDGRLRLAR LALVLLGWVS ASAPSSSVPS SSTSPAAFLA SGSAQPPPAE
RCPAACECSE AARTVKCVNR NLLEVPADLP PYVRNLFLTG NQMTVLPAGA FARQPPLADL
EALNLSGNHL KEVCAGAFEH LPGLRRLDLS HNPLTNLSAF AFAGSNASVS APSPLEELIL
NHIVPPEDQR QNGSFEGMVA FEGMVAAALR SGLALRGLTR LELASNHFLF LPRDLLAQLP
SLRYLDLRNN SLVSLTYASF RNLTHLESLH LEDNALKVLH NSTLAEWHGL AHVKVFLDNN
PWVCDCYMAD MVAWLKETEV VPDKARLTCA FPEKMRNRGL LDLNSSDLDC DAVLPQSLQT
SYVFLGIVLA LIGAIFLLVL YLNRKGIKKW MHNIRDACRD HMEGYHYRYE INADPRLTNL
SSNSDV


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