TPBG_MOUSE
ID TPBG_MOUSE Reviewed; 426 AA.
AC Q9Z0L0; Q3UPI2; Q6PE98; Q8BQA4;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Trophoblast glycoprotein;
DE AltName: Full=5T4 oncofetal trophoblast glycoprotein;
DE Short=5T4 oncotrophoblast glycoprotein;
DE AltName: Full=Wnt-activated inhibitory factor 1;
DE Short=WAIF1;
DE Flags: Precursor;
GN Name=Tpbg; Synonyms=5t4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC STRAIN=129/Sv;
RX PubMed=10366710; DOI=10.1016/s0167-4781(99)00055-x;
RA King K.W., Sheppard F.C., Westwater C., Stern P.L., Myers K.A.;
RT "Organisation of the mouse and human 5T4 oncofetal leucine-rich
RT glycoprotein gene and expression in foetal and adult murine tissues.";
RL Biochim. Biophys. Acta 1445:257-270(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-281.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
CC -!- FUNCTION: May function as an inhibitor of Wnt/beta-catenin signaling by
CC indirectly interacting with LRP6 and blocking Wnt3a-dependent LRP6
CC internalization. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in embryo and placenta. In adult,
CC expressed only in brain and ovary. Not detected in kidney small
CC intestine, heart, spleen, testis, liver, lung, thymus and stomach.
CC {ECO:0000269|PubMed:10366710}.
CC -!- DOMAIN: The C-terminus of LRR N-terminal cap (LRRNT) and LRR 1 are
CC essential for the inhibition of the Wnt signaling pathway.
CC {ECO:0000250}.
CC -!- PTM: Highly glycosylated. {ECO:0000250}.
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DR EMBL; AJ012160; CAA09931.1; -; Genomic_DNA.
DR EMBL; AK051162; BAC34540.1; -; mRNA.
DR EMBL; AK143519; BAE25413.1; -; mRNA.
DR EMBL; BC058198; AAH58198.1; -; mRNA.
DR CCDS; CCDS23380.1; -.
DR RefSeq; NP_001158264.1; NM_001164792.1.
DR RefSeq; NP_035757.2; NM_011627.4.
DR RefSeq; XP_017168769.1; XM_017313280.1.
DR RefSeq; XP_017168770.1; XM_017313281.1.
DR RefSeq; XP_017168771.1; XM_017313282.1.
DR AlphaFoldDB; Q9Z0L0; -.
DR SMR; Q9Z0L0; -.
DR BioGRID; 204285; 2.
DR STRING; 10090.ENSMUSP00000006559; -.
DR GlyConnect; 2801; 6 N-Linked glycans (3 sites).
DR GlyGen; Q9Z0L0; 4 sites, 6 N-linked glycans (3 sites).
DR iPTMnet; Q9Z0L0; -.
DR PhosphoSitePlus; Q9Z0L0; -.
DR SwissPalm; Q9Z0L0; -.
DR MaxQB; Q9Z0L0; -.
DR PaxDb; Q9Z0L0; -.
DR PeptideAtlas; Q9Z0L0; -.
DR PRIDE; Q9Z0L0; -.
DR ProteomicsDB; 258820; -.
DR Antibodypedia; 2135; 295 antibodies from 32 providers.
DR DNASU; 21983; -.
DR Ensembl; ENSMUST00000006559; ENSMUSP00000006559; ENSMUSG00000035274.
DR Ensembl; ENSMUST00000098500; ENSMUSP00000096101; ENSMUSG00000035274.
DR GeneID; 21983; -.
DR KEGG; mmu:21983; -.
DR UCSC; uc009qwz.2; mouse.
DR CTD; 7162; -.
DR MGI; MGI:1341264; Tpbg.
DR VEuPathDB; HostDB:ENSMUSG00000035274; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000154868; -.
DR HOGENOM; CLU_064866_0_0_1; -.
DR InParanoid; Q9Z0L0; -.
DR OMA; EDCPEVH; -.
DR OrthoDB; 785938at2759; -.
DR PhylomeDB; Q9Z0L0; -.
DR TreeFam; TF351115; -.
DR BioGRID-ORCS; 21983; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Tpbg; mouse.
DR PRO; PR:Q9Z0L0; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9Z0L0; protein.
DR Bgee; ENSMUSG00000035274; Expressed in ureter smooth muscle and 208 other tissues.
DR Genevisible; Q9Z0L0; MM.
DR GO; GO:0043679; C:axon terminus; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0030425; C:dendrite; IDA:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0060326; P:cell chemotaxis; IMP:MGI.
DR GO; GO:0140059; P:dendrite arborization; IMP:MGI.
DR GO; GO:0090497; P:mesenchymal cell migration; IMP:MGI.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IGI:MGI.
DR GO; GO:0008355; P:olfactory learning; IMP:MGI.
DR GO; GO:0050921; P:positive regulation of chemotaxis; IGI:MGI.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IGI:MGI.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IGI:MGI.
DR GO; GO:0051965; P:positive regulation of synapse assembly; IDA:MGI.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:MGI.
DR GO; GO:0051932; P:synaptic transmission, GABAergic; IMP:MGI.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000372; LRRNT.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF01462; LRRNT; 1.
DR SMART; SM00369; LRR_TYP; 6.
DR SMART; SM00082; LRRCT; 1.
DR SMART; SM00013; LRRNT; 1.
DR PROSITE; PS51450; LRR; 4.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Glycoprotein; Leucine-rich repeat; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..426
FT /note="Trophoblast glycoprotein"
FT /id="PRO_0000019593"
FT TOPO_DOM 32..361
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 362..382
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 383..426
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 53..91
FT /note="LRRNT"
FT REPEAT 92..113
FT /note="LRR 1"
FT REPEAT 116..139
FT /note="LRR 2"
FT REPEAT 141..163
FT /note="LRR 3"
FT REPEAT 172..210
FT /note="LRR 4"
FT REPEAT 215..238
FT /note="LRR 5"
FT REPEAT 239..261
FT /note="LRR 6"
FT REPEAT 262..281
FT /note="LRR 7"
FT DOMAIN 289..352
FT /note="LRRCT"
FT REGION 33..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 424
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5PQV5"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 281
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT DISULFID 62..68
FT /evidence="ECO:0000250"
FT DISULFID 66..77
FT /evidence="ECO:0000250"
FT DISULFID 304..329
FT /evidence="ECO:0000250"
FT DISULFID 306..350
FT /evidence="ECO:0000250"
FT CONFLICT 47
FT /note="A -> D (in Ref. 1; CAA09931)"
FT /evidence="ECO:0000305"
FT CONFLICT 161
FT /note="A -> V (in Ref. 1; CAA09931)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="R -> C (in Ref. 3; AAH58198)"
FT /evidence="ECO:0000305"
FT CONFLICT 288
FT /note="H -> Q (in Ref. 1; CAA09931 and 3; AAH58198)"
FT /evidence="ECO:0000305"
SQ 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
