TPBG_RAT
ID TPBG_RAT Reviewed; 426 AA.
AC Q5PQV5; Q9QYD9;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 121.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Cerebellum;
RA Ninkina N.N., Buchman V.L.;
RT "Structure and expression of the rat 5T4 gene.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-424, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-124, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24090084; DOI=10.1021/pr400783j;
RA Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
RA Graham M.E., Packer N.H., Cordwell S.J.;
RT "Site-specific glycan-peptide analysis for determination of N-glycoproteome
RT heterogeneity.";
RL J. Proteome Res. 12:5791-5800(2013).
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 -!- 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; AF063939; AAF21770.1; -; mRNA.
DR EMBL; BC087011; AAH87011.1; -; mRNA.
DR RefSeq; NP_113995.1; NM_031807.1.
DR RefSeq; XP_006243561.1; XM_006243499.3.
DR RefSeq; XP_008764679.1; XM_008766457.2.
DR RefSeq; XP_017451424.1; XM_017595935.1.
DR AlphaFoldDB; Q5PQV5; -.
DR SMR; Q5PQV5; -.
DR STRING; 10116.ENSRNOP00000014326; -.
DR GlyGen; Q5PQV5; 3 sites, 2 N-linked glycans (1 site).
DR iPTMnet; Q5PQV5; -.
DR PhosphoSitePlus; Q5PQV5; -.
DR PaxDb; Q5PQV5; -.
DR Ensembl; ENSRNOT00000014326; ENSRNOP00000014326; ENSRNOG00000010694.
DR Ensembl; ENSRNOT00000089491; ENSRNOP00000075124; ENSRNOG00000010694.
DR Ensembl; ENSRNOT00000104677; ENSRNOP00000085521; ENSRNOG00000010694.
DR GeneID; 83684; -.
DR KEGG; rno:83684; -.
DR UCSC; RGD:621453; rat.
DR CTD; 7162; -.
DR RGD; 621453; Tpbg.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000154868; -.
DR HOGENOM; CLU_064866_0_0_1; -.
DR InParanoid; Q5PQV5; -.
DR OMA; EDCPEVH; -.
DR OrthoDB; 785938at2759; -.
DR PhylomeDB; Q5PQV5; -.
DR TreeFam; TF351115; -.
DR PRO; PR:Q5PQV5; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000010694; Expressed in ovary and 19 other tissues.
DR Genevisible; Q5PQV5; RN.
DR GO; GO:0043679; C:axon terminus; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0030425; C:dendrite; ISO:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0060326; P:cell chemotaxis; ISO:RGD.
DR GO; GO:0140059; P:dendrite arborization; ISO:RGD.
DR GO; GO:0090497; P:mesenchymal cell migration; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0008355; P:olfactory learning; ISO:RGD.
DR GO; GO:0050921; P:positive regulation of chemotaxis; ISO:RGD.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:RGD.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:RGD.
DR GO; GO:0051965; P:positive regulation of synapse assembly; ISO:RGD.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:RGD.
DR GO; GO:0051932; P:synaptic transmission, GABAergic; ISO:RGD.
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; 5.
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_0000019594"
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 34..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 424
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 281
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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 416
FT /note="R -> S (in Ref. 1; AAF21770)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 426 AA; 46508 MW; 4EEFF69F86B545B0 CRC64;
MPGAGSRGPS AGDGRLRLAR LALVLLGWVS ASAPSSSLPS SSTSPAAFLA SGSAQPPPAE
RCPAACECSE AARTVKCVNR NLLEVPADLP PYVRNLFLTG NQMTVLPAGA FARQPPLADL
AVLNLSGNHL KEVGAGAFEH LPGLRRLDLS HNPLTNLSAF TFAGSNVSVS TPSPLLELIL
NHIVPPEDQR QNGSFEGMVA FEGMVAAALR SGLALRGLHH LELASNHFLY LPRDLLDQLP
SLKHLDLRNN SLVSLTYASF RNLTHLESLH LEDNALKVLH NSTLAEWQGL AHVRVFLDNN
PWVCDCYMAD MVSWLKETEV VPDKARLTCA FPEKMRNRGL LDLTSSDLDC DATLPQSLQT
SYVFLGIVLA LIGAIFLLVL YLNRKGIKKW MHNIRDACRD HMEGYHYRYE INADPRLTNL
SSNSDV
