ID   TPBG_MACFA              Reviewed;         420 AA.
AC   Q4R8Y9;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Trophoblast glycoprotein;
DE   AltName: Full=Wnt-activated inhibitory factor 1;
DE            Short=WAIF1;
DE   Flags: Precursor;
GN   Name=TPBG; ORFNames=QtsA-11109;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB168308; BAE00432.1; -; mRNA.
DR   RefSeq; NP_001306553.1; NM_001319624.1.
DR   AlphaFoldDB; Q4R8Y9; -.
DR   SMR; Q4R8Y9; -.
DR   STRING; 9541.XP_005552540.1; -.
DR   GeneID; 102132149; -.
DR   CTD; 7162; -.
DR   eggNOG; KOG0619; Eukaryota.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; Glycoprotein; Leucine-rich repeat; Membrane;
KW   Phosphoprotein; Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000255"
FT   CHAIN           35..420
FT                   /note="Trophoblast glycoprotein"
FT                   /id="PRO_0000019592"
FT   TOPO_DOM        35..355
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        356..376
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        377..420
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..204
FT                   /note="LRR 4"
FT   REPEAT          209..232
FT                   /note="LRR 5"
FT   REPEAT          233..255
FT                   /note="LRR 6"
FT   REPEAT          256..275
FT                   /note="LRR 7"
FT   DOMAIN          283..346
FT                   /note="LRRCT"
FT   MOD_RES         418
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5PQV5"
FT   CARBOHYD        81
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        124
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        275
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        298..323
FT                   /evidence="ECO:0000250"
FT   DISULFID        300..344
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   420 AA;  45828 MW;  1BB8F69E4B6C6894 CRC64;
     MPGGCSRGPA AGDGRLRLAR LALVLLGWVS SSSSTSSASS SSSSAPFLAS AASAQPPLPD
     QCPALCECSE AARTVKCVNR NLTEVPTDLP LYVRNLFLTG NQLAVLPAGA FARRPPLAEL
     AALNLSGSRL DEVRGGAFEH LPSLRQLDLS HNPLAYLSPF AFSGSNASIS APSPLVELIL
     NHIVPPDDKR QNRSFEGMVA AALVAGRALQ GLHLLELASN HFLYLPRDVL AQLPSLRYLD
     LSNNSLVSLT YVSFRNLTHL ESLHLEDNAL KVLHNGTLAE LQGLPHVRVF LDNNPWVCDC
     HMADMVTWLK QTGVVQGKDR LTCAFPEKMR NRVLLELNSA DLDCDPILPP SLQTSYVFLG
     IVLALIGAIF LLVLYLNRKG IKKWMHNIRD ACRDHMEGYH YRYEINADPR LTNLSSNSDV