AGRA2_MOUSE
ID AGRA2_MOUSE Reviewed; 1336 AA.
AC Q91ZV8; B2RRK0;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Adhesion G protein-coupled receptor A2 {ECO:0000305};
DE AltName: Full=G-protein coupled receptor 124 {ECO:0000303|PubMed:21071672};
DE AltName: Full=Tumor endothelial marker 5 {ECO:0000303|PubMed:11559528};
DE Flags: Precursor;
GN Name=Adgra2 {ECO:0000312|MGI:MGI:1925810};
GN Synonyms=Gpr124 {ECO:0000303|PubMed:21071672, ECO:0000312|MGI:MGI:1925810},
GN Tem5 {ECO:0000303|PubMed:11559528};
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 [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=11559528;
RA Carson-Walter E.B., Watkins D.N., Nanda A., Vogelstein B., Kinzler K.W.,
RA St Croix B.;
RT "Cell surface tumor endothelial markers are conserved in mice and humans.";
RL Cancer Res. 61:6649-6655(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 DEVELOPMENTAL STAGE.
RX PubMed=18848646; DOI=10.1016/j.gep.2008.09.004;
RA Homma S., Shimada T., Hikake T., Yaginuma H.;
RT "Expression pattern of LRR and Ig domain-containing protein (LRRIG protein)
RT in the early mouse embryo.";
RL Gene Expr. Patterns 9:1-26(2009).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=21071672; DOI=10.1126/science.1196554;
RA Kuhnert F., Mancuso M.R., Shamloo A., Wang H.T., Choksi V., Florek M.,
RA Su H., Fruttiger M., Young W.L., Heilshorn S.C., Kuo C.J.;
RT "Essential regulation of CNS angiogenesis by the orphan G protein-coupled
RT receptor GPR124.";
RL Science 330:985-989(2010).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=21282641; DOI=10.1073/pnas.1019761108;
RA Anderson K.D., Pan L., Yang X.M., Hughes V.C., Walls J.R., Dominguez M.G.,
RA Simmons M.V., Burfeind P., Xue Y., Wei Y., Macdonald L.E., Thurston G.,
RA Daly C., Lin H.C., Economides A.N., Valenzuela D.M., Murphy A.J.,
RA Yancopoulos G.D., Gale N.W.;
RT "Angiogenic sprouting into neural tissue requires Gpr124, an orphan G
RT protein-coupled receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:2807-2812(2011).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21421844; DOI=10.1073/pnas.1017192108;
RA Cullen M., Elzarrad M.K., Seaman S., Zudaire E., Stevens J., Yang M.Y.,
RA Li X., Chaudhary A., Xu L., Hilton M.B., Logsdon D., Hsiao E., Stein E.V.,
RA Cuttitta F., Haines D.C., Nagashima K., Tessarollo L., St Croix B.;
RT "GPR124, an orphan G protein-coupled receptor, is required for CNS-specific
RT vascularization and establishment of the blood-brain barrier.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:5759-5764(2011).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25373781; DOI=10.1016/j.devcel.2014.08.018;
RA Zhou Y., Nathans J.;
RT "Gpr124 controls CNS angiogenesis and blood-brain barrier integrity by
RT promoting ligand-specific canonical wnt signaling.";
RL Dev. Cell 31:248-256(2014).
RN [9]
RP FUNCTION, INTERACTION WITH DLG1, SUBCELLULAR LOCATION, DOMAIN LRR, MOTIF
RP PDZ-BINDING, AND MUTAGENESIS OF ASP-364 AND 1333-GLU--VAL-1336.
RX PubMed=25558062; DOI=10.1016/j.celrep.2014.12.020;
RA Posokhova E., Shukla A., Seaman S., Volate S., Hilton M.B., Wu B.,
RA Morris H., Swing D.A., Zhou M., Zudaire E., Rubin J.S., St Croix B.;
RT "GPR124 functions as a WNT7-specific coactivator of canonical beta-catenin
RT signaling.";
RL Cell Rep. 10:123-130(2015).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28288111; DOI=10.1038/nm.4309;
RA Chang J., Mancuso M.R., Maier C., Liang X., Yuki K., Yang L., Kwong J.W.,
RA Wang J., Rao V., Vallon M., Kosinski C., Zhang J.J., Mah A.T., Xu L.,
RA Li L., Gholamin S., Reyes T.F., Li R., Kuhnert F., Han X., Yuan J.,
RA Chiou S.H., Brettman A.D., Daly L., Corney D.C., Cheshier S.H.,
RA Shortliffe L.D., Wu X., Snyder M., Chan P., Giffard R.G., Chang H.Y.,
RA Andreasson K., Kuo C.J.;
RT "Gpr124 is essential for blood-brain barrier integrity in central nervous
RT system disease.";
RL Nat. Med. 23:450-460(2017).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH RECK.
RX PubMed=28803732; DOI=10.1016/j.neuron.2017.07.031;
RA Cho C., Smallwood P.M., Nathans J.;
RT "Reck and Gpr124 Are Essential Receptor Cofactors for Wnt7a/Wnt7b-specific
RT signaling in mammalian CNS angiogenesis and blood-brain barrier
RT regulation.";
RL Neuron 95:1056-1073(2017).
CC -!- FUNCTION: Endothelial receptor which functions together with RECK to
CC enable brain endothelial cells to selectively respond to Wnt7 signals
CC (WNT7A or WNT7B) (PubMed:25373781, PubMed:25558062, PubMed:28803732).
CC Plays a key role in Wnt7-specific responses, such as endothelial cell
CC sprouting and migration in the forebrain and neural tube, and
CC establishment of the blood-brain barrier (PubMed:21071672,
CC PubMed:21282641, PubMed:21421844, PubMed:25373781, PubMed:28288111).
CC Acts as a Wnt7-specific coactivator of canonical Wnt signaling:
CC required to deliver RECK-bound Wnt7 to frizzled by assembling a higher-
CC order RECK-ADGRA2-Fzd-LRP5-LRP6 complex (By similarity). ADGRA2-
CC tethering function does not rely on its G-protein coupled receptor
CC (GPCR) structure but instead on its combined capacity to interact with
CC RECK extracellularly and recruit the Dishevelled scaffolding protein
CC intracellularly (By similarity). Binds to the glycosaminoglycans
CC heparin, heparin sulfate, chondroitin sulfate and dermatan sulfate (By
CC similarity). {ECO:0000250|UniProtKB:Q96PE1,
CC ECO:0000269|PubMed:21071672, ECO:0000269|PubMed:21282641,
CC ECO:0000269|PubMed:21421844, ECO:0000269|PubMed:25373781,
CC ECO:0000269|PubMed:25558062, ECO:0000269|PubMed:28288111,
CC ECO:0000269|PubMed:28803732}.
CC -!- SUBUNIT: Interacts with RECK; the interaction is direct
CC (PubMed:28803732). Interacts (via PDZ-binding motif) with DLG1 (via PDZ
CC domains) (PubMed:25558062). The cleaved extracellular subunit interacts
CC with the integrin heterodimer ITGAV:ITGB3 (By similarity).
CC {ECO:0000250|UniProtKB:Q96PE1, ECO:0000269|PubMed:25558062,
CC ECO:0000269|PubMed:28803732}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25558062,
CC ECO:0000269|PubMed:28803732}; Multi-pass membrane protein
CC {ECO:0000255}. Cell projection, filopodium
CC {ECO:0000250|UniProtKB:Q96PE1}. Note=Enriched at lateral cell borders
CC and also at sites of cell-ECM (extracellular matrix) contact.
CC {ECO:0000250|UniProtKB:Q96PE1}.
CC -!- TISSUE SPECIFICITY: Abundantly expressed in the vasculature of the
CC developing embryo (PubMed:11559528, PubMed:21071672, PubMed:21282641).
CC Expression in normal adult tissues is specifically vascular with
CC endothelial expression in CNS, including brain and retina and more
CC widespread pericyte expression in the brain and organs, including the
CC kidney, pancreas and corpus luteum (PubMed:21071672).
CC {ECO:0000269|PubMed:11559528, ECO:0000269|PubMed:21071672,
CC ECO:0000269|PubMed:21282641}.
CC -!- DEVELOPMENTAL STAGE: At 10 dpc expressed in a wide variety of tissues
CC with relatively more abundant expression in limb buds
CC (PubMed:18848646). At 10.5-12.5 dpc, detected in vessels of the
CC developing CNS and perineural vascular plexus (PNVP) (PubMed:21282641).
CC Expressed in both endothelial cells and pericytes, most prominently in
CC brain and neural tube, and to a lesser degrees in non-CNS embryonic
CC organs, including the liver, heart, and kidney (PubMed:18848646,
CC PubMed:21282641). Expressed also in embryonic epithelium of lung and
CC esophagus and in mesenchyme (PubMed:18848646, PubMed:21282641).
CC Detected in mesenchyme of the palatal shelf at 12.5 dpc
CC (PubMed:21282641). {ECO:0000269|PubMed:18848646,
CC ECO:0000269|PubMed:21282641}.
CC -!- INDUCTION: Up-regulated by the growth factors activin AB (INHBA: INHBB
CC dimer) and TGFB1 in vitro. {ECO:0000269|PubMed:21282641}.
CC -!- DOMAIN: The leucine-rich repeats (LRRs) are important for potentiation
CC of Wnt7 signaling. {ECO:0000269|PubMed:25558062}.
CC -!- DOMAIN: The RGD motif is involved in integrin ITGAV:ITGB3 binding.
CC {ECO:0000250|UniProtKB:Q96PE1}.
CC -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:Q96PE1}.
CC -!- PTM: Proteolytically cleaved into two subunits, an extracellular
CC subunit and a seven-transmembrane subunit. Cleaved by thrombin (F2) and
CC MMP1. Also cleaved by MMP9, with lower efficiency. Presence of the
CC protein disulfide-isomerase P4HB at the cell surface is additionally
CC required for shedding of the extracellular subunit, suggesting that the
CC subunits are linked by disulfide bonds. Shedding is enhanced by the
CC growth factor FGF2 and may promote cell survival during angiogenesis.
CC {ECO:0000250|UniProtKB:Q96PE1}.
CC -!- DISRUPTION PHENOTYPE: No viable adults (PubMed:21071672,
CC PubMed:21282641, PubMed:21421844). Beginning at 11 dpc, deficient
CC embryos exhibit completely penetrant, progressive CNS hemorrhage
CC originating in forebrain telencephalon and ventral neural tube leading
CC to embryonic lethality from 15.5 dpc (PubMed:21071672, PubMed:21282641,
CC PubMed:21421844). Embryos at 11.5 dpc display selective CNS-specific
CC vascular patterning defects, with markedly reduced angiogenic sprouting
CC into the forebrain telencephalon and thickening of the underlying
CC periventricular vascular plexus rendering the telencephalon virtually
CC avascular (PubMed:21071672, PubMed:21282641, PubMed:21421844,
CC PubMed:25373781). Remaining CNS vessels show significantly increased
CC permeability (PubMed:21421844). Lung size is reduced in 15.5 dpc
CC embryos (PubMed:21282641). Cleft palate is present at 15.5 dpc or later
CC (PubMed:21282641). Conditional knockout mice lacking Adgra2 in the
CC endothelia of adult mice show blood-brain barrier integrity defects in
CC a stroke model and glioblastoma (PubMed:28288111).
CC {ECO:0000269|PubMed:21071672, ECO:0000269|PubMed:21282641,
CC ECO:0000269|PubMed:21421844, ECO:0000269|PubMed:25373781,
CC ECO:0000269|PubMed:28288111}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC Adhesion G-protein coupled receptor (ADGR) subfamily. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-8 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI38452.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI38453.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAL11996.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF378759; AAL11996.1; ALT_INIT; mRNA.
DR EMBL; BC138451; AAI38452.1; ALT_INIT; mRNA.
DR EMBL; BC138452; AAI38453.1; ALT_INIT; mRNA.
DR CCDS; CCDS22210.2; -.
DR RefSeq; NP_473385.2; NM_054044.2.
DR AlphaFoldDB; Q91ZV8; -.
DR SMR; Q91ZV8; -.
DR STRING; 10090.ENSMUSP00000033876; -.
DR GlyGen; Q91ZV8; 7 sites.
DR iPTMnet; Q91ZV8; -.
DR PhosphoSitePlus; Q91ZV8; -.
DR jPOST; Q91ZV8; -.
DR MaxQB; Q91ZV8; -.
DR PaxDb; Q91ZV8; -.
DR PRIDE; Q91ZV8; -.
DR ProteomicsDB; 296125; -.
DR Antibodypedia; 1931; 330 antibodies from 32 providers.
DR DNASU; 78560; -.
DR Ensembl; ENSMUST00000033876; ENSMUSP00000033876; ENSMUSG00000031486.
DR GeneID; 78560; -.
DR KEGG; mmu:78560; -.
DR UCSC; uc009lhx.2; mouse.
DR CTD; 25960; -.
DR MGI; MGI:1925810; Adgra2.
DR VEuPathDB; HostDB:ENSMUSG00000031486; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000158941; -.
DR InParanoid; Q91ZV8; -.
DR OMA; IRWYHNQ; -.
DR OrthoDB; 31536at2759; -.
DR PhylomeDB; Q91ZV8; -.
DR TreeFam; TF331206; -.
DR BioGRID-ORCS; 78560; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Adgra2; mouse.
DR PRO; PR:Q91ZV8; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q91ZV8; protein.
DR Bgee; ENSMUSG00000031486; Expressed in umbilical cord and 163 other tissues.
DR ExpressionAtlas; Q91ZV8; baseline and differential.
DR Genevisible; Q91ZV8; MM.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:1990909; C:Wnt signalosome; ISS:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0001525; P:angiogenesis; IMP:MGI.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007417; P:central nervous system development; IMP:UniProtKB.
DR GO; GO:0043542; P:endothelial cell migration; IMP:UniProtKB.
DR GO; GO:1900747; P:negative regulation of vascular endothelial growth factor signaling pathway; IMP:MGI.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IDA:UniProtKB.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; IDA:MGI.
DR GO; GO:0045765; P:regulation of angiogenesis; IMP:UniProtKB.
DR GO; GO:0050920; P:regulation of chemotaxis; IMP:UniProtKB.
DR GO; GO:0090210; P:regulation of establishment of blood-brain barrier; IMP:UniProtKB.
DR GO; GO:0002040; P:sprouting angiogenesis; IMP:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 2.60.220.50; -; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.80.10.10; -; 2.
DR Gene3D; 4.10.1240.10; -; 1.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR046338; GAIN_dom_sf.
DR InterPro; IPR017981; GPCR_2-like.
DR InterPro; IPR036445; GPCR_2_extracell_dom_sf.
DR InterPro; IPR001879; GPCR_2_extracellular_dom.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR017983; GPCR_2_secretin-like_CS.
DR InterPro; IPR000203; GPS.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF01825; GPS; 1.
DR Pfam; PF13855; LRR_8; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00369; LRR_TYP; 4.
DR SMART; SM00082; LRRCT; 1.
DR SUPFAM; SSF111418; SSF111418; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
DR PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR PROSITE; PS50221; GPS; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS51450; LRR; 3.
PE 1: Evidence at protein level;
KW Angiogenesis; Cell membrane; Cell projection; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Immunoglobulin domain;
KW Leucine-rich repeat; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Transducer; Transmembrane;
KW Transmembrane helix; Wnt signaling pathway.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..1336
FT /note="Adhesion G protein-coupled receptor A2"
FT /id="PRO_0000012899"
FT TOPO_DOM 34..769
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q96PE1"
FT TRANSMEM 770..790
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 791..805
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 806..826
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 827..830
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 831..851
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 852..884
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 885..905
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 906..922
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 923..943
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 944..1016
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1017..1037
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1038..1044
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1045..1065
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1066..1336
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q96PE1"
FT REPEAT 85..106
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 109..130
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 133..154
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 157..178
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT DOMAIN 190..241
FT /note="LRRCT"
FT /evidence="ECO:0000255"
FT DOMAIN 247..344
FT /note="Ig-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 708..756
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT REGION 1084..1310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 362..364
FT /note="RGD"
FT /evidence="ECO:0000250|UniProtKB:Q96PE1"
FT MOTIF 1333..1336
FT /note="PDZ-binding"
FT /evidence="ECO:0000269|PubMed:25558062"
FT COMPBIAS 1167..1184
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1209..1233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 369..370
FT /note="Cleavage; by thrombin"
FT /evidence="ECO:0000250|UniProtKB:Q96PE1"
FT SITE 398..399
FT /note="Cleavage; by thrombin"
FT /evidence="ECO:0000250|UniProtKB:Q96PE1"
FT MOD_RES 1104
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96PE1"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 602
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 691
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 735
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 268..328
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT MUTAGEN 364
FT /note="D->E: No effect on potentiation of WNT7A signaling."
FT /evidence="ECO:0000269|PubMed:25558062"
FT MUTAGEN 1333..1336
FT /note="Missing: Fails to interact with DLG1. No effect on
FT cell surface localization."
FT /evidence="ECO:0000269|PubMed:25558062"
SQ SEQUENCE 1336 AA; 143170 MW; C65354E5331F049F CRC64;
MGAGGRRMPV PPARLLLLPL LPCLLLLAPG TRGAPGCPVP IRGCKCSGER PKGLSGGAHN
PARRRVVCGG GDLPEPPDPG LLPNGTITLL LSNNKITGLR NGSFLGLSLL EKLDLRSNVI
STVQPGAFLG LGELKRLDLS NNRIGCLTSE TFQGLPRLLR LNISGNIYSS LQPGVFDELP
ALKIVDFGTE FLTCDCRLRW LLPWARNHSL QLSERTLCAY PSALHAHALS SLQESQLRCE
GALELHTHYL IPSLRQVVFQ GDRLPFQCSA SYLGNDTRIH WYHNGAPMES DEQAGIVLAE
NLIHDCTFIT SELTLSHIGV WASGEWECSV STVQGNTSKK VEIVVLETSA SYCPAERVTN
NRGDFRWPRT LAGITAYQSC LQYPFTSVPL SGGAPGTRAS RRCDRAGRWE PGDYSHCLYT
NDITRVLYTF VLMPINASNA LTLAHQLRVY TAEAASFSDM MDVVYVAQMI QKFLGYVDQI
KELVEVMVDM ASNLMLVDEH LLWLAQREDK ACSGIVGALE RIGGAALSPH AQHISVNSRN
VALEAYLIKP HSYVGLTCTA FQRREVGVSG AQPSSVGQDA PVEPEPLADQ QLRFRCTTGR
PNISLSSFHI KNSVALASIQ LPPSLFSTLP AALAPPVPPD CTLQLLVFRN GRLFRSHGNN
TSRPGAAGPG KRRGVATPVI FAGTSGCGVG NLTEPVAVSL RHWAEGADPM AAWWNQDGPG
GWSSEGCRLR YSQPNVSSLY CQHLGNVAVL MELNAFPREA GGSGAGLHPV VYPCTALLLL
CLFSTIITYI LNHSSIHVSR KGWHMLLNLC FHMAMTSAVF VGGVTLTNYQ MVCQAVGITL
HYSSLSSLLW MGVKARVLHK ELSWRAPPLE EGEAAPPGPR PMLRFYLIAG GIPLIICGIT
AAVNIHNYRD HSPYCWLVWR PSLGAFYIPV ALILPITWIY FLCAGLHLRS HVAQNPKQGN
RISLEPGEEL RGSTRLRSSG VLLNDSGSLL ATVSAGVGTP APPEDGDGVY SPGVQLGALM
TTHFLYLAMW ACGALAVSQR WLPRVVCSCL YGVAASALGL FVFTHHCARR RDVRASWRAC
CPPASPSASH VPARALPTAT EDGSPVLGEG PASLKSSPSG SSGRAPPPPC KLTNLQVAQS
QVCEASVAAR GDGEPEPTGS RGSLAPRHHN NLHHGRRVHK SRAKGHRAGE TGGKSRLKAL
RAGTSPGAPE LLSSESGSLH NSPSDSYPGS SRNSPGDGLP LEGEPMLTPS EGSDTSAAPI
AETGRPGQRR SASRDNLKGS GSALERESKR RSYPLNTTSL NGAPKGGKYE DASVTGAEAI
AGGSMKTGLW KSETTV
