ID   AGRB2_HUMAN             Reviewed;        1585 AA.
AC   O60241; B9EGK9; Q5T6K0; Q8NGW8; Q96GZ9;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 2.
DT   13-FEB-2019, entry version 177.
DE   RecName: Full=Adhesion G protein-coupled receptor B2 {ECO:0000303|PubMed:25713288};
DE   AltName: Full=Brain-specific angiogenesis inhibitor 2;
DE   Flags: Precursor;
GN   Name=ADGRB2 {ECO:0000312|HGNC:HGNC:944}; Synonyms=BAI2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=Fetal brain;
RX   PubMed=9533023;
RA   Shiratsuchi T., Nishimori H., Ichise H., Nakamura Y., Tokino T.;
RT   "Cloning and characterization of BAI2 and BAI3, novel genes homologous
RT   to brain-specific angiogenesis inhibitor 1 (BAI1).";
RL   Cytogenet. Cell Genet. 79:103-108(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Suwa M., Sato T., Okouchi I., Arita M., Futami K., Matsumoto S.,
RA   Tsutsumi S., Aburatani H., Asai K., Akiyama Y.;
RT   "Genome-wide discovery and analysis of human seven transmembrane helix
RT   receptor genes.";
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA   Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA   Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA   McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA   Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA   Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA   Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA   Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA   Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA   Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA   Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA   Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA   Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA   Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA   Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA   Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA   Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA   Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA   Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA   Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA   Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA   Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA   Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1293-1585 (ISOFORM 1).
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   CLEAVAGE BY FURIN, PROTEOLYTIC PROCESSING, MUTAGENESIS OF TRP-889;
RP   CYS-908 AND SER-912, SUBUNIT, PROTEIN SEQUENCE OF 296-306,
RP   GLYCOSYLATION, FUNCTION, AND ACTIVITY REGULATION.
RX   PubMed=20367554; DOI=10.3109/10799891003671139;
RA   Okajima D., Kudo G., Yokota H.;
RT   "Brain-specific angiogenesis inhibitor 2 (BAI2) may be activated by
RT   proteolytic processing.";
RL   J. Recept. Signal Transduct. 30:143-153(2010).
RN   [6]
RP   INTERACTION WITH TAX1BP3.
RX   PubMed=21787750; DOI=10.1016/j.bbrc.2011.07.029;
RA   Zencir S., Ovee M., Dobson M.J., Banerjee M., Topcu Z., Mohanty S.;
RT   "Identification of brain-specific angiogenesis inhibitor 2 as an
RT   interaction partner of glutaminase interacting protein.";
RL   Biochem. Biophys. Res. Commun. 411:792-797(2011).
RN   [7]
RP   NOMENCLATURE.
RX   PubMed=25713288; DOI=10.1124/pr.114.009647;
RA   Hamann J., Aust G., Arac D., Engel F.B., Formstone C., Fredriksson R.,
RA   Hall R.A., Harty B.L., Kirchhoff C., Knapp B., Krishnan A.,
RA   Liebscher I., Lin H.H., Martinelli D.C., Monk K.R., Peeters M.C.,
RA   Piao X., Promel S., Schoneberg T., Schwartz T.W., Singer K.,
RA   Stacey M., Ushkaryov Y.A., Vallon M., Wolfrum U., Wright M.W., Xu L.,
RA   Langenhan T., Schioth H.B.;
RT   "International union of basic and clinical pharmacology. XCIV.
RT   Adhesion G protein-coupled receptors.";
RL   Pharmacol. Rev. 67:338-367(2015).
RN   [8]
RP   SUBCELLULAR LOCATION, VARIANT TRP-1465, CHARACTERIZATION OF VARIANT
RP   TRP-1465, INTERACTION WITH SH3GL2 AND GNAZ, AND FUNCTION.
RX   PubMed=28891236; DOI=10.1002/humu.23336;
RA   Purcell R.H., Toro C., Gahl W.A., Hall R.A.;
RT   "A disease-associated mutation in the adhesion GPCR BAI2 (ADGRB2)
RT   increases receptor signaling activity.";
RL   Hum. Mutat. 38:1751-1760(2017).
CC   -!- FUNCTION: Orphan G-protein coupled receptor involved in cell
CC       adhesion and probably in cell-cell interactions. Activates NFAT-
CC       signaling pathway, a transcription factor, via the G-protein GNAZ
CC       (PubMed:20367554, PubMed:28891236). Involved in angiogenesis
CC       inhibition (By similarity). {ECO:0000250|UniProtKB:Q8CGM1,
CC       ECO:0000269|PubMed:20367554, ECO:0000269|PubMed:28891236}.
CC   -!- ACTIVITY REGULATION: Receptor activity is regulated by proteolytic
CC       processing. The long N-terminal has a an inhibitory effect on the
CC       constitutive signaling activity. Removal of the N-terminal region
CC       induces an increase of the receptor activity.
CC       {ECO:0000269|PubMed:20367554, ECO:0000269|PubMed:28891236}.
CC   -!- SUBUNIT: Heterodimer of 2 chains generated by proteolytic
CC       processing; the large extracellular N-terminal fragment and the
CC       membrane-bound C-terminal fragment predominantly remain associated
CC       and non-covalently linked. Interacts with GABPB2 (By similarity).
CC       Interacts (via carboxy-terminus) with TAX1BP3 (PubMed:21787750).
CC       Interacts with GNAZ (PubMed:28891236). Interacts with SH3GL2
CC       (PubMed:28891236). {ECO:0000250|UniProtKB:Q8CGM1,
CC       ECO:0000269|PubMed:21787750, ECO:0000269|PubMed:28891236}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28891236};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=O60241-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O60241-2; Sequence=VSP_037047;
CC       Name=3;
CC         IsoId=O60241-3; Sequence=VSP_037045;
CC       Name=4;
CC         IsoId=O60241-4; Sequence=VSP_037046, VSP_037047;
CC   -!- TISSUE SPECIFICITY: Strongly expressed in brain. Also detected in
CC       heart, thymus, skeletal muscle, and different cell lines.
CC   -!- PTM: Autoproteolytic processes at the GPS domain; this cleavage
CC       modulates receptor activity. Additionally, furin is involved in
CC       the cleavage at another site, in the middle of the extracellular
CC       domain, generating a soluble fragment.
CC       {ECO:0000269|PubMed:20367554}.
CC   -!- PTM: Glycosylated. {ECO:0000269|PubMed:20367554}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC       Adhesion G-protein coupled receptor (ADGR) subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA25362.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AB005298; BAA25362.1; ALT_INIT; mRNA.
DR   EMBL; AB065648; BAC05874.1; -; Genomic_DNA.
DR   EMBL; AC114488; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL354919; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC009035; AAH09035.1; -; mRNA.
DR   EMBL; BC136533; AAI36534.1; -; mRNA.
DR   CCDS; CCDS72746.1; -. [O60241-4]
DR   CCDS; CCDS72747.1; -. [O60241-2]
DR   PIR; T00027; T00027.
DR   RefSeq; NP_001281264.1; NM_001294335.1. [O60241-2]
DR   RefSeq; NP_001281265.1; NM_001294336.1. [O60241-4]
DR   RefSeq; XP_011540150.1; XM_011541848.2. [O60241-1]
DR   RefSeq; XP_011540151.1; XM_011541849.2. [O60241-3]
DR   RefSeq; XP_016857388.1; XM_017001899.1. [O60241-1]
DR   RefSeq; XP_016857389.1; XM_017001900.1. [O60241-2]
DR   RefSeq; XP_016857394.1; XM_017001905.1. [O60241-4]
DR   UniGene; Hs.524138; -.
DR   ProteinModelPortal; O60241; -.
DR   SMR; O60241; -.
DR   BioGrid; 107052; 3.
DR   IntAct; O60241; 4.
DR   MINT; O60241; -.
DR   STRING; 9606.ENSP00000362762; -.
DR   MEROPS; P02.029; -.
DR   TCDB; 9.A.14.6.6; the g-protein-coupled receptor (gpcr) family.
DR   CarbonylDB; O60241; -.
DR   iPTMnet; O60241; -.
DR   PhosphoSitePlus; O60241; -.
DR   BioMuta; ADGRB2; -.
DR   EPD; O60241; -.
DR   jPOST; O60241; -.
DR   PaxDb; O60241; -.
DR   PeptideAtlas; O60241; -.
DR   PRIDE; O60241; -.
DR   ProteomicsDB; 49271; -.
DR   ProteomicsDB; 49272; -. [O60241-2]
DR   ProteomicsDB; 49273; -. [O60241-3]
DR   ProteomicsDB; 49274; -. [O60241-4]
DR   Ensembl; ENST00000373655; ENSP00000362759; ENSG00000121753. [O60241-2]
DR   Ensembl; ENST00000373658; ENSP00000362762; ENSG00000121753. [O60241-1]
DR   Ensembl; ENST00000527361; ENSP00000435397; ENSG00000121753. [O60241-4]
DR   GeneID; 576; -.
DR   KEGG; hsa:576; -.
DR   UCSC; uc001btn.4; human. [O60241-1]
DR   CTD; 576; -.
DR   DisGeNET; 576; -.
DR   EuPathDB; HostDB:ENSG00000121753.12; -.
DR   GeneCards; ADGRB2; -.
DR   H-InvDB; HIX0023509; -.
DR   HGNC; HGNC:944; ADGRB2.
DR   HPA; HPA052612; -.
DR   HPA; HPA054617; -.
DR   MIM; 602683; gene.
DR   neXtProt; NX_O60241; -.
DR   OpenTargets; ENSG00000121753; -.
DR   PharmGKB; PA25248; -.
DR   eggNOG; ENOG410IEA0; Eukaryota.
DR   eggNOG; ENOG4111FBM; LUCA.
DR   GeneTree; ENSGT00940000160103; -.
DR   HOGENOM; HOG000230916; -.
DR   HOVERGEN; HBG004813; -.
DR   InParanoid; O60241; -.
DR   KO; K04597; -.
DR   OMA; CNNTATC; -.
DR   OrthoDB; 27621at2759; -.
DR   PhylomeDB; O60241; -.
DR   TreeFam; TF331634; -.
DR   ChiTaRS; ADGRB2; human.
DR   GeneWiki; Brain-specific_angiogenesis_inhibitor_2; -.
DR   GenomeRNAi; 576; -.
DR   PRO; PR:O60241; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   Bgee; ENSG00000121753; Expressed in 145 organ(s), highest expression level in right frontal lobe.
DR   ExpressionAtlas; O60241; baseline and differential.
DR   Genevisible; O60241; HS.
DR   GO; GO:0005813; C:centrosome; IDA:HPA.
DR   GO; GO:0016021; C:integral component of membrane; TAS:GDB.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IMP:UniProtKB.
DR   GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0033173; P:calcineurin-NFAT signaling cascade; IMP:UniProtKB.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR   GO; GO:0016525; P:negative regulation of angiogenesis; IEA:InterPro.
DR   GO; GO:0007422; P:peripheral nervous system development; IBA:GO_Central.
DR   GO; GO:0051965; P:positive regulation of synapse assembly; IEA:Ensembl.
DR   Gene3D; 2.20.100.10; -; 4.
DR   Gene3D; 4.10.1240.10; -; 1.
DR   InterPro; IPR032471; GAIN_dom_N.
DR   InterPro; IPR017981; GPCR_2-like.
DR   InterPro; IPR008077; GPCR_2_brain_angio_inhib.
DR   InterPro; IPR036445; GPCR_2_extracell_dom_sf.
DR   InterPro; IPR001879; GPCR_2_extracellular_dom.
DR   InterPro; IPR000832; GPCR_2_secretin-like.
DR   InterPro; IPR000203; GPS.
DR   InterPro; IPR000884; TSP1_rpt.
DR   InterPro; IPR036383; TSP1_rpt_sf.
DR   Pfam; PF00002; 7tm_2; 1.
DR   Pfam; PF16489; GAIN; 1.
DR   Pfam; PF01825; GPS; 1.
DR   Pfam; PF00090; TSP_1; 4.
DR   PRINTS; PR01694; BAIPRECURSOR.
DR   PRINTS; PR00249; GPCRSECRETIN.
DR   SMART; SM00303; GPS; 1.
DR   SMART; SM00008; HormR; 1.
DR   SMART; SM00209; TSP1; 4.
DR   SUPFAM; SSF82895; SSF82895; 4.
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; PS50092; TSP1; 4.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Complete proteome;
KW   Direct protein sequencing; Disease mutation; Disulfide bond;
KW   G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein;
KW   Polymorphism; Receptor; Reference proteome; Repeat; Signal;
KW   Transducer; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     32       {ECO:0000255}.
FT   CHAIN        33   1585       Adhesion G protein-coupled receptor B2.
FT                                /FTId=PRO_0000012864.
FT   TOPO_DOM     33    936       Extracellular. {ECO:0000305}.
FT   TRANSMEM    937    957       Helical; Name=1. {ECO:0000255}.
FT   TOPO_DOM    958    965       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    966    986       Helical; Name=2. {ECO:0000255}.
FT   TOPO_DOM    987    994       Extracellular. {ECO:0000305}.
FT   TRANSMEM    995   1015       Helical; Name=3. {ECO:0000255}.
FT   TOPO_DOM   1016   1036       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1037   1057       Helical; Name=4. {ECO:0000255}.
FT   TOPO_DOM   1058   1078       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1079   1099       Helical; Name=5. {ECO:0000255}.
FT   TOPO_DOM   1100   1121       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1122   1142       Helical; Name=6. {ECO:0000255}.
FT   TOPO_DOM   1143   1153       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1154   1174       Helical; Name=7. {ECO:0000255}.
FT   TOPO_DOM   1175   1585       Cytoplasmic. {ECO:0000305}.
FT   DOMAIN      309    362       TSP type-1 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00210}.
FT   DOMAIN      364    417       TSP type-1 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00210}.
FT   DOMAIN      419    472       TSP type-1 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00210}.
FT   DOMAIN      475    528       TSP type-1 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00210}.
FT   DOMAIN      871    923       GPS. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00098}.
FT   COMPBIAS    129    134       Poly-Glu.
FT   COMPBIAS    189    192       Poly-Asn.
FT   COMPBIAS    234    237       Poly-Thr.
FT   COMPBIAS   1315   1318       Poly-Pro.
FT   COMPBIAS   1364   1370       Poly-Gly.
FT   COMPBIAS   1425   1430       Poly-Pro.
FT   SITE        296    297       Cleavage; by furin.
FT                                {ECO:0000269|PubMed:20367554}.
FT   MOD_RES    1351   1351       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:Q8CGM1}.
FT   CARBOHYD    106    106       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    191    191       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    192    192       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    356    356       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    437    437       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    560    560       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    645    645       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    867    867       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    321    355       {ECO:0000255|PROSITE-ProRule:PRU00210}.
FT   DISULFID    325    361       {ECO:0000255|PROSITE-ProRule:PRU00210}.
FT   DISULFID    336    345       {ECO:0000255|PROSITE-ProRule:PRU00210}.
FT   DISULFID    376    411       {ECO:0000255|PROSITE-ProRule:PRU00210}.
FT   DISULFID    380    416       {ECO:0000255|PROSITE-ProRule:PRU00210}.
FT   DISULFID    391    401       {ECO:0000255|PROSITE-ProRule:PRU00210}.
FT   DISULFID    431    466       {ECO:0000255|PROSITE-ProRule:PRU00210}.
FT   DISULFID    435    471       {ECO:0000255|PROSITE-ProRule:PRU00210}.
FT   DISULFID    446    456       {ECO:0000255|PROSITE-ProRule:PRU00210}.
FT   DISULFID    487    522       {ECO:0000255|PROSITE-ProRule:PRU00210}.
FT   DISULFID    491    527       {ECO:0000255|PROSITE-ProRule:PRU00210}.
FT   DISULFID    502    512       {ECO:0000255|PROSITE-ProRule:PRU00210}.
FT   DISULFID    534    569       {ECO:0000255|PROSITE-ProRule:PRU00210}.
FT   DISULFID    557    587       {ECO:0000255|PROSITE-ProRule:PRU00210}.
FT   DISULFID    874    906       {ECO:0000255|PROSITE-ProRule:PRU00210}.
FT   DISULFID    894    908       {ECO:0000255|PROSITE-ProRule:PRU00210}.
FT   VAR_SEQ       1     12       Missing (in isoform 3). {ECO:0000305}.
FT                                /FTId=VSP_037045.
FT   VAR_SEQ    1119   1151       Missing (in isoform 4).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_037046.
FT   VAR_SEQ    1473   1473       Missing (in isoform 2 and isoform 4).
FT                                {ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|PubMed:9533023}.
FT                                /FTId=VSP_037047.
FT   VARIANT    1465   1465       R -> W (probable disease-associated
FT                                mutation found in a patient with
FT                                progressive spastic paraparesis and other
FT                                neurological symptoms; enhances receptor
FT                                surface expression; increases the
FT                                constitutive signaling activity; does not
FT                                affect interaction with GNAZ; promotes
FT                                enhanced interaction with GNAI1;
FT                                decreases interaction with SH3GL2;
FT                                dbSNP:rs778361520).
FT                                {ECO:0000269|PubMed:28891236}.
FT                                /FTId=VAR_079840.
FT   MUTAGEN     889    889       W->S: Inhibits autoproteolytic cleavage.
FT                                {ECO:0000269|PubMed:20367554}.
FT   MUTAGEN     908    908       C->W: Inhibits autoproteolytic cleavage.
FT                                {ECO:0000269|PubMed:20367554}.
FT   MUTAGEN     912    912       S->P: Inhibits autoproteolytic cleavage.
FT                                {ECO:0000269|PubMed:20367554}.
FT   CONFLICT    325    325       C -> R (in Ref. 4; AAI36534).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1585 AA;  172656 MW;  56D253AE0AB1552D CRC64;
     MENTGWMGKG HRMTPACPLL LSVILSLRLA TAFDPAPSAC SALASGVLYG AFSLQDLFPT
     IASGCSWTLE NPDPTKYSLY LRFNRQEQVC AHFAPRLLPL DHYLVNFTCL RPSPEEAVAQ
     AESEVGRPEE EEAEAAAGLE LCSGSGPFTF LHFDKNFVQL CLSAEPSEAP RLLAPAALAF
     RFVEVLLINN NNSSQFTCGV LCRWSEECGR AAGRACGFAQ PGCSCPGEAG AGSTTTTSPG
     PPAAHTLSNA LVPGGPAPPA EADLHSGSSN DLFTTEMRYG EEPEEEPKVK TQWPRSADEP
     GLYMAQTGDP AAEEWSPWSV CSLTCGQGLQ VRTRSCVSSP YGTLCSGPLR ETRPCNNSAT
     CPVHGVWEEW GSWSLCSRSC GRGSRSRMRT CVPPQHGGKA CEGPELQTKL CSMAACPVEG
     QWLEWGPWGP CSTSCANGTQ QRSRKCSVAG PAWATCTGAL TDTRECSNLE CPATDSKWGP
     WNAWSLCSKT CDTGWQRRFR MCQATGTQGY PCEGTGEEVK PCSEKRCPAF HEMCRDEYVM
     LMTWKKAAAG EIIYNKCPPN ASGSASRRCL LSAQGVAYWG LPSFARCISH EYRYLYLSLR
     EHLAKGQRML AGEGMSQVVR SLQELLARRT YYSGDLLFSV DILRNVTDTF KRATYVPSAD
     DVQRFFQVVS FMVDAENKEK WDDAQQVSPG SVHLLRVVED FIHLVGDALK AFQSSLIVTD
     NLVISIQREP VSAVSSDITF PMRGRRGMKD WVRHSEDRLF LPKEVLSLSS PGKPATSGAA
     GSPGRGRGPG TVPPGPGHSH QRLLPADPDE SSYFVIGAVL YRTLGLILPP PRPPLAVTSR
     VMTVTVRPPT QPPAEPLITV ELSYIINGTT DPHCASWDYS RADASSGDWD TENCQTLETQ
     AAHTRCQCQH LSTFAVLAQP PKDLTLELAG SPSVPLVIGC AVSCMALLTL LAIYAAFWRF
     IKSERSIILL NFCLSILASN ILILVGQSRV LSKGVCTMTA AFLHFFFLSS FCWVLTEAWQ
     SYLAVIGRMR TRLVRKRFLC LGWGLPALVV AVSVGFTRTK GYGTSSYCWL SLEGGLLYAF
     VGPAAVIVLV NMLIGIIVFN KLMARDGISD KSKKQRAGSE RCPWASLLLP CSACGAVPSP
     LLSSASARNA MASLWSSCVV LPLLALTWMS AVLAMTDRRS VLFQALFAVF NSAQGFVITA
     VHCFLRREVQ DVVKCQMGVC RADESEDSPD SCKNGQLQIL SDFEKDVDLA CQTVLFKEVN
     TCNPSTITGT LSRLSLDEDE EPKSCLVGPE GSLSFSPLPG NILVPMAASP GLGEPPPPQE
     ANPVYMCGEG GLRQLDLTWL RPTEPGSEGD YMVLPRRTLS LQPGGGGGGG EDAPRARPEG
     TPRRAAKTVA HTEGYPSFLS VDHSGLGLGP AYGSLQNPYG MTFQPPPPTP SARQVPEPGE
     RSRTMPRTVP GSTMKMGSLE RKKLRYSDLD FEKVMHTRKR HSELYHELNQ KFHTFDRYRS
     QSTAKREKRW SVSSGGAAER SVCTDKPSPG ERPSLSQHRR HQSWSTFKSM TLGSLPPKPR
     ERLTLHRAAA WEPTEPPDGD FQTEV
//