AGRB2_HUMAN
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 03-AUG-2022, entry version 196.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Fetal brain;
RX PubMed=9533023; DOI=10.1159/000134693;
RA Shiratsuchi T., Nishimori H., Ichise H., Nakamura Y., Tokino T.;
RT "Cloning and characterization of BAI2 and BAI3, novel genes homologous to
RT 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., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., 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., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., 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., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., 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 SEQUENCE
RP [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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP CLEAVAGE BY FURIN, PROTEOLYTIC PROCESSING, MUTAGENESIS OF TRP-889; CYS-908
RP AND SER-912, SUBUNIT, PROTEIN SEQUENCE OF 296-306, GLYCOSYLATION, FUNCTION,
RP 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., Liebscher I.,
RA Lin H.H., Martinelli D.C., Monk K.R., Peeters M.C., Piao X., Promel S.,
RA Schoneberg T., Schwartz T.W., Singer K., Stacey M., Ushkaryov Y.A.,
RA Vallon M., Wolfrum U., Wright M.W., Xu L., Langenhan T., Schioth H.B.;
RT "International union of basic and clinical pharmacology. XCIV. Adhesion G
RT 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) increases
RT receptor signaling activity.";
RL Hum. Mutat. 38:1751-1760(2017).
CC -!- FUNCTION: Orphan G-protein coupled receptor involved in cell adhesion
CC and probably in cell-cell interactions. Activates NFAT-signaling
CC pathway, a transcription factor, via the G-protein GNAZ
CC (PubMed:20367554, PubMed:28891236). Involved in angiogenesis inhibition
CC (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 processing;
CC the large extracellular N-terminal fragment and the membrane-bound C-
CC terminal fragment predominantly remain associated and non-covalently
CC linked. Interacts with GABPB2 (By similarity). Interacts (via carboxy-
CC terminus) with TAX1BP3 (PubMed:21787750). Interacts with GNAZ
CC (PubMed:28891236). Interacts with SH3GL2 (PubMed:28891236).
CC {ECO:0000250|UniProtKB:Q8CGM1, ECO:0000269|PubMed:21787750,
CC 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 the
CC cleavage at another site, in the middle of the extracellular domain,
CC generating a soluble fragment. {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. {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 AlphaFoldDB; O60241; -.
DR SMR; O60241; -.
DR BioGRID; 107052; 9.
DR IntAct; O60241; 9.
DR MINT; O60241; -.
DR STRING; 9606.ENSP00000362759; -.
DR MEROPS; P02.029; -.
DR TCDB; 9.A.14.6.6; the g-protein-coupled receptor (gpcr) family.
DR CarbonylDB; O60241; -.
DR GlyGen; O60241; 8 sites.
DR iPTMnet; O60241; -.
DR PhosphoSitePlus; O60241; -.
DR BioMuta; ADGRB2; -.
DR jPOST; O60241; -.
DR MassIVE; O60241; -.
DR PaxDb; O60241; -.
DR PeptideAtlas; O60241; -.
DR PRIDE; O60241; -.
DR ProteomicsDB; 49271; -. [O60241-1]
DR ProteomicsDB; 49272; -. [O60241-2]
DR ProteomicsDB; 49273; -. [O60241-3]
DR ProteomicsDB; 49274; -. [O60241-4]
DR Antibodypedia; 16794; 300 antibodies from 33 providers.
DR DNASU; 576; -.
DR Ensembl; ENST00000373655.6; ENSP00000362759.2; ENSG00000121753.13. [O60241-2]
DR Ensembl; ENST00000373658.8; ENSP00000362762.3; ENSG00000121753.13. [O60241-1]
DR Ensembl; ENST00000527361.5; ENSP00000435397.1; ENSG00000121753.13. [O60241-4]
DR GeneID; 576; -.
DR KEGG; hsa:576; -.
DR MANE-Select; ENST00000373658.8; ENSP00000362762.3; NM_001364857.2; NP_001351786.1.
DR UCSC; uc001btn.4; human. [O60241-1]
DR CTD; 576; -.
DR DisGeNET; 576; -.
DR GeneCards; ADGRB2; -.
DR HGNC; HGNC:944; ADGRB2.
DR HPA; ENSG00000121753; Tissue enriched (brain).
DR MIM; 602683; gene.
DR neXtProt; NX_O60241; -.
DR OpenTargets; ENSG00000121753; -.
DR PharmGKB; PA25248; -.
DR VEuPathDB; HostDB:ENSG00000121753; -.
DR eggNOG; ENOG502QRKJ; Eukaryota.
DR GeneTree; ENSGT00940000160103; -.
DR InParanoid; O60241; -.
DR OMA; NILMPMA; -.
DR OrthoDB; 27621at2759; -.
DR PhylomeDB; O60241; -.
DR TreeFam; TF331634; -.
DR PathwayCommons; O60241; -.
DR SignaLink; O60241; -.
DR BioGRID-ORCS; 576; 24 hits in 698 CRISPR screens.
DR ChiTaRS; ADGRB2; human.
DR GeneWiki; Brain-specific_angiogenesis_inhibitor_2; -.
DR GenomeRNAi; 576; -.
DR Pharos; O60241; Tbio.
DR PRO; PR:O60241; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O60241; protein.
DR Bgee; ENSG00000121753; Expressed in right frontal lobe and 130 other tissues.
DR ExpressionAtlas; O60241; baseline and differential.
DR Genevisible; O60241; HS.
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 Gene3D; 2.20.100.10; -; 4.
DR Gene3D; 2.60.220.50; -; 1.
DR Gene3D; 4.10.1240.10; -; 1.
DR InterPro; IPR043838; AGRB_N.
DR InterPro; IPR032471; GAIN_dom_N.
DR InterPro; IPR046338; GAIN_dom_sf.
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; PF19188; AGRB_N; 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; Direct protein sequencing;
KW Disease variant; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
KW Transducer; Transmembrane; Transmembrane helix.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..1585
FT /note="Adhesion G protein-coupled receptor B2"
FT /id="PRO_0000012864"
FT TOPO_DOM 33..936
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 937..957
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 958..965
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 966..986
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 987..994
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 995..1015
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1016..1036
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1037..1057
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1058..1078
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1079..1099
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1100..1121
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1122..1142
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1143..1153
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1154..1174
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1175..1585
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 309..362
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 364..417
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 419..472
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 475..528
FT /note="TSP type-1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 871..923
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT REGION 229..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 767..806
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1359..1385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1423..1454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1498..1585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 296..297
FT /note="Cleavage; by furin"
FT /evidence="ECO:0000269|PubMed:20367554"
FT MOD_RES 1351
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8CGM1"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 356
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 437
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 560
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 645
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 867
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 321..355
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 325..361
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 336..345
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 376..411
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 380..416
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 391..401
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 431..466
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 435..471
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 446..456
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 487..522
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 491..527
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 502..512
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 534..569
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 557..587
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 874..906
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 894..908
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT VAR_SEQ 1..12
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_037045"
FT VAR_SEQ 1119..1151
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_037046"
FT VAR_SEQ 1473
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9533023"
FT /id="VSP_037047"
FT VARIANT 1465
FT /note="R -> W (probable disease-associated variant found in
FT a patient with progressive spastic paraparesis and other
FT neurological symptoms; enhances receptor surface
FT expression; increases the constitutive signaling activity;
FT does not affect interaction with GNAZ; promotes enhanced
FT interaction with GNAI1; decreases interaction with SH3GL2;
FT dbSNP:rs778361520)"
FT /evidence="ECO:0000269|PubMed:28891236"
FT /id="VAR_079840"
FT MUTAGEN 889
FT /note="W->S: Inhibits autoproteolytic cleavage."
FT /evidence="ECO:0000269|PubMed:20367554"
FT MUTAGEN 908
FT /note="C->W: Inhibits autoproteolytic cleavage."
FT /evidence="ECO:0000269|PubMed:20367554"
FT MUTAGEN 912
FT /note="S->P: Inhibits autoproteolytic cleavage."
FT /evidence="ECO:0000269|PubMed:20367554"
FT CONFLICT 325
FT /note="C -> R (in Ref. 4; AAI36534)"
FT /evidence="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
