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Database: UniProt
Entry: A0A1S3WQ24_ERIEU
LinkDB: A0A1S3WQ24_ERIEU
Original site: A0A1S3WQ24_ERIEU 
ID   A0A1S3WQ24_ERIEU        Unreviewed;      1552 AA.
AC   A0A1S3WQ24;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Adhesion G protein-coupled receptor B2 isoform X2 {ECO:0000313|RefSeq:XP_016048445.1};
GN   Name=ADGRB2 {ECO:0000313|RefSeq:XP_016048445.1};
OS   Erinaceus europaeus (Western European hedgehog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC   Erinaceus.
OX   NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_016048445.1};
RN   [1] {ECO:0000313|RefSeq:XP_016048445.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   RefSeq; XP_016048445.1; XM_016192959.1.
DR   CTD; 576; -.
DR   OrthoDB; 4181250at2759; -.
DR   Proteomes; UP000079721; Unplaced.
DR   GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR   GO; GO:0016525; P:negative regulation of angiogenesis; IEA:InterPro.
DR   CDD; cd15988; 7tmB2_BAI2; 1.
DR   Gene3D; 1.25.40.610; -; 1.
DR   Gene3D; 2.60.220.50; -; 1.
DR   Gene3D; 4.10.1240.10; GPCR, family 2, extracellular hormone receptor domain; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 4.
DR   InterPro; IPR043838; AGRB_N.
DR   InterPro; IPR032471; GAIN_dom_N.
DR   InterPro; IPR046338; GAIN_dom_sf.
DR   InterPro; IPR017981; GPCR_2-like_7TM.
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   PANTHER; PTHR10239:SF32; ADHESION G PROTEIN-COUPLED RECEPTOR B2; 1.
DR   PANTHER; PTHR10239; ISTHMIN-2; 1.
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; SSF81321; Family A G protein-coupled receptor-like; 1.
DR   SUPFAM; SSF82895; TSP-1 type 1 repeat; 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   4: Predicted;
KW   G-protein coupled receptor {ECO:0000256|ARBA:ARBA00023040};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170,
KW   ECO:0000313|RefSeq:XP_016048445.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000079721};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transducer {ECO:0000256|ARBA:ARBA00023224};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..1552
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010353534"
FT   TRANSMEM        923..944
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        956..977
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        989..1013
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1025..1043
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1063..1090
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1111..1129
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1141..1161
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1168..1188
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          507..577
FT                   /note="G-protein coupled receptors family 2 profile 1"
FT                   /evidence="ECO:0000259|PROSITE:PS50227"
FT   DOMAIN          919..1193
FT                   /note="G-protein coupled receptors family 2 profile 2"
FT                   /evidence="ECO:0000259|PROSITE:PS50261"
FT   REGION          216..257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          264..283
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          753..786
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1346..1371
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1406..1440
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1482..1552
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        264..279
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        755..770
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1490..1519
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1552 AA;  169355 MW;  2E7EA82C5A30D5D5 CRC64;
     MTPACPLLLS VILSLRLATA FDPAPSACSA LASGVLYGAF SLQDLFPTIA SGCSWTLENP
     DPTKYSLYLR FNRQEQVCTH FAPRLLPLDH YLVNFTCLRP NPEEALAQVE SEVGRPEEEE
     EAAGLELCGG SGPFTFLHFD KNFVQLCLSA EPSEAPRLLA PAALAFRFVE VLLINNNNSS
     QFTCGVLCRW SEECGRAAGR ACGFAQPGCS CPGEAGAGPP TTTPPGPPVA HTLSNALVPG
     GPAPPAEADL HSGSSNDLFT TEMRYGEEPE EEPKVKTQWP RSADEPGLYM AQTGDPAAEE
     WSPWSVCSLT CGQGLQVRTR SCVSSPYGTL CSGPLRETRP CNNSATCPVH GVWEEWGSWS
     LCSRSCGRGS RSRMRTCVPP QHGGKACEGP ELQTKLCSMA ACPVEGQWLE WGPWGPCSTS
     CANGTQQRSR KCSVAGPAWA TCSGALTDTR ECSNLECPAT DGKWGPWNSW SLCSKTCDTG
     WQRRFRMCQA TGTQGYPCEG TGEEVKPCSE KRCPAFHEMC RDEYVMLMTW KKAAAGEIIY
     NKCPPNASGS ASRRCLLSAQ GVAYWGLPSF ARCISHEYRY LYLSLREHLA KGQRMLAGEG
     MSQVVRSLQE LLARRTYYSG DLLFSVDILR NVTDTFKRAT YVPSADDVQR FFQVVSFMVD
     AENKDKWDDA QQVSPGSVHL LRVVEDFIHL VGDALKAFQS SLIVTDNLVI SIQREPISAV
     SSDITFPMRG RRGMKDWVRH SEDRLFLPKE VLSLSSPGKP TTTGTVSSPG RGRGPGTVPP
     GPGYSHQRLL PADPEEASSY FVIGAVLYRT LGLILPPPRP PLAVTSRVMT VTVRPPTQPP
     AEPLITVELS YIINGTTDPH CASWDYSSTD ANSGDWDMES CHTLETHAAH TRCQCQHLST
     FAVLAQPPKD LTLELVGSPS VPLVIGCAVS CMALLTLLAI YAAFWRFIKS ERSIILLNFC
     LSILASNILI LVGQSPVLSK GVCTMTAAFL HFFFLSSFCW VLTEAWQSYL AVIGRMRTRL
     VRKRFLCLGW GLPALVVAVS VGFTRTKGYG TSSYCWLSLE GGLLYAFVGP AAVIVLVNML
     IGIIVFNKLM ARDGISDKSK KQRAGSERCP WASLLLPCSA CGAVPSPLLS SASARNAMAS
     LWSSCVVLPL LALTWMSAVL AMTDRRSVLF QALFAVFNSA QGFVITAVHC FLRREVQDVV
     KCQMGVCRAD ESEDSPDSCK NGQLQILSDF EKDVDLACQT VLFKEVNTCN PSTITGTLSR
     LSLDEDEEPK SCLVGPEGGL SFSPLPGNIL VPMASSPGLG EPPPPQEANP VYMCGEGGLR
     QLDLTWLRQT EPGSEGDYMV LPRRTLSLQP GGGGGGGEDL PRARPEGTPR RAAKALTHTE
     GYPSFLSVEH SSLGLGPAYG SLQNPYGMTF QPPPPTPSPH QVSEPGERSR TMPRTVPGST
     MKLGSLERKK LRYSDLDFEV MHTRKRHSEL YHELNQKFHT FDRYRSQSTA KEKPSPGERP
     SLSQQRRHQS WSTFKSMTLG SLPPKPRERL ALHRTPAWEP AEPPDGDFQT EV
//
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