ID A0A3B4CF19_PYGNA Unreviewed; 1505 AA.
AC A0A3B4CF19;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Adhesion G protein-coupled receptor L2 {ECO:0000313|Ensembl:ENSPNAP00000010557.1};
GN Name=ADGRL2 {ECO:0000313|Ensembl:ENSPNAP00000010557.1};
OS Pygocentrus nattereri (Red-bellied piranha).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Pygocentrus.
OX NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000010557.1, ECO:0000313|Proteomes:UP000261440};
RN [1] {ECO:0000313|Ensembl:ENSPNAP00000010557.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 Ensembl; ENSPNAT00000017260.1; ENSPNAP00000010557.1; ENSPNAG00000016300.1.
DR GeneTree; ENSGT00940000156348; -.
DR Proteomes; UP000261440; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0048731; P:system development; IEA:UniProt.
DR CDD; cd22845; Gal_Rha_Lectin_LPHN2; 1.
DR Gene3D; 1.25.40.610; -; 1.
DR Gene3D; 2.60.120.740; -; 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 InterPro; IPR032471; GAIN_dom_N.
DR InterPro; IPR046338; GAIN_dom_sf.
DR InterPro; IPR017981; GPCR_2-like_7TM.
DR InterPro; IPR036445; GPCR_2_extracell_dom_sf.
DR InterPro; IPR001879; GPCR_2_extracellular_dom.
DR InterPro; IPR003924; GPCR_2_latrophilin.
DR InterPro; IPR003334; GPCR_2_latrophilin_rcpt_C.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR017983; GPCR_2_secretin-like_CS.
DR InterPro; IPR000203; GPS.
DR InterPro; IPR000922; Lectin_gal-bd_dom.
DR InterPro; IPR043159; Lectin_gal-bd_sf.
DR InterPro; IPR003112; Olfac-like_dom.
DR PANTHER; PTHR12011:SF61; ADHESION G PROTEIN-COUPLED RECEPTOR L2; 1.
DR PANTHER; PTHR12011; ADHESION G-PROTEIN COUPLED RECEPTOR; 1.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF16489; GAIN; 1.
DR Pfam; PF02140; Gal_Lectin; 1.
DR Pfam; PF01825; GPS; 1.
DR Pfam; PF02793; HRM; 1.
DR Pfam; PF02354; Latrophilin; 1.
DR Pfam; PF02191; OLF; 1.
DR PRINTS; PR00249; GPCRSECRETIN.
DR PRINTS; PR01444; LATROPHILIN.
DR SMART; SM00303; GPS; 1.
DR SMART; SM00008; HormR; 1.
DR SMART; SM00284; OLF; 1.
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 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; PS51132; OLF; 1.
DR PROSITE; PS50228; SUEL_LECTIN; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00446};
KW G-protein coupled receptor {ECO:0000256|ARBA:ARBA00023040};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Signal {ECO:0000256|ARBA:ARBA00022729, 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..47
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 48..1505
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017219876"
FT TRANSMEM 867..888
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 930..954
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 966..985
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1005..1028
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1049..1072
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1078..1101
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 63..152
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50228"
FT DOMAIN 162..421
FT /note="Olfactomedin-like"
FT /evidence="ECO:0000259|PROSITE:PS51132"
FT DOMAIN 491..553
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 861..1102
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 462..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1341..1360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1382..1448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..491
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1396..1448
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 163..345
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00446"
SQ SEQUENCE 1505 AA; 168655 MW; FDF8959CCA35D899 CRC64;
MDCCDCSDFR PNMRRMSKPS TMACSAWSLS TLCCLMFALA AIQCTEGFSR AALPFGLVRR
ELSCEGYPID LRCPGSDVIM IESANYGRTD DKICDADPFQ MENINCYLPD AYKIMSQRCN
NRTQCIVITG SDVFPDPCPG TYKYLEVQYE CVPYKVEQKV FVCPGTLKAV GDPSFLFEAE
QQAGAWCKDP LQAGDKVYFM PWTPYRTDTL IEYSSLDDFQ NSRQTTTYKL PHRVDGTGFV
VYDGAVFFNK ERTRNIVKFD LRTRIKSGEA IINNANYHDT SPYKWGGKTD IDLAVDENGL
WVIYATEQNN GMMVLSQLNP YTLRFEATWE TAYDKRSASN AFMICGVLYV VRSTYEDNEN
EVSKGLIDYI YNTKQSHGEF VDINFPNQYQ YIAAVEYNPR DNQLYVWNNF YILRYNLVFG
PPDPAHAPPI SEVTSAPVLP RTTTTTTTTT TQQKGLVTTI TTTGTRVGNK PPKPPAAPPR
TTTPPSLDSF PPPERFCDSV ERRDIIWPQT QRGMLVERPC PKGTRGTASY LCVLSTGAWH
PKGPDLSNCT SHWVNQVAQK IRSGENAANL ANELAKHTKG PIFPGDISST MRLMEQLVDI
LDAQLQELRP SEKDSTGRSF NKAIVDTVDN LLRPEALKSW RDMNSTEQTH AATMLLDTLE
EGAFVLADNL MEPAIVKVPA SNIILDVYVL STDGQVQDFK FPQSSKGSIS IQLSANTVKL
NSRNGVAKLV FALYKNLGQF LSTENATIKL GSEAHGRNLS VAVNSDVIAA SINKESSRVF
ITEPVIFTLE HIDMQHYFNS NCSFWNYSER SMMGYWSTQG CRLIDSNKTH TTCSCSHLTN
FAILMAHQEV LGPDGLHKLL LTVITRVGIV VSLICLGMCI FTFCFFRGLQ SDRNTIHKNF
CINLFIAELT FLIGIDMTEY RIDCSVIAGI LHYFFLASFA WMCLEGVQLY LMLVEVFESE
YSRKKYYYVS GYLLPAIVVG VSAVVDYRSY GTTKACWLRV DNHFIWSFIG PVTFIIMLNL
IFLVITMYKM VKHSTSLKPD SSRLENIKSW TLGAFALLCL VSLTWSFGLF FINEKSVVLA
YLFTIFNTFQ GMFIFIFYCL LQKKVRREYS KCFRHTYCCG GLPTENSHSS TKTATTRTSA
RYSSGTQSRI RRMWNDTVRK QSESSFISGD INSTSTLNQG MTGNYLLTNP LLRPQGTNNP
YNTLLAETVV CNTPTAPVFN SPVTYRETRH SMNNARDTSA MDTLPLNGNF NNSYSLRNGD
YGDSVQVVDC GLGLDDAAFE KMIISELVHN NLRACGKSHR SESRINTKKV AGADVGSQDD
IIVAETSSLV HLGTETNHIV GGLSLHPHHH HTHNPHHPRE LEAPLIPQRT HSLLYHTQER
ARTEPAAPLP PHSYATQLPA QPQAQDSLQS PNRDSLYASL PNLRDSPSAE SGPDTLEDLS
PSKQSESEDV YYKSMPNLGA SSQQLHAYYQ ISRGSSDGYI IPITKEGCIP EGDVREGQMQ
LVTSL
//
