ID A0A3Q3CSD1_HAPBU Unreviewed; 1506 AA.
AC A0A3Q3CSD1;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Adhesion G protein-coupled receptor L2 {ECO:0000313|Ensembl:ENSHBUP00000029497.1};
GN Name=ADGRL2 {ECO:0000313|Ensembl:ENSHBUP00000029497.1};
OS Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000029497.1, ECO:0000313|Proteomes:UP000264840};
RN [1] {ECO:0000313|Ensembl:ENSHBUP00000029497.1}
RP IDENTIFICATION.
RG Ensembl;
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_005923440.1; XM_005923378.2.
DR Ensembl; ENSHBUT00000019630.1; ENSHBUP00000029497.1; ENSHBUG00000014145.1.
DR GeneID; 102292857; -.
DR CTD; 57987; -.
DR GeneTree; ENSGT00940000156348; -.
DR OrthoDB; 1114672at2759; -.
DR Proteomes; UP000264840; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000264840};
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..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1506
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018790750"
FT TRANSMEM 865..886
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 898..916
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 928..952
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 964..983
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1003..1026
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1047..1070
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1076..1099
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 42..131
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50228"
FT DOMAIN 161..420
FT /note="Olfactomedin-like"
FT /evidence="ECO:0000259|PROSITE:PS51132"
FT DOMAIN 494..551
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 859..1100
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 450..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1295..1340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1396..1448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..489
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1307..1328
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1397..1428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 162..344
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00446"
SQ SEQUENCE 1506 AA; 169544 MW; 4314245B1EE81E25 CRC64;
MSCSLWKLPT FCWFLITLAQ VHSTEGFSRA ALPFGLVRRE LSCEGYPIDL RCPGSDVIMI
ESANYGRTDD KICDADPFQM ENINCYLPDA YKIMSQRCNN RTQCIVITGS DVFPDPCPGT
YKYLEVQYEC VPYSPCPTRI GPRTQNVSYR NCPEVEQKVF LCPGTLKAVG EPSFIFEAEQ
QAGAWCKDPL QAGDKIYFMP WTPYRTDTLI EYSSLDDFQN ARQTITYKLP HRVDGTGFVV
YDGAVFFNKE RTRNIVKFDL RTRIKSGEAI INNANYHDTS PYKWGGKTDI DLAVDENGLW
VIYATEQNNG MMVISQLNPY TLRFEATWET TYDKRSASNA FMVCGVLYVV RSTYEDNESE
VSKSLIDYIY NTKQNRGEYV DIHFPNQYQY IAAVDYNPRD NQLYVWNNFY ILRYNLEFGL
PDPAHAPPFS EVTTTPPTKT TTTTTTTTVH WGVDNNTTTT GYKERSRGAP RPRPVIPQTP
SPPPLESFPL PERFCKAIEK RDIMWPQTQR GMLVERPCPK GTRGTASYLC VLSTGDWHPK
GPDLSNCTSH WVNQVAQKIR SGENAANLAN ELAKHTKGPI FAGDVSSSVR LMEQLVDILD
AQLQELRPSE KDSAGRSFNK AIVDTVDNLL RPEALKSWQD MNSTEQTHAA TMLLDTLEEG
AFVLADNLME PAIVKVPADN IILEVYVLST DGQVQDFKFP QIGKSGISIQ LSANTVKLNS
RNGVAKLVFM LYKNLSQFLS TENATIKMDN DAYARNVSVA VNSDIIAASI NKESSRVFIN
DPVIFTLEHI DMEHYFNSNC SFWNYSERSM MGYWSTQGCK LLDSNKTHTT CSCSHLTNFA
ILMAHRETSA SSEVHELLLT VITRVGIVVS LVCLMISIFT FCFFRGLQSD RNTIHKNLCI
NLFIAELIFL IGIDMTEPRI GCAIIAGILH FFFLASFSWM CLEGVQLYLM LVEVFESEYS
RKKYYYVSGY LFPAIVVGVS AAIDYRSYGT KKACWLSVDN HFIWSFIGPV TCIIMLNLIF
LVITMYKMVK HSTTLKPDSS RLENIKSWVM GAFALLCLLG LTWSFGLFFI SEASIVMAYL
FTIFNTFQGM FIFIFHCLLQ KKVRKEYSKC FRHTYCCGGL PTESSHGSAK TSTTRTSARY
SSGTQSRIRR MWNDTVRKQS ESSFISGDIN STSTLNQGMT GNYLLTNPLL RPQGTNNPYN
TLLAETVVCN TPTAPVFNSP VTYRETRHSL NNAVRDTSAM DTLPLNGNFN NSYSLRNGDF
GDSVQVVDCG LSLDDAAFEK MIISELVHNN LRACNKSHQQ QQQQHHSLHH PPHHQQPPQY
HHHHHTERAP PKVTVVGGSS SEDDAIVADA SSLVHVGDTV GLELHQELEA PLIPQRTHSL
LYAPQKKVRT DGGVDTFVSE LTPTNPDDSL QSPNRDSLYT SMPNLKDSPY PESSPDVVED
LSPSKRSENE DVYYKSMPNL GGGQQLQAYY QIGRGSSDGY IIPITKEDSI PEGDVREGQM
QLVTSL
//
