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Database: UniProt
Entry: I3JT66_ORENI
LinkDB: I3JT66_ORENI
Original site: I3JT66_ORENI 
ID   I3JT66_ORENI            Unreviewed;      1511 AA.
AC   I3JT66;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 2.
DT   27-MAR-2024, entry version 73.
DE   SubName: Full=Adhesion G protein-coupled receptor L2 {ECO:0000313|Ensembl:ENSONIP00000012061.2};
GN   Name=LOC100702950 {ECO:0000313|Ensembl:ENSONIP00000012061.2};
OS   Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX   NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000012061.2, ECO:0000313|Proteomes:UP000005207};
RN   [1] {ECO:0000313|Proteomes:UP000005207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Broad Institute Genome Assembly Team;
RG   Broad Institute Sequencing Platform;
RA   Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSONIP00000012061.2}
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   STRING; 8128.ENSONIP00000012060; -.
DR   Ensembl; ENSONIT00000012070.2; ENSONIP00000012061.2; ENSONIG00000009599.2.
DR   GeneTree; ENSGT00940000156348; -.
DR   HOGENOM; CLU_002753_1_0_1; -.
DR   Proteomes; UP000005207; Linkage group LG18.
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; cd16006; 7tmB2_Latrophilin-2; 1.
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   SUPFAM; SSF111418; Hormone receptor domain; 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:UP000005207};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
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   TRANSMEM        868..889
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        901..919
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        931..955
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        967..986
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1006..1029
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1050..1073
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1079..1102
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          44..133
FT                   /note="SUEL-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50228"
FT   DOMAIN          141..400
FT                   /note="Olfactomedin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51132"
FT   DOMAIN          491..547
FT                   /note="G-protein coupled receptors family 2 profile 1"
FT                   /evidence="ECO:0000259|PROSITE:PS50227"
FT   DOMAIN          862..1103
FT                   /note="G-protein coupled receptors family 2 profile 2"
FT                   /evidence="ECO:0000259|PROSITE:PS50261"
FT   REGION          449..488
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1124..1148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1288..1328
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1384..1475
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        456..472
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1291..1310
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1384..1426
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1434..1449
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        142..324
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00446"
SQ   SEQUENCE   1511 AA;  168271 MW;  5A4F5A8689A214C9 CRC64;
     MDYITLLSAG ILPFFPLLLL LLLLLLFFTD RAALPFGLVR RELSCEGYAI DLRCPGSDVI
     MIETANYGRT DDKICDADPF QMENVQCYLP DAYKIISQRC NNRTQCVVVT GSDVFPDPCP
     GTYKYLEVQY ECVPYSKYLF ICPGTLKSIG AATFLFEGEQ QAGSWCKDPL QAGDKIFFMP
     WTPYRTDTLI EYASLEDLKN GRQTTTYKLP HRVDGTGFVA YDGAIFFNKE RTRNIVKFDL
     RTRIKSGEAI VNNANYHDTS PYRWGGKTDI DLAVDERGLW VIYATEQNNG RIVVSQLNPY
     TLRFEATWET AYDKRSASNA FMVCGVLHVV RSTYEENESE ASRSQIDYIY NTKLSQGEYT
     DILFPNQYQY ITAVDYNPRD NQLYVWNNFY ILRYDLDFGP MFMSRALTAS LLSPSLSLSV
     VPTTEDASVS SAMPKTTTIT TTTAVSTVKG RGDTTVAGAD PRDGRDPFED SRGLSTAEPT
     IPELPPTPRR FCEVTRRRAI DWPQTHTGTT VERPCPKGTR GIASFLCTMA GTWCSKGPDL
     SNCTSHWVTQ VAQKIRSGEN AANLANELAR HTQGPVFAGD VSSSVRLMEQ LVDILDAQLQ
     ELKPNEKDSA GRTDKFVLSP WIQAIVDTVD NLLRPEALKS WKDMNSTEQT HAATMLLDTL
     EEGAFVLAEN LIEPAIVKVP AENILLEVCV LSTDGQVQDF RFPQTSKSGM TLQLSSNTVK
     VNSKNGVAKL VFVLYKHLGQ FLSTENATLR GMGDLNKHNL SLTVNSHILS ASITKESSRV
     FVADPVIFTL EHLDKEHYYN PNCSFWNYSE RSMMGYWSTQ GCKLLETNKS HTTCSCSHLT
     NFAILMAHRG NVRDGSVHEV LLTVITRMGI AVSLVCLAIS LFTFCFFRGL QSDRNTIHKN
     LCLNLFIGEL LFLVGINMTE PKLVCSIIAG VLHFCFLAAF VWMCLEGVQL YLMLVEVFES
     EFSRRKYYYM SGYLIPAVVV GISAAIDYRS YGTQRACWLR VDNHFIWSFI GPVTFIIVVN
     VIFLVVTMYK MVKHSTSMKP DSSRLGGIRS WVLGAFALLC LLGLTWSFGL FFLNESSIVM
     AYLFTIFNTL QGMFIFIFHC LLQKKVRKEY SKCFRQSQCC GALPSEGSHS SAKTATSRST
     ARYSSATQSR IRRMWNDTVR KQSESSFISG DINSTSTLNQ GMTGNYLLTN PLLRTHDTNP
     YNNLLAETVV CNTPSPPAFH SPGSLSNSRD ISAMDTLPLN GNFNNSYSLR DDDYEAVGVR
     APGDLGGLNL DDATFEKLII SEIVHNNLRP RGAPKGRDAP RERDRVLPPQ TRVTVDRGGG
     GSGSEDDAIV ADHADASSPQ RGSGRGGHAT LELLLHPHHK EVLEAPLLPQ RTHSLLYSSQ
     KAPRCLEGQS SHGSETVTAE EDMGSHSPSN NRDSLYTSMP NLRDSPSPSA SPYPPEEEEE
     EEEELSPSPQ SESEDAYHKS MPELGDAPQP LSYYHINRGT SDGCIIPPNN EDCAHDGEAP
     ADGQMQLITS L
//
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