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Database: UniProt
Entry: A0A3Q0S1H0_AMPCI
LinkDB: A0A3Q0S1H0_AMPCI
Original site: A0A3Q0S1H0_AMPCI 
ID   A0A3Q0S1H0_AMPCI        Unreviewed;      1236 AA.
AC   A0A3Q0S1H0;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Adhesion G protein-coupled receptor L3.1 {ECO:0000313|Ensembl:ENSACIP00000018704.1};
GN   Name=ADGRL3 {ECO:0000313|Ensembl:ENSACIP00000018704.1};
OS   Amphilophus citrinellus (Midas cichlid) (Cichlasoma citrinellum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; New World cichlids;
OC   Cichlasomatinae; Heroini; Amphilophus.
OX   NCBI_TaxID=61819 {ECO:0000313|Ensembl:ENSACIP00000018704.1, ECO:0000313|Proteomes:UP000261340};
RN   [1] {ECO:0000313|Ensembl:ENSACIP00000018704.1}
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   AlphaFoldDB; A0A3Q0S1H0; -.
DR   STRING; 61819.ENSACIP00000018704; -.
DR   Ensembl; ENSACIT00000019208.1; ENSACIP00000018704.1; ENSACIG00000014545.1.
DR   GeneTree; ENSGT00940000155527; -.
DR   OMA; NENTMIM; -.
DR   Proteomes; UP000261340; 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:0071391; P:cellular response to estrogen stimulus; IEA:Ensembl.
DR   GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
DR   GO; GO:0048731; P:system development; IEA:UniProt.
DR   CDD; cd22846; Gal_Rha_Lectin_LPHN3; 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:SF60; ADHESION G PROTEIN-COUPLED RECEPTOR L3; 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   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        887..910
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        922..940
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        946..968
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        989..1009
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1029..1052
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1073..1096
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1102..1125
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          70..159
FT                   /note="SUEL-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50228"
FT   DOMAIN          169..428
FT                   /note="Olfactomedin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51132"
FT   DOMAIN          506..563
FT                   /note="G-protein coupled receptors family 2 profile 1"
FT                   /evidence="ECO:0000259|PROSITE:PS50227"
FT   DOMAIN          885..1126
FT                   /note="G-protein coupled receptors family 2 profile 2"
FT                   /evidence="ECO:0000259|PROSITE:PS50261"
FT   REGION          438..498
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1147..1169
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        447..485
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        170..352
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00446"
SQ   SEQUENCE   1236 AA;  138340 MW;  296D0A719402BFAD CRC64;
     MWTRCLLLIS TFFSPIAIGK DIVTLISALR LYKYVRSISA NNMSISMNVS VCPVYGRAPI
     PMAVVRRELS CESYPIELRC PGTDVIMIES ANYGRTDDKI CDSDPVQMEN TRCYLPDAYK
     IMSLRCNNRT QCAVVAGPDV FPDPCPGTYK YLEVQYECVP YKVEQKVFLC PGILRGVYQS
     EHLFESDHQS GAWCKDPLQA SDKIYYMPWT PYRTDTLTEY SSKEDFIAGR PTTTYKLPHR
     VDGTGFVVYD GALFFNKERT RNIVKFDLRT RIKSGEAIIA NANYHDTSPY RWGGKSDIDL
     AVDENGLWVI YATEQNNGRI VVSQLNPYTL RIEGSWDTSY DKRSASNAFM ICGVLYVVKT
     VYEDDDNEGT GNKIDYMYNT DKGKEMTVNI PFPNSYQYIA AVDYNPRDNL LYVWNNYHVV
     KYSLDFGNND FRPPPIIPPN RGVVPIGGGG SSSSTSRAAT TTRSPPYYTT PSNQIPDTNQ
     KAGGRSPPVQ VPPAPPQPPV LPPQDFCSPM VTADISWPRT QQGQTAKQPC PVGTLGVATY
     VCVAHLGHWD TQGPDLSNCT SPWVNHIMQK LRSGETAAIV ARELAEQTKG LLHPGDVPST
     VRAMVQLVEL LDVQLRNLTP GGKDSAARSL TKLQKRERSC RFFTQAMVET VNNLLHPRAE
     KAWRELPTSE QLHSATLLLD TVETGAFMLA DNLLKTDTVQ ETTDYIQLEV ARLSTDGNLA
     DLTFPQSEQH GNSIQLSAST LKQHGRNGEI RMAFVLYKNL GSYLSTENAS VRLSSDTVYP
     NYSVIVNSPV ITASINKESN KVYLSEPVVF TVKHLQHSEK NFNPNCSFWS YSKRTMTGFW
     STQDCRLLAT NRTHTSCSCT HLTSFAVLMA HVEVKVTDSM HDVLLDVITW VGILLSLVCL
     LICIFTFCFF RGLQSDRNTI HKNLCISLFI AESLFLVGIN KADQPIVCAV FAALLHFFFL
     AAFTWMFLEG VQLYIMLVEV FESEHSRTKY FYLAGYGVPA VIVAVSAAVD YRSYGTDRVC
     WLRLDTYFIW SFIGPATLII MLNVIFLGIA LYKMFHHTAI LKPDSGCLDN IKSWVIGAIA
     LLCLLGLTWA FGLMYINEST VIMAYLFTIF NSLQGMFIFI FHCILQKKVR KEYGKCLRTH
     CCSGKSVETS ISSSSKTTTS RTPGRYSTGS QSRIRRMWND TVRKQESSFI TGDINSSATL
     NRGNHGIPTI CILITVTIST LLIAGGTDGI RCHLAK
//
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