ID A0A3Q2WT54_HAPBU Unreviewed; 1533 AA.
AC A0A3Q2WT54;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Latrophilin-3-like {ECO:0000313|Ensembl:ENSHBUP00000029974.1};
GN Name=ADGRL3 {ECO:0000313|Ensembl:ENSHBUP00000029974.1};
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:ENSHBUP00000029974.1, ECO:0000313|Proteomes:UP000264840};
RN [1] {ECO:0000313|Ensembl:ENSHBUP00000029974.1}
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 STRING; 8153.ENSHBUP00000029974; -.
DR Ensembl; ENSHBUT00000032770.1; ENSHBUP00000029974.1; ENSHBUG00000014840.1.
DR GeneTree; ENSGT00940000155527; -.
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: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; 2.
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..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1533
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018607289"
FT TRANSMEM 884..907
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 943..965
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 986..1006
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1026..1049
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1070..1093
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1099..1122
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 35..124
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50228"
FT DOMAIN 134..393
FT /note="Olfactomedin-like"
FT /evidence="ECO:0000259|PROSITE:PS51132"
FT DOMAIN 503..560
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 882..1123
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 398..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1144..1166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1318..1351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1372..1401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1418..1472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1494..1533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..482
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..500
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1318..1336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1374..1398
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 135..317
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00446"
SQ SEQUENCE 1533 AA; 170757 MW; 51776DE627AFFCA1 CRC64;
MWTRCLLLIS TFFSPIAIVY GRAPIPMAVV RRELSCESYP IELRCPGTDV IMIESANYGR
TDDKICDSDP VQMENTRCYL PDAYKIMSLR CNNRTQCAVV AGPDVFPDPC PGTYKYLEVQ
YECVPYKVEQ KVFLCPGILR GVYQSEHLFE SDHQSGAWCK DPLQASDKIY YMPWTPYRTD
TLTEYSSKED FIAGRPTTTY KLPHRVDGTG FVVYDGALFF NKERTRNIVK FDLRTRIKSG
EAIIANANYH DTSPYRWGGK SDIDLAVDEN GLWVIYATEQ NNGRIVVSQL NPYTLRIEGS
WDTSYDKRSA SNAFMICGVL YVVKTVYEDD DNEGTGNKID YMYNTDKGKE MTVNIPFPNS
YQYIAAVDYN PRDNLLYVWN NYHVVKYSLD FGNNDFRPPP IIPPNRGGGP IGGGGSSSST
SRAATTTRSP PSYTTPRPLL TTSPGQRYRT TTTVRQPILV PPGGSSSDSN QIPDTNQKVG
GRSPPVQVPP APPQPPILPP QDFCNPVVTA DISWPRTQQG QTAKQPCPVG TLGVATYMCV
AHLGHWDTQG PDLSNCTSPW VNHIMQKLRS GETAAIVARE LAEQTKGLLH PGDVPSTVRA
MVQLVELLDV QLRNLTPGGK DSAARSLTKL QKRERSCRFF AQAMVETVNN LLHPRAEKAW
RELPTSEQLH SATLLLDTVE TGAFMLADNL LKTDTVQETN DYILLEVARL STDGNLADLT
FPQSEQHGNS IQLSASTLKQ HGRNGEIRMV FVMYKNLGSY LSTENASVRL SSDAIYPNYS
VIVNSPVITA SINKESNKVY LSEPVVFTVK HLQHSEKNFN PNCSFWSYSK RTMTGFWSTQ
DCRLLATNRT HTSCSCTHLT SFAVLMAHVE VKKTDSMHDV LLDVITWVGI LLSLVCLLIC
IFTFCFFRGL QSDRNTIHKN LCISLFIAES LFLYGINKAD QPIVCAVFAA LLHFFFLAAF
TWMFLEGVQL YIMLVEVFES EHSRTKYFYL AGYGVPAVIV AVSAAVDYRS YGTDRVCWLR
LDTYFIWSFI GPATLIIMLN VIFLGIALYK MFHHTAILKP DSGCLDNIKS WVIGAIALLC
LLGLTWAFGL MYINESTVIM AYLFTIFNSL QGMFIFIFHC ILQKKVRKEY GKCLRTHCCS
GKSVETSISS SSKTTTSRTP GRYSTGSQSR IRRMWNDTVR KQESSFITGD INSSATLNRV
YNNPAVGMYN TQAPYRDTKG ILNNARDSSV MDTLPLNGNH ANNYSMASSE YLSDCVQILD
RSAGYGTHGN HKETTLEKKI LKELTSNYIP SYLNNHERAT TERNHNLMNK LVNSSMANGG
SLAGGSSSSS SSGVGGCVGG SKEDNGPMVL DNSVAFPHEE NLGLEIIREE SNAPLLPPRP
PPPDSHPPPP PPPHSFSRPR RIPQETSESF FPLLTNEHTD EHTHSPNHRD SLYTSMPVLT
DLPDGQMNGL TDGEEDSSGE LQPCKSATAP ELDDVYYKSM PNLGSRNHLH ELQSYYHMGR
GGSDGYMVSG SKDESDSSPE EPPVDPSHLV TSL
//
