ID A0A2I3FZ28_NOMLE Unreviewed; 1569 AA.
AC A0A2I3FZ28;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Adhesion G protein-coupled receptor L3 {ECO:0000313|Ensembl:ENSNLEP00000025704.1};
GN Name=ADGRL3 {ECO:0000313|Ensembl:ENSNLEP00000025704.1};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000025704.1, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000025704.1, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000025704.1}
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 EMBL; ADFV01043876; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01043877; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01043878; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01043879; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01043880; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01043881; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01043882; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01043883; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01043884; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01043885; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 61853.ENSNLEP00000025704; -.
DR Ensembl; ENSNLET00000050478.1; ENSNLEP00000025704.1; ENSNLEG00000008957.3.
DR GeneTree; ENSGT00940000155527; -.
DR InParanoid; A0A2I3FZ28; -.
DR OMA; XEIRVAF; -.
DR Proteomes; UP000001073; Chromosome 9.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
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 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 Reference proteome {ECO:0000313|Proteomes:UP000001073};
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..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1569
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014138135"
FT TRANSMEM 943..966
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1002..1024
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1045..1065
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1085..1104
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1132..1154
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1160..1183
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 101..190
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50228"
FT DOMAIN 195..454
FT /note="Olfactomedin-like"
FT /evidence="ECO:0000259|PROSITE:PS51132"
FT DOMAIN 562..618
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 941..1184
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 54..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 487..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1202..1227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1545..1569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..537
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 196..378
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00446"
SQ SEQUENCE 1569 AA; 174986 MW; 4D6E528C58C79A6D CRC64;
MWPSQLLIFM MLLAPIIHGG KHSERHPALA APLRHAERSP GGALPLRHLL QQPAAERTAA
HRGQGPRGAT RGVRGPGAKE HRLQPFSRAP IPMAVVRREL SCESYPIELR CPGTDVIMIE
SANYGRTDDK ICDSDPAQME NIRCYLPDAY KIMSQRCNNR TQCAVVAGPD VFPDPCPGTY
KYLEVQYECV PYIFLCPGLL KGVYQSEHLF ESDHQSGAWC KDPLQASDKI YYMPWTPYRT
DTLTEYSSKD DFIAGRPTTT YKLPHRVDGT GFVVYDGALF FNKERTRNIV KFDLRTRIKS
GEAIIANANY HDTSPYRWGG KSDIDLAVDE NGLWVIYATE QNNGKIVISQ LNPYTLRIEG
TWDTAYDKRS ASNAFMICGI LYVVKSVYED DDNEATGNKI DYIYNTDQSK DSLVDVPFPN
SYQYIAAVDY NPRDNLLYVW NNYHVVKYSL DFGPLDSRSG QAHHGQVSYI SPPVHLDSEL
ERPSVKGDSN VVEFGPLGMG STTTSTTLRT TTLSPGRSTT PSASGRRNRS TSTPSPAVEV
LDDMTTHLPS ASSQIPALEE SCEAVEAREI MWFKTRQGQI AKQPCPAGTI GVSTYLCLAP
DGIWDPQGPD LSNCSSPWVN HITQKLKSGE TAANIARELA EQTRNHLNAG DITYSVRAMD
QLVGLLDVQL RNLTPGGKDS AARSLNKLQK RERSCRAYVQ AMVETVNNLL QPQALNAWRD
LTTSDQLRAA TMLLHTVEES AFVLADNLLK TDIVRENTDN IKLEVARLST EGNLEDLKFP
ENMGHGSTIQ LSANTLKQNG RNGEIRVAFV LYNNLGPYLS TENASMKLGT EALSTNHSVI
VNSPVITAAI NKEFSNKVYL ADPVVFTVKH IKQSEENFNP NCSFWSYSKR TMTGYWSTQG
CRLLTTNKTH TTCSCNHLTN FAVLMAHVEV KHSDAVHDLL LDVITWVGIL LSLVCLLICI
FTFCFFRGLQ SDRNTIHKNL CISLFVAELL FLIGINRTDQ PIACAVFAAL LHFFFLAAFT
WMFLEGVQLY IMLVEVFESE HSRRKYFYLV GYGMPALIVA VSAAVDYRSY GTDKCWIFLE
AKQMCIIRSM LNVIFLGIAL YKMFHHTAIL KPESGCLDNI NYEDNRPFIK SWVIGAIALL
CLLGLTWAFG LMYINESTVI MAYLFTIFNS LQGMFIFIFH CVLQKKVRKE YGKCLRTHCC
NGSSTESSIG SGKTSGSRTP GRYSTGSQSR IRRMWNDTVR KQSESSFITG DINSSASLNR
GAMANHLISN ALLRPHGTNN PYNTLLGEPA VCNNPSVSMY NAQEGLLNNA RDTSVMDTLP
LNGNHGNSYS IASGEYLSNC VQIIDRGYNH NETALEKKIL KELTSSYIPS YLNNHERSSE
QNRNLMNKLV NNLGSGREDD AIVLDDATSF NHEESLGLEL IHEESDAPLL PPRVYSTENH
QPHHYTRRRI PQDHSESFFP LLTNEHTEDL QSPHRDSLYT SMPTLAGVAA TESVTTSTQT
EPPPAKCGDA EDVYYKSMPN LGSRNHVHQL HTYYQLGRGS SDGFIVPPNK DGTPPEGSSK
GPAHLVTSL
//