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Database: UniProt
Entry: A0A2K5TQ03_MACFA
LinkDB: A0A2K5TQ03_MACFA
Original site: A0A2K5TQ03_MACFA 
ID   A0A2K5TQ03_MACFA        Unreviewed;      1427 AA.
AC   A0A2K5TQ03;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 2.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Adhesion G protein-coupled receptor L2 {ECO:0000313|Ensembl:ENSMFAP00000002131.2};
GN   Name=ADGRL2 {ECO:0000313|Ensembl:ENSMFAP00000002131.2};
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000002131.2, ECO:0000313|Proteomes:UP000233100};
RN   [1] {ECO:0000313|Ensembl:ENSMFAP00000002131.2, ECO:0000313|Proteomes:UP000233100}
RP   NUCLEOTIDE SEQUENCE.
RA   Warren W., Wilson R.K.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSMFAP00000002131.2}
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   Ensembl; ENSMFAT00000027273.2; ENSMFAP00000002131.2; ENSMFAG00000035421.2.
DR   VEuPathDB; HostDB:ENSMFAG00000035421; -.
DR   GeneTree; ENSGT00940000156348; -.
DR   OrthoDB; 1114672at2759; -.
DR   Proteomes; UP000233100; Chromosome 1.
DR   Bgee; ENSMFAG00000035421; Expressed in lung and 13 other cell types or tissues.
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; 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; 2.
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; 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:UP000233100};
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..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..1427
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5030050415"
FT   TRANSMEM        845..872
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        906..939
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        959..982
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1003..1026
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1032..1055
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          41..130
FT                   /note="SUEL-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50228"
FT   DOMAIN          135..394
FT                   /note="Olfactomedin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51132"
FT   DOMAIN          468..525
FT                   /note="G-protein coupled receptors family 2 profile 1"
FT                   /evidence="ECO:0000259|PROSITE:PS50227"
FT   DOMAIN          847..1056
FT                   /note="G-protein coupled receptors family 2 profile 2"
FT                   /evidence="ECO:0000259|PROSITE:PS50261"
FT   REGION          419..456
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1326..1368
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1326..1349
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        136..318
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00446"
SQ   SEQUENCE   1427 AA;  159517 MW;  ED8AE123175930A1 CRC64;
     MVSSGCRMRS LWFIIVISFL PNTEGFSRAA LPFGLVRREL SCEGYSIDLR CPGSDVIMIE
     SANYGRTDDK ICDADPFQME NTDCYLPDAF KIMTQRCNNR TQCIVVTGSD VFPDPCPGTY
     KYLEVQYECV PYIFVCPGTL KAIVDSPCIY EAEQKAGAWC KDPLQAADKI YFMPWTPYRT
     DTLIEYASLE DFQNSRQTTT YKLPNRVDGT GFVVYDGAVF FNKERTRNIV KFDLRTRIKS
     GEAIINYANY HDTSPYRWGG KTDIDLAVDE NGLWVIYATE QNNGMIVISQ LNPYTLRFEA
     TWETVYDKRA ASNAFMICGV LYVVRSVYQD NESETGKNAI DYIYNTRLNR GEYVDVPFPN
     QYQYIAAVDY NPRDNQLYVW NNNFILRYSL EFGPPDPAQV PTTAVTITSS AELFKTTIST
     TSTTSQKGPM STTVAGSQEG SKGTKPPPAV STTKIPPVTN IFPLPERFCE ALDSKGIKWP
     QTQRGMMVER PCPKGTRGTA SYLCMVSTGT WNPKGPDLSN CTSHWVNQLA QKIRSGENAA
     SLANELAKHT KGPVFAGDVS SSVRLMEQLV DILDAQLQEL KPSEKDSAGR SYNKLQKREK
     TCRAYLKAIV DTVDNLLRPE ALESWKHMNS SEQAHTATML LDTLEEGAFV LADNLLEPTR
     VSMPTENIVL EVAVLSTEGQ IQDFKFPLGI KGAGSSIQLS ANTVKQNSRN GLAKLVFIIY
     RSLGQFLSTE NATIKLGADF LGRNSTIAVN SHVISVSINK ESSRVYLTDP VLFTLPHIDP
     DNYFNANCSF WNYSERTMMG YWSTQGCKLV DTNKTRTTCS CSHLTNFAIL MAHREIAYKD
     GVHELLLTVI TWVGIVISLV CLAICIFTFC FFRGLQSDRN TIHKNLCINL FIAEFIFLIG
     IDKTKYAIAC PIFAGLLHFF FLAAFAWMCL EVVGVSAAID YKSYGTEKAC WLHVDNYFIW
     SFIGPVTFII LLNIVFLVIT LCKMVKHSNT LKPDSSRLEN IKSWVLGAFA LLCLLGLTWS
     FGLLFINEET IVMAYLFTIF NAFQGVFIFI FHCALQKKVR KEYGKCFRHS YCCGGLPTES
     PHSSVKASTT RTSARYSSGT QSRIRRMWND TVRKQSESSF ISGDINSTST LNQGMTGNYL
     LTNPLLRPHG TNNPYNTLLA ETVVCNAPSA PVFNSPGHSL NNARDTSAMD TLPLNGNFNN
     SYSLRKGDYN DSVQVVDCGL SLNDTAFEKM IISELVHNNL RGSSKTHNLE LTLPVKPVIG
     GSSSEDDAIV ADASSLMHSD NPGLELHHKE LEAPLIPQRT HSLLYQPQKK VKSEGTDSYV
     SQLTAEAEDH LQSPNRDSLY TSMPNLRDSP YPESSPDMEE ELSPSRRSEN EDIYYKSMPN
     LGAGHQLQMC YQISRGNSDG YIIPINKEGC IPEGDVREGQ MQLVTSL
//
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