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Database: UniProt
Entry: A0A2K6G668_PROCO
LinkDB: A0A2K6G668_PROCO
Original site: A0A2K6G668_PROCO 
ID   A0A2K6G668_PROCO        Unreviewed;      1151 AA.
AC   A0A2K6G668;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Adhesion G protein-coupled receptor L2 {ECO:0000313|Ensembl:ENSPCOP00000021715.1};
GN   Name=ADGRL2 {ECO:0000313|Ensembl:ENSPCOP00000021715.1};
OS   Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS   coquereli).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC   Indriidae; Propithecus.
OX   NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000021715.1, ECO:0000313|Proteomes:UP000233160};
RN   [1] {ECO:0000313|Ensembl:ENSPCOP00000021715.1}
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; A0A2K6G668; -.
DR   Ensembl; ENSPCOT00000032382.1; ENSPCOP00000021715.1; ENSPCOG00000022804.1.
DR   GeneTree; ENSGT00940000156348; -.
DR   Proteomes; UP000233160; Unplaced.
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; 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; 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; 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:UP000233160};
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..1151
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014419533"
FT   TRANSMEM        832..859
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        871..888
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        900..927
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        939..958
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        978..1001
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1022..1045
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1051..1074
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          834..1075
FT                   /note="G-protein coupled receptors family 2 profile 2"
FT                   /evidence="ECO:0000259|PROSITE:PS50261"
FT   REGION          418..456
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        136..318
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00446"
SQ   SEQUENCE   1151 AA;  129435 MW;  B3F61003F0A2CF2E CRC64;
     MVSSGCRMRS LWFVIIISFL 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 AELFKTTVST
     TSTTSQKGPM STTVAGSQEG SKGTKPPPAV STTKIPPVTN IFPLPERFCE ALDSRGIRWP
     QTQRGMMVER PCPKGTRGTA SYLCMVSTGT WNPKGPDLSN CTSHWVNQLA QKIRSGENAA
     SLANELAKHT KGPVFAGDVS SSVRLMEQLV DILDAQLQEL KPSEKDSAGR SYNKAIVDTV
     DNLLRPEALE SWKHMNSSEQ AHTATMLLDT LEEGAFVLAD NLLEPTRVSM PTENIVLEVA
     VLSTEGQVQD FKFPLGIKGA GSSIQLSANT VKQNSRNGLA KLVFIIYRSL GQFLSTENAT
     IKLGADFIGR NSTIAVNSHV ISVSINKESS RVYLTDPVLF TLPHIDPDNY FNANCSFWNY
     SERTMMGYWS TQGCKLVDTN KTRTTCACSH LTNFAILMAH REIVYKDGVH ELLLTVITWV
     GIVISLVCLA ICIFTFCFFR GLQSDRNTIH KNLCINLFIA EFIFLIGIDK TKYTIACPIF
     AGLLHFFFLA AFAWMCLEGV QLYLMLVEVF ESEYSRKKYY YVAGYLFPAT VVGVSAAIDY
     KSYGTEKACW LHVDNYFIWS FIGPVTFIIL LNIIFLVITL CKMVKHSNTL KPDSSRLENI
     KSWVLGAFAL LCLLGLTWSF GLLFINEETI VMAYLFTIFN AFQGVFIFIF HCALQKKVRK
     EYGKCFRHSY CCGGLPTESP HSSVKASTTR TSARYSSEIS NISAFDLHGH GVYGPVLYSR
     LCWFIRCCHC D
//
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