ID A0A2K6ULX8_SAIBB Unreviewed; 1177 AA.
AC A0A2K6ULX8;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Adhesion G protein-coupled receptor L2 {ECO:0000313|Ensembl:ENSSBOP00000032910.1};
GN Name=ADGRL2 {ECO:0000313|Ensembl:ENSSBOP00000032910.1};
OS Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Saimiriinae; Saimiri.
OX NCBI_TaxID=39432 {ECO:0000313|Ensembl:ENSSBOP00000032910.1, ECO:0000313|Proteomes:UP000233220};
RN [1] {ECO:0000313|Ensembl:ENSSBOP00000032910.1}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A2K6ULX8; -.
DR Ensembl; ENSSBOT00000049818.1; ENSSBOP00000032910.1; ENSSBOG00000032564.1.
DR GeneTree; ENSGT00940000156348; -.
DR Proteomes; UP000233220; 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; 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; 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:UP000233220};
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..1177
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014414753"
FT TRANSMEM 832..857
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 869..887
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 893..917
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 938..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 417..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1100..1119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 136..318
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00446"
SQ SEQUENCE 1177 AA; 132157 MW; F6E6EC5B514FBFA0 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 AELFKTTAST
TSTTSQKGPM STTVAGSQEG SKGTKPPPAL STTKIPPVTN IFPLPERFCE ALDSRGIKWP
QTQRGVMVER PCPKGTRGTA SYLCMVSTGT WNPKGPDLSN CTSHWVNQLA QKIRSGENAA
SLANELAKHT KGPVFAGDVS SSVRLMEQLV DILDAQLQEL KPSEKDSAGR SYNKAIVDTV
DNLLRPEALE SWKHMNSSEQ AHTATMLLDT LEEGAFVLAD NLLEPTRVSM PTENIVLEVA
VLSTEGQIQD FKFPLGIKGA GSSIQLSANT VKQNSRNGLA KLVFIIYRSL GQFLSTENAT
IKLGADFIGR NSTIAVNSHV ISVSINKESS RVYLTDPVLF TLPHIDPDNY FNANCSFWNY
SERTMMGYWS TQGCKLVDTN KTRTTCACSH LTNFAILMAH REIAYKDGVH ELLLTVITWV
GIVISLVCLA ICIFTFCFFR GLQSDRNTIH KNLCINLFIA EFIFLIGIDK TKYAIACPIF
AGLLHFFFLA AFAWMCLEGV QLYLMLVEVF ESEYSRKKYY YVAGYLFPAT VVGVSAAIDY
KSYGTEKACW LHVDNYFIWS FIGPVTFIIL LNIIFLVITL CKMVKHSNTL KPDSSRLENI
KSWVLGAFAL LCLLGLTWSF GLLFINEETI VMAYLFTIFN AFQGVFIFIF HCALQKKVRK
EYGKCFRHSY CCGGLPTESP HSSVKASTTR TSARYSSGTQ SRIRRMWNDT VRKQSESSFI
SGDINSTSTL NQGLTSHGLR AHLQDLYHLE LLLGQIA
//
