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Database: UniProt
Entry: A0A286XVD5_CAVPO
LinkDB: A0A286XVD5_CAVPO
Original site: A0A286XVD5_CAVPO 
ID   A0A286XVD5_CAVPO        Unreviewed;      1413 AA.
AC   A0A286XVD5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Adhesion G protein-coupled receptor L2 {ECO:0000313|Ensembl:ENSCPOP00000029435.1};
GN   Name=ADGRL2 {ECO:0000313|Ensembl:ENSCPOP00000029435.1};
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000029435.1, ECO:0000313|Proteomes:UP000005447};
RN   [1] {ECO:0000313|Proteomes:UP000005447}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSCPOP00000029435.1}
RP   IDENTIFICATION.
RC   STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000029435.1};
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; AAKN02004917; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAKN02004918; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAKN02004919; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAKN02004920; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_012998372.1; XM_013142918.1.
DR   Ensembl; ENSCPOT00000044787.1; ENSCPOP00000029435.1; ENSCPOG00000002947.4.
DR   GeneID; 100713240; -.
DR   CTD; 23266; -.
DR   VEuPathDB; HostDB:ENSCPOG00000002947; -.
DR   GeneTree; ENSGT00940000156348; -.
DR   OrthoDB; 1114672at2759; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   Bgee; ENSCPOG00000002947; Expressed in heart left ventricle and 11 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; cd16006; 7tmB2_Latrophilin-2; 1.
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; 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   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:UP000005447};
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..1413
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011648564"
FT   TRANSMEM        845..872
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        884..901
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        913..940
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        952..971
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        991..1014
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1035..1058
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1064..1087
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..1088
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   REGION          1316..1357
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1316..1338
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        136..318
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00446"
SQ   SEQUENCE   1413 AA;  158449 MW;  6D5C5E8D4B263E99 CRC64;
     MVSSGCRMRS LWFIIVISFL QNTEGFSRAA LPFGLVRREL SCEGYSIDLR CPGSDVIMIE
     SANYGRTDDK ICDADPFQME NTDCYLPDAF KIMTQRCNNR TQCIVVTGSD VFPDPCPGTY
     KYLEVQYECV PYIFVCPGTL KAIVDSPCIY EAEQKAGAWC KDPLQAADKI YFMPWTPYRT
     DTLIEYASIE DFQNSRQTTT YKLPNRVDGT GFVVYDGAVF FNKERTRNIV KFDLRTRIKS
     GEAIINYANY HDTSPYRWGG KTDIDLAVDE NGLWVIYATE QNNGMIVISQ LNPYTLRFEA
     TWETVYDKRA ASNAFMICGV LYVVRSVYQD NESETGKNAI DYIYNTRLNR GEYVDVPFPN
     QYQYIAAVDY NPRDNQLYVW NNNFILRYSL EFGPPDPAQV PTTAVTITSS AELFKTTVST
     TSTTSQKGPL STTVAGSQEG SKGTKPPPAV STTKIPPVTN IFPLPERFCE ALEARGIKWP
     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 IGRNSTIAVN SHVISVSINK ESSRVYLTDP VLFTLPHIDP
     DNYFNANCSF WNYSERTMMG YWSTQGCKLV DTNKTRTTCA CSHLTNFAIL MAHREIAYKD
     GVHQLLLTVI TWVGIVISLV CLAICIFTFC FFRGLQSDRN TIHKNLCINL FIAEFIFLIG
     IDKTKYTIAC PIFAGLLHFF FLAAFAWMCL EGVQLYLMLV EVFESEYSRK KYYYVAGYLF
     PATVVGISAA IDYKSYGTKT ACWLHVDNYF IWSFIGPVTF IILLNIIFLV ITLCKMVKHS
     NTLKPDSSRL ENIKSWVLGA FALLCLLGLT WSFGLLFVNE ETIVMAYLFT IFNAFQGVFI
     FIFHCALQKK VRKEYGKCFR HSYCCGSLPT ESPHSSVKAS TTRTSARYSS GTQSRIRRMW
     NDTVRKQSES SFISGDINST STLNQGHSLN NARDTSAMDT LPLNGNFNNS YSLRKGDYSD
     SVQVVDCGLS LNDTAFEKMI ISELVHNNLR GGGKTHNLEL TLPVKPVIGG GGSEEDALVA
     DASSLMHGDN PGLELHHKEL EAPLIPQRTH SLLYQPQKKV KPEGTDSYVS QLTAEAEDHL
     QSPNRDSLYT SMPNLRDSPY PESSPDMEED LSPSRRSENE DIYYKSMPNL GSGHHQLQMC
     YQISRGNSDG YIIPINKEGC IPEGMLEKGR CSW
//
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