ID   E7EW95_HUMAN            Unreviewed;      1512 AA.
AC   E7EW95;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   05-DEC-2018, entry version 65.
DE   SubName: Full=Adhesion G protein-coupled receptor L3 {ECO:0000313|Ensembl:ENSP00000421627};
GN   Name=ADGRL3 {ECO:0000313|Ensembl:ENSP00000421627};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000421627, ECO:0000313|Proteomes:UP000005640};
RN   [1] {ECO:0000313|Ensembl:ENSP00000421627, ECO:0000313|Proteomes:UP000005640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA   Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA   Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA   Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA   Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA   Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA   Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA   Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA   Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA   Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA   Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA   Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA   Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA   Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA   Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA   Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA   Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA   Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA   McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA   Waterston R.H., Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2
RT   and 4.";
RL   Nature 434:724-731(2005).
RN   [2] {ECO:0000313|Ensembl:ENSP00000421627}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2011) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC       {ECO:0000256|SAAS:SAAS00547938}.
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DR   EMBL; AC020741; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC092643; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC092668; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC096723; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC104813; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC108161; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KF457762; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KF457763; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   ProteinModelPortal; E7EW95; -.
DR   PRIDE; E7EW95; -.
DR   Ensembl; ENST00000508946; ENSP00000421627; ENSG00000150471.
DR   UCSC; uc062wxz.1; human.
DR   EuPathDB; HostDB:ENSG00000150471.15; -.
DR   HGNC; HGNC:20974; ADGRL3.
DR   OpenTargets; ENSG00000150471; -.
DR   eggNOG; KOG3545; Eukaryota.
DR   eggNOG; KOG4193; Eukaryota.
DR   eggNOG; KOG4729; Eukaryota.
DR   eggNOG; ENOG410XSD2; LUCA.
DR   GeneTree; ENSGT00940000155527; -.
DR   ChiTaRS; ADGRL3; human.
DR   Proteomes; UP000005640; Chromosome 4.
DR   Bgee; ENSG00000150471; Expressed in 201 organ(s), highest expression level in adrenal tissue.
DR   ExpressionAtlas; E7EW95; baseline and differential.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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   Gene3D; 4.10.1240.10; -; 1.
DR   InterPro; IPR032471; GAIN_dom_N.
DR   InterPro; IPR017981; GPCR_2-like.
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; IPR015630; Latrophilin-3.
DR   InterPro; IPR000922; Lectin_gal-bd_dom.
DR   InterPro; IPR003112; Olfac-like_dom.
DR   PANTHER; PTHR12011:SF60; PTHR12011:SF60; 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   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   1: Evidence at protein level;
KW   Complete proteome {ECO:0000313|Proteomes:UP000005640};
KW   Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00446};
KW   G-protein coupled receptor {ECO:0000256|SAAS:SAAS00978998};
KW   Membrane {ECO:0000256|SAAS:SAAS00501090, ECO:0000256|SAM:Phobius};
KW   Proteomics identification {ECO:0000213|EPD:E7EW95,
KW   ECO:0000213|MaxQB:E7EW95, ECO:0000213|PeptideAtlas:E7EW95};
KW   Receptor {ECO:0000256|SAAS:SAAS00978998};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transducer {ECO:0000256|SAAS:SAAS00978998};
KW   Transmembrane {ECO:0000256|SAAS:SAAS00501090,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS00501090,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL        1     19       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        20   1512       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5003217581.
FT   TRANSMEM    879    902       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    914    932       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    938    960       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    981   1001       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1021   1044       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1075   1097       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1103   1126       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       35    124       SUEL-type lectin.
FT                                {ECO:0000259|PROSITE:PS50228}.
FT   DOMAIN      134    393       Olfactomedin-like.
FT                                {ECO:0000259|PROSITE:PS51132}.
FT   DOMAIN      498    554       G_PROTEIN_RECEP_F2_3.
FT                                {ECO:0000259|PROSITE:PS50227}.
FT   DOMAIN      815    866       GPS. {ECO:0000259|PROSITE:PS50221}.
FT   DOMAIN      877   1127       G_PROTEIN_RECEP_F2_4.
FT                                {ECO:0000259|PROSITE:PS50261}.
FT   DISULFID    135    317       {ECO:0000256|PROSITE-ProRule:PRU00446}.
SQ   SEQUENCE   1512 AA;  169129 MW;  62CEDF17EEB821CC CRC64;
     MWPSQLLIFM MLLAPIIHAF SRAPIPMAVV RRELSCESYP IELRCPGTDV IMIESANYGR
     TDDKICDSDP AQMENIRCYL PDAYKIMSQR CNNRTQCAVV AGPDVFPDPC PGTYKYLEVQ
     YECVPYKVEQ KVFLCPGLLK GVYQSEHLFE SDHQSGAWCK DPLQASDKIY YMPWTPYRTD
     TLTEYSSKDD FIAGRPTTTY KLPHRVDGTG FVVYDGALFF NKERTRNIVK FDLRTRIKSG
     EAIIANANYH DTSPYRWGGK SDIDLAVDEN GLWVIYATEQ NNGKIVISQL NPYTLRIEGT
     WDTAYDKRSA SNAFMICGIL YVVKSVYEDD DNEATGNKID YIYNTDQSKD SLVDVPFPNS
     YQYIAAVDYN PRDNLLYVWN NYHVVKYSLD FGPLDSRSGQ AHHGQVSYIS PPIHLDSELE
     RPSVKDISTT GPLGMGSTTT STTLRTTTLS PGRSTTPSVS GRRNRSTSTP SPAVEVLDDM
     TTHLPSASSQ IPALEESCEA VEAREIMWFK TRQGQIAKQP CPAGTIGVST YLCLAPDGIW
     DPQGPDLSNC SSPWVNHITQ KLKSGETAAN IARELAEQTR NHLNAGDITY SVRAMDQLVG
     LLDVQLRNLT PGGKDSAARS LNKLQKRERS CRAYVQAMVE TVNNLLQPQA LNAWRDLTTS
     DQLRAATMLL HTVEESAFVL ADNLLKTDIV RENTDNIKLE VARLSTEGNL EDLKFPENMG
     HGSTIQLSAN TLKQNGRNGE IRVAFVLYNN LGPYLSTENA SMKLGTEALS TNHSVIVNSP
     VITAAINKEF SNKVYLADPV VFTVKHIKQS EENFNPNCSF WSYSKRTMTG YWSTQGCRLL
     TTNKTHTTCS CNHLTNFAVL MAHVEVKHSD AVHDLLLDVI TWVGILLSLV CLLICIFTFC
     FFRGLQSDRN TIHKNLCISL FVAELLFLIG INRTDQPIAC AVFAALLHFF FLAAFTWMFL
     EGVQLYIMLV EVFESEHSRR KYFYLVGYGM PALIVAVSAA VDYRSYGTDK VCWLRLDTYF
     IWSFIGPATL IIMLNVIFLG IALYKMFHHT AILKPESGCL DNINYEDNRP FIKSWVIGAI
     ALLCLLGLTW AFGLMYINES TVIMAYLFTI FNSLQGMFIF IFHCVLQKKV RKEYGKCLRT
     HCCSGKSTES SIGSGKTSGS RTPGRYSTGS QSRIRRMWND TVRKQSESSF ITGDINSSAS
     LNRGAMANHL ISNALLRPHG TNNPYNTLLG EPAVCNNPSV SMYNAQEGLL NNARDTSVMD
     TLPLNGNHGN SYSIASGEYL SNCVQIIDRG YNHNETALEK KILKELTSNY IPSYLNNHER
     SSEQNRNLMN KLVNNLGSGR EDDAIVLDDA TSFNHEESLG LELIHEESDA PLLPPRVYST
     ENHQPHHYTR RRIPQDHSES FFPLLTNEHT EDLQSPHRDS LYTSMPTLAG VAATESVTTS
     TQTEPPPAKC GDAEDVYYKS MPNLGSRNHV HQLHTYYQLG RGSSDGFIVP PNKDGTPPEG
     SSKGPAHLVT SL
//