ID A0A2I2Y2R6_GORGO Unreviewed; 1681 AA.
AC A0A2I2Y2R6;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Adhesion G protein-coupled receptor L1 {ECO:0000313|Ensembl:ENSGGOP00000029196.1};
GN Name=ADGRL1 {ECO:0000313|Ensembl:ENSGGOP00000029196.1};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000029196.1, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000029196.1, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scally A.;
RT "Insights into the evolution of the great apes provided by the gorilla
RT genome.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGGOP00000029196.1, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000029196.1}
RP IDENTIFICATION.
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; CABD030111922; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030111923; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030111924; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030111925; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_018870036.1; XM_019014491.1.
DR STRING; 9593.ENSGGOP00000029196; -.
DR Ensembl; ENSGGOT00000059293.1; ENSGGOP00000029196.1; ENSGGOG00000015214.3.
DR GeneTree; ENSGT00940000159684; -.
DR InParanoid; A0A2I2Y2R6; -.
DR OMA; EQSPPWA; -.
DR Proteomes; UP000001519; Chromosome 19.
DR Bgee; ENSGGOG00000015214; Expressed in frontal cortex and 6 other cell types or tissues.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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 GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd16007; 7tmB2_Latrophilin-1; 1.
DR CDD; cd22844; Gal_Rha_Lectin_LPHN1; 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; IPR031234; Latrophilin-1_TM.
DR InterPro; IPR000922; Lectin_gal-bd_dom.
DR InterPro; IPR043159; Lectin_gal-bd_sf.
DR InterPro; IPR003112; Olfac-like_dom.
DR PANTHER; PTHR12011:SF62; ADHESION G PROTEIN-COUPLED RECEPTOR L1; 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 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:UP000001519};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
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 TRANSMEM 1065..1092
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1104..1121
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1136..1160
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1172..1191
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1211..1234
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1255..1278
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1284..1307
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 247..336
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50228"
FT DOMAIN 346..605
FT /note="Olfactomedin-like"
FT /evidence="ECO:0000259|PROSITE:PS51132"
FT DOMAIN 684..743
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 1067..1308
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 90..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 607..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1455..1480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1501..1535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1567..1636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1658..1681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..638
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1508..1522
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1567..1585
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1611..1631
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 347..529
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00446"
SQ SEQUENCE 1681 AA; 183693 MW; 9A3E0B1444671C99 CRC64;
MGIPRRKVGG WKRGAPWEQG VRSAGTDLGS AGHAARGRVC VRARTPWFPE PSCSRGLHCG
CAAEGLVSQG SGLIAFPSQR PWIQKPLLPV RSGAASTPNP VGGGERRRKE GKSSPGFRAG
SWGAQAGCGG QSRAATPGRV LRAPTAPLPE RVRRGAGRAS GLSLLVPGAG SLVGGGAGPG
EGRDTEAALA PLPPTRFPPA PAPGDVPGGG PGFAEPQERH AGPTPERRWT GLSRAGLPFG
LMRRELACEG YPIELRCPGS DVIMVENANY GRTDDKICDA DPFQMENVQC YLPDAFKIMS
QRCNNRTQCV VVAGSDAFPD PCPGTYKYLE VQYDCVPYKV EQKVFVCPGT LQKVLEPTST
HESEHQSGAW CKDPLQAGDR IYVMPWIPYR TDTLTEYASW EDYVAARHTT TYRLPNRVDG
TGFVVYDGAV FYNKERTRNI VKYDLRTRIK SGETVINTAN YHDTSPYRWG GKTDIDLAVD
ENGLWVIYAT EGNNGRLVVS QLNPYTLRFE GTWETGYDKR SASNAFMVCG VLYVLRSVYV
DDDSEAAGNR VDYAFNTNAN REEPVSLTFP NPYQFISSVD YNPRDNQLYV WNNYFVVRYS
LEFGPPDPSA GPATSPPLST TTTARPTPLT STASPAATTP LRRAPLTTHP VGAINQLGPD
LPPATAPVPS TRRPPAPNLH VSPELFCEPR EVRRVQWPAT QQGMLVERPC PKGTRGIASF
QCLPALGLWN PRGPDLSNCT SPWVNQVAQK IKSGENAANI ASELARHTRG SIYAGDVSSS
VKLMEQLLDI LDAQLQALRP IERESAGKNY NKMHKRERTC KDYIKAVVET VDNLLRPEAL
ESWKDMNATE QVHTATMLLD VLEEGAFLLA DNVREPARFL AAKENVVLEV TVLNTEGQVQ
ELVFPQEEYP RKNSIQLSAK TIKQNSRNGV VKVVFILYNN LGLFLSTENA TVKLAGEAGP
GGPGGASLVV NSQVIAASIN KESSRVFLMD PVIFTVAHLE DKNHFNANCS FWNYSERSML
GYWSTQGCRL VESNKTHTTC ACSHLTNFAV LMAHREIYQG RINELLLSVI TWVGIVISLV
CLAICISTFC FLRGLQTDRN TIHKNLCINL FLAELLFLVG IDKTQYEIAC PIFAGLLHYF
FLAAFSWLCL EGVHLYLLLV EVFESEYSRT KYYYLGGYCF PALVVGIAAA IDYRSYGTEK
ACWLRVDNYF IWSFIGPVSF VIVVNLVFLM VTLHKMIRSS SVLKPDSSRL DNIKSWALGA
IALLFLLGLT WAFGLLFINK ESVVMAYLFT TFNAFQGVFI FVFHCALQKK VHKEYSKCLR
HSYCCIRSPP GGTHGSLKTS AMRSNTRYYT GTQSRIRRMW NDTVRKQTES SFMAGDINST
PTLNRGTMGN HLLTNPVLQP RGGTSPYNTL IAESVGFNPS SPPVFNSPGS YREPKHPLGG
REACGMDTLP LNGNFNNSYS LRSGDFPPGD GGPEPPRGRN LADAAAFEKM IISELVHNNL
RGSSSAAKGP PPPEPPVPPV PGGGGEEEAG GPGGADRAEI ELLYKALEEP LLLPRAQSVL
YQSDLDESES CTAEDGATSR PLSSPPGRDS LYASGANLRD SPSYPDSSPE GPSEALPPPP
PAPPGPPEIY YTSRPPALVA RNPLQGYYQV RRPSHEGYLA APGLEGPGPD GDGQMQLVTS
L
//
