ID A0A2K5EQE5_AOTNA Unreviewed; 1499 AA.
AC A0A2K5EQE5;
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 L1 {ECO:0000313|Ensembl:ENSANAP00000035434.1};
GN Name=ADGRL1 {ECO:0000313|Ensembl:ENSANAP00000035434.1};
OS Aotus nancymaae (Ma's night monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC Aotus.
OX NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000035434.1, ECO:0000313|Proteomes:UP000233020};
RN [1] {ECO:0000313|Ensembl:ENSANAP00000035434.1}
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 Ensembl; ENSANAT00000053502.1; ENSANAP00000035434.1; ENSANAG00000034947.1.
DR GeneTree; ENSGT00940000159684; -.
DR Proteomes; UP000233020; 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; 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:UP000233020};
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..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1499
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014391438"
FT TRANSMEM 857..884
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 896..913
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 928..952
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 964..983
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1003..1026
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1047..1070
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1076..1099
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 40..129
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50228"
FT DOMAIN 138..397
FT /note="Olfactomedin-like"
FT /evidence="ECO:0000259|PROSITE:PS51132"
FT DOMAIN 476..535
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 859..1100
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 399..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1149..1169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1273..1298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1319..1353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1385..1454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1476..1499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1326..1340
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1385..1403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1429..1449
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 139..321
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00446"
SQ SEQUENCE 1499 AA; 165056 MW; DCA43F47FABA42A6 CRC64;
MARLAAVLWN LCVTAVLVTS ATQGLSRAGL PFGLMRRELA CEGYPIELRC PGSDVIMVEN
ANYGRTDDKI CDADPFQMEN VQCYLPDAFK IMSQRCNNRT QCVVVAGSDA FPDPCPGTYK
YLEVQYDCVP YSESSFFVCP GTLQKVLEPT STHESEHQSG AWCKDPLQAG DRIYVMPWIP
YRTDTLTEYA SWEDYVAARH TTTYRLPNRV DGTGFVVYDG AVFYNKERTR NIVKYDLRTR
IKSGETVINT ANYHDTSPYR WGGKTDIDLA VDENGLWVIY ATEGNNGRLV VSQLNPYTLR
FEGTWETGYD KRSASNAFMV CGVLYVLRSV YVDDDSEAAG NRVDYAFNTN ANREEPVSLA
FPNPYQFISS VDYNPRDNQL YVWNNYFVVR YSLEFGPPDP SAGPATSPPL STTTTARPTP
LTSTASPAAT TPLRRAPLTT HPVGAINQLG PDLPPATAPA PSTRRPPAPN LHVSPELFCE
PREVRRVQWP ATQQGMLVER PCPKGTRGIA SFQCLPALGL WNPRGPDLSN CTSPWVNQVA
QKIKSGENAA NIASELARHT RGSIYAGDVS SSVKLMEQLL DILDAQLQAL RPIERESAGK
NYNKMHKRER TCKDYIKAVV ETVDNLLRPE ALESWKDMNA TEQVHTATML LDVLEEGAFL
LADNVREPAR FLAAKENVVL EVTVLNTEGQ VQELVFPQEE YPRKNSIQLS AKTIKQNSRN
GVVKVVFILY NNLGLFLSTE NATVKLAGEA GPGGPGGASL VVNSQVIAAS INKESSRVFL
MDPVIFTVAH LEDKNHFNAN CSFWNYSERS MLGYWSTQGC RLVESNKTHT TCACSHLTNF
AVLMAHREIY QGRINELLLS VITWVGIVIS LVCLAICIST FCFLRGLQTD RNTIHKNLCI
NLFLAELLFL VGIDKTQYEI ACPIFAGLLH YFFLAAFSWL CLEGVHLYLL LVEVFESEYS
RTKYYYLGGY CFPALVVGIA AAIDYRSYGT EKACWLRVDN YFIWSFIGPV SFVIVVNLVF
LMVTLHKMIR SSSVLKPDSS RLDNIKSWAL GAIALLFLLG LTWAFGLLFI NKESVVMAYL
FTTFNAFQGV FIFVFHCALQ KKVHKEYSKC LRHSYCCIRS PPGGTHGSLK TSAMRSNTRY
YTGTQVSRQA GLPGQSQMPE GGWPKGPLTS GLCPQSRIRR MWNDTVRKQT ESSFMAGDIN
STPTLNRGTM GNHLLTNPVL QPRGGTSPYN TLIAESVGFN PSSPPVFNSP GEEHPLGGRE
ACGMDTLPLN GNFNNSYSLR SGDFPPGDGG PEPPRGRNLA DAAAFEKMII SELVHNNLRG
SSSVAKGPPP PEPPVPPVPG GGGEEEAGGP GGADRAEIEL LYKALEEPLL LPRAQSVLYQ
SDLDESESCT AEDGATSRPL SSPPGRDSLY ASGANLRDSP SYPDSSPEGP SEALPPPPPA
PPGPPEIYYT SRPPALVARN PLQGYYQVRR PSHEGYLAAP GLEGPGPDGD GQMQLVTSL
//
