ID A0A2Y9MAT9_DELLE Unreviewed; 1468 AA.
AC A0A2Y9MAT9;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Adhesion G protein-coupled receptor L1 isoform X4 {ECO:0000313|RefSeq:XP_022414543.1};
GN Name=ADGRL1 {ECO:0000313|RefSeq:XP_022414543.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022414543.1};
RN [1] {ECO:0000313|RefSeq:XP_022414543.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022414543.1};
RG RefSeq;
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 RefSeq; XP_022414543.1; XM_022558835.2.
DR Proteomes; UP000248483; 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 ECO:0000313|RefSeq:XP_022414543.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000248483};
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..1468
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016126903"
FT TRANSMEM 858..885
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 897..914
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 929..953
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 965..984
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1004..1027
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1048..1071
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1077..1100
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 140..399
FT /note="Olfactomedin-like"
FT /evidence="ECO:0000259|PROSITE:PS51132"
FT DOMAIN 478..537
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 860..1101
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 401..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1246..1266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1286..1322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1354..1423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1445..1468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1295..1309
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1354..1372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1398..1418
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 141..323
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00446"
SQ SEQUENCE 1468 AA; 161717 MW; C97B80554D0E0E06 CRC64;
MARLAAVLWS LCVTAVLVTS ATQGLSRAGL PFGLMRRELA CEGYPIELRC PGSDVIMVEN
ANYGRTDDKI CDADPFQMEN VQCYLPDAFK IMSQRCNNRT QCVVVAGSDA FPDPCPGTYK
YLEVQYDCVP YIEVEQKVFV CPGTLQKVLD PTSTHESEHQ SGAWCKDPLQ AGDRIYVMPW
IPYRTDTLTE YASWEDYVAA RHTTTYRLPN RVDGTGFVVY DGAVFYNKER TRNIVKYDLR
TRIKSGETVI NTANYHDTSP YRWGGKTDID LAVDENGLWV IYATEGNNGR LVVSQLNPYT
LRFEGTWETG YDKRSASNAF MVCGVLYVLR SVYVDDDSEA AGNRVDYAFN TNANREEPVS
LAFPNPYQFV SSVDYNPRDN QLYVWNNYFV VRYSLEFGPP DPSAGPATSP PLSTTTTARP
TPLTSTASPA ATTPLRRAPL TTHPVGAINQ LGPDLPPATA PAPSTRRPPA PNLHVSPELF
CEPREVRRVQ WPATQQGMLV ERPCPKGTRG IASFQCLPAL GLWNPRGPDL SNCTSPWVNQ
VAQKIKSGEN AANIASELAR HTRGSIYAGD VSSSVKLMEQ LLDILDAQLQ ALRPIERESA
GKNYNKMHKR ERTCKDYIKA VVETVDNLLR PEALESWKDM NATEQVHTAT MLLDVLEEGA
FLLADNVREP ARFLAAKQNV VLEVTVLNTE GQVQELVFPQ EYPSENSIQL SANTIKQNSR
NGVVKVVFIL YNNLGLFLST ENATVKLAGE AGAGGLGGAS LVVNSQVIAA SINKESSRVF
LMDPVIFTVA HLEAKNHFNA NCSFWNYSER SMLGYWSTQG CRLVESNKTH TTCACSHLTN
FAVLMAHREI YQGRINELLL SVITWVGIVI SLVCLAICIS TFCFLRGLQT DRNTIHKNLC
INLFLAELLF LVGIDKTQYE IACPIFAGLL HYFFLAAFSW LCLEGVHLYL LLVEVFESEY
SRTKYYYLGG YCFPALVVGI AAAIDYRSYG TEKACWLRVD NYFIWSFIGP VSFVIVVNLV
FLMVTLHKMI RSSSVLKPDS SRLDNIKSWA LGAIALLFLL GLTWAFGLLF INKESVVMAY
LFTTFNAFQG VFIFVFHCAL QKKVHKEYSK CLRHSYCCIR SPPGGAHGSL KTSAIRSNTR
YYTGTQSRIR RMWNDTVRKQ TESSFMAGDI NSTPTLNRGT MGNHLLTNPV LQPRGGTSPY
NTLIAESVGF NPSSPAVFNS PEHPLGGREA CGMDTLPLNG NFNNSYSLRS GDFPPGDGAP
EPPRGRNLAD AAAFEKMIIS ELVHNNLRGG SSGARGPPPP EPPVPPVPGG SGEEEAGGPG
GADRAEIELL YKALEEPLLL PRAQSVLYQS DLDESESCTA EDGATSRPLS SPPGRDSLYA
SGANLRDSPS YPDSSPEGPS EALPPPPPAP PGPPEIYYTS RPPALVARNP LQGYYQVRRP
SHEGYLAAPG LEGPGPDGDG QMQLVTSL
//
