ID A0A384A475_BALAS Unreviewed; 1467 AA.
AC A0A384A475;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Adhesion G protein-coupled receptor L1 {ECO:0000313|RefSeq:XP_007182123.1};
GN Name=ADGRL1 {ECO:0000313|RefSeq:XP_007182123.1};
OS Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS (Balaenoptera davidsoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC Balaenopteridae; Balaenoptera.
OX NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_007182123.1};
RN [1] {ECO:0000313|RefSeq:XP_007182123.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_007182123.1};
RG RefSeq;
RL Submitted (JAN-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_007182123.1; XM_007182061.1.
DR STRING; 310752.A0A384A475; -.
DR KEGG; bacu:102999459; -.
DR CTD; 22859; -.
DR InParanoid; A0A384A475; -.
DR OrthoDB; 1114672at2759; -.
DR Proteomes; UP000261681; 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_007182123.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000261681};
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..1467
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016863323"
FT TRANSMEM 851..878
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 890..907
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 922..946
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 958..977
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 997..1020
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1041..1064
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1070..1093
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 134..393
FT /note="Olfactomedin-like"
FT /evidence="ECO:0000259|PROSITE:PS51132"
FT DOMAIN 472..531
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 853..1094
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 395..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1245..1265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1285..1321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1353..1422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1444..1467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..464
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1294..1308
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1353..1371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1397..1417
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 135..317
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00446"
SQ SEQUENCE 1467 AA; 161579 MW; 534EDDE9417D5EB4 CRC64;
MARLAAVLWS LCVTAVLVTS ATQGLSRAGL PFGLMRRELA CEGYPIELRC PGSDVIMVEN
ANYGRTDDKI CDADPFQMEN VQCYLPDAFK IMSQRCNNRT QCVVVAGSDA FPDPCPGTYK
YLEVQYDCVP YIFVCPGTLQ KVLDPTSTHE SEHQSGAWCK DPLQAGDRIY VMPWIPYRTD
TLTEYASWED YVAARHTTTY RLPNRVDGTG FVVYDGAVFY NKERTRNIVK YDLRTRIKSG
ETVINTANYH DTSPYRWGGK TDIDLAVDEN GLWVIYATEG NNGRLVVSQL NPYTLRFEGT
WETGYDKRSA SNAFMVCGVL YVLRSVYVDD DSEAAGNRVD YAFNTNANRE EPVSLAFPNP
YQFVSSVDYN PRDNQLYVWN NYFVVRYSLE FGPPDPSAGP ATSPPLSTTT TARPTPLTST
ASPVATTPPP RAPLTTHPVG AINQLGPDLP PATAPAPSTR RPPAPNLHVS PELFCEPREV
RRVQWPATQQ GMLVERPCPK GTRGIASFQC LPALGLWNPR GPDLSNCTSP WVNQVAQKIK
SGENAANIAS ELARHTRGSI YAGDVSSSVK LMEQLLDILD AQLQALRPIE RESAGKNYNK
MHKRERTCKD YIKAVVETVD NLLRPEALES WKDMNATEQV HTATMLLDVL EEGAFLLADN
VREPARFLAA KQNVVLEVTV LNTEGQVQEL VFPQEYPSEN SIQLSANTIK QNSRNGVVKV
VFILYNNLGL FLSTENATVK LAEAGAGGLG GASLVVNSQV IAASINKESS RVFLMDPVIF
TVAHLEAKNH FNANCSFWNY SERSMLGYWS TQGCRLVESN KTHTTCACSH LTNFAVLMAH
REIYQGRINE LLLSVITWVG IVISLVCLAI CISTFCFLRG LQTDRNTIHK NLCINLFLAE
LLFLVGIDKT QYEIACPIFA GLLHYFFLAA FSWLCLEGVH LYLLLVEVFE SEYSRTKYYY
LGGYCFPALV VGIAAAIDYR SYGTEKACWL RVDNYFIWSF IGPVSFVIVV NLVFLMVTLH
KMIRSSSVLK PDSSRLDNIK SWALGAIALL FLLGLTWAFG LLFINKESVV MAYLFTTFNA
FQGVFIFVFH CALQKKVHKE YSKCLRHSYC CIRSPPGGAH GSLKTSAMRS NTRYYTGTQS
RIRRMWNDTV RKQTESSFMA GDINSTPTLN RGTMGNHLLT NPVLQPRGGT SPYNTLIAES
VGFNPSSPAV FNSPGSYREP KHPLGGREAC GMDTLPLNGN FNNSYSLRSG DFPPGDGAPE
PPRGRNLADA AAFEKMIISE LVHNNLRGGS SGAKGPPPPE PPVPPVPGGS GEEEAGGPGG
ADRAEIELLY KALEEPLLLP RAQSVLYQSD LDESESCTAE DGATSRPLSS PPGRDSLYAS
GANLRDSPSY PDSSPEGPSE ALPPPPPAPP GPPEIYYTSR PPALVARNPL QGYYQVRRPS
HEGYLAAPGL EGPGPDGDGQ MQLVTSL
//
