ID A0A2R8MIU3_CALJA Unreviewed; 1534 AA.
AC A0A2R8MIU3;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 3.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Adhesion G protein-coupled receptor L3 {ECO:0000313|Ensembl:ENSCJAP00000060530.3};
GN Name=ADGRL3 {ECO:0000313|Ensembl:ENSCJAP00000060530.3};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000060530.3, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000060530.3}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCJAP00000060530.3}
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 Ensembl; ENSCJAT00000084280.3; ENSCJAP00000060530.3; ENSCJAG00000020576.6.
DR GeneTree; ENSGT00940000155527; -.
DR OrthoDB; 1114672at2759; -.
DR Proteomes; UP000008225; Chromosome 3.
DR Bgee; ENSCJAG00000020576; Expressed in frontal cortex and 2 other cell types or tissues.
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; cd16005; 7tmB2_Latrophilin-3; 1.
DR CDD; cd22846; Gal_Rha_Lectin_LPHN3; 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; IPR000922; Lectin_gal-bd_dom.
DR InterPro; IPR043159; Lectin_gal-bd_sf.
DR InterPro; IPR003112; Olfac-like_dom.
DR PANTHER; PTHR12011:SF60; ADHESION G PROTEIN-COUPLED RECEPTOR L3; 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; 2.
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:UP000008225};
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..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1534
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5035213843"
FT TRANSMEM 942..965
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 977..995
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1001..1023
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1044..1064
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1093..1118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1139..1162
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1168..1191
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 103..192
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50228"
FT DOMAIN 197..456
FT /note="Olfactomedin-like"
FT /evidence="ECO:0000259|PROSITE:PS51132"
FT DOMAIN 561..617
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 940..1192
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 21..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 489..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1211..1234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1454..1473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1507..1534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..536
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1454..1469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 198..380
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00446"
SQ SEQUENCE 1534 AA; 171052 MW; 1F036613B0C6BBEB CRC64;
MWPSQLLIFM TLLAPIIHGG KHSERHPALP APLRHAERSP GGALPPRHLL QQPAAERTSA
HRGQGPRGAT RGVRGPGAQG AQIAAQAFSR APIPMAVVRR ELSCESYPIE LRCPGTDVIM
IESANYGRTD DKICDSDPAQ MENIRCYLPD AYKIMSQRCN NRTQCAVVAG PDVFPDPCPG
TYKYLEVQYE CVPYIFLCPG LLKGVYQSEH LFESDHQSGA WCKDPLQASD KIYYMPWTPY
RTDTLTEYSS KDDFIAGRPT TTYKLPHRVD GTGFVVYDGA LFFNKERTRN IVKFDLRTRI
KSGEAIIANA NYHDTSPYRW GGKSDIDLAV DENGLWVIYA TEQNNGKIVI SQLNPYTLRI
EGTWDTAYDK RSASNAFMIC GILYVVKSVY EDDDNEATGN KIDYIYNTDQ SKDSLVDVPF
PNSYQYIAAV DYNPRDNLLY VWNNYHVVKY SLDFGPLDSR SGQAHHGQVS YISPPIHLDS
ELERPSVKDI STTGPLGMGS TTTSTTLRTT TLGPGRSTTP SVSGRRNRST STPSPAVEVL
DDMTTHFPSA SSQIPALEES CEAVEAREIM WFKTRQGQIA KQPCPAGTIG VSTYLCLAPD
GIWDPQGPDL SNCSSPWVNH ITQKLKSGET AANIARELAE QTRNHLNAGD ITYSVRAMDQ
LVGLLDVQLR NLTPGGKDSA ARSLNKLQKR ERSCRAYVQA MVETVNNLLQ PQALNAWRDL
TTSDQLRAAT MLLHTVEESA FVLADNLLKT DIVRENTDNI KLEVARLSTE GNLEDLKFPE
NMGHGSTIQL SANTLKQNGR NGEIRVAFVL YDNLGPYLST ENASMKLGTE ALSTNHSVIV
NSPVITAAIN KEFSNKVYLA DPVVFTVKHI KQSEENFNPN CSFWSYSKRT MTGYWSTQGC
RLLTTNKTHT TCSCNHLTNF AVLMAHVEVK HSDAVHDLLL DVITWVGILL SLVCLLICIF
TFCFFRGLQS DRNTIHKNLC ISLFVAELLF LIGINRTDQP IACAVFAALL HFFFLAAFTW
MFLEGVQLYI MLVEVFESEH SRRKYFYLVG YGMPALIVAV SAAVDYRSYG TDKVFRGTCE
GLLYRCWLRL DTYFIWSFIG PATLIIMLNV IFLGIALYKM FHHTAILKPE SGCLDNIKSW
VIGAIALLCL LGLTWAFGLM YINESTVIMA YLFTIFNSLQ GMFIFIFHCV LQKKVRKEYG
KCLRTHCCSG KSTESSIGSG KTSGSRTPGR YSTGSQSRIR RMWNDTVRKQ SESSFITGDI
NSSASLNREG LLNNARDTSV MDTLPLNGNH GNSYSIASGE YLSNCVQIID RGYNHNETAL
EKKILKELTS NYIPSYLNNH ERSSEQNRNL MNKLVNNLGS GREDDAIVLD DATSFNHEES
LGLELIHEES DAPLLPPRVY STENHQLHHF TRRRIPQDHS ESFFPLLTNE HTEELQSPHR
DSLYTSMPTL AGAAATESVT TSTQTEPPSA KCGDAEDVYY KSMPNLGSRN HVHQLHTYYQ
LGRGSSDGFI VPPNKDGTPP EGSSKGPAHL VTSL
//