ID F7IQX8_CALJA Unreviewed; 1351 AA.
AC F7IQX8;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 2.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Adhesion G protein-coupled receptor L3 {ECO:0000313|Ensembl:ENSCJAP00000038246.3};
GN Name=ADGRL3 {ECO:0000313|Ensembl:ENSCJAP00000038246.3};
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:ENSCJAP00000038246.3, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000038246.3}
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:ENSCJAP00000038246.3}
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}.
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 RefSeq; XP_017826016.1; XM_017970527.1.
DR Ensembl; ENSCJAT00000040407.4; ENSCJAP00000038246.3; ENSCJAG00000020576.6.
DR GeneID; 100395781; -.
DR CTD; 23284; -.
DR GeneTree; ENSGT00940000155527; -.
DR HOGENOM; CLU_002753_0_0_1; -.
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; 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; 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: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..1351
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015327864"
FT TRANSMEM 947..970
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 982..1000
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1006..1028
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1049..1069
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1089..1112
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1143..1165
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1171..1194
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 202..461
FT /note="Olfactomedin-like"
FT /evidence="ECO:0000259|PROSITE:PS51132"
FT DOMAIN 566..622
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 945..1195
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 494..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1213..1238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..541
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 203..385
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00446"
SQ SEQUENCE 1351 AA; 150775 MW; 24A045DFB6A74FF8 CRC64;
MWPSQLLIFM TLLAPIIHGG KHSERHPALP APLRHAERSP GGALPPRHLL QQPAAERTSA
HRGQGPRGAT RGVRGPGAQG AQIAAQAFSR APIPMAVVRR ELSCESYPIE LRCPGTDVIM
IESANYGRTD DKICDSDPAQ MENIRCYLPD AYKIMSQRCN NRTQCAVVAG PDVFPDPCPG
TYKYLEVQYE CVPYKVEQKV FLCPGLLKGV YQSEHLFESD HQSGAWCKDP LQASDKIYYM
PWTPYRTDTL TEYSSKDDFI AGRPTTTYKL PHRVDGTGFV VYDGALFFNK ERTRNIVKFD
LRTRIKSGEA IIANANYHDT SPYRWGGKSD IDLAVDENGL WVIYATEQNN GKIVISQLNP
YTLRIEGTWD TAYDKRSASN AFMICGILYV VKSVYEDDDN EATGNKIDYI YNTDQSKDSL
VDVPFPNSYQ YIAAVDYNPR DNLLYVWNNY HVVKYSLDFG PLDSRSGQAH HGQVSYISPP
IHLDSELERP SVKDISTTGP LGMGSTTTST TLRTTTLGPG RSTTPSVSGR RNRSTSTPSP
AVEVLDDMTT HFPSASSQIP ALEESCEAVE AREIMWFKTR QGQIAKQPCP AGTIGVSTYL
CLAPDGIWDP QGPDLSNCSS PWVNHITQKL KSGETAANIA RELAEQTRNH LNAGDITYSV
RAMDQLVGLL DVQLRNLTPG GKDSAARSLN KLQKRERSCR AYVQAMVETV NNLLQPQALN
AWRDLTTSDQ LRAATMLLHT VEESAFVLAD NLLKTDIVRE NTDNIKLEVA RLSTEGNLED
LKFPENMGHG STIQLSANTL KQNGRNGEIR VAFVLYDNLG PYLSTENASM KLGTEALSTN
HSVIVNSPVI TAAINKEFSN KVYLADPVVF TVKHIKQSEE NFNPNCSFWS YSKRTMTGYW
STQGCRLLTT NKTHTTCSCN HLTNFAVLMA HVEVKHSDAV HDLLLDVITW VGILLSLVCL
LICIFTFCFF RGLQSDRNTI HKNLCISLFV AELLFLIGIN RTDQPIACAV FAALLHFFFL
AAFTWMFLEG VQLYIMLVEV FESEHSRRKY FYLVGYGMPA LIVAVSAAVD YRSYGTDKVC
WLRLDTYFIW SFIGPATLII MLNVIFLGIA LYKMFHHTAI LKPESGCLDN INYEDNRPFI
KSWVIGAIAL LCLLGLTWAF GLMYINESTV IMAYLFTIFN SLQGMFIFIF HCVLQKKVRK
EYGKCLRTHC CSGKSTESSI GSGKTSGSRT PGRYSTGSQS RIRRMWNDTV RKQSESSFIT
GDINSSASLN RGAMANHLIS NALLRPHGTN NPYNTLLGEP AVCNNPSVSM YNAQEPYRET
SMGVKLNIAY QIGASEQCQG YKCHGYSTTE W
//
