ID U3CDR4_CALJA Unreviewed; 1469 AA.
AC U3CDR4;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE SubName: Full=Latrophilin-3 {ECO:0000313|EMBL:JAB16439.1};
GN Name=LPHN3 {ECO:0000313|EMBL:JAB16439.1};
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|EMBL:JAB16439.1};
RN [1] {ECO:0000313|EMBL:JAB16439.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Cerebellum {ECO:0000313|EMBL:JAB48995.1}, Cerebral cortex
RC {ECO:0000313|EMBL:JAB29684.1}, and Hippocampus
RC {ECO:0000313|EMBL:JAB16439.1};
RX PubMed=25243066; DOI=10.1186/2047-217X-3-14;
RA Maudhoo M.D., Ren D., Gradnigo J.S., Gibbs R.M., Lubker A.C.,
RA Moriyama E.N., French J.A., Norgren R.B.Jr.;
RT "De novo assembly of the common marmoset transcriptome from NextGen mRNA
RT sequences.";
RL Gigascience 3:14-14(2014).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; GAMS01006697; JAB16439.1; -; mRNA.
DR EMBL; GAMR01004248; JAB29684.1; -; mRNA.
DR EMBL; GAMP01003760; JAB48995.1; -; mRNA.
DR MEROPS; P02.011; -.
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; 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 2: Evidence at transcript level;
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 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..1469
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015101326"
FT TRANSMEM 879..902
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 914..932
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 938..960
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 981..1001
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1021..1044
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1075..1097
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1103..1126
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 35..124
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 498..554
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 877..1127
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 426..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1145..1169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1389..1408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1443..1469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1389..1404
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 135..317
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00446"
SQ SEQUENCE 1469 AA; 164531 MW; 40ECE0420BE60681 CRC64;
MWPSQLLIFM TLLAPIIHAF SRAPIPMAVV RRELSCESYP IELRCPGTDV IMIESANYGR
TDDKICDSDP AQMENIRCYL PDAYKIMSQR CNNRTQCAVV AGPDVFPDPC PGTYKYLEVQ
YECVPYKVEQ KVFLCPGLLK GVYQSEHLFE SDHQSGAWCK DPLQASDKIY YMPWTPYRTD
TLTEYSSKDD FIAGRPTTTY KLPHRVDGTG FVVYDGALFF NKERTRNIVK FDLRTRIKSG
EAIIANANYH DTSPYRWGGK SDIDLAVDEN GLWVIYATEQ NNGKIVISQL NPYTLRIEGT
WDTAYDKRSA SNAFMICGIL YVVKSVYEDD DNEATGNKID YIYNTDQSKD SLVDVPFPNS
YQYIAAVDYN PRDNLLYVWN NYHVVKYSLD FGPLDSRSGQ AHHGQVSYIS PPIHLDSELE
RPSVKDISTT GPLGMGSTTT STTLRTTTLG PGRSTTPSVS GRRNRSTSTP SPAVEVLDDM
TTHFPSASSQ IPALEESCEA VEAREIMWFK TRQGQIAKQP CPAGTIGVST YLCLAPDGIW
DPQGPDLSNC SSPWVNHITQ KLKSGETAAN IARELAEQTR NHLNAGDITY SVRAMDQLVG
LLDVQLRNLT PGGKDSAARS LNKLQKRERS CRAYVQAMVE TVNNLLQPQA LNAWRDLTTS
DQLRAATMLL HTVEESAFVL ADNLLKTDIV RENTDNIKLE VARLSTEGNL EDLKFPENMG
HGSTIQLSAN TLKQNGRNGE IRVAFVLYDN LGPYLSTENA SMKLGTEALS TNHSVIVNSP
VITAAINKEF SNKVYLADPV VFTVKHIKQS EENFNPNCSF WSYSKRTMTG YWSTQGCRLL
TTNKTHTTCS CNHLTNFAVL MAHVEVKHSD AVHDLLLDVI TWVGILLSLV CLLICIFTFC
FFRGLQSDRN TIHKNLCISL FVAELLFLIG INRTDQPIAC AVFAALLHFF FLAAFTWMFL
EGVQLYIMLV EVFESEHSRR KYFYLVGYGM PALIVAVSAA VDYRSYGTDK VCWLRLDTYF
IWSFIGPATL IIMLNVIFLG IALYKMFHHT AILKPESGCL DNINYEDNRP FIKSWVIGAI
ALLCLLGLTW AFGLMYINES TVIMAYLFTI FNSLQGMFIF IFHCVLQKKV RKEYGKCLRT
HCCSGKSTES SIGSGKTSGS RTPGRYSTGS QSRIRRMWND TVRKQSESSF ITGDINSSAS
LNREGLLNNA RDTSVMDTLP LNGNHGNSYS IASGEYLSNC VQIIDRGYNH NETALEKKIL
KELTSNYIPS YLNNHERSSE QNRNLMNKLV NNLGSGREDD AIVLDDATSF NHEESLGLEL
IHEESDAPLL PPRVYSTENH QLHHFTRRRI PQDHSESFFP LLTNEHTEEL QSPHRDSLYT
SMPTLAGAAA TESVTTSTQT EPPSAKCGDA EDVYYKSMPN LGSRNHVHQL HTYYQLGRGS
SDGFIVPPNK DGTPPEGSSK GPAHLVTSL
//
