LPLT1_CAEEL
ID LPLT1_CAEEL Reviewed; 1014 AA.
AC G5EDW2; G5EEH7; Q7JM97;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Latrophilin-like protein 1;
DE Flags: Precursor;
GN Name=lat-1 {ECO:0000312|EMBL:CAA91091.1, ECO:0000312|WormBase:B0457.1a};
GN ORFNames=B0457.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAQ84877.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
RA Mastwal S.S., Yu D., Hedgecock E.M.;
RT "Molecular and evolutionary characterization of family B G-protein coupled
RT receptors in Caenorhabditis elegans.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=14594448; DOI=10.1042/bj20031213;
RA Mee C.J., Tomlinson S.R., Perestenko P.V., De Pomerai D., Duce I.R.,
RA Usherwood P.N., Bell D.R.;
RT "Latrophilin is required for toxicity of black widow spider venom in
RT Caenorhabditis elegans.";
RL Biochem. J. 378:185-191(2004).
RN [3] {ECO:0000312|EMBL:CAA91091.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CAA91091.1};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [4] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=15296755; DOI=10.1016/j.cub.2004.07.056;
RA Willson J., Amliwala K., Davis A., Cook A., Cuttle M.F., Kriek N.,
RA Hopper N.A., O'Connor V., Harder A., Walker R.J., Holden-Dye L.;
RT "Latrotoxin receptor signaling engages the UNC-13-dependent vesicle-priming
RT pathway in C. elegans.";
RL Curr. Biol. 14:1374-1379(2004).
RN [5] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17583712; DOI=10.1016/j.ijpara.2007.05.006;
RA Guest M., Bull K., Walker R.J., Amliwala K., O'Connor V., Harder A.,
RA Holden-Dye L., Hopper N.A.;
RT "The calcium-activated potassium channel, SLO-1, is required for the action
RT of the novel cyclo-octadepsipeptide anthelmintic, emodepside, in
RT Caenorhabditis elegans.";
RL Int. J. Parasitol. 37:1577-1588(2007).
RN [6] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=19853563; DOI=10.1016/j.devcel.2009.08.008;
RA Langenhan T., Promel S., Mestek L., Esmaeili B., Waller-Evans H.,
RA Hennig C., Kohara Y., Avery L., Vakonakis I., Schnabel R., Russ A.P.;
RT "Latrophilin signaling links anterior-posterior tissue polarity and
RT oriented cell divisions in the C. elegans embryo.";
RL Dev. Cell 17:494-504(2009).
RN [7] {ECO:0000305}
RP FUNCTION, SUBUNIT, DOMAIN, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF HIS-528
RP AND THR-530.
RX PubMed=22938866; DOI=10.1016/j.celrep.2012.06.015;
RA Promel S., Frickenhaus M., Hughes S., Mestek L., Staunton D., Woollard A.,
RA Vakonakis I., Schoneberg T., Schnabel R., Russ A.P., Langenhan T.;
RT "The GPS motif is a molecular switch for bimodal activities of adhesion
RT class G protein-coupled receptors.";
RL Cell Rep. 2:321-331(2012).
CC -!- FUNCTION: Has a role in the establishment of anterior-posterior
CC polarity in tissues during embryogenesis. Required for the alignment of
CC the mitotic spindles and division planes. May have a role in cell death
CC events. Required for normal defection and oocyte fertilization.
CC Involved in sperm function. Operates in pharyngeal pumping during
CC feeding. {ECO:0000269|PubMed:14594448, ECO:0000269|PubMed:15296755,
CC ECO:0000269|PubMed:17583712, ECO:0000269|PubMed:19853563,
CC ECO:0000269|PubMed:22938866}.
CC -!- SUBUNIT: Monomer and homodimer. {ECO:0000269|PubMed:22938866}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19853563};
CC Multi-pass membrane protein {ECO:0000269|PubMed:19853563}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=a {ECO:0000269|PubMed:14594448, ECO:0000269|PubMed:9851916,
CC ECO:0000269|Ref.1};
CC IsoId=G5EDW2-1; Sequence=Displayed;
CC Name=b {ECO:0000269|PubMed:9851916, ECO:0000269|Ref.1};
CC IsoId=G5EDW2-2; Sequence=VSP_046293, VSP_046295;
CC Name=c {ECO:0000269|PubMed:9851916};
CC IsoId=G5EDW2-3; Sequence=VSP_046292, VSP_046294;
CC -!- TISSUE SPECIFICITY: Expressed in epidermal precursor cells and
CC pharyngeal primordium. In adults expression is seen in pharyngeal
CC muscle cells and nervous system, the nerve ring, the gonad, and the
CC vulva. {ECO:0000269|PubMed:15296755, ECO:0000269|PubMed:19853563}.
CC -!- DEVELOPMENTAL STAGE: Expressed during oogenesis, embryogenesis, and
CC organogenesis. {ECO:0000269|PubMed:19853563}.
CC -!- DOMAIN: The GPS domain is required for signaling.
CC {ECO:0000269|PubMed:22938866}.
CC -!- DISRUPTION PHENOTYPE: Approximately 17% arrest during embryogenesis and
CC 56% arrest at the L1 developmental stage. Defects present in seam cell
CC positioning and division plane. Unfertilized oocytes in hermaphrodites.
CC Five-fold less sensitive to the inhibitory effects of emodepside or
CC imipramine on pharyngeal pumping. Irregular defecation.
CC {ECO:0000269|PubMed:14594448, ECO:0000269|PubMed:15296755,
CC ECO:0000269|PubMed:17583712, ECO:0000269|PubMed:22938866}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family. LN-TM7
CC subfamily. {ECO:0000255}.
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DR EMBL; AY314770; AAQ84877.1; -; mRNA.
DR EMBL; AY314771; AAQ84878.1; -; mRNA.
DR EMBL; Z54306; CAA91091.1; -; Genomic_DNA.
DR EMBL; Z54306; CAD59141.1; -; Genomic_DNA.
DR EMBL; Z54306; CAE54881.1; -; Genomic_DNA.
DR PIR; T18759; T18759.
DR RefSeq; NP_001021897.1; NM_001026726.3.
DR RefSeq; NP_495894.1; NM_063493.3.
DR RefSeq; NP_871949.1; NM_182149.4.
DR AlphaFoldDB; G5EDW2; -.
DR SMR; G5EDW2; -.
DR BioGRID; 39746; 2.
DR IntAct; G5EDW2; 1.
DR STRING; 6239.B0457.1a; -.
DR EPD; G5EDW2; -.
DR PaxDb; G5EDW2; -.
DR PeptideAtlas; G5EDW2; -.
DR EnsemblMetazoa; B0457.1a.1; B0457.1a.1; WBGene00002251. [G5EDW2-1]
DR EnsemblMetazoa; B0457.1b.1; B0457.1b.1; WBGene00002251. [G5EDW2-2]
DR EnsemblMetazoa; B0457.1c.1; B0457.1c.1; WBGene00002251. [G5EDW2-3]
DR UCSC; B0457.1a; c. elegans.
DR WormBase; B0457.1a; CE02945; WBGene00002251; lat-1. [G5EDW2-1]
DR WormBase; B0457.1b; CE32789; WBGene00002251; lat-1. [G5EDW2-2]
DR WormBase; B0457.1c; CE36086; WBGene00002251; lat-1. [G5EDW2-3]
DR eggNOG; KOG4193; Eukaryota.
DR eggNOG; KOG4729; Eukaryota.
DR HOGENOM; CLU_293252_0_0_1; -.
DR InParanoid; G5EDW2; -.
DR OMA; FLYNTND; -.
DR OrthoDB; 388923at2759; -.
DR PhylomeDB; G5EDW2; -.
DR PRO; PR:G5EDW2; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00002251; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:WormBase.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0004175; F:endopeptidase activity; IDA:WormBase.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; ISS:WormBase.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IMP:WormBase.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0097264; P:self proteolysis; IDA:WormBase.
DR GO; GO:0019953; P:sexual reproduction; IMP:WormBase.
DR Gene3D; 2.60.120.740; -; 1.
DR Gene3D; 2.60.220.50; -; 1.
DR Gene3D; 4.10.1240.10; -; 1.
DR InterPro; IPR032471; GAIN_dom_N.
DR InterPro; IPR046338; GAIN_dom_sf.
DR InterPro; IPR017981; GPCR_2-like.
DR InterPro; IPR036445; GPCR_2_extracell_dom_sf.
DR InterPro; IPR001879; GPCR_2_extracellular_dom.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR000203; GPS.
DR InterPro; IPR000922; Lectin_gal-bd_dom.
DR InterPro; IPR043159; Lectin_gal-bd_sf.
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 PRINTS; PR00249; GPCRSECRETIN.
DR SMART; SM00303; GPS; 1.
DR SMART; SM00008; HormR; 1.
DR SUPFAM; SSF111418; SSF111418; 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; PS50228; SUEL_LECTIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; G-protein coupled receptor;
KW Glycoprotein; Lectin; Membrane; Receptor; Reference proteome; Signal;
KW Transducer; Transmembrane; Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..1014
FT /note="Latrophilin-like protein 1"
FT /id="PRO_0000421981"
FT TOPO_DOM 28..555
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 556..576
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 577..584
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 585..605
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 606..613
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 614..634
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 635..653
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 654..674
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 675..692
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 693..713
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 714..745
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 746..766
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 767..770
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 771..791
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 792..1014
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 43..134
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00260"
FT DOMAIN 494..541
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098,
FT ECO:0000269|PubMed:19853563"
FT REGION 814..833
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 932..994
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 939..954
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 955..994
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 4
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 473
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 518
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 99..114
FT /note="KCNGDSMCYFTVDKKT -> NYHDDYNHNYINYYNR (in isoform c)"
FT /evidence="ECO:0000303|PubMed:9851916"
FT /id="VSP_046292"
FT VAR_SEQ 103..124
FT /note="DSMCYFTVDKKTFTEDPCPNTP -> KQTCRFFVDTFLFDDACPMMS (in
FT isoform b)"
FT /evidence="ECO:0000303|PubMed:9851916, ECO:0000303|Ref.1"
FT /id="VSP_046293"
FT VAR_SEQ 115..1014
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000303|PubMed:9851916"
FT /id="VSP_046294"
FT VAR_SEQ 130..136
FT /note="KYNCVVP -> QHECHE (in isoform b)"
FT /evidence="ECO:0000303|PubMed:9851916, ECO:0000303|Ref.1"
FT /id="VSP_046295"
FT MUTAGEN 528
FT /note="H->A: Abolishes autocatalytic cleavage activity."
FT /evidence="ECO:0000269|PubMed:22938866"
FT MUTAGEN 530
FT /note="T->A: Abolishes autocatalytic cleavage activity."
FT /evidence="ECO:0000269|PubMed:22938866"
SQ SEQUENCE 1014 AA; 113025 MW; 74CC38DE6D82FB40 CRC64;
MRRNKTTYSL LQTILVACLL TVTPTFASNK PTTDESGTIS HTICDGEAAE LSCPAGKVIS
IVLGNYGRFS VAVCLPDNDI VPSNINCQNH KTKSILEKKC NGDSMCYFTV DKKTFTEDPC
PNTPKYLEVK YNCVVPATTT TTTTTTSTTT TDSSLIVDEE EEAQKDALNS DVIKPVKKKE
DVFCSATNRR GVNWQNTKSG TTSSAPCPEG SSGKQLWACT EEGQWLTEFP NSAGCESNWI
SSRNSVLSGV ISSEDVSGLP EFLRNLGSET RRPMVGGDLP KVLHLLEKTV NVIAEESWAY
QHLPLSNKGA VEVMNYMLRN QEIWGSWDVT KRKEFASRFI LAAEKAMVAS AKGMMTSAES
NVIVQPAITV EISHKIKMSS QPTDYILFPS AALWNGQNVD NVNIPRDAIL KINKDETQVF
FSSFDNLGAQ MTPSDVTVAI AGTDQTEVRK RRVVSRIVGA SLIENGKERR VENLTQPVRI
TFYHKESSVR HLSNPTCVWW NHHELKWKPS GCKLSYHNKT MTSCDCTHLT HFAVLMDVRG
HDLNEIDQTL LTLLTYVGCI ISIICLLLTF FAYLIFSRNG GDRVFIHENL CLSLAIAEIT
FLAGITRTED SLQCGIIAVA LMYMFLSALT WMLLEGYHIH RMLTEVFPSD PRRFTYLLVG
YIPPAIITLV AYLYNSDGFG TPDHCWLSTQ NNFIWFFAGP ACFIFCANSL VLVKTLCTVY
QHTSGGYLPC RHDVDSGRSI RNWVKGSLAL ASLLGVTWIF GLFWVEDSRS IVMAYVFTIS
NSLQGLFIFL FHVVFAEKMR KDVGHWMYRR GCGGSSNSSP NHKRHNVQRD LMSPGVNSST
GSDFLYNTND KYLTNSDTTN RLVYNGIMNH PNQMSVYQQH PHHQIYEQQP GTYDYATIAY
GDMMPGHRVA APPAYQRLAV AEGRYGSQHQ LYQGWHHRPP PEFSPPPPPL STGPPNSRHY
GTGSSGRRPP SSKMSDDSAY SDGSSSMLTT EVTPQGQTVL RIDLNKPSMY CQDL
