LPLT2_CAEEL
ID LPLT2_CAEEL Reviewed; 1338 AA.
AC G5ECX0; B2MZA8;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Latrophilin-like protein LAT-2 {ECO:0000312|EMBL:CCD61661.1, ECO:0000312|WormBase:B0286.2b};
DE Flags: Precursor;
GN Name=lat-2 {ECO:0000312|EMBL:CCD61661.1, ECO:0000312|WormBase:B0286.2a};
GN ORFNames=B0286.2;
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:0000312|EMBL:AAQ84879.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
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 (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305, ECO:0000312|EMBL:CCD61661.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CCD61661.1};
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 [3] {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 [4] {ECO:0000305}
RP TISSUE SPECIFICITY.
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).
CC -!- FUNCTION: May have a role in pharyngeal pumping during feeding.
CC {ECO:0000269|PubMed:17583712}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000269|PubMed:9851916, ECO:0000269|Ref.1};
CC IsoId=G5ECX0-1; Sequence=Displayed;
CC Name=b {ECO:0000269|PubMed:9851916};
CC IsoId=G5ECX0-2; Sequence=VSP_046486;
CC -!- TISSUE SPECIFICITY: Pharyngeal primordium.
CC {ECO:0000269|PubMed:19853563}.
CC -!- DISRUPTION PHENOTYPE: Reduced response to the inhibitory action of
CC emodepside in pharyngeal pumping. {ECO:0000269|PubMed:17583712}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family. LN-TM7
CC subfamily. {ECO:0000255}.
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 EMBL; AY314772; AAQ84879.1; -; mRNA.
DR EMBL; FO080154; CCD61661.1; -; Genomic_DNA.
DR EMBL; FO080154; CCD61662.1; -; Genomic_DNA.
DR RefSeq; NP_001040724.1; NM_001047259.2. [G5ECX0-1]
DR RefSeq; NP_001040725.1; NM_001047260.1. [G5ECX0-2]
DR AlphaFoldDB; G5ECX0; -.
DR SMR; G5ECX0; -.
DR BioGRID; 39127; 1.
DR STRING; 6239.B0286.2a; -.
DR MEROPS; S01.A54; -.
DR TCDB; 9.A.14.6.5; the g-protein-coupled receptor (gpcr) family.
DR EPD; G5ECX0; -.
DR PaxDb; G5ECX0; -.
DR EnsemblMetazoa; B0286.2a.1; B0286.2a.1; WBGene00002252. [G5ECX0-1]
DR EnsemblMetazoa; B0286.2b.1; B0286.2b.1; WBGene00002252. [G5ECX0-2]
DR GeneID; 173771; -.
DR KEGG; cel:CELE_B0286.2; -.
DR CTD; 173771; -.
DR WormBase; B0286.2a; CE36968; WBGene00002252; lat-2. [G5ECX0-1]
DR WormBase; B0286.2b; CE39661; WBGene00002252; lat-2. [G5ECX0-2]
DR eggNOG; KOG4193; Eukaryota.
DR GeneTree; ENSGT00940000166745; -.
DR HOGENOM; CLU_270428_0_0_1; -.
DR InParanoid; G5ECX0; -.
DR OMA; MCNQASQ; -.
DR OrthoDB; 388923at2759; -.
DR PhylomeDB; G5ECX0; -.
DR Reactome; R-CEL-373080; Class B/2 (Secretin family receptors).
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR PRO; PR:G5ECX0; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00002252; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0097264; P:self proteolysis; IDA:WormBase.
DR Gene3D; 2.60.120.740; -; 1.
DR Gene3D; 2.60.220.50; -; 1.
DR Gene3D; 3.10.100.10; -; 2.
DR Gene3D; 4.10.1240.10; -; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR000742; EGF-like_dom.
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 PRINTS; PR00249; GPCRSECRETIN.
DR SMART; SM00034; CLECT; 2.
DR SMART; SM00303; GPS; 1.
DR SMART; SM00008; HormR; 1.
DR SUPFAM; SSF56436; SSF56436; 2.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 2.
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 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Disulfide bond; EGF-like domain;
KW G-protein coupled receptor; Lectin; Membrane; Receptor; Reference proteome;
KW Repeat; Signal; Transducer; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1338
FT /note="Latrophilin-like protein LAT-2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000422177"
FT TOPO_DOM 20..901
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 902..922
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 923..930
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 931..951
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 952..959
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 960..980
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 981..999
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1000..1020
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1021..1040
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1041..1061
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1062..1085
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1086..1106
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1107..1115
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1116..1136
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1137..1338
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 25..64
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 59..193
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 180..219
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 233..322
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00260"
FT DOMAIN 838..885
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT REGION 1300..1338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 29..40
FT /evidence="ECO:0000255"
FT DISULFID 52..63
FT /evidence="ECO:0000255"
FT DISULFID 80..192
FT /evidence="ECO:0000255"
FT DISULFID 167..184
FT /evidence="ECO:0000255"
FT DISULFID 209..218
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..879
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000303|PubMed:9851916"
FT /id="VSP_046486"
SQ SEQUENCE 1338 AA; 147302 MW; 43B63CFE3FD47BC6 CRC64;
MAKQLKYPFL IFIISLAQCQ VSNQNVNLCQ SNICQNGGTC LVASSVPATA TCPKNSIYYM
GSCYVFDTTL RNWNDAALYC NNMNSATLPL VESAEDQAFF AGYLQAMIPS NPPADMRPPP
DGIWTAVRGV NNVTRASWVY YPGSFLVTDT FWAPQEPNIY VNYNDVCVAL QSDSFYREWT
TALCTILKYT VCKVAPTQIQ AKYVAQCSCP NGYGGQTCET QSTTNQQAST QRTCGSNDFQ
FSCPNDQTIT VDFASFGAQE SSMCNQASQS REQTCSNVNS LQTVINACQG LQSCEIRNLT
STFSNTPCPV PQEQYLETRM RCETAQQPSC LSGLIQFDSR CYSMTIETNE KKQRTMEDAQ
TYCSQSGGSI ITSPPDALLQ QIVQKVNAET KKTVNFWIGT PNNCQLLMVT GSSTSYSQCP
SSPSSTANVI CSTVPQSTAS VSARPTQSAP VDPVSQTMAR REVYTGVQPP SVPDSINKPR
YCKKEKKDGI TYEQTRACML HEQPCPDPQN VEGTVTRYCN CQTAKWETPD TTNCTHRWVA
EMETAIKDNQ PVEDISSTVN RQLKSTIERT LFGGDITGTV RLSNDMLSLA RNQFSVLNDR
NLRENKARNF TENLGGSGDQ LLSPVAATVW DQLSSTIRIQ HASKLMSVLE QSVLLLGDYM
TDQKLNLQYI NWAMEVERSE PEVQTFGAAA SPNVQDDMGM MRVMAAAPPA PQPETNTTIM
FPSLKLSPTI TLPSASLLSS LASPTPVAGG GPSILSSFQD DTPVGMASTP NLNRNPVKLG
YYAFAGFGQL LNNNNDHTLI NSQVIGASIQ NATQSVTLPV DHPVTFTFQH LTTKGVSNPR
CVYWDLMESK WSTLGCTLIA TSSNSSQCSC THLTSFAILM DISGQVGRLS GGLASALDVV
STIGCAISIV CLALSVCVFT FFRNLQNVRN SIHRNLCLCL LIAELVFVIG MDRTGNRTGC
GVVAILLHYF FLSSFCWMLL EGYQLYMMLI QVFEPNRTRI FLYYLFCYGT PAVVVAISAG
IKWEDYGTDS YCWIDTSTPT IWAFVAPIIV IIAANIIFLL IALKVVLSVQ SRDRTKWGRI
IGWLKGSATL LCLLGITWIF GFLTAVKGGT GTAFAWIFTI LNCTQGIFIF VLHVVLNEKV
RASIVRWLRT GICCLPETSS AAYNSRSFLS SRQRILNMIK VNGHSYPSTA STDDKEKQLT
PITKTTDWLS RLPNQDSVSI PESNFNNLNG TLENSNLNSA EIKEEDEIPE LRRRVTVDLN
PMIVSNNEIE RMSHASSDPR GSQIIEVTAV EKKAPVKRIK FPLGAKQSER GSQHRTKAKV
IAPPESPVSE SGSKDYRF
