ID A0A0V1HE23_9BILA Unreviewed; 1326 AA.
AC A0A0V1HE23;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Latrophilin-like protein LAT-2 {ECO:0000313|EMBL:KRZ08958.1};
GN Name=lat-2 {ECO:0000313|EMBL:KRZ08958.1};
GN ORFNames=T11_10293 {ECO:0000313|EMBL:KRZ08958.1};
OS Trichinella zimbabwensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ08958.1, ECO:0000313|Proteomes:UP000055024};
RN [1] {ECO:0000313|EMBL:KRZ08958.1, ECO:0000313|Proteomes:UP000055024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ08958.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family. LN-TM7
CC subfamily. {ECO:0000256|ARBA:ARBA00010933}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRZ08958.1}.
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DR EMBL; JYDP01000079; KRZ08958.1; -; Genomic_DNA.
DR STRING; 268475.A0A0V1HE23; -.
DR Proteomes; UP000055024; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
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; cd00037; CLECT; 2.
DR CDD; cd22840; Gal_Rha_Lectin_LAT2; 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; 2.10.25.10; Laminin; 1.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 2.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 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_7TM.
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 PANTHER; PTHR12011; ADHESION G-PROTEIN COUPLED RECEPTOR; 1.
DR PANTHER; PTHR12011:SF473; FI21270P1-RELATED; 1.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF16489; GAIN; 1.
DR Pfam; PF01825; GPS; 1.
DR Pfam; PF00059; Lectin_C; 2.
DR PRINTS; PR00249; GPCRSECRETIN.
DR SMART; SM00034; CLECT; 2.
DR SMART; SM00303; GPS; 1.
DR SMART; SM00008; HormR; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 2.
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 2.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_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; PS50228; SUEL_LECTIN; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW G-protein coupled receptor {ECO:0000256|ARBA:ARBA00023040};
KW Lectin {ECO:0000256|ARBA:ARBA00022734};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000055024};
KW Signal {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..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1326
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006879082"
FT TRANSMEM 972..995
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1007..1025
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1031..1053
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1074..1094
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1114..1136
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1157..1180
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1186..1209
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 61..196
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 270..365
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50228"
FT DOMAIN 383..540
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 538..630
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 970..1210
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 1235..1271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1235..1259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1326 AA; 150415 MW; 79476C9CE68595DF CRC64;
MKANSLIQVA IFVAFALLST EDCEAVTPSH CHKNVCQNGG ICFQVSNSLK SSWCKSGEVP
FDRSCFFLNS RKLTWKKARE FCHGRNSTLV SINSLEQQKF LASIMQLTMF AQIPIIYVGT
ENIWTAGHLL TNDSEFQWIW DLEKQIPVEL HKTEMFWQDR QSIFQTDKNC IALTARSRYK
VWVPKNCSEK YLALCERPEL DMGDGKGLYS YQCRCPLGFY GHYCEIKDSK LFAQLDHSDG
KNILENSSKF DVVRSESSDG FVQFWSSKLN CNNERIVISC RNSELHNSTI VMDYAFYGIT
NIFTRYTRKY CDSNLFNGHS CLVENTLPKM SHYCDGREDC HLPPLKKLFP VSPCQPTDTK
FSLEYRFRCV KNNITCPLHM IQYNSTCYEI YDSQRNKDAA TWEEARVLCL KSGGDLAGPL
SDHENKVLFN ETHLSQFENI RFWIGLRAAP FIAPSLNAEF PWTVKSYSNP SELFEDETLS
TDPKLQWTNG VSLNSTKLLA NITEKAEGCV AMTVRCNSSK NCSIVWILED CNMKLNFICQ
ASAGNLYRRK WLHLPEEKQS PDISKINNNL KCSPVNVRSI QWPSVHVGKS VKMPCPNGTI
GYAIWSCVNI NGNIRFYPEN PDLSNCSHPW FSDIDEMIYS KNSIFKVIRM VEKNVELTDQ
LYGGDLKKIV DLLQTLITIF PKQLNENVAT FSNDTFQRGS IKNFSYEIAK LSNFLIDKKT
LDVWKDLQEN DKHDAASTLM GNVENLTHYF GDSLLKFDGF SLSFKNLDMT FEVTRPLLGN
HKLRKRYANN DRKLGARFVS STKLASILLP VNAMLKTISK EIEATTVFFA RTASESMPAK
IPTVSFGYFA YKDGLTNLLQ PAKDVNNDAG QKFINSEIVG ACVNYPSSLR TLESAPAIIK
LSHIKQDKVK NPRCVYWNVI ERKWDTNGCS INESTAEYTV CSCHHLTSFA ILMDFVGFSD
DLTPRNKQAM SLLSMLACSF SCTCLVFCII VFSCFRSLRG ARTTIHLNLC ICLLIGQLLF
VFGVGQTKNE ILCRSVAAFL HFFFLAAFCW MLAEGYQLYV MLVKVFDDKN NWSFSQHLLV
YGMPLVIVAI SLWLDFNSYG TQDYCWINLH SSTIWAFVGP VIVVIFSNIC VIGLALKTVF
SVASGQNRSH SQIILGWLRG SAMLLCLLGI TWGVGLFVAV QPLGYISSYL FTVLNGSQGI
FIFVFHVILN DNARTALSRW MKKHVPMFTF SSTNNQHDSF SGTKSLKTSS NLKTSKSTES
TDLNAKKAEE NEQINRTSLE FKNRNAFTYN QPASSISTFN ADYAKTTYRP CARLQEISKK
SSTSNF
//
