ID A0A0V1LKP4_9BILA Unreviewed; 1371 AA.
AC A0A0V1LKP4;
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-3 {ECO:0000313|EMBL:KRZ60107.1};
GN Name=LPHN3 {ECO:0000313|EMBL:KRZ60107.1};
GN ORFNames=T02_9014 {ECO:0000313|EMBL:KRZ60107.1};
OS Trichinella nativa.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ60107.1, ECO:0000313|Proteomes:UP000054721};
RN [1] {ECO:0000313|EMBL:KRZ60107.1, ECO:0000313|Proteomes:UP000054721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS10 {ECO:0000313|EMBL:KRZ60107.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (MAY-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:KRZ60107.1}.
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DR EMBL; JYDW01000033; KRZ60107.1; -; Genomic_DNA.
DR STRING; 6335.A0A0V1LKP4; -.
DR Proteomes; UP000054721; 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:SF470; LATROPHILIN-LIKE PROTEIN LAT-2; 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:UP000054721};
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 TRANSMEM 1017..1040
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1052..1070
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1076..1098
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1119..1139
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1159..1181
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1202..1225
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1231..1254
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 88..223
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 297..392
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50228"
FT DOMAIN 410..567
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 565..657
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 1015..1255
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 1286..1320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1286..1307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1371 AA; 155838 MW; 117D6A3EC97040AB CRC64;
MFNRISNTTS QGIFPRFRLK KQKLLFKMKA NSLIPVAIFV AFALLSTKDC VAVTPSHCHK
NVCQNGGICF QVSNSLKSSW CQSGEVPFDR SCFFLNGRTY TWEKAREFCH SRNSTLVFID
SLEKQRFLAS IMQLTMFAQI PIVYVGTQNI WTAGHLLTNG SEFQWIWDLE KQIPVELHKT
EMFWQNRQSI FQPDKNCIVL TARSRYRVWV PKNCSEKYLV LCERPERAMG DARELYSYQC
RCPLGFYGHY CEIKDFQLFA QLDHSNGRNI LKNSSKFDVV RSETSDGFVQ FWSSKLNCNN
ERIVISCRNS ELHNSTIVMD YAFYGITNIF TRYTRKYCDS NLFNGHSCLV ENTLAKMSHY
CDGREDCHLP PLKKLFPVSP CQPADIKFSL EYRFRCVKNN ITCPLHMIQY NSTCYEIYDS
QRNKDAATWG EARVQCLKSG GDLAGPLSDH ENKVLFNETH LSQYENIRFW IGLRTVPFII
SSLNTEFPWT VKSYSDPSEL LDAETLSTDS RLQWINGASL NSTKLSSNIT EKAEGCVAMT
VRCNNSKNCS IVWVLEDCNM KLNFICQASA GNLYRRKLLH LPEEKQSSEI SEINNNLKCS
PINVRSIQWP SVHVGKSVKM PCPNGTIGYA IWSCVNINGN IHFYPENPDL SNCSHPWFSD
IDEMIYSKNS IFKVIRMVEK HVELTNQLYG GDLRKIVDLL QTLITIFPKQ LNQNIATFSN
DTFQRGSIKN FSYEIAKLSN FLIDKKTLDV WKDLQQKDKH DAASTLMENV ENLTRYFGDS
LLKFDGFSLS FKNLDMTFEV TRPLLGNHKL RKRYANNDRK LGARFVSSTK LASILLPVNA
MLSKYSFACD GKNLQSMLFK ETISKEIEAT TVFFARTASD SMPAKIPTVS FGYFAYKDGL
TNLLQPANDV NNDAGQKFIN SEIVGACVNY PSSLRTLESV PAIIKLSHIK QDKVKNPRCV
YWNVIERKWD TNGCSINEST ADYTVCSCHH LTSFAILMDF VGFSDDLTPH NKQAMSLLSM
LACSFSCTCL VFCIIVFSCF RSLRGARTTI HLNLCICLLI GQLLFVFGVG QTKNEILCRS
VAAFLHFFFL AAFCWMLAEG YQLYVMLVRV FDDKNNWSFS QHLLVYGMPL VIVAISLWLD
FNSYGTQDYC WINLHSSTIW AFVGPVIVVI FSNICVIGLA LKTVFSVASG QNRSHSQIIL
GWLRGSAMLL CLLGITWGVG LFVAVQPLGY ISSYLFTVLN GSQGIFIFVF HVILNDKART
ALCRWMKKHV PMFTFSSTNN QHDAFSGTNS LKTSSNLKTS KSTGSTDLNA KKSEESEQIN
RTSLEFKNRN AFTYNQPASS IATFNADFAK ATYRPCARLQ GISKKSSTSN F
//
