Full text data of LPHN2
LPHN2
(KIAA0786, LEC1, LPHH1)
[Confidence: low (only semi-automatic identification from reviews)]
Latrophilin-2 (Calcium-independent alpha-latrotoxin receptor 2; CIRL-2; Latrophilin homolog 1; Lectomedin-1; Flags: Precursor)
Latrophilin-2 (Calcium-independent alpha-latrotoxin receptor 2; CIRL-2; Latrophilin homolog 1; Lectomedin-1; Flags: Precursor)
UniProt
O95490
ID LPHN2_HUMAN Reviewed; 1459 AA.
AC O95490; A5XEI2; B1ALT8; B1ALT9; B1ALU0; B1ALU2; B1ALU4; B1ALU5;
read moreAC B1ALU6; O94882; Q5VX76; Q9UKY5; Q9UKY6;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2004, sequence version 2.
DT 22-JAN-2014, entry version 113.
DE RecName: Full=Latrophilin-2;
DE AltName: Full=Calcium-independent alpha-latrotoxin receptor 2;
DE Short=CIRL-2;
DE AltName: Full=Latrophilin homolog 1;
DE AltName: Full=Lectomedin-1;
DE Flags: Precursor;
GN Name=LPHN2; Synonyms=KIAA0786, LEC1, LPHH1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RX PubMed=10030676; DOI=10.1038/sj.onc.1202487;
RA White G.R.M., Varley J.M., Heighway J.;
RT "Isolation and characterisation of a human homologue of the
RT latrophilin gene from a region of 1p31.1 implicated in breast
RT cancer.";
RL Oncogene 17:3513-3519(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10760572; DOI=10.1016/S0167-4781(00)00020-8;
RA White G.R.M., Varley J.M., Heighway J.;
RT "Genomic structure and expression profile of LPHH1, a 7TM gene
RT variably expressed in breast cancer cell lines.";
RL Biochim. Biophys. Acta 1491:75-92(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4).
RA Hayflick J.S.;
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 439-1459 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XI.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 5:277-286(1998).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 973-1070 (ISOFORM 6).
RX PubMed=17456239; DOI=10.1186/gb-2007-8-4-r64;
RA Clark T.A., Schweitzer A.C., Chen T.X., Staples M.K., Lu G., Wang H.,
RA Williams A., Blume J.E.;
RT "Discovery of tissue-specific exons using comprehensive human exon
RT microarrays.";
RL Genome Biol. 8:R64.1-R64.16(2007).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-629, AND MASS
RP SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of
RT multiple enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1430, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Calcium-independent receptor of low affinity for alpha-
CC latrotoxin, an excitatory neurotoxin present in black widow spider
CC venom which triggers massive exocytosis from neurons and
CC neuroendocrine cells. Receptor propably implicated in the
CC regulation of exocytosis (By similarity).
CC -!- SUBUNIT: Forms a heterodimer, consisting of a large extracellular
CC region (p120) non-covalently linked to a seven-transmembrane
CC moiety (p85) (By similarity).
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1;
CC IsoId=O95490-1; Sequence=Displayed;
CC Name=2; Synonyms=Lectomedin-1 gamma;
CC IsoId=O95490-2; Sequence=VSP_010104, VSP_010107;
CC Name=3; Synonyms=Lectomedin-1 beta;
CC IsoId=O95490-3; Sequence=VSP_010104, VSP_010105, VSP_010106;
CC Name=4; Synonyms=Lectomedin-1 alpha;
CC IsoId=O95490-4; Sequence=VSP_010104, VSP_010107, VSP_010108,
CC VSP_010109;
CC Name=5;
CC IsoId=O95490-5; Sequence=VSP_010107;
CC Note=No experimental confirmation;
CC Name=6;
CC IsoId=O95490-6; Sequence=VSP_042267;
CC Name=7;
CC IsoId=O95490-7; Sequence=VSP_010104, VSP_042267;
CC Note=No experimental confirmation;
CC -!- TISSUE SPECIFICITY: Expressed very widely in all normal tissues
CC tested. Expression is variable in tumor cell lines, apparently
CC elevated in some lines and absent or markedly reduced in others.
CC -!- PTM: Proteolytically cleaved into 2 subunits, an extracellular
CC subunit and a seven-transmembrane subunit (By similarity).
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC LN-TM7 subfamily.
CC -!- SIMILARITY: Contains 1 GPS domain.
CC -!- SIMILARITY: Contains 1 olfactomedin-like domain.
CC -!- SIMILARITY: Contains 1 SUEL-type lectin domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI22406.1; Type=Erroneous gene model prediction;
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/LPHH1ID313.html";
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DR EMBL; AJ131581; CAA10458.1; -; mRNA.
DR EMBL; AJ244492; CAB60229.1; -; Genomic_DNA.
DR EMBL; AJ244493; CAB60229.1; JOINED; Genomic_DNA.
DR EMBL; AJ244494; CAB60229.1; JOINED; Genomic_DNA.
DR EMBL; AJ244496; CAB60229.1; JOINED; Genomic_DNA.
DR EMBL; AJ244497; CAB60229.1; JOINED; Genomic_DNA.
DR EMBL; AJ244498; CAB60229.1; JOINED; Genomic_DNA.
DR EMBL; AJ244499; CAB60229.1; JOINED; Genomic_DNA.
DR EMBL; AJ244501; CAB60229.1; JOINED; Genomic_DNA.
DR EMBL; AJ244502; CAB60229.1; JOINED; Genomic_DNA.
DR EMBL; AJ244503; CAB60229.1; JOINED; Genomic_DNA.
DR EMBL; AJ244504; CAB60229.1; JOINED; Genomic_DNA.
DR EMBL; AJ244505; CAB60229.1; JOINED; Genomic_DNA.
DR EMBL; AJ244506; CAB60229.1; JOINED; Genomic_DNA.
DR EMBL; AJ244507; CAB60229.1; JOINED; Genomic_DNA.
DR EMBL; AJ244510; CAB60229.1; JOINED; Genomic_DNA.
DR EMBL; AJ244511; CAB60229.1; JOINED; Genomic_DNA.
DR EMBL; AJ244512; CAB60229.1; JOINED; Genomic_DNA.
DR EMBL; AJ244516; CAB60229.1; JOINED; Genomic_DNA.
DR EMBL; AF104266; AAD54675.1; -; mRNA.
DR EMBL; AF104938; AAD54676.1; -; mRNA.
DR EMBL; AF104939; AAD54677.1; -; mRNA.
DR EMBL; AL359705; CAH71340.1; -; Genomic_DNA.
DR EMBL; AC113949; CAH71340.1; JOINED; Genomic_DNA.
DR EMBL; AL157903; CAH71340.1; JOINED; Genomic_DNA.
DR EMBL; AL359705; CAH71341.1; -; Genomic_DNA.
DR EMBL; AC113949; CAH71341.1; JOINED; Genomic_DNA.
DR EMBL; AL157903; CAH71341.1; JOINED; Genomic_DNA.
DR EMBL; AL359705; CAH71342.1; -; Genomic_DNA.
DR EMBL; AC113949; CAH71342.1; JOINED; Genomic_DNA.
DR EMBL; AL157903; CAH71342.1; JOINED; Genomic_DNA.
DR EMBL; AL359705; CAH71343.1; -; Genomic_DNA.
DR EMBL; AC113949; CAH71343.1; JOINED; Genomic_DNA.
DR EMBL; AL157903; CAH71343.1; JOINED; Genomic_DNA.
DR EMBL; AL359705; CAH71345.1; -; Genomic_DNA.
DR EMBL; AC113949; CAH71345.1; JOINED; Genomic_DNA.
DR EMBL; AL157903; CAH71345.1; JOINED; Genomic_DNA.
DR EMBL; AL359705; CAH71346.1; -; Genomic_DNA.
DR EMBL; AC113949; CAH71346.1; JOINED; Genomic_DNA.
DR EMBL; AL157903; CAH71346.1; JOINED; Genomic_DNA.
DR EMBL; AL359705; CAH71347.1; -; Genomic_DNA.
DR EMBL; AC113949; CAH71347.1; JOINED; Genomic_DNA.
DR EMBL; AL157903; CAH71347.1; JOINED; Genomic_DNA.
DR EMBL; AL157903; CAI22397.1; -; Genomic_DNA.
DR EMBL; AC113949; CAI22397.1; JOINED; Genomic_DNA.
DR EMBL; AL359705; CAI22397.1; JOINED; Genomic_DNA.
DR EMBL; AL157903; CAI22398.1; -; Genomic_DNA.
DR EMBL; AC113949; CAI22398.1; JOINED; Genomic_DNA.
DR EMBL; AL359705; CAI22398.1; JOINED; Genomic_DNA.
DR EMBL; AL157903; CAI22399.1; -; Genomic_DNA.
DR EMBL; AC113949; CAI22399.1; JOINED; Genomic_DNA.
DR EMBL; AL359705; CAI22399.1; JOINED; Genomic_DNA.
DR EMBL; AL157903; CAI22401.1; -; Genomic_DNA.
DR EMBL; AC113949; CAI22401.1; JOINED; Genomic_DNA.
DR EMBL; AL359705; CAI22401.1; JOINED; Genomic_DNA.
DR EMBL; AL157903; CAI22402.1; -; Genomic_DNA.
DR EMBL; AC113949; CAI22402.1; JOINED; Genomic_DNA.
DR EMBL; AL359705; CAI22402.1; JOINED; Genomic_DNA.
DR EMBL; AL157903; CAI22403.1; -; Genomic_DNA.
DR EMBL; AC113949; CAI22403.1; JOINED; Genomic_DNA.
DR EMBL; AL359705; CAI22403.1; JOINED; Genomic_DNA.
DR EMBL; AL157903; CAI22405.1; -; Genomic_DNA.
DR EMBL; AC113949; CAI22405.1; JOINED; Genomic_DNA.
DR EMBL; AL359705; CAI22405.1; JOINED; Genomic_DNA.
DR EMBL; AL157903; CAI22406.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC113949; CAI22406.1; JOINED; Genomic_DNA.
DR EMBL; CH471059; EAX06327.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX06330.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX06333.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX06335.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX06336.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX06339.1; -; Genomic_DNA.
DR EMBL; AB018329; BAA34506.1; -; mRNA.
DR EMBL; DQ925675; ABL59902.1; -; mRNA.
DR RefSeq; NP_036434.1; NM_012302.2.
DR RefSeq; XP_005270723.1; XM_005270666.1.
DR RefSeq; XP_005270726.1; XM_005270669.1.
DR RefSeq; XP_005270727.1; XM_005270670.1.
DR RefSeq; XP_005270730.1; XM_005270673.1.
DR RefSeq; XP_005270731.1; XM_005270674.1.
DR UniGene; Hs.24212; -.
DR UniGene; Hs.649282; -.
DR ProteinModelPortal; O95490; -.
DR SMR; O95490; 30-132, 465-824.
DR IntAct; O95490; 3.
DR MINT; MINT-143559; -.
DR STRING; 9606.ENSP00000322270; -.
DR MEROPS; S63.012; -.
DR PhosphoSite; O95490; -.
DR PaxDb; O95490; -.
DR PRIDE; O95490; -.
DR Ensembl; ENST00000319517; ENSP00000322270; ENSG00000117114.
DR Ensembl; ENST00000335786; ENSP00000337306; ENSG00000117114.
DR Ensembl; ENST00000359929; ENSP00000353006; ENSG00000117114.
DR Ensembl; ENST00000370713; ENSP00000359748; ENSG00000117114.
DR Ensembl; ENST00000370715; ENSP00000359750; ENSG00000117114.
DR Ensembl; ENST00000370717; ENSP00000359752; ENSG00000117114.
DR Ensembl; ENST00000370723; ENSP00000359758; ENSG00000117114.
DR Ensembl; ENST00000370725; ENSP00000359760; ENSG00000117114.
DR Ensembl; ENST00000370728; ENSP00000359763; ENSG00000117114.
DR Ensembl; ENST00000370730; ENSP00000359765; ENSG00000117114.
DR Ensembl; ENST00000394879; ENSP00000378344; ENSG00000117114.
DR GeneID; 23266; -.
DR KEGG; hsa:23266; -.
DR UCSC; uc001diw.3; human.
DR CTD; 23266; -.
DR GeneCards; GC01P081771; -.
DR HGNC; HGNC:18582; LPHN2.
DR HPA; HPA013573; -.
DR MIM; 607018; gene.
DR neXtProt; NX_O95490; -.
DR PharmGKB; PA38589; -.
DR eggNOG; NOG253931; -.
DR HOGENOM; HOG000049065; -.
DR HOVERGEN; HBG052337; -.
DR KO; K04593; -.
DR OMA; FQMENTD; -.
DR PhylomeDB; O95490; -.
DR ChiTaRS; LPHN2; human.
DR GeneWiki; LPHN2; -.
DR GenomeRNAi; 23266; -.
DR NextBio; 45018; -.
DR PRO; PR:O95490; -.
DR ArrayExpress; O95490; -.
DR Bgee; O95490; -.
DR CleanEx; HS_LPHN2; -.
DR Genevestigator; O95490; -.
DR GO; GO:0016021; C:integral to membrane; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004930; F:G-protein coupled receptor activity; TAS:GDB.
DR GO; GO:0016524; F:latrotoxin receptor activity; NAS:UniProtKB.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IEA:InterPro.
DR InterPro; IPR022624; DUF3497.
DR InterPro; IPR017981; GPCR_2-like.
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_dom.
DR InterPro; IPR000922; Lectin_gal-bd_dom.
DR InterPro; IPR003112; Olfac-like.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF12003; DUF3497; 1.
DR Pfam; PF02140; Gal_Lectin; 1.
DR Pfam; PF01825; GPS; 1.
DR Pfam; PF02793; HRM; 1.
DR Pfam; PF02354; Latrophilin; 1.
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 PROSITE; PS00649; G_PROTEIN_RECEP_F2_1; FALSE_NEG.
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 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Complete proteome;
KW Disulfide bond; G-protein coupled receptor; Glycoprotein; Lectin;
KW Membrane; Phosphoprotein; Receptor; Reference proteome; Signal;
KW Transducer; Transmembrane; Transmembrane helix.
FT SIGNAL 1 25 Potential.
FT CHAIN 26 1459 Latrophilin-2.
FT /FTId=PRO_0000012910.
FT TOPO_DOM 39 851 Extracellular (Potential).
FT TRANSMEM 852 872 Helical; Name=1; (Potential).
FT TOPO_DOM 873 880 Cytoplasmic (Potential).
FT TRANSMEM 881 901 Helical; Name=2; (Potential).
FT TOPO_DOM 902 907 Extracellular (Potential).
FT TRANSMEM 908 928 Helical; Name=3; (Potential).
FT TOPO_DOM 929 952 Cytoplasmic (Potential).
FT TRANSMEM 953 973 Helical; Name=4; (Potential).
FT TOPO_DOM 974 990 Extracellular (Potential).
FT TRANSMEM 991 1011 Helical; Name=5; (Potential).
FT TOPO_DOM 1012 1037 Cytoplasmic (Potential).
FT TRANSMEM 1038 1058 Helical; Name=6; (Potential).
FT TOPO_DOM 1059 1062 Extracellular (Potential).
FT TRANSMEM 1063 1083 Helical; Name=7; (Potential).
FT TOPO_DOM 1084 1459 Cytoplasmic (Potential).
FT DOMAIN 41 130 SUEL-type lectin.
FT DOMAIN 135 394 Olfactomedin-like.
FT DOMAIN 784 836 GPS.
FT SITE 824 825 Cleavage (By similarity).
FT MOD_RES 1374 1374 Phosphoserine (By similarity).
FT MOD_RES 1430 1430 Phosphoserine.
FT CARBOHYD 99 99 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 331 331 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 520 520 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 629 629 N-linked (GlcNAc...).
FT CARBOHYD 731 731 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 744 744 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 787 787 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 792 792 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 813 813 N-linked (GlcNAc...) (Potential).
FT DISULFID 136 318 By similarity.
FT VAR_SEQ 595 607 Missing (in isoform 2, isoform 3, isoform
FT 4 and isoform 7).
FT /FTId=VSP_010104.
FT VAR_SEQ 1034 1034 K -> NNYRVCDGYYNTDLPG (in isoform 6 and
FT isoform 7).
FT /FTId=VSP_042267.
FT VAR_SEQ 1134 1136 SRI -> DIH (in isoform 3).
FT /FTId=VSP_010105.
FT VAR_SEQ 1137 1459 Missing (in isoform 3).
FT /FTId=VSP_010106.
FT VAR_SEQ 1167 1209 Missing (in isoform 2, isoform 4 and
FT isoform 5).
FT /FTId=VSP_010107.
FT VAR_SEQ 1210 1233 HSLNNARDTSAMDTLPLNGNFNNS -> LTSHGLRAHLQDL
FT YHLELLLGQIA (in isoform 4).
FT /FTId=VSP_010108.
FT VAR_SEQ 1234 1459 Missing (in isoform 4).
FT /FTId=VSP_010109.
FT CONFLICT 1059 1059 N -> S (in Ref. 7; ABL59902).
SQ SEQUENCE 1459 AA; 163349 MW; 30707B7C3C069029 CRC64;
MVSSGCRMRS LWFIIVISFL PNTEGFSRAA LPFGLVRREL SCEGYSIDLR CPGSDVIMIE
SANYGRTDDK ICDADPFQME NTDCYLPDAF KIMTQRCNNR TQCIVVTGSD VFPDPCPGTY
KYLEVQYECV PYIFVCPGTL KAIVDSPCIY EAEQKAGAWC KDPLQAADKI YFMPWTPYRT
DTLIEYASLE DFQNSRQTTT YKLPNRVDGT GFVVYDGAVF FNKERTRNIV KFDLRTRIKS
GEAIINYANY HDTSPYRWGG KTDIDLAVDE NGLWVIYATE QNNGMIVISQ LNPYTLRFEA
TWETVYDKRA ASNAFMICGV LYVVRSVYQD NESETGKNSI DYIYNTRLNR GEYVDVPFPN
QYQYIAAVDY NPRDNQLYVW NNNFILRYSL EFGPPDPAQV PTTAVTITSS AELFKTIIST
TSTTSQKGPM STTVAGSQEG SKGTKPPPAV STTKIPPITN IFPLPERFCE ALDSKGIKWP
QTQRGMMVER PCPKGTRGTA SYLCMISTGT WNPKGPDLSN CTSHWVNQLA QKIRSGENAA
SLANELAKHT KGPVFAGDVS SSVRLMEQLV DILDAQLQEL KPSEKDSAGR SYNKLQKREK
TCRAYLKAIV DTVDNLLRPE ALESWKHMNS SEQAHTATML LDTLEEGAFV LADNLLEPTR
VSMPTENIVL EVAVLSTEGQ IQDFKFPLGI KGAGSSIQLS ANTVKQNSRN GLAKLVFIIY
RSLGQFLSTE NATIKLGADF IGRNSTIAVN SHVISVSINK ESSRVYLTDP VLFTLPHIDP
DNYFNANCSF WNYSERTMMG YWSTQGCKLV DTNKTRTTCA CSHLTNFAIL MAHREIAYKD
GVHELLLTVI TWVGIVISLV CLAICIFTFC FFRGLQSDRN TIHKNLCINL FIAEFIFLIG
IDKTKYAIAC PIFAGLLHFF FLAAFAWMCL EGVQLYLMLV EVFESEYSRK KYYYVAGYLF
PATVVGVSAA IDYKSYGTEK ACWLHVDNYF IWSFIGPVTF IILLNIIFLV ITLCKMVKHS
NTLKPDSSRL ENIKSWVLGA FALLCLLGLT WSFGLLFINE ETIVMAYLFT IFNAFQGVFI
FIFHCALQKK VRKEYGKCFR HSYCCGGLPT ESPHSSVKAS TTRTSARYSS GTQSRIRRMW
NDTVRKQSES SFISGDINST STLNQGMTGN YLLTNPLLRP HGTNNPYNTL LAETVVCNAP
SAPVFNSPGH SLNNARDTSA MDTLPLNGNF NNSYSLHKGD YNDSVQVVDC GLSLNDTAFE
KMIISELVHN NLRGSSKTHN LELTLPVKPV IGGSSSEDDA IVADASSLMH SDNPGLELHH
KELEAPLIPQ RTHSLLYQPQ KKVKSEGTDS YVSQLTAEAE DHLQSPNRDS LYTSMPNLRD
SPYPESSPDM EEDLSPSRRS ENEDIYYKSM PNLGAGHQLQ MCYQISRGNS DGYIIPINKE
GCIPEGDVRE GQMQLVTSL
//
ID LPHN2_HUMAN Reviewed; 1459 AA.
AC O95490; A5XEI2; B1ALT8; B1ALT9; B1ALU0; B1ALU2; B1ALU4; B1ALU5;
read moreAC B1ALU6; O94882; Q5VX76; Q9UKY5; Q9UKY6;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2004, sequence version 2.
DT 22-JAN-2014, entry version 113.
DE RecName: Full=Latrophilin-2;
DE AltName: Full=Calcium-independent alpha-latrotoxin receptor 2;
DE Short=CIRL-2;
DE AltName: Full=Latrophilin homolog 1;
DE AltName: Full=Lectomedin-1;
DE Flags: Precursor;
GN Name=LPHN2; Synonyms=KIAA0786, LEC1, LPHH1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RX PubMed=10030676; DOI=10.1038/sj.onc.1202487;
RA White G.R.M., Varley J.M., Heighway J.;
RT "Isolation and characterisation of a human homologue of the
RT latrophilin gene from a region of 1p31.1 implicated in breast
RT cancer.";
RL Oncogene 17:3513-3519(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10760572; DOI=10.1016/S0167-4781(00)00020-8;
RA White G.R.M., Varley J.M., Heighway J.;
RT "Genomic structure and expression profile of LPHH1, a 7TM gene
RT variably expressed in breast cancer cell lines.";
RL Biochim. Biophys. Acta 1491:75-92(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4).
RA Hayflick J.S.;
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 439-1459 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XI.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 5:277-286(1998).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 973-1070 (ISOFORM 6).
RX PubMed=17456239; DOI=10.1186/gb-2007-8-4-r64;
RA Clark T.A., Schweitzer A.C., Chen T.X., Staples M.K., Lu G., Wang H.,
RA Williams A., Blume J.E.;
RT "Discovery of tissue-specific exons using comprehensive human exon
RT microarrays.";
RL Genome Biol. 8:R64.1-R64.16(2007).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-629, AND MASS
RP SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of
RT multiple enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1430, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Calcium-independent receptor of low affinity for alpha-
CC latrotoxin, an excitatory neurotoxin present in black widow spider
CC venom which triggers massive exocytosis from neurons and
CC neuroendocrine cells. Receptor propably implicated in the
CC regulation of exocytosis (By similarity).
CC -!- SUBUNIT: Forms a heterodimer, consisting of a large extracellular
CC region (p120) non-covalently linked to a seven-transmembrane
CC moiety (p85) (By similarity).
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1;
CC IsoId=O95490-1; Sequence=Displayed;
CC Name=2; Synonyms=Lectomedin-1 gamma;
CC IsoId=O95490-2; Sequence=VSP_010104, VSP_010107;
CC Name=3; Synonyms=Lectomedin-1 beta;
CC IsoId=O95490-3; Sequence=VSP_010104, VSP_010105, VSP_010106;
CC Name=4; Synonyms=Lectomedin-1 alpha;
CC IsoId=O95490-4; Sequence=VSP_010104, VSP_010107, VSP_010108,
CC VSP_010109;
CC Name=5;
CC IsoId=O95490-5; Sequence=VSP_010107;
CC Note=No experimental confirmation;
CC Name=6;
CC IsoId=O95490-6; Sequence=VSP_042267;
CC Name=7;
CC IsoId=O95490-7; Sequence=VSP_010104, VSP_042267;
CC Note=No experimental confirmation;
CC -!- TISSUE SPECIFICITY: Expressed very widely in all normal tissues
CC tested. Expression is variable in tumor cell lines, apparently
CC elevated in some lines and absent or markedly reduced in others.
CC -!- PTM: Proteolytically cleaved into 2 subunits, an extracellular
CC subunit and a seven-transmembrane subunit (By similarity).
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC LN-TM7 subfamily.
CC -!- SIMILARITY: Contains 1 GPS domain.
CC -!- SIMILARITY: Contains 1 olfactomedin-like domain.
CC -!- SIMILARITY: Contains 1 SUEL-type lectin domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI22406.1; Type=Erroneous gene model prediction;
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/LPHH1ID313.html";
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DR EMBL; AJ131581; CAA10458.1; -; mRNA.
DR EMBL; AJ244492; CAB60229.1; -; Genomic_DNA.
DR EMBL; AJ244493; CAB60229.1; JOINED; Genomic_DNA.
DR EMBL; AJ244494; CAB60229.1; JOINED; Genomic_DNA.
DR EMBL; AJ244496; CAB60229.1; JOINED; Genomic_DNA.
DR EMBL; AJ244497; CAB60229.1; JOINED; Genomic_DNA.
DR EMBL; AJ244498; CAB60229.1; JOINED; Genomic_DNA.
DR EMBL; AJ244499; CAB60229.1; JOINED; Genomic_DNA.
DR EMBL; AJ244501; CAB60229.1; JOINED; Genomic_DNA.
DR EMBL; AJ244502; CAB60229.1; JOINED; Genomic_DNA.
DR EMBL; AJ244503; CAB60229.1; JOINED; Genomic_DNA.
DR EMBL; AJ244504; CAB60229.1; JOINED; Genomic_DNA.
DR EMBL; AJ244505; CAB60229.1; JOINED; Genomic_DNA.
DR EMBL; AJ244506; CAB60229.1; JOINED; Genomic_DNA.
DR EMBL; AJ244507; CAB60229.1; JOINED; Genomic_DNA.
DR EMBL; AJ244510; CAB60229.1; JOINED; Genomic_DNA.
DR EMBL; AJ244511; CAB60229.1; JOINED; Genomic_DNA.
DR EMBL; AJ244512; CAB60229.1; JOINED; Genomic_DNA.
DR EMBL; AJ244516; CAB60229.1; JOINED; Genomic_DNA.
DR EMBL; AF104266; AAD54675.1; -; mRNA.
DR EMBL; AF104938; AAD54676.1; -; mRNA.
DR EMBL; AF104939; AAD54677.1; -; mRNA.
DR EMBL; AL359705; CAH71340.1; -; Genomic_DNA.
DR EMBL; AC113949; CAH71340.1; JOINED; Genomic_DNA.
DR EMBL; AL157903; CAH71340.1; JOINED; Genomic_DNA.
DR EMBL; AL359705; CAH71341.1; -; Genomic_DNA.
DR EMBL; AC113949; CAH71341.1; JOINED; Genomic_DNA.
DR EMBL; AL157903; CAH71341.1; JOINED; Genomic_DNA.
DR EMBL; AL359705; CAH71342.1; -; Genomic_DNA.
DR EMBL; AC113949; CAH71342.1; JOINED; Genomic_DNA.
DR EMBL; AL157903; CAH71342.1; JOINED; Genomic_DNA.
DR EMBL; AL359705; CAH71343.1; -; Genomic_DNA.
DR EMBL; AC113949; CAH71343.1; JOINED; Genomic_DNA.
DR EMBL; AL157903; CAH71343.1; JOINED; Genomic_DNA.
DR EMBL; AL359705; CAH71345.1; -; Genomic_DNA.
DR EMBL; AC113949; CAH71345.1; JOINED; Genomic_DNA.
DR EMBL; AL157903; CAH71345.1; JOINED; Genomic_DNA.
DR EMBL; AL359705; CAH71346.1; -; Genomic_DNA.
DR EMBL; AC113949; CAH71346.1; JOINED; Genomic_DNA.
DR EMBL; AL157903; CAH71346.1; JOINED; Genomic_DNA.
DR EMBL; AL359705; CAH71347.1; -; Genomic_DNA.
DR EMBL; AC113949; CAH71347.1; JOINED; Genomic_DNA.
DR EMBL; AL157903; CAH71347.1; JOINED; Genomic_DNA.
DR EMBL; AL157903; CAI22397.1; -; Genomic_DNA.
DR EMBL; AC113949; CAI22397.1; JOINED; Genomic_DNA.
DR EMBL; AL359705; CAI22397.1; JOINED; Genomic_DNA.
DR EMBL; AL157903; CAI22398.1; -; Genomic_DNA.
DR EMBL; AC113949; CAI22398.1; JOINED; Genomic_DNA.
DR EMBL; AL359705; CAI22398.1; JOINED; Genomic_DNA.
DR EMBL; AL157903; CAI22399.1; -; Genomic_DNA.
DR EMBL; AC113949; CAI22399.1; JOINED; Genomic_DNA.
DR EMBL; AL359705; CAI22399.1; JOINED; Genomic_DNA.
DR EMBL; AL157903; CAI22401.1; -; Genomic_DNA.
DR EMBL; AC113949; CAI22401.1; JOINED; Genomic_DNA.
DR EMBL; AL359705; CAI22401.1; JOINED; Genomic_DNA.
DR EMBL; AL157903; CAI22402.1; -; Genomic_DNA.
DR EMBL; AC113949; CAI22402.1; JOINED; Genomic_DNA.
DR EMBL; AL359705; CAI22402.1; JOINED; Genomic_DNA.
DR EMBL; AL157903; CAI22403.1; -; Genomic_DNA.
DR EMBL; AC113949; CAI22403.1; JOINED; Genomic_DNA.
DR EMBL; AL359705; CAI22403.1; JOINED; Genomic_DNA.
DR EMBL; AL157903; CAI22405.1; -; Genomic_DNA.
DR EMBL; AC113949; CAI22405.1; JOINED; Genomic_DNA.
DR EMBL; AL359705; CAI22405.1; JOINED; Genomic_DNA.
DR EMBL; AL157903; CAI22406.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC113949; CAI22406.1; JOINED; Genomic_DNA.
DR EMBL; CH471059; EAX06327.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX06330.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX06333.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX06335.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX06336.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX06339.1; -; Genomic_DNA.
DR EMBL; AB018329; BAA34506.1; -; mRNA.
DR EMBL; DQ925675; ABL59902.1; -; mRNA.
DR RefSeq; NP_036434.1; NM_012302.2.
DR RefSeq; XP_005270723.1; XM_005270666.1.
DR RefSeq; XP_005270726.1; XM_005270669.1.
DR RefSeq; XP_005270727.1; XM_005270670.1.
DR RefSeq; XP_005270730.1; XM_005270673.1.
DR RefSeq; XP_005270731.1; XM_005270674.1.
DR UniGene; Hs.24212; -.
DR UniGene; Hs.649282; -.
DR ProteinModelPortal; O95490; -.
DR SMR; O95490; 30-132, 465-824.
DR IntAct; O95490; 3.
DR MINT; MINT-143559; -.
DR STRING; 9606.ENSP00000322270; -.
DR MEROPS; S63.012; -.
DR PhosphoSite; O95490; -.
DR PaxDb; O95490; -.
DR PRIDE; O95490; -.
DR Ensembl; ENST00000319517; ENSP00000322270; ENSG00000117114.
DR Ensembl; ENST00000335786; ENSP00000337306; ENSG00000117114.
DR Ensembl; ENST00000359929; ENSP00000353006; ENSG00000117114.
DR Ensembl; ENST00000370713; ENSP00000359748; ENSG00000117114.
DR Ensembl; ENST00000370715; ENSP00000359750; ENSG00000117114.
DR Ensembl; ENST00000370717; ENSP00000359752; ENSG00000117114.
DR Ensembl; ENST00000370723; ENSP00000359758; ENSG00000117114.
DR Ensembl; ENST00000370725; ENSP00000359760; ENSG00000117114.
DR Ensembl; ENST00000370728; ENSP00000359763; ENSG00000117114.
DR Ensembl; ENST00000370730; ENSP00000359765; ENSG00000117114.
DR Ensembl; ENST00000394879; ENSP00000378344; ENSG00000117114.
DR GeneID; 23266; -.
DR KEGG; hsa:23266; -.
DR UCSC; uc001diw.3; human.
DR CTD; 23266; -.
DR GeneCards; GC01P081771; -.
DR HGNC; HGNC:18582; LPHN2.
DR HPA; HPA013573; -.
DR MIM; 607018; gene.
DR neXtProt; NX_O95490; -.
DR PharmGKB; PA38589; -.
DR eggNOG; NOG253931; -.
DR HOGENOM; HOG000049065; -.
DR HOVERGEN; HBG052337; -.
DR KO; K04593; -.
DR OMA; FQMENTD; -.
DR PhylomeDB; O95490; -.
DR ChiTaRS; LPHN2; human.
DR GeneWiki; LPHN2; -.
DR GenomeRNAi; 23266; -.
DR NextBio; 45018; -.
DR PRO; PR:O95490; -.
DR ArrayExpress; O95490; -.
DR Bgee; O95490; -.
DR CleanEx; HS_LPHN2; -.
DR Genevestigator; O95490; -.
DR GO; GO:0016021; C:integral to membrane; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004930; F:G-protein coupled receptor activity; TAS:GDB.
DR GO; GO:0016524; F:latrotoxin receptor activity; NAS:UniProtKB.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IEA:InterPro.
DR InterPro; IPR022624; DUF3497.
DR InterPro; IPR017981; GPCR_2-like.
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_dom.
DR InterPro; IPR000922; Lectin_gal-bd_dom.
DR InterPro; IPR003112; Olfac-like.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF12003; DUF3497; 1.
DR Pfam; PF02140; Gal_Lectin; 1.
DR Pfam; PF01825; GPS; 1.
DR Pfam; PF02793; HRM; 1.
DR Pfam; PF02354; Latrophilin; 1.
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 PROSITE; PS00649; G_PROTEIN_RECEP_F2_1; FALSE_NEG.
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 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Complete proteome;
KW Disulfide bond; G-protein coupled receptor; Glycoprotein; Lectin;
KW Membrane; Phosphoprotein; Receptor; Reference proteome; Signal;
KW Transducer; Transmembrane; Transmembrane helix.
FT SIGNAL 1 25 Potential.
FT CHAIN 26 1459 Latrophilin-2.
FT /FTId=PRO_0000012910.
FT TOPO_DOM 39 851 Extracellular (Potential).
FT TRANSMEM 852 872 Helical; Name=1; (Potential).
FT TOPO_DOM 873 880 Cytoplasmic (Potential).
FT TRANSMEM 881 901 Helical; Name=2; (Potential).
FT TOPO_DOM 902 907 Extracellular (Potential).
FT TRANSMEM 908 928 Helical; Name=3; (Potential).
FT TOPO_DOM 929 952 Cytoplasmic (Potential).
FT TRANSMEM 953 973 Helical; Name=4; (Potential).
FT TOPO_DOM 974 990 Extracellular (Potential).
FT TRANSMEM 991 1011 Helical; Name=5; (Potential).
FT TOPO_DOM 1012 1037 Cytoplasmic (Potential).
FT TRANSMEM 1038 1058 Helical; Name=6; (Potential).
FT TOPO_DOM 1059 1062 Extracellular (Potential).
FT TRANSMEM 1063 1083 Helical; Name=7; (Potential).
FT TOPO_DOM 1084 1459 Cytoplasmic (Potential).
FT DOMAIN 41 130 SUEL-type lectin.
FT DOMAIN 135 394 Olfactomedin-like.
FT DOMAIN 784 836 GPS.
FT SITE 824 825 Cleavage (By similarity).
FT MOD_RES 1374 1374 Phosphoserine (By similarity).
FT MOD_RES 1430 1430 Phosphoserine.
FT CARBOHYD 99 99 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 331 331 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 520 520 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 629 629 N-linked (GlcNAc...).
FT CARBOHYD 731 731 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 744 744 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 787 787 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 792 792 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 813 813 N-linked (GlcNAc...) (Potential).
FT DISULFID 136 318 By similarity.
FT VAR_SEQ 595 607 Missing (in isoform 2, isoform 3, isoform
FT 4 and isoform 7).
FT /FTId=VSP_010104.
FT VAR_SEQ 1034 1034 K -> NNYRVCDGYYNTDLPG (in isoform 6 and
FT isoform 7).
FT /FTId=VSP_042267.
FT VAR_SEQ 1134 1136 SRI -> DIH (in isoform 3).
FT /FTId=VSP_010105.
FT VAR_SEQ 1137 1459 Missing (in isoform 3).
FT /FTId=VSP_010106.
FT VAR_SEQ 1167 1209 Missing (in isoform 2, isoform 4 and
FT isoform 5).
FT /FTId=VSP_010107.
FT VAR_SEQ 1210 1233 HSLNNARDTSAMDTLPLNGNFNNS -> LTSHGLRAHLQDL
FT YHLELLLGQIA (in isoform 4).
FT /FTId=VSP_010108.
FT VAR_SEQ 1234 1459 Missing (in isoform 4).
FT /FTId=VSP_010109.
FT CONFLICT 1059 1059 N -> S (in Ref. 7; ABL59902).
SQ SEQUENCE 1459 AA; 163349 MW; 30707B7C3C069029 CRC64;
MVSSGCRMRS LWFIIVISFL PNTEGFSRAA LPFGLVRREL SCEGYSIDLR CPGSDVIMIE
SANYGRTDDK ICDADPFQME NTDCYLPDAF KIMTQRCNNR TQCIVVTGSD VFPDPCPGTY
KYLEVQYECV PYIFVCPGTL KAIVDSPCIY EAEQKAGAWC KDPLQAADKI YFMPWTPYRT
DTLIEYASLE DFQNSRQTTT YKLPNRVDGT GFVVYDGAVF FNKERTRNIV KFDLRTRIKS
GEAIINYANY HDTSPYRWGG KTDIDLAVDE NGLWVIYATE QNNGMIVISQ LNPYTLRFEA
TWETVYDKRA ASNAFMICGV LYVVRSVYQD NESETGKNSI DYIYNTRLNR GEYVDVPFPN
QYQYIAAVDY NPRDNQLYVW NNNFILRYSL EFGPPDPAQV PTTAVTITSS AELFKTIIST
TSTTSQKGPM STTVAGSQEG SKGTKPPPAV STTKIPPITN IFPLPERFCE ALDSKGIKWP
QTQRGMMVER PCPKGTRGTA SYLCMISTGT WNPKGPDLSN CTSHWVNQLA QKIRSGENAA
SLANELAKHT KGPVFAGDVS SSVRLMEQLV DILDAQLQEL KPSEKDSAGR SYNKLQKREK
TCRAYLKAIV DTVDNLLRPE ALESWKHMNS SEQAHTATML LDTLEEGAFV LADNLLEPTR
VSMPTENIVL EVAVLSTEGQ IQDFKFPLGI KGAGSSIQLS ANTVKQNSRN GLAKLVFIIY
RSLGQFLSTE NATIKLGADF IGRNSTIAVN SHVISVSINK ESSRVYLTDP VLFTLPHIDP
DNYFNANCSF WNYSERTMMG YWSTQGCKLV DTNKTRTTCA CSHLTNFAIL MAHREIAYKD
GVHELLLTVI TWVGIVISLV CLAICIFTFC FFRGLQSDRN TIHKNLCINL FIAEFIFLIG
IDKTKYAIAC PIFAGLLHFF FLAAFAWMCL EGVQLYLMLV EVFESEYSRK KYYYVAGYLF
PATVVGVSAA IDYKSYGTEK ACWLHVDNYF IWSFIGPVTF IILLNIIFLV ITLCKMVKHS
NTLKPDSSRL ENIKSWVLGA FALLCLLGLT WSFGLLFINE ETIVMAYLFT IFNAFQGVFI
FIFHCALQKK VRKEYGKCFR HSYCCGGLPT ESPHSSVKAS TTRTSARYSS GTQSRIRRMW
NDTVRKQSES SFISGDINST STLNQGMTGN YLLTNPLLRP HGTNNPYNTL LAETVVCNAP
SAPVFNSPGH SLNNARDTSA MDTLPLNGNF NNSYSLHKGD YNDSVQVVDC GLSLNDTAFE
KMIISELVHN NLRGSSKTHN LELTLPVKPV IGGSSSEDDA IVADASSLMH SDNPGLELHH
KELEAPLIPQ RTHSLLYQPQ KKVKSEGTDS YVSQLTAEAE DHLQSPNRDS LYTSMPNLRD
SPYPESSPDM EEDLSPSRRS ENEDIYYKSM PNLGAGHQLQ MCYQISRGNS DGYIIPINKE
GCIPEGDVRE GQMQLVTSL
//
MIM
607018
*RECORD*
*FIELD* NO
607018
*FIELD* TI
*607018 LATROPHILIN 2; LPHN2
;;LATROPHILIN HOMOLOG 1; LPHH1;;
LECTOMEDIN 1
*FIELD* TX
read more
CLONING
In a study of breast tumor samples, Hoggard et al. (1995) reported a
region, 1p31.1, with a high frequency of loss of heterozygosity (LOH).
To identify candidate sequences, mutation of which might contribute to
the development of breast cancer, White et al. (1998) carried out
mapping studies of ESTs localized to 1p31.1. They identified and
characterized a novel gene, which they designated LPHH1 (latrophilin
homolog-1), located adjacent to the smallest region of overlapping loss
seen in tumors. The 4,212-bp open reading frame of the 7-kb LPHH1
transcript encoded a peptide that showed approximately 65% identity to
rat latrophilin, a G-coupled, 7-transmembrane protein that binds
alpha-latrotoxin. Surprisingly, whereas expression of the rat gene was
strictly restricted to neurologic and perhaps some endocrine cells, the
human sequence appeared to be expressed widely in all normal tissues
tested. The range of transcripts encoded in a breast tumor cell line,
compared to normal breast, suggested that gene product variability was
higher in the tumor.
MAPPING
White et al. (1998) identified the LPHH1 gene on chromosome 1p31.1.
*FIELD* RF
1. Hoggard, N.; Brintell, B.; Howell, A.; Weissenbach, J.; Varley,
J.: Allelic imbalance on chromosome 1 in human breast cancer. II.
Microsatellite repeat analysis. Genes Chromosomes Cancer 12: 24-31,
1995.
2. White, G. R. M.; Varley, J. M.; Heighway, J.: Isolation and characterization
of a human homologue of the latrophilin gene from a region of 1p31.1
implicated in breast cancer. Oncogene 17: 3513-3519, 1998. Note:
Erratum: Oncogene 18: 2167 only, 1999.
*FIELD* CD
Victor A. McKusick: 6/6/2002
*FIELD* ED
carol: 12/11/2012
alopez: 6/6/2002
*RECORD*
*FIELD* NO
607018
*FIELD* TI
*607018 LATROPHILIN 2; LPHN2
;;LATROPHILIN HOMOLOG 1; LPHH1;;
LECTOMEDIN 1
*FIELD* TX
read more
CLONING
In a study of breast tumor samples, Hoggard et al. (1995) reported a
region, 1p31.1, with a high frequency of loss of heterozygosity (LOH).
To identify candidate sequences, mutation of which might contribute to
the development of breast cancer, White et al. (1998) carried out
mapping studies of ESTs localized to 1p31.1. They identified and
characterized a novel gene, which they designated LPHH1 (latrophilin
homolog-1), located adjacent to the smallest region of overlapping loss
seen in tumors. The 4,212-bp open reading frame of the 7-kb LPHH1
transcript encoded a peptide that showed approximately 65% identity to
rat latrophilin, a G-coupled, 7-transmembrane protein that binds
alpha-latrotoxin. Surprisingly, whereas expression of the rat gene was
strictly restricted to neurologic and perhaps some endocrine cells, the
human sequence appeared to be expressed widely in all normal tissues
tested. The range of transcripts encoded in a breast tumor cell line,
compared to normal breast, suggested that gene product variability was
higher in the tumor.
MAPPING
White et al. (1998) identified the LPHH1 gene on chromosome 1p31.1.
*FIELD* RF
1. Hoggard, N.; Brintell, B.; Howell, A.; Weissenbach, J.; Varley,
J.: Allelic imbalance on chromosome 1 in human breast cancer. II.
Microsatellite repeat analysis. Genes Chromosomes Cancer 12: 24-31,
1995.
2. White, G. R. M.; Varley, J. M.; Heighway, J.: Isolation and characterization
of a human homologue of the latrophilin gene from a region of 1p31.1
implicated in breast cancer. Oncogene 17: 3513-3519, 1998. Note:
Erratum: Oncogene 18: 2167 only, 1999.
*FIELD* CD
Victor A. McKusick: 6/6/2002
*FIELD* ED
carol: 12/11/2012
alopez: 6/6/2002