ID AGRL2_HUMAN Reviewed; 1459 AA. AC O95490; A5XEI2; B1ALT8; B1ALT9; B1ALU0; B1ALU2; B1ALU4; B1ALU5; AC B1ALU6; O94882; Q5VX76; Q9UKY5; Q9UKY6; DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 26-APR-2004, sequence version 2. DT 13-FEB-2019, entry version 162. DE RecName: Full=Adhesion G protein-coupled receptor L2 {ECO:0000303|PubMed:25713288}; DE AltName: Full=Calcium-independent alpha-latrotoxin receptor 2; DE Short=CIRL-2; DE AltName: Full=Latrophilin homolog 1; DE AltName: Full=Latrophilin-2; DE AltName: Full=Lectomedin-1; DE Flags: Precursor; GN Name=ADGRL2 {ECO:0000312|HGNC:HGNC:18582}; GN Synonyms=KIAA0786, LEC1, LPHH1, LPHN2; 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. 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 IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1430, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [12] RP VARIANT THR-467. RX PubMed=23647072; DOI=10.1111/epi.12201; RA Veeramah K.R., Johnstone L., Karafet T.M., Wolf D., Sprissler R., RA Salogiannis J., Barth-Maron A., Greenberg M.E., Stuhlmann T., RA Weinert S., Jentsch T.J., Pazzi M., Restifo L.L., Talwar D., RA Erickson R.P., Hammer M.F.; RT "Exome sequencing reveals new causal mutations in children with RT epileptic encephalopathies."; RL Epilepsia 54:1270-1281(2013). RN [13] RP NOMENCLATURE. RX PubMed=25713288; DOI=10.1124/pr.114.009647; RA Hamann J., Aust G., Arac D., Engel F.B., Formstone C., Fredriksson R., RA Hall R.A., Harty B.L., Kirchhoff C., Knapp B., Krishnan A., RA Liebscher I., Lin H.H., Martinelli D.C., Monk K.R., Peeters M.C., RA Piao X., Promel S., Schoneberg T., Schwartz T.W., Singer K., RA Stacey M., Ushkaryov Y.A., Vallon M., Wolfrum U., Wright M.W., Xu L., RA Langenhan T., Schioth H.B.; RT "International union of basic and clinical pharmacology. XCIV. RT Adhesion G protein-coupled receptors."; RL Pharmacol. Rev. 67:338-367(2015). 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 probably implicated in the CC regulation of exocytosis. {ECO:0000250|UniProtKB:O88923}. CC -!- SUBUNIT: Forms a heterodimer, consisting of a large extracellular CC region non-covalently linked to a seven-transmembrane moiety. CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane CC protein {ECO:0000255}. 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 {ECO:0000269|PubMed:10030676}. CC -!- PTM: Proteolytically cleaved into 2 subunits, an extracellular CC subunit and a seven-transmembrane subunit. CC {ECO:0000250|UniProtKB:O88917}. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family. CC Adhesion G-protein coupled receptor (ADGR) subfamily. CC {ECO:0000305}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology CC and Haematology; CC URL="http://atlasgeneticsoncology.org/Genes/LPHH1ID313.html"; 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; 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; AC113949; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL157903; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL359705; -; NOT_ANNOTATED_CDS; 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 CCDS; CCDS689.1; -. [O95490-2] DR CCDS; CCDS72811.1; -. [O95490-4] DR CCDS; CCDS76174.1; -. [O95490-3] DR CCDS; CCDS81345.1; -. [O95490-5] DR RefSeq; NP_001284633.1; NM_001297704.1. [O95490-2] DR RefSeq; NP_001284634.1; NM_001297705.1. [O95490-4] DR RefSeq; NP_001284635.1; NM_001297706.1. [O95490-3] DR RefSeq; NP_001317574.1; NM_001330645.1. [O95490-5] DR RefSeq; NP_036434.1; NM_012302.3. [O95490-2] DR RefSeq; XP_005270723.1; XM_005270666.4. [O95490-1] DR RefSeq; XP_016856276.1; XM_017000787.1. DR UniGene; Hs.24212; -. DR UniGene; Hs.406863; -. DR UniGene; Hs.649282; -. DR ProteinModelPortal; O95490; -. DR SMR; O95490; -. DR BioGrid; 116868; 13. DR IntAct; O95490; 9. DR MINT; O95490; -. DR STRING; 9606.ENSP00000322270; -. DR MEROPS; P02.009; -. DR GlyConnect; 994; -. DR iPTMnet; O95490; -. DR PhosphoSitePlus; O95490; -. DR BioMuta; ADGRL2; -. DR EPD; O95490; -. DR jPOST; O95490; -. DR MaxQB; O95490; -. DR PaxDb; O95490; -. DR PeptideAtlas; O95490; -. DR PRIDE; O95490; -. DR ProteomicsDB; 50917; -. DR ProteomicsDB; 50918; -. [O95490-2] DR ProteomicsDB; 50919; -. [O95490-3] DR ProteomicsDB; 50920; -. [O95490-4] DR ProteomicsDB; 50921; -. [O95490-5] DR ProteomicsDB; 50922; -. [O95490-6] DR ProteomicsDB; 50923; -. [O95490-7] DR Ensembl; ENST00000319517; ENSP00000322270; ENSG00000117114. [O95490-2] DR Ensembl; ENST00000359929; ENSP00000353006; ENSG00000117114. [O95490-2] DR Ensembl; ENST00000370713; ENSP00000359748; ENSG00000117114. [O95490-3] DR Ensembl; ENST00000370715; ENSP00000359750; ENSG00000117114. [O95490-4] DR Ensembl; ENST00000370717; ENSP00000359752; ENSG00000117114. [O95490-1] DR Ensembl; ENST00000370723; ENSP00000359758; ENSG00000117114. [O95490-7] DR Ensembl; ENST00000370725; ENSP00000359760; ENSG00000117114. [O95490-6] DR Ensembl; ENST00000370728; ENSP00000359763; ENSG00000117114. [O95490-1] DR Ensembl; ENST00000370730; ENSP00000359765; ENSG00000117114. [O95490-5] DR GeneID; 23266; -. DR KEGG; hsa:23266; -. DR UCSC; uc001dit.5; human. [O95490-1] DR CTD; 23266; -. DR DisGeNET; 23266; -. DR EuPathDB; HostDB:ENSG00000117114.19; -. DR GeneCards; ADGRL2; -. DR HGNC; HGNC:18582; ADGRL2. DR HPA; HPA043447; -. DR MIM; 607018; gene. DR neXtProt; NX_O95490; -. DR OpenTargets; ENSG00000117114; -. DR PharmGKB; PA38589; -. DR eggNOG; KOG3545; Eukaryota. DR eggNOG; KOG4193; Eukaryota. DR eggNOG; KOG4729; Eukaryota. DR eggNOG; ENOG410XSD2; LUCA. DR GeneTree; ENSGT00940000156348; -. DR HOGENOM; HOG000049065; -. DR HOVERGEN; HBG052337; -. DR InParanoid; O95490; -. DR KO; K04593; -. DR OMA; LQMYYQI; -. DR PhylomeDB; O95490; -. DR TreeFam; TF351999; -. DR ChiTaRS; ADGRL2; human. DR GeneWiki; LPHN2; -. DR GenomeRNAi; 23266; -. DR PRO; PR:O95490; -. DR Proteomes; UP000005640; Chromosome 1. DR Bgee; ENSG00000117114; Expressed in 103 organ(s), highest expression level in right lung. DR ExpressionAtlas; O95490; baseline and differential. DR Genevisible; O95490; HS. DR GO; GO:0016021; C:integral component of membrane; TAS:GDB. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0043005; C:neuron projection; IBA:GO_Central. DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW. DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central. DR GO; GO:0016524; F:latrotoxin receptor activity; NAS:UniProtKB. DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central. DR GO; GO:0007420; P:brain development; IBA:GO_Central. DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro. DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:GDB. DR Gene3D; 4.10.1240.10; -; 1. DR InterPro; IPR032471; GAIN_dom_N. DR InterPro; IPR017981; GPCR_2-like. DR InterPro; IPR036445; GPCR_2_extracell_dom_sf. 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. DR InterPro; IPR031240; Latrophilin-2. DR InterPro; IPR000922; Lectin_gal-bd_dom. DR InterPro; IPR003112; Olfac-like_dom. DR PANTHER; PTHR12011:SF61; PTHR12011:SF61; 1. 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 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 SUPFAM; SSF111418; SSF111418; 1. 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; Complete proteome; Disulfide bond; KW G-protein coupled receptor; Glycoprotein; Lectin; Membrane; KW Phosphoprotein; Polymorphism; Receptor; Reference proteome; Signal; KW Transducer; Transmembrane; Transmembrane helix. FT SIGNAL 1 25 {ECO:0000255}. FT CHAIN 26 1459 Adhesion G protein-coupled receptor L2. FT /FTId=PRO_0000012910. FT TOPO_DOM 26 851 Extracellular. {ECO:0000305}. FT TRANSMEM 852 872 Helical; Name=1. {ECO:0000255}. FT TOPO_DOM 873 880 Cytoplasmic. {ECO:0000305}. FT TRANSMEM 881 901 Helical; Name=2. {ECO:0000255}. FT TOPO_DOM 902 907 Extracellular. {ECO:0000305}. FT TRANSMEM 908 928 Helical; Name=3. {ECO:0000255}. FT TOPO_DOM 929 952 Cytoplasmic. {ECO:0000305}. FT TRANSMEM 953 973 Helical; Name=4. {ECO:0000255}. FT TOPO_DOM 974 990 Extracellular. {ECO:0000305}. FT TRANSMEM 991 1011 Helical; Name=5. {ECO:0000255}. FT TOPO_DOM 1012 1037 Cytoplasmic. {ECO:0000305}. FT TRANSMEM 1038 1058 Helical; Name=6. {ECO:0000255}. FT TOPO_DOM 1059 1062 Extracellular. {ECO:0000305}. FT TRANSMEM 1063 1083 Helical; Name=7. {ECO:0000255}. FT TOPO_DOM 1084 1459 Cytoplasmic. {ECO:0000305}. FT DOMAIN 41 130 SUEL-type lectin. {ECO:0000255|PROSITE- FT ProRule:PRU00260}. FT DOMAIN 135 394 Olfactomedin-like. {ECO:0000255|PROSITE- FT ProRule:PRU00446}. FT DOMAIN 784 836 GPS. {ECO:0000255|PROSITE- FT ProRule:PRU00098}. FT SITE 824 825 Cleavage. {ECO:0000250}. FT MOD_RES 1374 1374 Phosphoserine. FT {ECO:0000250|UniProtKB:Q8JZZ7}. FT MOD_RES 1409 1409 Phosphoserine. FT {ECO:0000250|UniProtKB:Q8JZZ7}. FT MOD_RES 1430 1430 Phosphoserine. FT {ECO:0000244|PubMed:21406692, FT ECO:0000244|PubMed:24275569}. FT CARBOHYD 99 99 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 331 331 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 520 520 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 629 629 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:19159218}. FT CARBOHYD 731 731 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 744 744 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 787 787 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 792 792 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 813 813 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 136 318 {ECO:0000255|PROSITE-ProRule:PRU00446}. FT VAR_SEQ 595 607 Missing (in isoform 2, isoform 3, isoform FT 4 and isoform 7). FT {ECO:0000303|PubMed:10030676, FT ECO:0000303|Ref.3}. FT /FTId=VSP_010104. FT VAR_SEQ 1034 1034 K -> NNYRVCDGYYNTDLPG (in isoform 6 and FT isoform 7). FT {ECO:0000303|PubMed:17456239}. FT /FTId=VSP_042267. FT VAR_SEQ 1134 1136 SRI -> DIH (in isoform 3). FT {ECO:0000303|Ref.3}. FT /FTId=VSP_010105. FT VAR_SEQ 1137 1459 Missing (in isoform 3). FT {ECO:0000303|Ref.3}. FT /FTId=VSP_010106. FT VAR_SEQ 1167 1209 Missing (in isoform 2, isoform 4 and FT isoform 5). {ECO:0000303|PubMed:10030676, FT ECO:0000303|Ref.3}. FT /FTId=VSP_010107. FT VAR_SEQ 1210 1233 HSLNNARDTSAMDTLPLNGNFNNS -> LTSHGLRAHLQDL FT YHLELLLGQIA (in isoform 4). FT {ECO:0000303|Ref.3}. FT /FTId=VSP_010108. FT VAR_SEQ 1234 1459 Missing (in isoform 4). FT {ECO:0000303|Ref.3}. FT /FTId=VSP_010109. FT VARIANT 467 467 R -> T (found in a child with sporadic FT epilepsy; unknown pathological FT significance). FT {ECO:0000269|PubMed:23647072}. FT /FTId=VAR_077836. FT CONFLICT 1059 1059 N -> S (in Ref. 7; ABL59902). FT {ECO:0000305}. 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 //