ID PTPRD_MOUSE Reviewed; 1912 AA. AC Q64487; G3X9S7; Q64486; Q64488; Q64495; Q8VBV0; DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 16-MAY-2012, sequence version 3. DT 27-MAR-2024, entry version 188. DE RecName: Full=Receptor-type tyrosine-protein phosphatase delta; DE Short=Protein-tyrosine phosphatase delta; DE Short=R-PTP-delta; DE EC=3.1.3.48; DE Flags: Precursor; GN Name=Ptprd; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), NUCLEOTIDE SEQUENCE [MRNA] OF 1-224 RP (ISOFORMS C/H/I), NUCLEOTIDE SEQUENCE [MRNA] OF 606-1018 (ISOFORMS B/C), RP AND ALTERNATIVE SPLICING (ISOFORMS A; B AND C). RC STRAIN=BALB/cJ; TISSUE=Brain; RX PubMed=8355697; DOI=10.1128/mcb.13.9.5513-5523.1993; RA Mizuno K., Hasegawa K., Katagiri T., Ogimoto M., Ichikawa T., Yakura H.; RT "MPTP delta, a putative murine homolog of HPTP delta, is expressed in RT specialized regions of the brain and in the B-cell lineage."; RL Mol. Cell. Biol. 13:5513-5523(1993). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM L). RC STRAIN=C57BL/6J, and DBA/2J; TISSUE=Brain; RX PubMed=11978849; DOI=10.1523/jneurosci.22-09-03730.2002; RA Fehr C., Shirley R.L., Belknap J.K., Crabbe J.C., Buck K.J.; RT "Congenic mapping of alcohol and pentobarbital withdrawal liability loci to RT a <1 centimorgan interval of murine chromosome 4: identification of Mpdz as RT a candidate gene."; RL J. Neurosci. 22:3730-3738(2002). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1446-1551. RC STRAIN=BALB/cJ; TISSUE=Brain; RX PubMed=7832766; DOI=10.1042/bj3050499; RA Hendriks W., Schepens J., Brugman C., Zeeuwen P., Wieringa B.; RT "A novel receptor-type protein tyrosine phosphatase with a single catalytic RT domain is specifically expressed in mouse brain."; RL Biochem. J. 305:499-504(1995). RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, and Lung; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [6] RP INTERACTION WITH IL1RAPL1, ALTERNATIVE SPLICING (ISOFORMS D/E/F/G/H/I/J/K), RP AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=21940441; DOI=10.1523/jneurosci.2136-11.2011; RA Yoshida T., Yasumura M., Uemura T., Lee S.J., Ra M., Taguchi R., RA Iwakura Y., Mishina M.; RT "IL-1 receptor accessory protein-like 1 associated with mental retardation RT and autism mediates synapse formation by trans-synaptic interaction with RT protein tyrosine phosphatase delta."; RL J. Neurosci. 31:13485-13499(2011). RN [7] {ECO:0007744|PDB:4YFD, ECO:0007744|PDB:4YFE, ECO:0007744|PDB:4YFG, ECO:0007744|PDB:4YH7, ECO:0007744|PDB:5Y32} RP X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) OF 21-1265 IN COMPLEXES WITH RP IL1RAPL1 AND IL1RAP, DISULFIDE BONDS, GLYCOSYLATION AT ASN-254 AND ASN-299, RP MUTAGENESIS OF ARG-68; ARG-189; TYR-266 AND GLU-279, FUNCTION, REGION, RP SITE, AND INTERACTION WITH IL1RAPL1 AND IL1RAP. RX PubMed=25908590; DOI=10.1038/ncomms7926; RA Yamagata A., Yoshida T., Sato Y., Goto-Ito S., Uemura T., Maeda A., RA Shiroshima T., Iwasawa-Okamoto S., Mori H., Mishina M., Fukai S.; RT "Mechanisms of splicing-dependent trans-synaptic adhesion by PTPdelta- RT IL1RAPL1/IL-1RAcP for synaptic differentiation."; RL Nat. Commun. 6:6926-6926(2015). RN [8] {ECO:0007744|PDB:4Y61} RP X-RAY CRYSTALLOGRAPHY (3.36 ANGSTROMS) OF 21-411 IN COMPLEX WITH SLITRK2, RP DISULFIDE BONDS, INTERACTION WITH SLITRK2 AND SLITRK4, REGION, RP GLYCOSYLATION AT ASN-254 AND ASN-299, MUTAGENESIS OF ARG-229 AND TYR-266, RP AND FUNCTION. RX PubMed=25989451; DOI=10.1038/srep09686; RA Yamagata A., Sato Y., Goto-Ito S., Uemura T., Maeda A., Shiroshima T., RA Yoshida T., Fukai S.; RT "Structure of Slitrk2-PTPdelta complex reveals mechanisms for splicing- RT dependent trans-synaptic adhesion."; RL Sci. Rep. 5:9686-9686(2015). CC -!- FUNCTION: Can bidirectionally induce pre- and post-synaptic CC differentiation of neurons by mediating interaction with IL1RAP and CC IL1RAPL1 trans-synaptically (PubMed:25908590). Involved in pre-synaptic CC differentiation through interaction with SLITRK2 (PubMed:25989451). CC {ECO:0000269|PubMed:25908590, ECO:0000269|PubMed:25989451}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA- CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, CC ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE- CC ProRule:PRU10044}; CC -!- SUBUNIT: Interacts with PPFIA1, PPFIA2 and PPFIA3 (By similarity). CC Interacts (via extracellular domain) with SLITRK4 (via LRR 1 and 2 CC repeats) (PubMed:25989451). Interacts with SLITRK2; induces presynaptic CC differentiation (PubMed:25989451). Interacts (via the second CC immunoglobilin domain) with IL1RAPL1 (via the first immunoglobilin CC domain); induces pre- and postsynaptic differentiation of neurons and CC synapse formation. Isoform G, isoform H, isoform I, isoform J, and CC isoform K do not interact with IL1RAPL1 (PubMed:25908590, CC PubMed:21940441). Interacts (via the third immunoglobilin domain) with CC IL1RAP (via the first immunoglobilin domain); induces pre- and CC postsynaptic differentiation of neurons (PubMed:25908590). CC {ECO:0000250|UniProtKB:P23468, ECO:0000269|PubMed:21940441, CC ECO:0000269|PubMed:25908590, ECO:0000269|PubMed:25989451}. CC -!- INTERACTION: CC Q64487; P59823: Il1rapl1; NbExp=6; IntAct=EBI-771834, EBI-5452114; CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=12; CC Comment=Additional isoforms seem to exist.; CC Name=D; Synonyms=delta; CC IsoId=Q64487-4; Sequence=Displayed; CC Name=C; CC IsoId=Q64487-1; Sequence=VSP_043549, VSP_043550, VSP_043552; CC Name=A; CC IsoId=Q64487-2; Sequence=VSP_043545, VSP_043546, VSP_043551, CC VSP_043553; CC Name=B; CC IsoId=Q64487-3; Sequence=VSP_043545, VSP_043546, VSP_043552; CC Name=E; Synonyms=delta-DelB; CC IsoId=Q64487-5; Sequence=VSP_043550; CC Name=F; Synonyms=deltaA6; CC IsoId=Q64487-6; Sequence=VSP_043548; CC Name=G; Synonyms=deltaA6-DelB; CC IsoId=Q64487-7; Sequence=VSP_043548, VSP_043550; CC Name=H; Synonyms=deltaA3; CC IsoId=Q64487-8; Sequence=VSP_043549; CC Name=I; Synonyms=deltaA3-DelB; CC IsoId=Q64487-9; Sequence=VSP_043549, VSP_043550; CC Name=J; Synonyms=delta-DelA; CC IsoId=Q64487-10; Sequence=VSP_043547; CC Name=K; Synonyms=delta-DelAB; CC IsoId=Q64487-11; Sequence=VSP_043547, VSP_043550; CC Name=L; Synonyms=delta A; CC IsoId=Q64487-12; Sequence=VSP_043551, VSP_043553; CC -!- TISSUE SPECIFICITY: Brain, kidney, heart, and some B-cell lines. CC -!- PTM: A cleavage occurs, separating the extracellular domain from the CC transmembrane segment. This process called 'ectodomain shedding' is CC thought to be involved in receptor desensitization, signal transduction CC and/or membrane localization (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. CC Receptor class 2A subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA03004.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; 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; D13903; BAA03003.1; -; mRNA. DR EMBL; D13905; BAA03005.1; -; mRNA. DR EMBL; D13904; BAA03004.1; ALT_INIT; mRNA. DR EMBL; AF326559; AAL37405.1; -; mRNA. DR EMBL; AF326560; AAL37406.1; -; mRNA. DR EMBL; AL844848; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL845517; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL929181; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; Z23051; CAA80586.1; -; mRNA. DR PIR; C54689; C54689. DR PIR; D54689; D54689. DR RefSeq; NP_035341.2; NM_011211.3. DR PDB; 4Y61; X-ray; 3.36 A; A=21-411. DR PDB; 4YFD; X-ray; 3.25 A; A=21-511. DR PDB; 4YFE; X-ray; 1.97 A; A/B=321-511. DR PDB; 4YFG; X-ray; 3.49 A; A/B=21-511. DR PDB; 4YH7; X-ray; 4.40 A; A=21-1265. DR PDB; 5XWT; X-ray; 4.18 A; A/C=20-410. DR PDB; 5XWU; X-ray; 3.16 A; A/C=20-321. DR PDB; 5Y32; X-ray; 2.70 A; A=21-318. DR PDB; 6KIP; X-ray; 1.91 A; A=1617-1912. DR PDB; 7CEG; X-ray; 3.85 A; A=21-411. DR PDBsum; 4Y61; -. DR PDBsum; 4YFD; -. DR PDBsum; 4YFE; -. DR PDBsum; 4YFG; -. DR PDBsum; 4YH7; -. DR PDBsum; 5XWT; -. DR PDBsum; 5XWU; -. DR PDBsum; 5Y32; -. DR PDBsum; 6KIP; -. DR PDBsum; 7CEG; -. DR AlphaFoldDB; Q64487; -. DR SMR; Q64487; -. DR BioGRID; 202495; 10. DR IntAct; Q64487; 4. DR STRING; 10090.ENSMUSP00000133468; -. DR GlyConnect; 2445; 1 N-Linked glycan (1 site). [Q64487-10] DR GlyConnect; 2667; 6 N-Linked glycans (1 site). DR GlyCosmos; Q64487; 4 sites, 6 glycans. DR GlyGen; Q64487; 4 sites, 6 N-linked glycans (1 site). DR iPTMnet; Q64487; -. DR PhosphoSitePlus; Q64487; -. DR SwissPalm; Q64487; -. DR jPOST; Q64487; -. DR MaxQB; Q64487; -. DR PeptideAtlas; Q64487; -. DR ProteomicsDB; 301961; -. [Q64487-4] DR ProteomicsDB; 301962; -. [Q64487-1] DR ProteomicsDB; 301963; -. [Q64487-2] DR ProteomicsDB; 301964; -. [Q64487-3] DR ProteomicsDB; 301965; -. [Q64487-5] DR ProteomicsDB; 301966; -. [Q64487-6] DR ProteomicsDB; 301967; -. [Q64487-7] DR ProteomicsDB; 301968; -. [Q64487-8] DR ProteomicsDB; 301969; -. [Q64487-9] DR ProteomicsDB; 301970; -. [Q64487-10] DR ProteomicsDB; 301971; -. [Q64487-11] DR ProteomicsDB; 301972; -. [Q64487-12] DR ABCD; Q64487; 1 sequenced antibody. DR Antibodypedia; 24342; 172 antibodies from 26 providers. DR DNASU; 19266; -. DR Ensembl; ENSMUST00000107289.9; ENSMUSP00000102910.3; ENSMUSG00000028399.19. [Q64487-4] DR GeneID; 19266; -. DR KEGG; mmu:19266; -. DR AGR; MGI:97812; -. DR CTD; 5789; -. DR MGI; MGI:97812; Ptprd. DR VEuPathDB; HostDB:ENSMUSG00000028399; -. DR eggNOG; KOG4228; Eukaryota. DR GeneTree; ENSGT00940000153617; -. DR InParanoid; Q64487; -. DR OMA; QWTISGI; -. DR OrthoDB; 2875525at2759; -. DR PhylomeDB; Q64487; -. DR Reactome; R-MMU-388844; Receptor-type tyrosine-protein phosphatases. DR Reactome; R-MMU-8849932; Synaptic adhesion-like molecules. DR BioGRID-ORCS; 19266; 0 hits in 28 CRISPR screens. DR ChiTaRS; Ptprd; mouse. DR PRO; PR:Q64487; -. DR Proteomes; UP000000589; Chromosome 4. DR RNAct; Q64487; Protein. DR Bgee; ENSMUSG00000028399; Expressed in saccule of membranous labyrinth and 275 other cell types or tissues. DR ExpressionAtlas; Q64487; baseline and differential. DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO. DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IDA:SynGO. DR GO; GO:0042734; C:presynaptic membrane; IDA:SynGO. DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO. DR GO; GO:0050839; F:cell adhesion molecule binding; IPI:BHF-UCL. DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central. DR GO; GO:0005102; F:signaling receptor binding; IPI:BHF-UCL. DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro. DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IDA:BHF-UCL. DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IDA:SynGO. DR GO; GO:0046426; P:negative regulation of receptor signaling pathway via JAK-STAT; IMP:MGI. DR GO; GO:0030182; P:neuron differentiation; IDA:BHF-UCL. DR GO; GO:0050775; P:positive regulation of dendrite morphogenesis; IDA:BHF-UCL. DR GO; GO:0051965; P:positive regulation of synapse assembly; IDA:UniProtKB. DR GO; GO:0099054; P:presynapse assembly; ISO:MGI. DR GO; GO:0097105; P:presynaptic membrane assembly; IDA:BHF-UCL. DR GO; GO:0050776; P:regulation of immune response; IMP:MGI. DR GO; GO:0099151; P:regulation of postsynaptic density assembly; IDA:SynGO. DR GO; GO:0099560; P:synaptic membrane adhesion; ISO:MGI. DR GO; GO:0099537; P:trans-synaptic signaling; IDA:SynGO. DR GO; GO:0099545; P:trans-synaptic signaling by trans-synaptic complex; ISO:MGI. DR CDD; cd00063; FN3; 8. DR CDD; cd05738; IgI_2_RPTP_IIa_LAR_like; 1. DR CDD; cd05739; IgI_3_RPTP_IIa_LAR_like; 1. DR CDD; cd14628; R-PTP-D-2; 1. DR CDD; cd14624; R-PTPc-D-1; 1. DR DisProt; DP02517; -. [Q64487-12] DR Gene3D; 2.60.40.10; Immunoglobulins; 11. DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 2. DR InterPro; IPR003961; FN3_dom. DR InterPro; IPR036116; FN3_sf. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR013098; Ig_I-set. DR InterPro; IPR003599; Ig_sub. DR InterPro; IPR003598; Ig_sub2. DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like. DR InterPro; IPR000242; PTP_cat. DR InterPro; IPR045905; R-PTP-delta_cat. DR InterPro; IPR016130; Tyr_Pase_AS. DR InterPro; IPR003595; Tyr_Pase_cat. DR InterPro; IPR000387; Tyr_Pase_dom. DR PANTHER; PTHR46957; CYTOKINE RECEPTOR; 1. DR PANTHER; PTHR46957:SF8; PROTEIN TYROSINE PHOSPHATASE RECEPTOR TYPE S; 1. DR Pfam; PF00041; fn3; 7. DR Pfam; PF07679; I-set; 1. DR Pfam; PF13927; Ig_3; 2. DR Pfam; PF00102; Y_phosphatase; 2. DR PRINTS; PR00014; FNTYPEIII. DR PRINTS; PR00700; PRTYPHPHTASE. DR SMART; SM00060; FN3; 8. DR SMART; SM00409; IG; 4. DR SMART; SM00408; IGc2; 3. DR SMART; SM00194; PTPc; 2. DR SMART; SM00404; PTPc_motif; 2. DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 2. DR SUPFAM; SSF49265; Fibronectin type III; 5. DR SUPFAM; SSF48726; Immunoglobulin; 3. DR PROSITE; PS50853; FN3; 8. DR PROSITE; PS50835; IG_LIKE; 3. DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 2. DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 2. DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2. DR Genevisible; Q64487; MM. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Disulfide bond; Glycoprotein; KW Hydrolase; Immunoglobulin domain; Membrane; Protein phosphatase; Receptor; KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1..20 FT /evidence="ECO:0000255" FT CHAIN 21..1912 FT /note="Receptor-type tyrosine-protein phosphatase delta" FT /id="PRO_0000025438" FT TOPO_DOM 21..1266 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 1267..1287 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 1288..1912 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 24..114 FT /note="Ig-like C2-type 1" FT DOMAIN 126..224 FT /note="Ig-like C2-type 2" FT DOMAIN 236..318 FT /note="Ig-like C2-type 3" FT DOMAIN 325..415 FT /note="Fibronectin type-III 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 420..516 FT /note="Fibronectin type-III 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 518..607 FT /note="Fibronectin type-III 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 612..709 FT /note="Fibronectin type-III 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 714..822 FT /note="Fibronectin type-III 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 823..916 FT /note="Fibronectin type-III 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 921..1016 FT /note="Fibronectin type-III 7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 1020..1106 FT /note="Fibronectin type-III 8" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 1357..1612 FT /note="Tyrosine-protein phosphatase 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160" FT DOMAIN 1644..1903 FT /note="Tyrosine-protein phosphatase 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160" FT REGION 181..189 FT /note="Mini-exon peptide A9; sufficient for interaction FT with IL1RAPL1" FT /evidence="ECO:0000269|PubMed:21940441, FT ECO:0000269|PubMed:25908590" FT REGION 227..230 FT /note="Mini-exon peptide B; required for interaction with FT SLITRK2 and in the function in pre-synaptic FT differentiation; Acts as an adjustable linker to control FT relative positions and orientations of the PTPRD second and FT third immunoglobilin domains for their simultaneous FT interactions with the first immunoglobilin domain of FT IL1RAPL1 and IL1RAP; Modulates affinity for IL1RAPL1 and FT IL1RAP" FT /evidence="ECO:0000269|PubMed:25908590, FT ECO:0000269|PubMed:25989451" FT REGION 1298..1319 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 1553 FT /note="Phosphocysteine intermediate" FT /evidence="ECO:0000250" FT ACT_SITE 1844 FT /note="Phosphocysteine intermediate" FT /evidence="ECO:0000250" FT BINDING 1521 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 1553..1559 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 1597 FT /ligand="substrate" FT /evidence="ECO:0000250" FT SITE 266 FT /note="Required for interaction with IL1RAP" FT /evidence="ECO:0000269|PubMed:25908590" FT SITE 1181..1182 FT /note="Cleavage" FT /evidence="ECO:0000250" FT CARBOHYD 254 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255, ECO:0000269|PubMed:25908590, FT ECO:0000269|PubMed:25989451, ECO:0007744|PDB:4Y61, FT ECO:0007744|PDB:4YFD, ECO:0007744|PDB:4YFG" FT CARBOHYD 299 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255, ECO:0000269|PubMed:25908590, FT ECO:0000269|PubMed:25989451, ECO:0007744|PDB:4Y61, FT ECO:0007744|PDB:4YFD, ECO:0007744|PDB:4YFG" FT CARBOHYD 724 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 832 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 45..98 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:25908590, ECO:0000269|PubMed:25989451, FT ECO:0007744|PDB:4Y61, ECO:0007744|PDB:4YFD, FT ECO:0007744|PDB:4YFG, ECO:0007744|PDB:4YH7, FT ECO:0007744|PDB:5Y32" FT DISULFID 147..207 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:25908590, ECO:0000269|PubMed:25989451, FT ECO:0007744|PDB:4Y61, ECO:0007744|PDB:4YFD, FT ECO:0007744|PDB:4YFG, ECO:0007744|PDB:5Y32" FT DISULFID 257..302 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:25908590, ECO:0000269|PubMed:25989451, FT ECO:0007744|PDB:4Y61, ECO:0007744|PDB:4YFD, FT ECO:0007744|PDB:4YFG, ECO:0007744|PDB:4YH7" FT VAR_SEQ 1 FT /note="M -> MCLTSCFILASHMLSCDLVFVP (in isoform A and FT isoform B)" FT /evidence="ECO:0000303|PubMed:8355697" FT /id="VSP_043545" FT VAR_SEQ 2..230 FT /note="Missing (in isoform A and isoform B)" FT /evidence="ECO:0000303|PubMed:8355697" FT /id="VSP_043546" FT VAR_SEQ 181..189 FT /note="Missing (in isoform J and isoform K)" FT /evidence="ECO:0000305" FT /id="VSP_043547" FT VAR_SEQ 181..183 FT /note="Missing (in isoform F and isoform G)" FT /evidence="ECO:0000305" FT /id="VSP_043548" FT VAR_SEQ 184..189 FT /note="Missing (in isoform C, isoform H and isoform I)" FT /evidence="ECO:0000305" FT /id="VSP_043549" FT VAR_SEQ 227..230 FT /note="Missing (in isoform C, isoform E, isoform G, isoform FT I and isoform K)" FT /evidence="ECO:0000305" FT /id="VSP_043550" FT VAR_SEQ 608..1018 FT /note="Missing (in isoform A and isoform L)" FT /evidence="ECO:0000303|PubMed:11978849, FT ECO:0000303|PubMed:8355697" FT /id="VSP_043551" FT VAR_SEQ 775..783 FT /note="Missing (in isoform B and isoform C)" FT /evidence="ECO:0000305" FT /id="VSP_043552" FT VAR_SEQ 1019 FT /note="V -> M (in isoform A and isoform L)" FT /evidence="ECO:0000303|PubMed:11978849, FT ECO:0000303|PubMed:8355697" FT /id="VSP_043553" FT MUTAGEN 68 FT /note="R->A: Reduces affinity with IL1RAPL1. Reduces the FT synaptogenic activity to ~7%." FT /evidence="ECO:0000269|PubMed:25908590" FT MUTAGEN 189 FT /note="R->A: Decreases affinity for interaction with FT IL1RAPL1." FT /evidence="ECO:0000269|PubMed:25908590" FT MUTAGEN 229 FT /note="R->E: Abolishes interaction with SLITRK2." FT /evidence="ECO:0000269|PubMed:25989451" FT MUTAGEN 266 FT /note="Y->A: No effect on interaction with SLITRK2. FT Decreases the affinity for IL1RAPL1. Abolishes interaction FT with IL1RAP." FT /evidence="ECO:0000269|PubMed:25908590, FT ECO:0000269|PubMed:25989451" FT MUTAGEN 279 FT /note="E->A: Decreases affinity for IL1RAP." FT /evidence="ECO:0000269|PubMed:25908590" FT CONFLICT 5 FT /note="A -> R (in Ref. 1; BAA03004)" FT /evidence="ECO:0000305" FT CONFLICT 349 FT /note="E -> G (in Ref. 1; BAA03003)" FT /evidence="ECO:0000305" FT CONFLICT 416 FT /note="A -> T (in Ref. 1; BAA03003)" FT /evidence="ECO:0000305" FT CONFLICT 551 FT /note="Y -> D (in Ref. 1; BAA03003)" FT /evidence="ECO:0000305" FT CONFLICT 588 FT /note="R -> T (in Ref. 1; BAA03003)" FT /evidence="ECO:0000305" FT CONFLICT 657 FT /note="F -> Y (in Ref. 1; BAA03005)" FT /evidence="ECO:0000305" FT CONFLICT 663..666 FT /note="LGIP -> IGNS (in Ref. 1; BAA03005)" FT /evidence="ECO:0000305" FT CONFLICT 696 FT /note="G -> W (in Ref. 1; BAA03005)" FT /evidence="ECO:0000305" FT CONFLICT 761..763 FT /note="GQP -> SA (in Ref. 1; BAA03005)" FT /evidence="ECO:0000305" FT CONFLICT 822 FT /note="A -> S (in Ref. 1; BAA03005)" FT /evidence="ECO:0000305" FT CONFLICT 852 FT /note="Missing (in Ref. 1; BAA03005)" FT /evidence="ECO:0000305" FT CONFLICT 1001 FT /note="G -> R (in Ref. 1; BAA03005)" FT /evidence="ECO:0000305" FT CONFLICT 1004 FT /note="P -> A (in Ref. 1; BAA03005)" FT /evidence="ECO:0000305" FT CONFLICT 1046..1055 FT /note="SAMPFKILYD -> PAILSKFFMMM (in Ref. 1; BAA03003)" FT /evidence="ECO:0000305" FT CONFLICT 1084 FT /note="V -> A (in Ref. 1; BAA03003)" FT /evidence="ECO:0000305" FT CONFLICT 1298 FT /note="E -> D (in Ref. 1; BAA03003)" FT /evidence="ECO:0000305" FT CONFLICT 1447..1448 FT /note="RS -> E (in Ref. 1; BAA03003)" FT /evidence="ECO:0000305" FT CONFLICT 1491..1502 FT /note="ATYCVRTFALYK -> HILCPDICTLN (in Ref. 1; BAA03003)" FT /evidence="ECO:0000305" FT CONFLICT 1510 FT /note="E -> K (in Ref. 1; BAA03003)" FT /evidence="ECO:0000305" FT CONFLICT 1531..1542 FT /note="FLAFLRRVKTCN -> VPSFLTESQNLH (in Ref. 1; BAA03003)" FT /evidence="ECO:0000305" FT CONFLICT 1684 FT /note="T -> G (in Ref. 1; BAA03003)" FT /evidence="ECO:0000305" FT CONFLICT 1786..1795 FT /note="EFKVTDARDG -> NSRSRMPGI (in Ref. 1; BAA03003)" FT /evidence="ECO:0000305" FT STRAND 22..28 FT /evidence="ECO:0007829|PDB:5Y32" FT STRAND 33..36 FT /evidence="ECO:0007829|PDB:5Y32" FT STRAND 41..51 FT /evidence="ECO:0007829|PDB:5Y32" FT STRAND 54..59 FT /evidence="ECO:0007829|PDB:5Y32" FT STRAND 69..73 FT /evidence="ECO:0007829|PDB:5Y32" FT STRAND 75..84 FT /evidence="ECO:0007829|PDB:5Y32" FT TURN 89..91 FT /evidence="ECO:0007829|PDB:5Y32" FT STRAND 94..101 FT /evidence="ECO:0007829|PDB:5Y32" FT STRAND 106..116 FT /evidence="ECO:0007829|PDB:5Y32" FT TURN 118..120 FT /evidence="ECO:0007829|PDB:5Y32" FT STRAND 127..130 FT /evidence="ECO:0007829|PDB:5Y32" FT STRAND 135..138 FT /evidence="ECO:0007829|PDB:5Y32" FT STRAND 143..150 FT /evidence="ECO:0007829|PDB:5Y32" FT STRAND 156..161 FT /evidence="ECO:0007829|PDB:5Y32" FT STRAND 174..179 FT /evidence="ECO:0007829|PDB:5Y32" FT STRAND 184..186 FT /evidence="ECO:0007829|PDB:5Y32" FT STRAND 188..194 FT /evidence="ECO:0007829|PDB:5Y32" FT HELIX 199..201 FT /evidence="ECO:0007829|PDB:5Y32" FT STRAND 203..211 FT /evidence="ECO:0007829|PDB:5Y32" FT STRAND 214..217 FT /evidence="ECO:0007829|PDB:5Y32" FT STRAND 221..226 FT /evidence="ECO:0007829|PDB:5Y32" FT STRAND 234..240 FT /evidence="ECO:0007829|PDB:5XWU" FT STRAND 245..247 FT /evidence="ECO:0007829|PDB:5XWU" FT STRAND 252..263 FT /evidence="ECO:0007829|PDB:5XWU" FT STRAND 266..271 FT /evidence="ECO:0007829|PDB:5XWU" FT STRAND 274..277 FT /evidence="ECO:0007829|PDB:5XWU" FT STRAND 284..293 FT /evidence="ECO:0007829|PDB:5XWU" FT STRAND 298..306 FT /evidence="ECO:0007829|PDB:5XWU" FT STRAND 309..319 FT /evidence="ECO:0007829|PDB:5XWU" FT STRAND 330..334 FT /evidence="ECO:0007829|PDB:4YFE" FT STRAND 339..342 FT /evidence="ECO:0007829|PDB:4YFE" FT STRAND 353..360 FT /evidence="ECO:0007829|PDB:4YFE" FT STRAND 368..373 FT /evidence="ECO:0007829|PDB:4YFE" FT STRAND 375..380 FT /evidence="ECO:0007829|PDB:4YFE" FT STRAND 388..396 FT /evidence="ECO:0007829|PDB:4YFE" FT STRAND 401..404 FT /evidence="ECO:0007829|PDB:4YFE" FT STRAND 408..411 FT /evidence="ECO:0007829|PDB:4YFE" FT STRAND 422..432 FT /evidence="ECO:0007829|PDB:4YFE" FT STRAND 434..439 FT /evidence="ECO:0007829|PDB:4YFE" FT STRAND 450..457 FT /evidence="ECO:0007829|PDB:4YFE" FT HELIX 463..465 FT /evidence="ECO:0007829|PDB:4YFE" FT STRAND 466..473 FT /evidence="ECO:0007829|PDB:4YFE" FT STRAND 475..479 FT /evidence="ECO:0007829|PDB:4YFE" FT STRAND 487..495 FT /evidence="ECO:0007829|PDB:4YFE" FT STRAND 507..510 FT /evidence="ECO:0007829|PDB:4YFE" FT HELIX 1622..1624 FT /evidence="ECO:0007829|PDB:6KIP" FT HELIX 1625..1633 FT /evidence="ECO:0007829|PDB:6KIP" FT HELIX 1643..1650 FT /evidence="ECO:0007829|PDB:6KIP" FT TURN 1651..1653 FT /evidence="ECO:0007829|PDB:6KIP" FT HELIX 1663..1665 FT /evidence="ECO:0007829|PDB:6KIP" FT HELIX 1667..1672 FT /evidence="ECO:0007829|PDB:6KIP" FT HELIX 1682..1684 FT /evidence="ECO:0007829|PDB:6KIP" FT TURN 1695..1698 FT /evidence="ECO:0007829|PDB:6KIP" FT STRAND 1701..1705 FT /evidence="ECO:0007829|PDB:6KIP" FT STRAND 1708..1710 FT /evidence="ECO:0007829|PDB:6KIP" FT STRAND 1714..1718 FT /evidence="ECO:0007829|PDB:6KIP" FT HELIX 1722..1724 FT /evidence="ECO:0007829|PDB:6KIP" FT HELIX 1725..1734 FT /evidence="ECO:0007829|PDB:6KIP" FT STRAND 1739..1742 FT /evidence="ECO:0007829|PDB:6KIP" FT STRAND 1746..1748 FT /evidence="ECO:0007829|PDB:6KIP" FT STRAND 1751..1754 FT /evidence="ECO:0007829|PDB:6KIP" FT STRAND 1760..1762 FT /evidence="ECO:0007829|PDB:6KIP" FT STRAND 1764..1766 FT /evidence="ECO:0007829|PDB:6KIP" FT STRAND 1769..1779 FT /evidence="ECO:0007829|PDB:6KIP" FT STRAND 1782..1791 FT /evidence="ECO:0007829|PDB:6KIP" FT TURN 1792..1794 FT /evidence="ECO:0007829|PDB:6KIP" FT STRAND 1797..1805 FT /evidence="ECO:0007829|PDB:6KIP" FT STRAND 1810..1812 FT /evidence="ECO:0007829|PDB:6KIP" FT HELIX 1818..1833 FT /evidence="ECO:0007829|PDB:6KIP" FT STRAND 1840..1849 FT /evidence="ECO:0007829|PDB:6KIP" FT HELIX 1850..1867 FT /evidence="ECO:0007829|PDB:6KIP" FT STRAND 1868..1870 FT /evidence="ECO:0007829|PDB:6KIP" FT HELIX 1872..1880 FT /evidence="ECO:0007829|PDB:6KIP" FT HELIX 1890..1904 FT /evidence="ECO:0007829|PDB:6KIP" FT HELIX 1908..1910 FT /evidence="ECO:0007829|PDB:6KIP" SQ SEQUENCE 1912 AA; 214410 MW; DEF494AA5A2CE814 CRC64; MVPVARPLSL LLTFFLCACA ETPPRFTRTP VDQTGVSGGV ASFICQATGD PRPKIVWNKK GKKVSNQRFE VIEFDDGSGS VLRIQPLRTP RDEAIYECVA SNNVGEISVS TRLTVLREDQ IPRGFPTIDM GPQLKVVERT RTATMLCAAS GNPDPEITWF KDFLPVDTSN NNGRIKQLRS ESIGGTPIRG ALQIEQSEES DQGKYECVAT NSAGTRYSAP ANLYVRELRE VRRVPPRFSI PPTNHEIMPG GSVNITCVAV GSPMPYVKWM LGAEDLTPED DMPIGRNVLE LNDVRQSANY TCVAMSTLGV IEAIAQITVK ALPKPPGTPV VTESTATSIT LTWDSGNPEP VSYYIIQHKP KNSEEPYKEI DGIATTRYSV AGLSPYSDYE FRVVAVNNIG RGPASEPVLT QTSEQAPSSA PRDVQARMLS STTILVQWKE PEEPNGQIQG YRVYYTMDPT QHVNNWMKHN VADSQITTIG NLVPQKTYSV KVLAFTSIGD GPLSSDIQVI TQTGVPGQPL NFKAEPESET SILLSWTPPR SDTIASYELV YRDGDQGEEQ RITIEPGTSY RLQGLKPNSL YYFRLSARSP QGLGASTAEI SARTMQSKPS APPQDISCTS PSSTSILVSW QPPPVEKQNG IITEYSLKYA AVDGEDFKPH EILGIPSDTT KYLLEQLEKW TEYRITVTAH TDVGPGPESL SVLIRTDEDV PSGPPRKVEV EAVNATAVKV SWRSPVPNKQ HGQIRGYQVH YVKMENGEPK GQPMLKDVML ADAQWEFDDT TEHDMIISGL QPETSYSLTV TAYTTKGDGA RSKPKLVSTT GAVPGKPRLV INHTQMNTAL IQWHPPVDTF GPLQGYRLKF GRKDMEPLTT LEFSEKEDHF TATDIHKGAS YVFRLSARNK VGFGEEMVKE ISVPEEIPTG FPQNLHSEGT TSTSVQLSWQ PPVLAERNGV ITKYTLLYRD INVPLLPMEH LIVPADTSMT LTGLKSDTTY DVKVRAHTSK GPGPYSPSVQ FRTLPVDQVF AKNFHVKAVM KTSVLLSWEI PENYNSAMPF KILYDDGKMV EEVDGRATQK LIVNLKPEKS YSFVLTNRGN SAGGLQHRVT AKTAPDVLRT KPAFIGKTNL DGMITVQLPD VPANENIKGY YIIIVPLKKS RGKFIKPWES PDEMELDELL KEISRKRRSI RYGREVELKP YIAAHFDVLP TEFTLGDDKH YGGFTNKQLQ SGQEYVFFVL AVMDHAESKM YATSPYSDPV VSMDLDPQPI TDEEEGLIWV VGPVLAVVFI ICIVIAILLY KRKRAESESR KSSLPNSKEV PSHHPTDPVE LRRLNFQTPG MASHPPIPIL ELADHIERLK ANDNLKFSQE YESIDPGQQF TWEHSNLEVN KPKNRYANVI AYDHSRVLLS AIEGIPGSDY VNANYIDGYR KQNAYIATQG SLPETFGDFW RMIWEQRSAT VVMMTKLEER SRVKCDQYWP SRGTETHGLV QVTLLDTVEL ATYCVRTFAL YKNGSSEKRE VRQFQFTAWP DHGVPEHPTP FLAFLRRVKT CNPPDAGPMV VHCSAGVGRT GCFIVIDAML ERIKHEKTVD IYGHVTLMRA QRNYMVQTED QYIFIHDALL EAVTCGNTEV PARNLYAYIQ KLTQIETGEN VTGMELEFKR LASSKAHTSR FISANLPCNK FKNRLVNIMP YESTRVCLQP IRGVEGSDYI NASFLDGYRQ QKAYIATQGP LAETTEDFWR MLWEHNSTIV VMLTKLREMG REKCHQYWPA ERSARYQYFV VDPMAEYNMP QYILREFKVT DARDGQSRTV RQFQFTDWPE QGVPKSGEGF IDFIGQVHKT KEQFGQDGPI SVHCSAGVGR TGVFITLSIV LERMRYEGVV DIFQTVKMLR TQRPAMVQTE DQYQFCYRAA LEYLGSFDHY AT //