PTPRD_MOUSE
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 03-AUG-2022, entry version 179.
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};
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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 GlyConnect; 2445; 1 N-Linked glycan (1 site). [Q64487-10]
DR GlyConnect; 2667; 6 N-Linked glycans (1 site).
DR GlyGen; Q64487; 4 sites, 6 N-linked glycans (1 site).
DR iPTMnet; Q64487; -.
DR PhosphoSitePlus; Q64487; -.
DR jPOST; Q64487; -.
DR MaxQB; Q64487; -.
DR PaxDb; Q64487; -.
DR PeptideAtlas; Q64487; -.
DR PRIDE; 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; 146 antibodies from 26 providers.
DR DNASU; 19266; -.
DR Ensembl; ENSMUST00000107289; ENSMUSP00000102910; ENSMUSG00000028399. [Q64487-4]
DR GeneID; 19266; -.
DR KEGG; mmu:19266; -.
DR CTD; 5789; -.
DR MGI; MGI:97812; Ptprd.
DR VEuPathDB; HostDB:ENSMUSG00000028399; -.
DR eggNOG; KOG4228; Eukaryota.
DR GeneTree; ENSGT00940000153617; -.
DR InParanoid; Q64487; -.
DR OMA; ERERIKC; -.
DR OrthoDB; 220353at2759; -.
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 25 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 274 other tissues.
DR ExpressionAtlas; Q64487; baseline and differential.
DR Genevisible; Q64487; MM.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IMP:SynGO.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IDA:SynGO.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IMP: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: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; IMP: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:0097105; P:presynaptic membrane assembly; IDA:BHF-UCL.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
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:1905606; P:regulation of presynapse assembly; ISO:MGI.
DR GO; GO:0099560; P:synaptic membrane adhesion; ISO:MGI.
DR GO; GO:0099545; P:trans-synaptic signaling by trans-synaptic complex; ISO:MGI.
DR CDD; cd00063; FN3; 8.
DR CDD; cd14624; R-PTPc-D-1; 1.
DR DisProt; DP02517; -. [Q64487-12]
DR Gene3D; 2.60.40.10; -; 11.
DR Gene3D; 3.90.190.10; -; 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 Pfam; PF00041; fn3; 7.
DR Pfam; PF07679; I-set; 2.
DR Pfam; PF00102; Y_phosphatase; 2.
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; SSF48726; SSF48726; 3.
DR SUPFAM; SSF49265; SSF49265; 5.
DR SUPFAM; SSF52799; SSF52799; 2.
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.
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
