PTPRD_HUMAN
ID PTPRD_HUMAN Reviewed; 1912 AA.
AC P23468; B1ALA0; F5GWT7; Q3KPJ0; Q3KPJ1; Q3KPJ2;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 222.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CLEAVAGE SITE, AND MUTAGENESIS OF
RP ARG-1178 AND ARG-1181.
RX PubMed=7896816; DOI=10.1074/jbc.270.12.6722;
RA Pulido R., Krueger N.X., Serra-Pages C., Saito H., Streuli M.;
RT "Molecular characterization of the human transmembrane protein-tyrosine
RT phosphatase delta. Evidence for tissue-specific expression of alternative
RT human transmembrane protein-tyrosine phosphatase delta isoforms.";
RL J. Biol. Chem. 270:6722-6728(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4; 5 AND 6).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 390-1912.
RC TISSUE=Placenta;
RX PubMed=2170109; DOI=10.1002/j.1460-2075.1990.tb07523.x;
RA Krueger N.X., Streuli M., Saito H.;
RT "Structural diversity and evolution of human receptor-like protein tyrosine
RT phosphatases.";
RL EMBO J. 9:3241-3252(1990).
RN [5]
RP INTERACTION WITH PPFIA1; PPFIA2 AND PPFIA3.
RX PubMed=9624153; DOI=10.1074/jbc.273.25.15611;
RA Serra-Pages C., Medley Q.G., Tang M., Hart A., Streuli M.;
RT "Liprins, a family of LAR transmembrane protein-tyrosine phosphatase-
RT interacting proteins.";
RL J. Biol. Chem. 273:15611-15620(1998).
RN [6]
RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA Hillman R.T., Green R.E., Brenner S.E.;
RT "An unappreciated role for RNA surveillance.";
RL Genome Biol. 5:R8.1-R8.16(2004).
RN [7]
RP STRUCTURE BY NMR OF 405-607.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the second and third FN3 domain of human receptor-
RT type tyrosine-protein phosphatase delta.";
RL Submitted (OCT-2006) to the PDB data bank.
RN [8]
RP VARIANTS [LARGE SCALE ANALYSIS] GLN-28; PRO-276 AND ALA-901.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Can bidirectionally induce pre- and post-synaptic
CC differentiation of neurons by mediating interaction with IL1RAP and
CC IL1RAPL1 trans-synaptically. Involved in pre-synaptic differentiation
CC through interaction with SLITRK2. {ECO:0000250|UniProtKB:Q64487}.
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 (PubMed:9624153).
CC Interacts (via extracellular domain) with SLITRK4 (via LRR 1 and 2
CC repeats). Interacts with SLITRK2; induces presynaptic differentiation.
CC Interacts (via the second immunoglobilin domain) with IL1RAPL1 (via the
CC first immunoglobilin domain); induces pre- and postsynaptic
CC differentiation of neurons and synapse formation. Interacts (via the
CC third immunoglobilin domain) with IL1RAP (via the first immunoglobilin
CC domain); induces pre- and postsynaptic differentiation of neurons (By
CC similarity). {ECO:0000250|UniProtKB:Q64487,
CC ECO:0000269|PubMed:9624153}.
CC -!- INTERACTION:
CC P23468; O14965: AURKA; NbExp=2; IntAct=EBI-2682990, EBI-448680;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=P23468-1; Sequence=Displayed;
CC Name=2; Synonyms=Kidney;
CC IsoId=P23468-2; Sequence=VSP_005147, VSP_005148, VSP_005149;
CC Name=3; Synonyms=Fetal brain;
CC IsoId=P23468-3; Sequence=VSP_005150;
CC Name=4;
CC IsoId=P23468-4; Sequence=VSP_043384, VSP_043385, VSP_043386,
CC VSP_043387, VSP_043390;
CC Name=5;
CC IsoId=P23468-5; Sequence=VSP_043386, VSP_043387, VSP_043388;
CC Name=6;
CC IsoId=P23468-6; Sequence=VSP_043386, VSP_043387, VSP_043389;
CC Name=7;
CC IsoId=P23468-7; Sequence=VSP_054220, VSP_054221, VSP_043388;
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. {ECO:0000269|PubMed:7896816}.
CC -!- MISCELLANEOUS: [Isoform 1]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 2A subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/PTPRDID41927ch9p23.html";
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DR EMBL; L38929; AAC41749.1; -; mRNA.
DR EMBL; AL137125; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL356584; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL445926; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL583805; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL590397; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL133479; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL135790; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL137069; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL137851; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL157826; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL353638; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL353733; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL354722; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL356054; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL390723; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL391864; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL441884; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL451130; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL513422; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL590307; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL591133; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL591622; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL596451; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL669908; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC106713; AAI06714.1; -; mRNA.
DR EMBL; BC106714; AAI06715.1; -; mRNA.
DR EMBL; BC106715; AAI06716.1; -; mRNA.
DR EMBL; X54133; CAA38068.1; -; mRNA.
DR CCDS; CCDS43786.1; -. [P23468-1]
DR CCDS; CCDS55288.1; -. [P23468-7]
DR CCDS; CCDS55289.1; -. [P23468-4]
DR CCDS; CCDS55290.1; -. [P23468-6]
DR CCDS; CCDS6472.2; -. [P23468-5]
DR PIR; A56178; A56178.
DR RefSeq; NP_001164496.1; NM_001171025.1. [P23468-4]
DR RefSeq; NP_002830.1; NM_002839.3. [P23468-1]
DR RefSeq; NP_569075.2; NM_130391.3. [P23468-5]
DR RefSeq; NP_569076.2; NM_130392.3. [P23468-6]
DR RefSeq; XP_006716895.1; XM_006716832.3. [P23468-4]
DR RefSeq; XP_006716896.1; XM_006716833.3. [P23468-5]
DR RefSeq; XP_006716898.1; XM_006716835.3. [P23468-7]
DR RefSeq; XP_011516294.1; XM_011517992.2. [P23468-1]
DR RefSeq; XP_016870480.1; XM_017014991.1. [P23468-6]
DR PDB; 1X5Z; NMR; -; A=506-607.
DR PDB; 2DLH; NMR; -; A=407-514.
DR PDB; 2YD6; X-ray; 1.35 A; A=21-226.
DR PDB; 2YD7; X-ray; 1.98 A; A/B=21-226.
DR PDB; 4RCA; X-ray; 2.99 A; A=21-322.
DR PDB; 5WY8; X-ray; 3.07 A; A=21-318.
DR PDB; 5XNP; X-ray; 3.73 A; D/E=21-320.
DR PDB; 6X3A; X-ray; 1.77 A; A=607-916.
DR PDBsum; 1X5Z; -.
DR PDBsum; 2DLH; -.
DR PDBsum; 2YD6; -.
DR PDBsum; 2YD7; -.
DR PDBsum; 4RCA; -.
DR PDBsum; 5WY8; -.
DR PDBsum; 5XNP; -.
DR PDBsum; 6X3A; -.
DR AlphaFoldDB; P23468; -.
DR SMR; P23468; -.
DR BioGRID; 111753; 127.
DR DIP; DIP-17023N; -.
DR IntAct; P23468; 63.
DR MINT; P23468; -.
DR STRING; 9606.ENSP00000370593; -.
DR GuidetoPHARMACOLOGY; 1853; -.
DR DEPOD; PTPRD; -.
DR GlyGen; P23468; 4 sites.
DR iPTMnet; P23468; -.
DR PhosphoSitePlus; P23468; -.
DR BioMuta; PTPRD; -.
DR DMDM; 1709906; -.
DR EPD; P23468; -.
DR jPOST; P23468; -.
DR MassIVE; P23468; -.
DR MaxQB; P23468; -.
DR PaxDb; P23468; -.
DR PeptideAtlas; P23468; -.
DR PRIDE; P23468; -.
DR ProteomicsDB; 24215; -.
DR ProteomicsDB; 54101; -. [P23468-1]
DR ProteomicsDB; 54102; -. [P23468-2]
DR ProteomicsDB; 54103; -. [P23468-3]
DR ProteomicsDB; 54104; -. [P23468-4]
DR ProteomicsDB; 54105; -. [P23468-5]
DR ProteomicsDB; 54106; -. [P23468-6]
DR ABCD; P23468; 1 sequenced antibody.
DR Antibodypedia; 24342; 146 antibodies from 26 providers.
DR DNASU; 5789; -.
DR Ensembl; ENST00000355233.9; ENSP00000347373.5; ENSG00000153707.19. [P23468-6]
DR Ensembl; ENST00000356435.9; ENSP00000348812.5; ENSG00000153707.19. [P23468-1]
DR Ensembl; ENST00000381196.9; ENSP00000370593.3; ENSG00000153707.19. [P23468-1]
DR Ensembl; ENST00000397606.7; ENSP00000380731.3; ENSG00000153707.19. [P23468-4]
DR Ensembl; ENST00000397611.7; ENSP00000380735.3; ENSG00000153707.19. [P23468-7]
DR Ensembl; ENST00000486161.5; ENSP00000417093.1; ENSG00000153707.19. [P23468-5]
DR Ensembl; ENST00000540109.5; ENSP00000438164.1; ENSG00000153707.19. [P23468-1]
DR Ensembl; ENST00000634556.2; ENSP00000489063.1; ENSG00000282932.4. [P23468-1]
DR Ensembl; ENST00000634583.1; ENSP00000489509.1; ENSG00000282932.4. [P23468-5]
DR Ensembl; ENST00000634608.1; ENSP00000489257.1; ENSG00000282932.4. [P23468-1]
DR Ensembl; ENST00000635012.1; ENSP00000489439.1; ENSG00000282932.4. [P23468-1]
DR Ensembl; ENST00000635279.1; ENSP00000488982.1; ENSG00000282932.4. [P23468-4]
DR Ensembl; ENST00000635611.1; ENSP00000489155.1; ENSG00000282932.4. [P23468-7]
DR Ensembl; ENST00000635613.1; ENSP00000489038.1; ENSG00000282932.4. [P23468-6]
DR GeneID; 5789; -.
DR KEGG; hsa:5789; -.
DR MANE-Select; ENST00000381196.9; ENSP00000370593.3; NM_002839.4; NP_002830.1.
DR UCSC; uc003zkp.4; human. [P23468-1]
DR CTD; 5789; -.
DR DisGeNET; 5789; -.
DR GeneCards; PTPRD; -.
DR HGNC; HGNC:9668; PTPRD.
DR HPA; ENSG00000153707; Tissue enhanced (brain).
DR MIM; 601598; gene.
DR neXtProt; NX_P23468; -.
DR OpenTargets; ENSG00000153707; -.
DR PharmGKB; PA34013; -.
DR VEuPathDB; HostDB:ENSG00000153707; -.
DR eggNOG; KOG4228; Eukaryota.
DR GeneTree; ENSGT00940000153617; -.
DR HOGENOM; CLU_001645_4_3_1; -.
DR InParanoid; P23468; -.
DR OMA; ERERIKC; -.
DR OrthoDB; 220353at2759; -.
DR PhylomeDB; P23468; -.
DR TreeFam; TF312900; -.
DR BRENDA; 3.1.3.48; 2681.
DR PathwayCommons; P23468; -.
DR Reactome; R-HSA-388844; Receptor-type tyrosine-protein phosphatases.
DR Reactome; R-HSA-8849932; Synaptic adhesion-like molecules.
DR SignaLink; P23468; -.
DR SIGNOR; P23468; -.
DR BioGRID-ORCS; 5789; 9 hits in 1063 CRISPR screens.
DR ChiTaRS; PTPRD; human.
DR EvolutionaryTrace; P23468; -.
DR GeneWiki; PTPRD; -.
DR GenomeRNAi; 5789; -.
DR Pharos; P23468; Tbio.
DR PRO; PR:P23468; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; P23468; protein.
DR Bgee; ENSG00000153707; Expressed in cortical plate and 94 other tissues.
DR ExpressionAtlas; P23468; baseline and differential.
DR Genevisible; P23468; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISS:BHF-UCL.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0005102; F:signaling receptor binding; ISS:BHF-UCL.
DR GO; GO:0005001; F:transmembrane receptor protein tyrosine phosphatase activity; TAS:ProtInc.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; ISS:BHF-UCL.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IEA:Ensembl.
DR GO; GO:0046426; P:negative regulation of receptor signaling pathway via JAK-STAT; IEA:Ensembl.
DR GO; GO:0030182; P:neuron differentiation; ISS:BHF-UCL.
DR GO; GO:0006796; P:phosphate-containing compound metabolic process; NAS:ProtInc.
DR GO; GO:0050775; P:positive regulation of dendrite morphogenesis; ISS:BHF-UCL.
DR GO; GO:0051965; P:positive regulation of synapse assembly; ISS:UniProtKB.
DR GO; GO:0097105; P:presynaptic membrane assembly; ISS:BHF-UCL.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR GO; GO:0050776; P:regulation of immune response; IEA:Ensembl.
DR GO; GO:0099151; P:regulation of postsynaptic density assembly; IEA:Ensembl.
DR GO; GO:1905606; P:regulation of presynapse assembly; IDA:SynGO.
DR GO; GO:0099560; P:synaptic membrane adhesion; IDA:SynGO.
DR GO; GO:0099545; P:trans-synaptic signaling by trans-synaptic complex; IDA:SynGO.
DR GO; GO:0007185; P:transmembrane receptor protein tyrosine phosphatase signaling pathway; TAS:ProtInc.
DR CDD; cd00063; FN3; 8.
DR CDD; cd14624; R-PTPc-D-1; 1.
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_0000025437"
FT TOPO_DOM 21..1265
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1266..1290
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1291..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 180..189
FT /note="Interaction with IL1RAPL1"
FT /evidence="ECO:0000250"
FT REGION 181..189
FT /note="Mini-exon peptide A9; sufficient for interaction
FT with IL1RAPL1"
FT /evidence="ECO:0000250|UniProtKB:Q64487"
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:0000250|UniProtKB:Q64487"
FT REGION 603..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1298..1318
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:0000250|UniProtKB:Q64487"
FT SITE 1181..1182
FT /note="Cleavage"
FT /evidence="ECO:0000305"
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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 DISULFID 147..207
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 257..302
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 181..189
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_005147"
FT VAR_SEQ 181..183
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000305"
FT /id="VSP_054220"
FT VAR_SEQ 184..189
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043384"
FT VAR_SEQ 226..229
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_005148"
FT VAR_SEQ 227..230
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043385"
FT VAR_SEQ 608..1019
FT /note="KPSAPPQDISCTSPSSTSILVSWQPPPVEKQNGIITEYSIKYTAVDGEDDKP
FT HEILGIPSDTTKYLLEQLEKWTEYRITVTAHTDVGPGPESLSVLIRTNEDVPSGPPRKV
FT EVEAVNSTSVKVSWRSPVPNKQHGQIRGYQVHYVRMENGEPKGQPMLKDVMLADAQWEF
FT DDTTEHDMIISGLQPETSYSLTVTAYTTKGDGARSKPKLVSTTGAVPGKPRLVINHTQM
FT NTALIQWHPPVDTFGPLQGYRLKFGRKDMEPLTTLEFSEKEDHFTATDIHKGASYVFRL
FT SARNKVGFGEEMVKEISIPEEVPTGFPQNLHSEGTTSTSVQLSWQPPVLAERNGIITKY
FT TLLYRDINIPLLPMEQLIVPADTTMTLTGLKPDTTYDVKVRAHTSKGPGPYSPSVQFRT
FT LPVDQV -> M (in isoform 7)"
FT /evidence="ECO:0000305"
FT /id="VSP_054221"
FT VAR_SEQ 608
FT /note="K -> M (in isoform 4, isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043386"
FT VAR_SEQ 609..1137
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_005150"
FT VAR_SEQ 609..1019
FT /note="Missing (in isoform 4, isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043387"
FT VAR_SEQ 775..783
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_005149"
FT VAR_SEQ 1291
FT /note="K -> KSKPD (in isoform 5 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043388"
FT VAR_SEQ 1291
FT /note="K -> KSSKPD (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043389"
FT VAR_SEQ 1330
FT /note="G -> GSDDSGYPGNLHSSS (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043390"
FT VARIANT 28
FT /note="R -> Q (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs1353675904)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035645"
FT VARIANT 276
FT /note="L -> P (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035646"
FT VARIANT 447
FT /note="Q -> E (in dbSNP:rs10977171)"
FT /id="VAR_024581"
FT VARIANT 901
FT /note="V -> A (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035647"
FT VARIANT 995
FT /note="R -> C (in dbSNP:rs35929428)"
FT /id="VAR_061761"
FT VARIANT 1078
FT /note="E -> D (in dbSNP:rs7869444)"
FT /id="VAR_051761"
FT MUTAGEN 1178
FT /note="R->A: 2.5-fold reduction in cleavage. 10-fold
FT reduction in cleavage; when associated with A-1181."
FT /evidence="ECO:0000269|PubMed:7896816"
FT MUTAGEN 1181
FT /note="R->A: No reduction in cleavage. 10-fold reduction in
FT cleavage; when associated with A-1178."
FT /evidence="ECO:0000269|PubMed:7896816"
FT STRAND 22..28
FT /evidence="ECO:0007829|PDB:2YD6"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:2YD6"
FT STRAND 41..51
FT /evidence="ECO:0007829|PDB:2YD6"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:2YD6"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:2YD6"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:2YD6"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:2YD6"
FT TURN 89..92
FT /evidence="ECO:0007829|PDB:2YD6"
FT STRAND 94..102
FT /evidence="ECO:0007829|PDB:2YD6"
FT STRAND 105..116
FT /evidence="ECO:0007829|PDB:2YD6"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:2YD6"
FT STRAND 127..130
FT /evidence="ECO:0007829|PDB:2YD6"
FT STRAND 135..138
FT /evidence="ECO:0007829|PDB:2YD6"
FT STRAND 143..150
FT /evidence="ECO:0007829|PDB:2YD6"
FT STRAND 156..161
FT /evidence="ECO:0007829|PDB:2YD6"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:4RCA"
FT STRAND 175..180
FT /evidence="ECO:0007829|PDB:2YD6"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:4RCA"
FT STRAND 190..194
FT /evidence="ECO:0007829|PDB:2YD6"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:2YD6"
FT STRAND 203..211
FT /evidence="ECO:0007829|PDB:2YD6"
FT STRAND 214..217
FT /evidence="ECO:0007829|PDB:2YD6"
FT STRAND 221..226
FT /evidence="ECO:0007829|PDB:2YD6"
FT STRAND 234..240
FT /evidence="ECO:0007829|PDB:4RCA"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:4RCA"
FT STRAND 251..263
FT /evidence="ECO:0007829|PDB:4RCA"
FT STRAND 266..271
FT /evidence="ECO:0007829|PDB:4RCA"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:4RCA"
FT STRAND 284..294
FT /evidence="ECO:0007829|PDB:4RCA"
FT STRAND 298..306
FT /evidence="ECO:0007829|PDB:4RCA"
FT STRAND 309..319
FT /evidence="ECO:0007829|PDB:4RCA"
FT STRAND 422..426
FT /evidence="ECO:0007829|PDB:2DLH"
FT STRAND 430..433
FT /evidence="ECO:0007829|PDB:2DLH"
FT STRAND 436..439
FT /evidence="ECO:0007829|PDB:2DLH"
FT STRAND 448..454
FT /evidence="ECO:0007829|PDB:2DLH"
FT TURN 463..465
FT /evidence="ECO:0007829|PDB:2DLH"
FT STRAND 475..477
FT /evidence="ECO:0007829|PDB:2DLH"
FT STRAND 487..498
FT /evidence="ECO:0007829|PDB:2DLH"
FT STRAND 507..510
FT /evidence="ECO:0007829|PDB:2DLH"
FT STRAND 520..525
FT /evidence="ECO:0007829|PDB:1X5Z"
FT STRAND 527..537
FT /evidence="ECO:0007829|PDB:1X5Z"
FT STRAND 546..549
FT /evidence="ECO:0007829|PDB:1X5Z"
FT STRAND 551..556
FT /evidence="ECO:0007829|PDB:1X5Z"
FT STRAND 566..573
FT /evidence="ECO:0007829|PDB:1X5Z"
FT STRAND 580..583
FT /evidence="ECO:0007829|PDB:1X5Z"
FT STRAND 585..588
FT /evidence="ECO:0007829|PDB:1X5Z"
FT STRAND 593..596
FT /evidence="ECO:0007829|PDB:1X5Z"
FT STRAND 600..603
FT /evidence="ECO:0007829|PDB:1X5Z"
FT STRAND 614..622
FT /evidence="ECO:0007829|PDB:6X3A"
FT STRAND 625..631
FT /evidence="ECO:0007829|PDB:6X3A"
FT HELIX 635..637
FT /evidence="ECO:0007829|PDB:6X3A"
FT STRAND 644..652
FT /evidence="ECO:0007829|PDB:6X3A"
FT STRAND 660..666
FT /evidence="ECO:0007829|PDB:6X3A"
FT STRAND 671..674
FT /evidence="ECO:0007829|PDB:6X3A"
FT STRAND 682..690
FT /evidence="ECO:0007829|PDB:6X3A"
FT STRAND 695..698
FT /evidence="ECO:0007829|PDB:6X3A"
FT STRAND 702..705
FT /evidence="ECO:0007829|PDB:6X3A"
FT STRAND 716..724
FT /evidence="ECO:0007829|PDB:6X3A"
FT STRAND 727..733
FT /evidence="ECO:0007829|PDB:6X3A"
FT HELIX 737..739
FT /evidence="ECO:0007829|PDB:6X3A"
FT STRAND 746..755
FT /evidence="ECO:0007829|PDB:6X3A"
FT STRAND 764..769
FT /evidence="ECO:0007829|PDB:6X3A"
FT HELIX 772..774
FT /evidence="ECO:0007829|PDB:6X3A"
FT TURN 776..780
FT /evidence="ECO:0007829|PDB:6X3A"
FT STRAND 783..787
FT /evidence="ECO:0007829|PDB:6X3A"
FT STRAND 795..804
FT /evidence="ECO:0007829|PDB:6X3A"
FT STRAND 807..811
FT /evidence="ECO:0007829|PDB:6X3A"
FT STRAND 815..818
FT /evidence="ECO:0007829|PDB:6X3A"
FT STRAND 828..834
FT /evidence="ECO:0007829|PDB:6X3A"
FT TURN 835..837
FT /evidence="ECO:0007829|PDB:6X3A"
FT STRAND 838..844
FT /evidence="ECO:0007829|PDB:6X3A"
FT STRAND 855..862
FT /evidence="ECO:0007829|PDB:6X3A"
FT STRAND 869..874
FT /evidence="ECO:0007829|PDB:6X3A"
FT STRAND 879..883
FT /evidence="ECO:0007829|PDB:6X3A"
FT STRAND 890..898
FT /evidence="ECO:0007829|PDB:6X3A"
FT STRAND 907..912
FT /evidence="ECO:0007829|PDB:6X3A"
SQ SEQUENCE 1912 AA; 214760 MW; 3AE8CBCD32182E26 CRC64;
MVHVARLLLL LLTFFLRTDA 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
KNSEELYKEI DGVATTRYSV AGLSPYSDYE FRVVAVNNIG RGPPSEPVLT QTSEQAPSSA
PRDVQARMLS STTILVQWKE PEEPNGQIQG YRVYYTMDPT QHVNNWMKHN VADSQITTIG
NLVPQKTYSV KVLAFTSIGD GPLSSDIQVI TQTGVPGQPL NFKAEPESET SILLSWTPPR
SDTIANYELV YKDGEHGEEQ RITIEPGTSY RLQGLKPNSL YYFRLAARSP QGLGASTAEI
SARTMQSKPS APPQDISCTS PSSTSILVSW QPPPVEKQNG IITEYSIKYT AVDGEDDKPH
EILGIPSDTT KYLLEQLEKW TEYRITVTAH TDVGPGPESL SVLIRTNEDV PSGPPRKVEV
EAVNSTSVKV SWRSPVPNKQ HGQIRGYQVH YVRMENGEPK GQPMLKDVML ADAQWEFDDT
TEHDMIISGL QPETSYSLTV TAYTTKGDGA RSKPKLVSTT GAVPGKPRLV INHTQMNTAL
IQWHPPVDTF GPLQGYRLKF GRKDMEPLTT LEFSEKEDHF TATDIHKGAS YVFRLSARNK
VGFGEEMVKE ISIPEEVPTG FPQNLHSEGT TSTSVQLSWQ PPVLAERNGI ITKYTLLYRD
INIPLLPMEQ LIVPADTTMT LTGLKPDTTY DVKVRAHTSK GPGPYSPSVQ FRTLPVDQVF
AKNFHVKAVM KTSVLLSWEI PENYNSAMPF KILYDDGKMV EEVDGRATQK LIVNLKPEKS
YSFVLTNRGN SAGGLQHRVT AKTAPDVLRT KPAFIGKTNL DGMITVQLPE VPANENIKGY
YIIIVPLKKS RGKFIKPWES PDEMELDELL KEISRKRRSI RYGREVELKP YIAAHFDVLP
TEFTLGDDKH YGGFTNKQLQ SGQEYVFFVL AVMEHAESKM YATSPYSDPV VSMDLDPQPI
TDEEEGLIWV VGPVLAVVFI ICIVIAILLY KRKRAESDSR KSSIPNNKEI 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 NASFIDGYRQ QKAYIATQGP LAETTEDFWR MLWEHNSTIV
VMLTKLREMG REKCHQYWPA ERSARYQYFV VDPMAEYNMP QYILREFKVT DARDGQSRTV
RQFQFTDWPE QGVPKSGEGF IDFIGQVHKT KEQFGQDGPI SVHCSAGVGR TGVFITLSIV
LERMRYEGVV DIFQTVKMLR TQRPAMVQTE DQYQFSYRAA LEYLGSFDHY AT
