PTPRD
Receptor-type tyrosine-protein phosphatase delta
Also known as: HPTP, PTPD, PTPRD_HUMAN
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- P23468
- Gene
- PTPRD
- Ensembl
- ENSG00000153707
- Chromosome
- 9
- Canonical length
- 1912 aa
- Protein class
- Enzymes, Plasma proteins, Predicted intracellular proteins, Predicted membrane proteins
- Subcellular location
- Nucleoplasm,Vesicles
- Secretome location
- Intracellular and membrane
OverviewNCBI Gene
The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP contains an extracellular region, a single transmembrane segment and two tandem intracytoplasmic catalytic domains, and thus represents a receptor-type PTP. The extracellular region of this protein is composed of three Ig-like and eight fibronectin type III-like domains. Studies of the similar genes in chicken and fly suggest the role of this PTP is in promoting neurite growth, and regulating neurons axon guidance. Multiple alternatively spliced transcript variants of this gene have been reported. A related pseudogene has been identified on chromosome 5. [provided by RefSeq, Jan 2010]
Canonical amino-acid sequenceUniProt
1912 residues, UniProt reviewed canonical sequence.
>P23468|PTPRD
1 MVHVARLLLL LLTFFLRTDA ETPPRFTRTP VDQTGVSGGV ASFICQATGD PRPKIVWNKK
61 GKKVSNQRFE VIEFDDGSGS VLRIQPLRTP RDEAIYECVA SNNVGEISVS TRLTVLREDQ
121 IPRGFPTIDM GPQLKVVERT RTATMLCAAS GNPDPEITWF KDFLPVDTSN NNGRIKQLRS
181 ESIGGTPIRG ALQIEQSEES DQGKYECVAT NSAGTRYSAP ANLYVRELRE VRRVPPRFSI
241 PPTNHEIMPG GSVNITCVAV GSPMPYVKWM LGAEDLTPED DMPIGRNVLE LNDVRQSANY
301 TCVAMSTLGV IEAIAQITVK ALPKPPGTPV VTESTATSIT LTWDSGNPEP VSYYIIQHKP
361 KNSEELYKEI DGVATTRYSV AGLSPYSDYE FRVVAVNNIG RGPPSEPVLT QTSEQAPSSA
421 PRDVQARMLS STTILVQWKE PEEPNGQIQG YRVYYTMDPT QHVNNWMKHN VADSQITTIG
481 NLVPQKTYSV KVLAFTSIGD GPLSSDIQVI TQTGVPGQPL NFKAEPESET SILLSWTPPR
541 SDTIANYELV YKDGEHGEEQ RITIEPGTSY RLQGLKPNSL YYFRLAARSP QGLGASTAEI
601 SARTMQSKPS APPQDISCTS PSSTSILVSW QPPPVEKQNG IITEYSIKYT AVDGEDDKPH
661 EILGIPSDTT KYLLEQLEKW TEYRITVTAH TDVGPGPESL SVLIRTNEDV PSGPPRKVEV
721 EAVNSTSVKV SWRSPVPNKQ HGQIRGYQVH YVRMENGEPK GQPMLKDVML ADAQWEFDDT
781 TEHDMIISGL QPETSYSLTV TAYTTKGDGA RSKPKLVSTT GAVPGKPRLV INHTQMNTAL
841 IQWHPPVDTF GPLQGYRLKF GRKDMEPLTT LEFSEKEDHF TATDIHKGAS YVFRLSARNK
901 VGFGEEMVKE ISIPEEVPTG FPQNLHSEGT TSTSVQLSWQ PPVLAERNGI ITKYTLLYRD
961 INIPLLPMEQ LIVPADTTMT LTGLKPDTTY DVKVRAHTSK GPGPYSPSVQ FRTLPVDQVF
1021 AKNFHVKAVM KTSVLLSWEI PENYNSAMPF KILYDDGKMV EEVDGRATQK LIVNLKPEKS
1081 YSFVLTNRGN SAGGLQHRVT AKTAPDVLRT KPAFIGKTNL DGMITVQLPE VPANENIKGY
1141 YIIIVPLKKS RGKFIKPWES PDEMELDELL KEISRKRRSI RYGREVELKP YIAAHFDVLP
1201 TEFTLGDDKH YGGFTNKQLQ SGQEYVFFVL AVMEHAESKM YATSPYSDPV VSMDLDPQPI
1261 TDEEEGLIWV VGPVLAVVFI ICIVIAILLY KRKRAESDSR KSSIPNNKEI PSHHPTDPVE
1321 LRRLNFQTPG MASHPPIPIL ELADHIERLK ANDNLKFSQE YESIDPGQQF TWEHSNLEVN
1381 KPKNRYANVI AYDHSRVLLS AIEGIPGSDY VNANYIDGYR KQNAYIATQG SLPETFGDFW
1441 RMIWEQRSAT VVMMTKLEER SRVKCDQYWP SRGTETHGLV QVTLLDTVEL ATYCVRTFAL
1501 YKNGSSEKRE VRQFQFTAWP DHGVPEHPTP FLAFLRRVKT CNPPDAGPMV VHCSAGVGRT
1561 GCFIVIDAML ERIKHEKTVD IYGHVTLMRA QRNYMVQTED QYIFIHDALL EAVTCGNTEV
1621 PARNLYAYIQ KLTQIETGEN VTGMELEFKR LASSKAHTSR FISANLPCNK FKNRLVNIMP
1681 YESTRVCLQP IRGVEGSDYI NASFIDGYRQ QKAYIATQGP LAETTEDFWR MLWEHNSTIV
1741 VMLTKLREMG REKCHQYWPA ERSARYQYFV VDPMAEYNMP QYILREFKVT DARDGQSRTV
1801 RQFQFTDWPE QGVPKSGEGF IDFIGQVHKT KEQFGQDGPI SVHCSAGVGR TGVFITLSIV
1861 LERMRYEGVV DIFQTVKMLR TQRPAMVQTE DQYQFSYRAA LEYLGSFDHY ATLocalizationUniProt · AlphaFold · HPA
Whether an antibody against PTPRD can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.
- Antibody reachability
- Cell surface
- Secreted
- No
- Transmembrane segments
- 1
- Mean surface accessibility (rSASA)
- 0.28
- Highest tissue expression
- 39 nTPM
Expression across tissuesHPA
Tissue
- spinal cord: 39 nTPM
- cerebellum: 34 nTPM
- midbrain: 22 nTPM
- cerebral cortex: 22 nTPM
- hippocampal formation: 22 nTPM
- parathyroid gland: 17 nTPM
Single-cell type
- brain excitatory neurons: 3,295 nCPM
- oligodendrocytes: 3,273 nCPM
- podocytes: 2,180 nCPM
- other brain neurons: 1,914 nCPM
- lactotrophs: 1,829 nCPM
- brain inhibitory neurons: 1,487 nCPM
Immune cell
- basophil: 0 nTPM
- classical monocyte: 0 nTPM
- eosinophil: 0 nTPM
- gdT-cell: 0 nTPM
- intermediate monocyte: 0 nTPM
- MAIT T-cell: 0 nTPM
Brain region
- white matter: 218 nTPM
- basal ganglia: 128 nTPM
- cerebral cortex: 124 nTPM
- pons: 118 nTPM
- thalamus: 112 nTPM
- medulla oblongata: 110 nTPM
Genetic constraint and essentialitygnomAD · DepMap
Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.
- gnomAD LOEUF (loss-of-function intolerance)
- 0.11
- gnomAD pLI
- 1
- gnomAD missense Z
- 0.27
- DepMap mean gene effect
- 0.05
- DepMap dependency class
- none
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 4% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- cell surface receptor protein tyrosine phosphatase signaling pathway
- heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules
- modulation of chemical synaptic transmission
- negative regulation of receptor signaling pathway via JAK-STAT
- nervous system development
- neuron differentiation
- phosphate-containing compound metabolic process
- positive regulation of dendritic spine morphogenesis
- positive regulation of synapse assembly
- presynapse assembly
- presynaptic membrane assembly
- regulation of immune response
- regulation of postsynaptic density assembly
- signal transduction
- synaptic membrane adhesion
- trans-synaptic signaling by trans-synaptic complex
Molecular functions
- cell adhesion molecule binding
- protein tyrosine phosphatase activity
- signaling receptor binding
- transmembrane receptor protein tyrosine phosphatase activity
Cellular components
Protein domainsUniProt · Pfam · InterPro
- Tyrosine-specific protein phosphatase, PTPase domain
- Tyrosine-specific protein phosphatases domain
- Protein-tyrosine phosphatase, catalytic
- Immunoglobulin subtype 2
- Immunoglobulin domain subtype
- Fibronectin type III
- Immunoglobulin-like domain
- Immunoglobulin I-set
- Immunoglobulin-like fold
- Protein-tyrosine phosphatase, active site
- Protein-tyrosine phosphatase-like
- Fibronectin type III superfamily
- Immunoglobulin-like domain superfamily
- Receptor-type Tyrosine-protein Phosphatases/Ushers
- Fibronectin type III domain
- Protein-tyrosine phosphatase
- Immunoglobulin I-set domain
- Immunoglobulin domain
- Receptor-type tyrosine-protein phosphatase delta, PTPase domain, repeat 1
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of PTPRD in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads PTPRD as an antibody target. Whether an autoantibody or antibody against PTPRD could matter depends on whether native PTPRD is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
PTPRD is annotated at the cell surface, where native PTPRD is exposed to circulating antibodies and is a prime autoantibody target that could block, deplete, or overstimulate it.
Annotation status
The present source text does not explicitly label PTPRD as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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