PTPRF

Protein identityUniProt · HPA

UniProt accession

P10586

Gene

PTPRF

Ensembl

ENSG00000142949

Chromosome

1

Canonical length

1907 aa

Protein class

Disease related genes, Enzymes, Plasma proteins, Potential drug targets, Predicted intracellular proteins, Predicted membrane proteins

Subcellular location

Golgi apparatus

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 possesses an extracellular region, a single transmembrane region, and two tandem intracytoplasmic catalytic domains, and thus represents a receptor-type PTP. The extracellular region contains three Ig-like domains, and nine non-Ig like domains similar to that of neural-cell adhesion molecule. This PTP was shown to function in the regulation of epithelial cell-cell contacts at adherents junctions, as well as in the control of beta-catenin signaling. An increased expression level of this protein was found in the insulin-responsive tissue of obese, insulin-resistant individuals, and may contribute to the pathogenesis of insulin resistance. Two alternatively spliced transcript variants of this gene, which encode distinct proteins, have been reported. [provided by RefSeq, Jul 2008]

Canonical amino-acid sequenceUniProt

1907 residues, UniProt reviewed canonical sequence.

>P10586|PTPRF
     1  MAPEPAPGRT MVPLVPALVM LGLVAGAHGD SKPVFIKVPE DQTGLSGGVA SFVCQATGEP
    61  KPRITWMKKG KKVSSQRFEV IEFDDGAGSV LRIQPLRVQR DEAIYECTAT NSLGEINTSA
   121  KLSVLEEEQL PPGFPSIDMG PQLKVVEKAR TATMLCAAGG NPDPEISWFK DFLPVDPATS
   181  NGRIKQLRSG ALQIESSEES DQGKYECVAT NSAGTRYSAP ANLYVRVRRV APRFSIPPSS
   241  QEVMPGGSVN LTCVAVGAPM PYVKWMMGAE ELTKEDEMPV GRNVLELSNV VRSANYTCVA
   301  ISSLGMIEAT AQVTVKALPK PPIDLVVTET TATSVTLTWD SGNSEPVTYY GIQYRAAGTE
   361  GPFQEVDGVA TTRYSIGGLS PFSEYAFRVL AVNSIGRGPP SEAVRARTGE QAPSSPPRRV
   421  QARMLSASTM LVQWEPPEEP NGLVRGYRVY YTPDSRRPPN AWHKHNTDAG LLTTVGSLLP
   481  GITYSLRVLA FTAVGDGPPS PTIQVKTQQG VPAQPADFQA EVESDTRIQL SWLLPPQERI
   541  IMYELVYWAA EDEDQQHKVT FDPTSSYTLE DLKPDTLYRF QLAARSDMGV GVFTPTIEAR
   601  TAQSTPSAPP QKVMCVSMGS TTVRVSWVPP PADSRNGVIT QYSVAYEAVD GEDRGRHVVD
   661  GISREHSSWD LVGLEKWTEY RVWVRAHTDV GPGPESSPVL VRTDEDVPSG PPRKVEVEPL
   721  NSTAVHVYWK LPVPSKQHGQ IRGYQVTYVR LENGEPRGLP IIQDVMLAEA QWRPEESEDY
   781  ETTISGLTPE TTYSVTVAAY TTKGDGARSK PKIVTTTGAV PGRPTMMIST TAMNTALLQW
   841  HPPKELPGEL LGYRLQYCRA DEARPNTIDF GKDDQHFTVT GLHKGTTYIF RLAAKNRAGL
   901  GEEFEKEIRT PEDLPSGFPQ NLHVTGLTTS TTELAWDPPV LAERNGRIIS YTVVFRDINS
   961  QQELQNITTD TRFTLTGLKP DTTYDIKVRA WTSKGSGPLS PSIQSRTMPV EQVFAKNFRV
  1021  AAAMKTSVLL SWEVPDSYKS AVPFKILYNG QSVEVDGHSM RKLIADLQPN TEYSFVLMNR
  1081  GSSAGGLQHL VSIRTAPDLL PHKPLPASAY IEDGRFDLSM PHVQDPSLVR WFYIVVVPID
  1141  RVGGSMLTPR WSTPEELELD ELLEAIEQGG EEQRRRRRQA ERLKPYVAAQ LDVLPETFTL
  1201  GDKKNYRGFY NRPLSPDLSY QCFVLASLKE PMDQKRYASS PYSDEIVVQV TPAQQQEEPE
  1261  MLWVTGPVLA VILIILIVIA ILLFKRKRTH SPSSKDEQSI GLKDSLLAHS SDPVEMRRLN
  1321  YQTPGMRDHP PIPITDLADN IERLKANDGL KFSQEYESID PGQQFTWENS NLEVNKPKNR
  1381  YANVIAYDHS RVILTSIDGV PGSDYINANY IDGYRKQNAY IATQGPLPET MGDFWRMVWE
  1441  QRTATVVMMT RLEEKSRVKC DQYWPARGTE TCGLIQVTLL DTVELATYTV RTFALHKSGS
  1501  SEKRELRQFQ FMAWPDHGVP EYPTPILAFL RRVKACNPLD AGPMVVHCSA GVGRTGCFIV
  1561  IDAMLERMKH EKTVDIYGHV TCMRSQRNYM VQTEDQYVFI HEALLEAATC GHTEVPARNL
  1621  YAHIQKLGQV PPGESVTAME LEFKLLASSK AHTSRFISAN LPCNKFKNRL VNIMPYELTR
  1681  VCLQPIRGVE GSDYINASFL DGYRQQKAYI ATQGPLAEST EDFWRMLWEH NSTIIVMLTK
  1741  LREMGREKCH QYWPAERSAR YQYFVVDPMA EYNMPQYILR EFKVTDARDG QSRTIRQFQF
  1801  TDWPEQGVPK TGEGFIDFIG QVHKTKEQFG QDGPITVHCS AGVGRTGVFI TLSIVLERMR
  1861  YEGVVDMFQT VKTLRTQRPA MVQTEDQYQL CYRAALEYLG SFDHYAT

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against PTPRF 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)

0.29

Highest tissue expression

102 nTPM

Expression across tissuesHPA

DiseaseUniProt · ClinVar · IEDB · PubMed

Four sources answering four different questions about PTPRF.

Disease | AllUniProt

Conditions PTPRF is implicated in, by any mechanism.

• Aplasia or hypoplasia of the breasts and/or nipples 2 (BNAH2) MIM:616001

Disease | GeneticClinVar

2 pathogenic / likely-pathogenic of 366 ClinVar records.

Conditions with pathogenic or likely-pathogenic variants.

• Breasts and/or nipples, aplasia or hypoplasia of, 2

Disease | ImmuneIEDB

Conditions an epitope on PTPRF was assayed in.

• invasive ductal carcinoma T cell

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)

0.19

gnomAD pLI

1

gnomAD missense Z

2.8

DepMap mean gene effect

-0.16

DepMap dependency class

selective

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 5% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).

OntologyGO

Biological processes

• cell adhesion
• cell migration
• cell surface receptor protein tyrosine phosphatase signaling pathway
• nervous system development
• neuron projection regeneration
• peptidyl-tyrosine dephosphorylation
• regulation of axon regeneration
• signal transduction
• synaptic membrane adhesion
• negative regulation of receptor binding

Molecular functions

• cell adhesion molecule binding
• chondroitin sulfate proteoglycan binding
• heparin binding
• phosphoprotein phosphatase activity
• protein tyrosine phosphatase activity
• protein-containing complex binding
• transmembrane receptor protein tyrosine phosphatase activity

Cellular components

• extracellular exosome
• neuron projection
• neuronal cell body
• plasma membrane

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

KeywordsUniProt

• Cell adhesion
• Disulfide bond
• Glycoprotein
• Heparin-binding
• Hydrolase
• Immunoglobulin domain
• Membrane
• Phosphoprotein
• Protein phosphatase
• Receptor
• Repeat
• Signal
• Transmembrane
• Transmembrane helix

InteractionsUniProt · HPA

Protein binding partners of PTPRF in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.

• GRIP1
• INSR
• PPFIA1
• PPFIA2
• PPFIA3
• PPFIA4
• LRRC4B
• CAV1
• EGFR
• FYN