PTPRF_RAT
ID PTPRF_RAT Reviewed; 1898 AA.
AC Q64604; Q4JFJ1; Q63294; Q63295; Q63296;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Receptor-type tyrosine-protein phosphatase F;
DE EC=3.1.3.48;
DE AltName: Full=Leukocyte common antigen related;
DE Short=LAR;
DE Flags: Precursor;
GN Name=Ptprf; Synonyms=Lar;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=8068021; DOI=10.1042/bj3020039;
RA Zhang W.-R., Hashimoto N., Ahmad F., Ding W., Goldstein B.J.;
RT "Molecular cloning and expression of a unique receptor-like protein-
RT tyrosine-phosphatase in the leucocyte-common-antigen-related phosphate
RT family.";
RL Biochem. J. 302:39-47(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1035-1898, AND FUNCTION.
RC TISSUE=Hypothalamus;
RX PubMed=1918076; DOI=10.1016/s0021-9258(18)55047-x;
RA Pot D.A., Woodford T.A., Remboutsika E., Haun R.S., Dixon J.E.;
RT "Cloning, bacterial expression, purification, and characterization of the
RT cytoplasmic domain of rat LAR, a receptor-like protein tyrosine
RT phosphatase.";
RL J. Biol. Chem. 266:19688-19696(1991).
CC -!- FUNCTION: Possible cell adhesion receptor. It possesses an intrinsic
CC protein tyrosine phosphatase activity (PTPase) and dephosphorylates
CC EPHA2 regulating its activity. {ECO:0000269|PubMed:1918076}.
CC -!- FUNCTION: The first PTPase domain has enzymatic activity, while the
CC second one seems to affect the substrate specificity of the first one.
CC {ECO:0000250}.
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 GRIP1. Interacts with PPFIA1, PPFIA2 and
CC PPFIA3. Interacts with PTPRF. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 2A subfamily. {ECO:0000305}.
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DR EMBL; L11586; AAC37655.1; -; mRNA.
DR EMBL; M60103; AAA41510.1; -; mRNA.
DR PIR; S46216; S46216.
DR RefSeq; NP_062122.1; NM_019249.1.
DR AlphaFoldDB; Q64604; -.
DR SMR; Q64604; -.
DR BioGRID; 261938; 3.
DR CORUM; Q64604; -.
DR IntAct; Q64604; 4.
DR MINT; Q64604; -.
DR STRING; 10116.ENSRNOP00000027271; -.
DR ChEMBL; CHEMBL2834; -.
DR GlyGen; Q64604; 6 sites.
DR iPTMnet; Q64604; -.
DR PhosphoSitePlus; Q64604; -.
DR jPOST; Q64604; -.
DR PaxDb; Q64604; -.
DR PRIDE; Q64604; -.
DR ABCD; Q64604; 2 sequenced antibodies.
DR GeneID; 360406; -.
DR KEGG; rno:360406; -.
DR UCSC; RGD:3453; rat.
DR CTD; 5792; -.
DR RGD; 3453; Ptprf.
DR eggNOG; KOG4228; Eukaryota.
DR InParanoid; Q64604; -.
DR OrthoDB; 220353at2759; -.
DR PhylomeDB; Q64604; -.
DR BRENDA; 3.1.3.48; 5301.
DR Reactome; R-RNO-388844; Receptor-type tyrosine-protein phosphatases.
DR Reactome; R-RNO-8849932; Synaptic adhesion-like molecules.
DR PRO; PR:Q64604; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005768; C:endosome; IDA:RGD.
DR GO; GO:0060076; C:excitatory synapse; IDA:RGD.
DR GO; GO:0030426; C:growth cone; IDA:RGD.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IDA:SynGO.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISO:RGD.
DR GO; GO:0035373; F:chondroitin sulfate proteoglycan binding; ISO:RGD.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0005158; F:insulin receptor binding; IDA:RGD.
DR GO; GO:0042301; F:phosphate ion binding; IDA:RGD.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:RGD.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; IPI:RGD.
DR GO; GO:0005001; F:transmembrane receptor protein tyrosine phosphatase activity; IDA:RGD.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IDA:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:RGD.
DR GO; GO:0031345; P:negative regulation of cell projection organization; IMP:RGD.
DR GO; GO:0001960; P:negative regulation of cytokine-mediated signaling pathway; IMP:RGD.
DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; IMP:RGD.
DR GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IMP:RGD.
DR GO; GO:0051387; P:negative regulation of neurotrophin TRK receptor signaling pathway; IMP:RGD.
DR GO; GO:1900121; P:negative regulation of receptor binding; ISS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IDA:RGD.
DR GO; GO:0031102; P:neuron projection regeneration; ISO:RGD.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; ISO:RGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:RGD.
DR GO; GO:0050775; P:positive regulation of dendrite morphogenesis; IMP:RGD.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; IMP:RGD.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:RGD.
DR GO; GO:0048679; P:regulation of axon regeneration; ISO:RGD.
DR GO; GO:0010975; P:regulation of neuron projection development; ISO:RGD.
DR GO; GO:0099175; P:regulation of postsynapse organization; IDA:SynGO.
DR GO; GO:0050803; P:regulation of synapse structure or activity; IMP:RGD.
DR GO; GO:0099560; P:synaptic membrane adhesion; IDA:SynGO.
DR CDD; cd00063; FN3; 8.
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; 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; 3.
DR Pfam; PF00102; Y_phosphatase; 2.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00060; FN3; 8.
DR SMART; SM00409; IG; 3.
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 2: Evidence at transcript level;
KW Cell adhesion; Disulfide bond; Glycoprotein; Heparin-binding; Hydrolase;
KW Immunoglobulin domain; Membrane; Phosphoprotein; Protein phosphatase;
KW Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..1898
FT /note="Receptor-type tyrosine-protein phosphatase F"
FT /id="PRO_5000142152"
FT TOPO_DOM 30..1254
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1255..1275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1276..1898
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 33..123
FT /note="Ig-like C2-type 1"
FT DOMAIN 135..224
FT /note="Ig-like C2-type 2"
FT DOMAIN 232..314
FT /note="Ig-like C2-type 3"
FT DOMAIN 321..411
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 416..510
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 514..604
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 609..706
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 711..810
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 811..905
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 909..1001
FT /note="Fibronectin type-III 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1005..1089
FT /note="Fibronectin type-III 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1343..1598
FT /note="Tyrosine-protein phosphatase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT DOMAIN 1630..1889
FT /note="Tyrosine-protein phosphatase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 693..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1539
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 1830
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 68..77
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250"
FT BINDING 1507
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1539..1545
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1583
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 1296
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10586"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 721
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 941
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 957
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 54..107
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 156..207
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 253..298
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 1073
FT /note="T -> S (in Ref. 2; AAA41510)"
FT /evidence="ECO:0000305"
FT CONFLICT 1434
FT /note="I -> T (in Ref. 2; AAA41510)"
FT /evidence="ECO:0000305"
FT CONFLICT 1639
FT /note="G -> N (in Ref. 2; AAA41510)"
FT /evidence="ECO:0000305"
FT CONFLICT 1643..1644
FT /note="RA -> HT (in Ref. 2; AAA41510)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1898 AA; 211494 MW; DF4D7E46F5896F4B CRC64;
MAPEPAPGRR MVPLVPALVM LGLMAGAHGD SKPVFVKVPE DQIGLSGGVA SFVCQATGEP
KPRITWMKKG KKVSSQRFEV IEFDDGAGSV LRIQPLRVQR DEAIYECTAT NSLGEINTSA
KLSVLEEDQL PSGFPTIDMG PQLKVVEKAR TATMLCAAGG NPDPEISWFK DFLPVDPASS
NGRIKQLRSG ALQIESSEES DQGKYECVAT NSAGTRYSAP ANLYVRVRRV APRFSIPPSS
QEVMPGGNVN LTCVAVGAPM PYVKWMMGAE ELTKEDEMPV GRNVLELSNV MRSANYTCVA
ISSLGMIEAT AQVTVKALPK PPIDLVVTET TATSVTLTWD SGNTEPVSFY GIQYRAAGTD
GPFQEVDGVA STRYSIGGLS PFSEYAFRVL AVNSIGRGPP SEAVRARTGE QAPSSPPRRV
QARMLSASTM LVQWEPPEEP NGLVRGYRVY YTPDSRRPLS AWHKHNTDAG LLTTVGSLLP
GITYSLRVLA FTAVGDGPPS PTIQVKTQQG VPAQPADFQA KAESDTRIQL SWLLPPQERI
IKYELVYWAA EDEGQQHKVT FDPTSSYTLE DLKPDTLYHF QLAARSDLGV GVFTPTVEAC
TAQSTPSAPP QKVTCVSTGS TTVRVSWVPP PADSRNGIIT QYSVAYEAVD GEDRKRHVVD
GISREHSSWD LLGLEKWTEY RVWVRAHTDV GPGPESSPVL VRTDEDVPSG PPRKVEVEPL
NSTAVHVSWK LPVPNKQHGQ IRGYQVTYVR LENGEPRGQP IIQDVMLAEA QETTISGLTP
ETTYSITVAA YTTKGDGARS KPKVVTTTGA VPGRPTMMVS TTAMHTALLQ WHPPKELPGE
LLGYRLQYRR ADEARPNTID FGKDDQHFTV TGLHKGATYI FRLAAKNRAG PGEEFEKEIT
TPEDAPSGFP QNLRVTGLTT STTELAWDPP VLAERNGRIT NYTVVYRDIN SQHELQNVTG
DVHLTLLGLK PDTTYDIKVR AHTSKGAGPL SPSIQSRTMP MEQVFAKNFR VAAAMKTSVL
LSWEVPDSYK SAVPFKILYN GQSVEVDGHS MRKLIADLQP NTEYSFVLMN RGTSAGGLQH
LVSIRTAPDL LPQKPLPASA FIEDGRFSLS MPQVQDPSLV RWFYIVVVPI DRVGGNLLAP
RWSTPEELEL DELLEAIEQG EEKQRRRRRQ AERLKPYVAA QVDELPETFT LGDKKNYRGF
YNRPLSPDLS YQCFVLASLK EPMDQKRYAS SPYSDEIVVQ VTPAQQQEEP EMLWVTGPVL
AVILIILIVI AILLFKRKRT HSPSSKDEQS IGLKDSLLAH SSDPVEMRRL NYQTPGMRDH
PPIPITDLAD NIERLKANDG LKFSQEYESI DPGQQFTWEN SNSEVNKPKN RYANVIAYDH
SRVLLTSIDG VPGSDYINAN YIDGYRKQNA YIATQGPLPE TMGDFWRMVW EQRIATVVMM
TRLEEKSRVK CDQYWPARGT ETYGLIQVTL VDTVELATYT MRTFALHKSG SSEKRELRQF
QFMAWPDHGV PEYPTPILAF LRRVKACNPL DAGPMVVHCS AGVGRTGCFI VIDAMLERMK
HEKTVDIYGH VTCMRSQRNY MVQTEDQYVF IHEALLEAAM CGHTEVLARN LYAHIQKLGQ
VPPGESVTAM ELEFKLLAGS KARASRFISA NLPCNKFKNR LVNIMPYELT RVCLQPIRGV
EGSDYINASF LDGYRQQKAY IATQGPLAES TEDFWRMLWE HNSTIIVMLT KLREMGREKC
HQYWPAERSA RYQYFVVDPM AEYNMPQYIL REFKVTDARD GQSRTIRQFQ FTDWPEQGVP
KTGEGFIDFI GQVHKTKEQF GQDGPITVHC SAGVGRTGVF ITLSIVLERM RYEGVVDMFQ
TVKTLRTQRP AMVQTEDQYQ LCYRAALEYL GSFDHYAT
