PTPRA_RAT
ID PTPRA_RAT Reviewed; 796 AA.
AC Q03348;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Receptor-type tyrosine-protein phosphatase alpha;
DE Short=Protein-tyrosine phosphatase alpha;
DE Short=R-PTP-alpha;
DE EC=3.1.3.48;
DE Flags: Precursor;
GN Name=Ptpra; Synonyms=Lrp;
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 TISSUE=Kidney;
RX PubMed=1417854; DOI=10.1016/0006-291x(92)92346-y;
RA Moriyama T., Fujiwara Y., Imai E., Takenaka M., Kawanishi S., Inoue T.,
RA Noguchi T., Tanaka T., Kamada T., Ueda N.;
RT "cDNA cloning of rat LRP, a receptor like protein tyrosine phosphatase, and
RT evidence for its gene regulation in cultured rat mesangial cells.";
RL Biochem. Biophys. Res. Commun. 188:34-39(1992).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-792, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Tyrosine protein phosphatase which is involved in integrin-
CC mediated focal adhesion formation (By similarity). Following integrin
CC engagement, specifically recruits BCAR3, BCAR1 and CRK to focal
CC adhesions thereby promoting SRC-mediated phosphorylation of BRAC1 and
CC the subsequent activation of PAK and small GTPase RAC1 and CDC42 (By
CC similarity). {ECO:0000250|UniProtKB:P18052}.
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: Part of a complex comprised of PTPRA, BCAR1, BCAR3 (via SH2
CC domain), and SRC (By similarity). Within the complex, interacts (when
CC phosphorylated on Tyr-792) with BCAR3 (via SH2 domain) (By similarity).
CC Interacts with GRB2 (By similarity). {ECO:0000250|UniProtKB:P18052}.
CC -!- INTERACTION:
CC Q03348; P28648: Cd63; NbExp=5; IntAct=EBI-7784341, EBI-7784314;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Single-pass type I
CC membrane protein {ECO:0000255}. Cell junction, focal adhesion
CC {ECO:0000250|UniProtKB:P18052}. Note=Localizes to focal adhesion sites
CC following integrin engagement. {ECO:0000250|UniProtKB:P18052}.
CC -!- PTM: Integrin binding to extracellular matrix induces phosphorylation
CC at Tyr-792 which induces PTPRA localization and recruitment of BCAR3,
CC BCAR1 and CRK to focal adhesions. {ECO:0000250|UniProtKB:P18052}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 4 subfamily. {ECO:0000305}.
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DR EMBL; L01702; AAA41983.1; -; mRNA.
DR PIR; JC1285; JC1285.
DR AlphaFoldDB; Q03348; -.
DR SMR; Q03348; -.
DR DIP; DIP-5790N; -.
DR IntAct; Q03348; 4.
DR MINT; Q03348; -.
DR STRING; 10116.ENSRNOP00000052657; -.
DR GlyGen; Q03348; 9 sites.
DR iPTMnet; Q03348; -.
DR PhosphoSitePlus; Q03348; -.
DR PaxDb; Q03348; -.
DR PRIDE; Q03348; -.
DR UCSC; RGD:3450; rat.
DR RGD; 3450; Ptpra.
DR eggNOG; KOG4228; Eukaryota.
DR InParanoid; Q03348; -.
DR PhylomeDB; Q03348; -.
DR Reactome; R-RNO-375165; NCAM signaling for neurite out-growth.
DR Reactome; R-RNO-5673001; RAF/MAP kinase cascade.
DR PRO; PR:Q03348; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005925; C:focal adhesion; ISS:UniProtKB.
DR GO; GO:0099699; C:integral component of synaptic membrane; ISO:RGD.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0043235; C:receptor complex; ISO:RGD.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:RGD.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0008286; P:insulin receptor signaling pathway; ISO:RGD.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:RGD.
DR GO; GO:0048709; P:oligodendrocyte differentiation; IEP:RGD.
DR GO; GO:0048714; P:positive regulation of oligodendrocyte differentiation; IMP:RGD.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; ISO:RGD.
DR GO; GO:0051893; P:regulation of focal adhesion assembly; ISS:UniProtKB.
DR Gene3D; 3.90.190.10; -; 2.
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 InterPro; IPR016336; Tyr_Pase_rcpt_a/e-type.
DR InterPro; IPR027262; Tyr_Pase_rcpt_alpha.
DR PANTHER; PTHR19134:SF433; PTHR19134:SF433; 1.
DR Pfam; PF00102; Y_phosphatase; 2.
DR PIRSF; PIRSF500808; PTPR_alpha; 1.
DR PIRSF; PIRSF002006; PTPR_alpha_epsilon; 1.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00194; PTPc; 2.
DR SMART; SM00404; PTPc_motif; 2.
DR SUPFAM; SSF52799; SSF52799; 2.
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 Cell junction; Cell membrane; Glycoprotein; Hydrolase; Membrane;
KW Phosphoprotein; Protein phosphatase; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..796
FT /note="Receptor-type tyrosine-protein phosphatase alpha"
FT /id="PRO_0000025435"
FT TOPO_DOM 20..145
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..796
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 235..495
FT /note="Tyrosine-protein phosphatase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT DOMAIN 527..785
FT /note="Tyrosine-protein phosphatase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 78..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 436
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 726
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 404
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 436..442
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 480
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18052"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18052"
FT MOD_RES 792
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 20
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 21
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 796 AA; 90260 MW; 4793796191056920 CRC64;
MDSWFILILF GSGLIHISAN NTTTVSPSLG TTRLIKTSTT ESAKEENKTS NSTSSVISLS
VTPTFSPNLT LEPTYVTTVN SSHSDNGTKR AASTESGGTT ISPNGTYGTW LTDNQFTDAR
TEPWEGNSSS AATTPETFPP ADETPIIAVM VALSSLLVIL FIIIVLYMLR FKKYKQAGSH
SNSFRLSNGR TEDVEPQSVP LLARSPSTNR KYPPLPVDKL EEEINRRMAD DNKLFREEFN
ALPACPIQAT CEAASKEENK EKNRYVNLLP YDHSRVHLTP VEGVPDSDYI NASFINGYQE
KNKFIAAQGP KEETVNDFWR MIWEQNTATI VMVTNLKERK ECKCAQYWPD QGCWPYGNVR
VSVEDVTVLV DYTVRKFCIQ QVGDVTNRKP QRLITQFHFT SWPDFGVPFT PIGMLKFLKK
VKACNPQYAG AIVVHCSAGV GRTGTFVVID AMLDMMHSER KVDVYGFVSR IRAQRCQMVQ
TDMQYVFIYQ ALLEHYLYGD TELEVTSLDT HLQKIYNKIP GTSNNGLEEE FKKLTSIKIQ
NDKMRTGYLP ANMKKNRVLQ IIPYEFNRVI IPVKRGEENT DYVNASFIDP YRQKDSYIAS
QGPLLHTTED FWRMIWEWKS CSIVMLTELE ERGQEKCAQY WPSDGLVSYG DITVELKKEE
ECESYTVRDL LVTNTRENKS RQIRQFHFHG WPEVGIPSDG KGMINIIAAV QKQQQQSGNH
PITVHCSAGA GRTGTFCALS TVLECVKAEG ILDVFQTVKT LRLQRPHMVQ ILEQYEFCYK
VVQEYIDAFS DYANFK
