PTPRA_HUMAN
ID PTPRA_HUMAN Reviewed; 802 AA.
AC P18433; A8K2G8; D3DVX5; Q14513; Q7Z2I2; Q96TD9;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 3.
DT 03-AUG-2022, entry version 227.
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=PTPA, PTPRL2;
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).
RX PubMed=2169617; DOI=10.1073/pnas.87.18.7000;
RA Kaplan R., Morse B., Huebner K., Croce C., Howk R., Ravera M., Ricca G.,
RA Jaye M., Schlessinger J.;
RT "Cloning of three human tyrosine phosphatases reveals a multigene family of
RT receptor-linked protein-tyrosine-phosphatases expressed in brain.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:7000-7004(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Kidney;
RX PubMed=2175890; DOI=10.1093/nar/18.23.7159;
RA Ohagi S., Nishi M., Steiner D.F.;
RT "Sequence of a cDNA encoding human LRP (leukocyte common antigen-related
RT peptide).";
RL Nucleic Acids Res. 18:7159-7159(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=2172030; DOI=10.1016/0014-5793(90)81094-5;
RA Jirik F.R., Janzen N.M., Melhado I.G., Harder K.W.;
RT "Cloning and chromosomal assignment of a widely expressed human receptor-
RT like protein-tyrosine phosphatase.";
RL FEBS Lett. 273:239-242(1990).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Lymph node;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Skin;
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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-798, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-798, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP IDENTIFICATION IN A COMPLEX WITH BCAR3; BCAR1 AND SRC, INTERACTION WITH
RP GRB2 AND BCAR3, PHOSPHORYLATION AT TYR-798, AND MUTAGENESIS OF TYR-798.
RX PubMed=22801373; DOI=10.1128/mcb.00214-12;
RA Sun G., Cheng S.Y., Chen M., Lim C.J., Pallen C.J.;
RT "Protein tyrosine phosphatase alpha phosphotyrosyl-789 binds BCAR3 to
RT position Cas for activation at integrin-mediated focal adhesions.";
RL Mol. Cell. Biol. 32:3776-3789(2012).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-798, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-798, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
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 (PubMed:22801373). Within the complex, interacts (when
CC phosphorylated on Tyr-798) with BCAR3 (via SH2 domain)
CC (PubMed:22801373). Interacts with GRB2 (PubMed:22801373).
CC {ECO:0000269|PubMed:22801373}.
CC -!- INTERACTION:
CC P18433; P00533: EGFR; NbExp=3; IntAct=EBI-2609645, EBI-297353;
CC P18433; P62993: GRB2; NbExp=13; IntAct=EBI-2609645, EBI-401755;
CC P18433; P12931: SRC; NbExp=4; IntAct=EBI-2609645, EBI-621482;
CC P18433; P39688: Fyn; Xeno; NbExp=2; IntAct=EBI-2609645, EBI-524514;
CC P18433; P00523: SRC; Xeno; NbExp=4; IntAct=EBI-2609645, EBI-848039;
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P18433-5; Sequence=Displayed;
CC Name=2;
CC IsoId=P18433-6; Sequence=VSP_059405;
CC -!- PTM: Integrin binding to extracellular matrix induces phosphorylation
CC at Tyr-798 which induces PTPRA localization and recruitment of BCAR3,
CC BCAR1 and CRK to focal adhesions. {ECO:0000269|PubMed:22801373}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 4 subfamily. {ECO:0000305}.
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DR EMBL; M34668; AAA36528.1; -; mRNA.
DR EMBL; X54130; CAA38065.1; -; mRNA.
DR EMBL; X54890; CAA38662.1; -; mRNA.
DR EMBL; X53364; CAA37447.1; -; mRNA.
DR EMBL; AK290233; BAF82922.1; -; mRNA.
DR EMBL; BX571753; CAE11878.1; -; mRNA.
DR EMBL; AL121905; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471133; EAX10562.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10563.1; -; Genomic_DNA.
DR EMBL; BC027308; AAH27308.1; -; mRNA.
DR CCDS; CCDS13038.1; -. [P18433-5]
DR CCDS; CCDS13039.1; -. [P18433-6]
DR PIR; A36065; A36065.
DR RefSeq; NP_002827.1; NM_002836.3. [P18433-5]
DR RefSeq; NP_543030.1; NM_080840.2. [P18433-6]
DR RefSeq; NP_543031.1; NM_080841.2. [P18433-6]
DR PDB; 6UZT; X-ray; 1.80 A; A/B=211-802.
DR PDBsum; 6UZT; -.
DR AlphaFoldDB; P18433; -.
DR SMR; P18433; -.
DR BioGRID; 111750; 135.
DR CORUM; P18433; -.
DR IntAct; P18433; 74.
DR MINT; P18433; -.
DR STRING; 9606.ENSP00000369756; -.
DR BindingDB; P18433; -.
DR ChEMBL; CHEMBL3918; -.
DR DEPOD; PTPRA; -.
DR GlyGen; P18433; 8 sites, 1 O-linked glycan (1 site).
DR iPTMnet; P18433; -.
DR PhosphoSitePlus; P18433; -.
DR BioMuta; PTPRA; -.
DR DMDM; 126467; -.
DR EPD; P18433; -.
DR jPOST; P18433; -.
DR MassIVE; P18433; -.
DR MaxQB; P18433; -.
DR PaxDb; P18433; -.
DR PeptideAtlas; P18433; -.
DR PRIDE; P18433; -.
DR Antibodypedia; 7130; 518 antibodies from 35 providers.
DR DNASU; 5786; -.
DR Ensembl; ENST00000216877.10; ENSP00000216877.6; ENSG00000132670.21. [P18433-6]
DR Ensembl; ENST00000318266.9; ENSP00000314568.5; ENSG00000132670.21. [P18433-6]
DR Ensembl; ENST00000356147.3; ENSP00000348468.3; ENSG00000132670.21. [P18433-6]
DR Ensembl; ENST00000399903.7; ENSP00000382787.2; ENSG00000132670.21. [P18433-5]
DR GeneID; 5786; -.
DR KEGG; hsa:5786; -.
DR MANE-Select; ENST00000399903.7; ENSP00000382787.2; NM_001385305.1; NP_001372234.1.
DR UCSC; uc002whj.4; human. [P18433-5]
DR CTD; 5786; -.
DR DisGeNET; 5786; -.
DR GeneCards; PTPRA; -.
DR HGNC; HGNC:9664; PTPRA.
DR HPA; ENSG00000132670; Low tissue specificity.
DR MIM; 176884; gene.
DR neXtProt; NX_P18433; -.
DR OpenTargets; ENSG00000132670; -.
DR PharmGKB; PA34009; -.
DR VEuPathDB; HostDB:ENSG00000132670; -.
DR eggNOG; KOG4228; Eukaryota.
DR GeneTree; ENSGT00940000159585; -.
DR HOGENOM; CLU_001645_8_0_1; -.
DR InParanoid; P18433; -.
DR OMA; YWPSDGT; -.
DR OrthoDB; 411281at2759; -.
DR PhylomeDB; P18433; -.
DR TreeFam; TF351829; -.
DR BRENDA; 3.1.3.48; 2681.
DR PathwayCommons; P18433; -.
DR Reactome; R-HSA-375165; NCAM signaling for neurite out-growth.
DR Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
DR SignaLink; P18433; -.
DR SIGNOR; P18433; -.
DR BioGRID-ORCS; 5786; 12 hits in 1078 CRISPR screens.
DR ChiTaRS; PTPRA; human.
DR GeneWiki; PTPRA; -.
DR GenomeRNAi; 5786; -.
DR Pharos; P18433; Tchem.
DR PRO; PR:P18433; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; P18433; protein.
DR Bgee; ENSG00000132670; Expressed in calcaneal tendon and 201 other tissues.
DR ExpressionAtlas; P18433; baseline and differential.
DR Genevisible; P18433; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0099699; C:integral component of synaptic membrane; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0043235; C:receptor complex; IDA:MGI.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; ISS:UniProtKB.
DR GO; GO:0005001; F:transmembrane receptor protein tyrosine phosphatase activity; TAS:ProtInc.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IEA:Ensembl.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IEA:Ensembl.
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 3D-structure; Alternative splicing; Cell junction; Cell membrane;
KW Glycoprotein; Hydrolase; Membrane; Phosphoprotein; Protein phosphatase;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..802
FT /note="Receptor-type tyrosine-protein phosphatase alpha"
FT /id="PRO_0000025433"
FT TOPO_DOM 20..151
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 175..802
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 241..501
FT /note="Tyrosine-protein phosphatase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT DOMAIN 533..791
FT /note="Tyrosine-protein phosphatase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 39..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 79..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 442
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 732
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 410
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 442..448
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 486
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18052"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18052"
FT MOD_RES 798
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:22801373,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT CARBOHYD 21
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 36
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 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 139..147
FT /note="Missing (in isoform 2)"
FT /id="VSP_059405"
FT VARIANT 109
FT /note="P -> L (in dbSNP:rs1178027)"
FT /id="VAR_057134"
FT MUTAGEN 798
FT /note="Y->F: Abolishes integrin-mediated interaction with
FT BCAR1 and BCAR3 and reduces interaction between BCAR1 and
FT CRK and, BCAR1 and SRC. Abolishes integrin-induced SRC-
FT mediated tyrosine phosphorylation of BCAR1. Abolishes
FT integrin-mediated recruitment of BCAR1, BCAR3, CRK and
FT PTPRA to focal adhesions. Reduces integrin-mediated
FT activation and membrane recruitment of RAC1 and CDC42."
FT /evidence="ECO:0000269|PubMed:22801373"
FT CONFLICT 114
FT /note="T -> M (in Ref. 3; CAA38662)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="E -> P (in Ref. 4; CAA37447)"
FT /evidence="ECO:0000305"
FT CONFLICT 289
FT /note="G -> E (in Ref. 3; CAA38662)"
FT /evidence="ECO:0000305"
FT CONFLICT 367
FT /note="V -> A (in Ref. 3; CAA38662)"
FT /evidence="ECO:0000305"
FT CONFLICT 493
FT /note="F -> S (in Ref. 3; CAA38662)"
FT /evidence="ECO:0000305"
FT CONFLICT 786
FT /note="K -> E (in Ref. 3; CAA38662)"
FT /evidence="ECO:0000305"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:6UZT"
FT HELIX 226..246
FT /evidence="ECO:0007829|PDB:6UZT"
FT HELIX 258..261
FT /evidence="ECO:0007829|PDB:6UZT"
FT HELIX 263..268
FT /evidence="ECO:0007829|PDB:6UZT"
FT TURN 278..280
FT /evidence="ECO:0007829|PDB:6UZT"
FT STRAND 281..283
FT /evidence="ECO:0007829|PDB:6UZT"
FT TURN 291..294
FT /evidence="ECO:0007829|PDB:6UZT"
FT STRAND 295..301
FT /evidence="ECO:0007829|PDB:6UZT"
FT STRAND 310..313
FT /evidence="ECO:0007829|PDB:6UZT"
FT HELIX 318..320
FT /evidence="ECO:0007829|PDB:6UZT"
FT HELIX 321..330
FT /evidence="ECO:0007829|PDB:6UZT"
FT STRAND 335..338
FT /evidence="ECO:0007829|PDB:6UZT"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:6UZT"
FT STRAND 356..362
FT /evidence="ECO:0007829|PDB:6UZT"
FT STRAND 365..374
FT /evidence="ECO:0007829|PDB:6UZT"
FT STRAND 376..387
FT /evidence="ECO:0007829|PDB:6UZT"
FT STRAND 398..405
FT /evidence="ECO:0007829|PDB:6UZT"
FT STRAND 410..412
FT /evidence="ECO:0007829|PDB:6UZT"
FT HELIX 418..430
FT /evidence="ECO:0007829|PDB:6UZT"
FT STRAND 438..441
FT /evidence="ECO:0007829|PDB:6UZT"
FT STRAND 443..446
FT /evidence="ECO:0007829|PDB:6UZT"
FT HELIX 447..465
FT /evidence="ECO:0007829|PDB:6UZT"
FT STRAND 466..468
FT /evidence="ECO:0007829|PDB:6UZT"
FT HELIX 470..477
FT /evidence="ECO:0007829|PDB:6UZT"
FT TURN 478..480
FT /evidence="ECO:0007829|PDB:6UZT"
FT HELIX 488..504
FT /evidence="ECO:0007829|PDB:6UZT"
FT HELIX 511..513
FT /evidence="ECO:0007829|PDB:6UZT"
FT HELIX 514..522
FT /evidence="ECO:0007829|PDB:6UZT"
FT STRAND 528..531
FT /evidence="ECO:0007829|PDB:6UZT"
FT HELIX 532..541
FT /evidence="ECO:0007829|PDB:6UZT"
FT HELIX 547..549
FT /evidence="ECO:0007829|PDB:6UZT"
FT HELIX 552..554
FT /evidence="ECO:0007829|PDB:6UZT"
FT TURN 556..558
FT /evidence="ECO:0007829|PDB:6UZT"
FT HELIX 559..561
FT /evidence="ECO:0007829|PDB:6UZT"
FT HELIX 571..573
FT /evidence="ECO:0007829|PDB:6UZT"
FT STRAND 574..576
FT /evidence="ECO:0007829|PDB:6UZT"
FT TURN 584..587
FT /evidence="ECO:0007829|PDB:6UZT"
FT STRAND 588..594
FT /evidence="ECO:0007829|PDB:6UZT"
FT STRAND 597..599
FT /evidence="ECO:0007829|PDB:6UZT"
FT STRAND 603..606
FT /evidence="ECO:0007829|PDB:6UZT"
FT HELIX 611..613
FT /evidence="ECO:0007829|PDB:6UZT"
FT HELIX 614..623
FT /evidence="ECO:0007829|PDB:6UZT"
FT STRAND 628..631
FT /evidence="ECO:0007829|PDB:6UZT"
FT STRAND 635..637
FT /evidence="ECO:0007829|PDB:6UZT"
FT STRAND 649..655
FT /evidence="ECO:0007829|PDB:6UZT"
FT STRAND 658..667
FT /evidence="ECO:0007829|PDB:6UZT"
FT STRAND 669..680
FT /evidence="ECO:0007829|PDB:6UZT"
FT TURN 681..684
FT /evidence="ECO:0007829|PDB:6UZT"
FT STRAND 685..694
FT /evidence="ECO:0007829|PDB:6UZT"
FT STRAND 699..701
FT /evidence="ECO:0007829|PDB:6UZT"
FT HELIX 707..722
FT /evidence="ECO:0007829|PDB:6UZT"
FT STRAND 728..731
FT /evidence="ECO:0007829|PDB:6UZT"
FT STRAND 733..736
FT /evidence="ECO:0007829|PDB:6UZT"
FT HELIX 737..755
FT /evidence="ECO:0007829|PDB:6UZT"
FT STRAND 756..758
FT /evidence="ECO:0007829|PDB:6UZT"
FT HELIX 760..770
FT /evidence="ECO:0007829|PDB:6UZT"
FT HELIX 778..794
FT /evidence="ECO:0007829|PDB:6UZT"
FT TURN 795..797
FT /evidence="ECO:0007829|PDB:6UZT"
SQ SEQUENCE 802 AA; 90719 MW; D1E6A5E86FE4D3F0 CRC64;
MDSWFILVLL GSGLICVSAN NATTVAPSVG ITRLINSSTA EPVKEEAKTS NPTSSLTSLS
VAPTFSPNIT LGPTYLTTVN SSDSDNGTTR TASTNSIGIT ISPNGTWLPD NQFTDARTEP
WEGNSSTAAT TPETFPPSGN SDSKDRRDET PIIAVMVALS SLLVIVFIII VLYMLRFKKY
KQAGSHSNSF RLSNGRTEDV EPQSVPLLAR SPSTNRKYPP LPVDKLEEEI NRRMADDNKL
FREEFNALPA CPIQATCEAA SKEENKEKNR YVNILPYDHS RVHLTPVEGV PDSDYINASF
INGYQEKNKF IAAQGPKEET VNDFWRMIWE QNTATIVMVT NLKERKECKC AQYWPDQGCW
TYGNIRVSVE DVTVLVDYTV RKFCIQQVGD MTNRKPQRLI TQFHFTSWPD FGVPFTPIGM
LKFLKKVKAC NPQYAGAIVV HCSAGVGRTG TFVVIDAMLD MMHTERKVDV YGFVSRIRAQ
RCQMVQTDMQ YVFIYQALLE HYLYGDTELE VTSLETHLQK IYNKIPGTSN NGLEEEFKKL
TSIKIQNDKM RTGNLPANMK KNRVLQIIPY EFNRVIIPVK RGEENTDYVN ASFIDGYRQK
DSYIASQGPL LHTIEDFWRM IWEWKSCSIV MLTELEERGQ EKCAQYWPSD GLVSYGDITV
ELKKEEECES YTVRDLLVTN TRENKSRQIR QFHFHGWPEV GIPSDGKGMI SIIAAVQKQQ
QQSGNHPITV HCSAGAGRTG TFCALSTVLE RVKAEGILDV FQTVKSLRLQ RPHMVQTLEQ
YEFCYKVVQE YIDAFSDYAN FK
