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 02-SEP-2026, entry version 245. 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=O-phospho-L-tyrosyl-[protein] + H2O = L-tyrosyl-[protein] + CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA- CC COMP:20101, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, CC ChEBI:CHEBI:61978; 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=17; IntAct=EBI-2609645, EBI-401755; CC P18433; P12931: SRC; NbExp=5; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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_001372234.1; NM_001385305.1. [P18433-5] DR RefSeq; NP_001372235.1; NM_001385306.1. [P18433-5] DR RefSeq; NP_001372236.1; NM_001385307.1. [P18433-5] DR RefSeq; NP_001372237.1; NM_001385308.1. [P18433-5] DR RefSeq; NP_001372240.1; NM_001385311.1. [P18433-6] DR RefSeq; NP_001375249.1; NM_001388320.1. [P18433-5] DR RefSeq; NP_001375250.1; NM_001388321.1. [P18433-6] DR RefSeq; NP_002827.1; NM_002836.4. [P18433-5] DR RefSeq; NP_543030.1; NM_080840.3. [P18433-6] DR RefSeq; NP_543031.1; NM_080841.3. [P18433-6] DR PDB; 6UZT; X-ray; 1.80 A; A/B=211-802. DR AlphaFoldDB; P18433; -. DR SMR; P18433; -. DR BioGRID; 111750; 150. DR CORUM; P18433; -. DR FunCoup; P18433; 1081. DR IntAct; P18433; 93. DR MINT; P18433; -. DR NDEx; IQUERY-CP-PTPRA; 3 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000369756; -. DR BindingDB; P18433; -. DR ChEMBL; CHEMBL3918; -. DR DEPOD; PTPRA; -. DR GlyCosmos; P18433; 8 sites, 1 glycan. DR GlyGen; P18433; 8 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site). DR iPTMnet; P18433; -. DR PhosphoSitePlus; P18433; -. DR BioMuta; PTPRA; -. DR DMDM; 126467; -. DR jPOST; P18433; -. DR MassIVE; P18433; -. DR PaxDb; 9606-ENSP00000369756; -. DR PeptideAtlas; P18433; -. DR Pumba; P18433; -. DR Antibodypedia; 7130; 508 antibodies from 36 providers. DR DNASU; 5786; -. DR Ensembl; ENST00000216877.10; ENSP00000216877.6; ENSG00000132670.22. [P18433-6] DR Ensembl; ENST00000318266.9; ENSP00000314568.5; ENSG00000132670.22. [P18433-6] DR Ensembl; ENST00000356147.3; ENSP00000348468.3; ENSG00000132670.22. [P18433-6] DR Ensembl; ENST00000399903.7; ENSP00000382787.2; ENSG00000132670.22. [P18433-5] DR Ensembl; ENST00000876898.1; ENSP00000546957.1; ENSG00000132670.22. [P18433-6] DR Ensembl; ENST00000876899.1; ENSP00000546958.1; ENSG00000132670.22. [P18433-6] DR Ensembl; ENST00000876900.1; ENSP00000546959.1; ENSG00000132670.22. [P18433-6] DR Ensembl; ENST00000876901.1; ENSP00000546960.1; ENSG00000132670.22. [P18433-6] DR Ensembl; ENST00000876902.1; ENSP00000546961.1; ENSG00000132670.22. [P18433-6] DR Ensembl; ENST00000876903.1; ENSP00000546962.1; ENSG00000132670.22. [P18433-5] DR Ensembl; ENST00000876904.1; ENSP00000546963.1; ENSG00000132670.22. [P18433-5] DR Ensembl; ENST00000876905.1; ENSP00000546964.1; ENSG00000132670.22. [P18433-5] DR Ensembl; ENST00000876906.1; ENSP00000546965.1; ENSG00000132670.22. [P18433-6] DR Ensembl; ENST00000876907.1; ENSP00000546966.1; ENSG00000132670.22. [P18433-5] DR Ensembl; ENST00000876915.1; ENSP00000546974.1; ENSG00000132670.22. [P18433-6] DR Ensembl; ENST00000876917.1; ENSP00000546976.1; ENSG00000132670.22. [P18433-6] DR Ensembl; ENST00000876918.1; ENSP00000546977.1; ENSG00000132670.22. [P18433-6] DR Ensembl; ENST00000876920.1; ENSP00000546979.1; ENSG00000132670.22. [P18433-6] DR Ensembl; ENST00000876922.1; ENSP00000546981.1; ENSG00000132670.22. [P18433-6] DR Ensembl; ENST00000876923.1; ENSP00000546982.1; ENSG00000132670.22. [P18433-6] DR Ensembl; ENST00000876925.1; ENSP00000546984.1; ENSG00000132670.22. [P18433-6] DR Ensembl; ENST00000876926.1; ENSP00000546985.1; ENSG00000132670.22. [P18433-6] DR Ensembl; ENST00000876927.1; ENSP00000546986.1; ENSG00000132670.22. [P18433-6] DR Ensembl; ENST00000876933.1; ENSP00000546992.1; ENSG00000132670.22. [P18433-6] DR Ensembl; ENST00000911874.1; ENSP00000581933.1; ENSG00000132670.22. [P18433-5] DR Ensembl; ENST00000911878.1; ENSP00000581937.1; ENSG00000132670.22. [P18433-6] DR Ensembl; ENST00000911883.1; ENSP00000581942.1; ENSG00000132670.22. [P18433-6] DR Ensembl; ENST00000911885.1; ENSP00000581944.1; ENSG00000132670.22. [P18433-6] DR Ensembl; ENST00000970270.1; ENSP00000640329.1; ENSG00000132670.22. [P18433-6] DR Ensembl; ENST00000970274.1; ENSP00000640333.1; ENSG00000132670.22. [P18433-6] DR Ensembl; ENST00000970276.1; ENSP00000640335.1; ENSG00000132670.22. [P18433-5] DR Ensembl; ENST00000970278.1; ENSP00000640337.1; ENSG00000132670.22. [P18433-5] DR Ensembl; ENST00000970282.1; ENSP00000640341.1; ENSG00000132670.22. [P18433-6] DR Ensembl; ENST00000970283.1; ENSP00000640342.1; ENSG00000132670.22. [P18433-6] DR Ensembl; ENST00000970285.1; ENSP00000640344.1; ENSG00000132670.22. [P18433-5] DR Ensembl; ENST00000970286.1; ENSP00000640345.1; ENSG00000132670.22. [P18433-5] DR Ensembl; ENST00000970287.1; ENSP00000640346.1; ENSG00000132670.22. [P18433-6] DR Ensembl; ENST00000970289.1; ENSP00000640348.1; ENSG00000132670.22. [P18433-6] DR Ensembl; ENST00000970290.1; ENSP00000640349.1; ENSG00000132670.22. [P18433-6] DR Ensembl; ENST00000970291.1; ENSP00000640350.1; ENSG00000132670.22. [P18433-6] 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 AGR; HGNC:9664; -. DR ClinPGx; PA34009; -. DR CTD; 5786; -. DR DisGeNET; 5786; -. DR GeneCards; PTPRA; -. DR HGNC; HGNC:9664; PTPRA. DR HPA; ENSG00000132670; Low tissue specificity. DR MalaCards; PTPRA; -. DR MIM; 176884; gene. DR OpenTargets; ENSG00000132670; -. DR VEuPathDB; HostDB:ENSG00000132670; -. DR eggNOG; KOG4228; Eukaryota. DR GeneTree; ENSGT00940000159585; -. DR HOGENOM; CLU_001645_8_0_1; -. DR InParanoid; P18433; -. DR OMA; TESWEGN; -. DR OrthoDB; 6144703at2759; -. DR PAN-GO; P18433; 2 GO annotations based on evolutionary models. DR PhylomeDB; P18433; -. 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 Agora; ENSG00000132670; -. DR BioGRID-ORCS; 5786; 13 hits in 1170 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 203 other cell types or tissues. DR ExpressionAtlas; P18433; baseline and differential. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005925; C:focal adhesion; ISS:UniProtKB. DR GO; GO:0016020; C:membrane; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0043235; C:signaling receptor complex; IDA:MGI. 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:0007229; P:integrin-mediated signaling pathway; ISS:UniProtKB. DR GO; GO:0051893; P:regulation of focal adhesion assembly; ISS:UniProtKB. DR GO; GO:0007165; P:signal transduction; IBA:GO_Central. DR CDD; cd14621; R-PTPc-A-1; 1. DR CDD; cd14623; R-PTPc-A-2; 1. DR FunFam; 3.90.190.10:FF:000007; Receptor-type tyrosine-protein phosphatase alpha; 1. DR FunFam; 3.90.190.10:FF:000021; Receptor-type tyrosine-protein phosphatase alpha; 1. DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 2. DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like. DR InterPro; IPR050348; Protein-Tyr_Phosphatase. 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; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE; 1. DR PANTHER; PTHR19134:SF433; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE ALPHA; 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; (Phosphotyrosine protein) phosphatases II; 2. DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 2. DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 2. DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2. DR PDBsum; 6UZT; -. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell junction; Cell membrane; KW Glycoprotein; Hydrolase; Membrane; Phosphoprotein; Protein phosphatase; KW Proteomics identification; Reference proteome; Repeat; Signal; KW 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..115 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 123..141 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 FT SRC-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 HELIX 284..286 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 314..317 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 HELIX 395..397 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 HELIX 578..580 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 607..610 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..723 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 //