PTPRG_HUMAN
ID PTPRG_HUMAN Reviewed; 1445 AA.
AC P23470; B2RU12; B7ZLX5; Q15623; Q59EE0; Q68DU5;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 4.
DT 03-AUG-2022, entry version 219.
DE RecName: Full=Receptor-type tyrosine-protein phosphatase gamma;
DE Short=Protein-tyrosine phosphatase gamma;
DE Short=R-PTP-gamma;
DE EC=3.1.3.48;
DE Flags: Precursor;
GN Name=PTPRG; Synonyms=PTPG;
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=8382771; DOI=10.1128/mcb.13.3.1497-1506.1993;
RA Barnea G., Silvennoinen O., Shaanan B., Honegger A.M., Canoll P.D.,
RA D'Eustachio P., Morse B., Levy J.B., Laforgia S., Huebner K.,
RA Musacchio J.M., Sap J., Schlessinger J.;
RT "Identification of a carbonic anhydrase-like domain in the extracellular
RT region of RPTP gamma defines a new subfamily of receptor tyrosine
RT phosphatases.";
RL Mol. Cell. Biol. 13:1497-1506(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT HIS-92.
RX PubMed=8833149; DOI=10.1006/geno.1996.0109;
RA Kastury K., Ohta M., Lasota J., Moir D., Dorman T., Laforgia S., Druck T.,
RA Huebner K.;
RT "Structure of the human receptor tyrosine phosphatase gamma gene (PTPRG)
RT and relation to the familial RCC t(3;8) chromosome translocation.";
RL Genomics 32:225-235(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Aortic endothelium;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [5]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP HIS-92.
RC TISSUE=Brain;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 711-1445 (ISOFORM 2).
RC TISSUE=Prostate;
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 836-1445.
RC TISSUE=Placenta;
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 [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 874-1118 AND 1175-1409.
RC TISSUE=Brain;
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 [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-113 AND ASN-444.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1182, AND IDENTIFICATION BY
RP 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 [12]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 827-1445, FUNCTION, CATALYTIC
RP ACTIVITY, SUBUNIT, AND MUTAGENESIS OF ARG-958; LYS-960; ASP-1305 AND
RP ASP-1306.
RX PubMed=19167335; DOI=10.1016/j.cell.2008.11.038;
RA Barr A.J., Ugochukwu E., Lee W.H., King O.N.F., Filippakopoulos P.,
RA Alfano I., Savitsky P., Burgess-Brown N.A., Mueller S., Knapp S.;
RT "Large-scale structural analysis of the classical human protein tyrosine
RT phosphatome.";
RL Cell 136:352-363(2009).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 830-1127.
RG Structural genomics consortium (SGC);
RT "Crystal structure of the human receptor phosphatase PTPRG.";
RL Submitted (JUL-2006) to the PDB data bank.
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 819-1130.
RG New York structural genomix research consortium (NYSGXRC);
RT "Structural genomics of protein phosphatases.";
RL Submitted (MAR-2008) to the PDB data bank.
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 56-320, INTERACTION WITH CNTN3;
RP CNTN4; CNTN5 AND CNTN6, AND DISULFIDE BOND.
RX PubMed=20133774; DOI=10.1073/pnas.0911235107;
RA Bouyain S., Watkins D.J.;
RT "The protein tyrosine phosphatases PTPRZ and PTPRG bind to distinct members
RT of the contactin family of neural recognition molecules.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:2443-2448(2010).
CC -!- FUNCTION: Possesses tyrosine phosphatase activity.
CC {ECO:0000269|PubMed:19167335}.
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, ECO:0000269|PubMed:19167335};
CC -!- SUBUNIT: Monomer; active form. Homodimer; inactive form (Probable).
CC Interacts with CNTN3, CNTN4, CNTN5 and CNTN6.
CC {ECO:0000269|PubMed:19167335, ECO:0000269|PubMed:20133774,
CC ECO:0000305}.
CC -!- INTERACTION:
CC P23470; P35222: CTNNB1; NbExp=2; IntAct=EBI-2258115, EBI-491549;
CC P23470; P00533: EGFR; NbExp=3; IntAct=EBI-2258115, EBI-297353;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P23470-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P23470-2; Sequence=VSP_024353;
CC -!- TISSUE SPECIFICITY: Found in a variety of tissues.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 5 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD93108.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/PTPRGID41930ch3p21.html";
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DR EMBL; L09247; AAA60224.1; -; mRNA.
DR EMBL; U46116; AAC50439.1; -; Genomic_DNA.
DR EMBL; U46089; AAC50439.1; JOINED; Genomic_DNA.
DR EMBL; U46090; AAC50439.1; JOINED; Genomic_DNA.
DR EMBL; U46091; AAC50439.1; JOINED; Genomic_DNA.
DR EMBL; U46092; AAC50439.1; JOINED; Genomic_DNA.
DR EMBL; U46093; AAC50439.1; JOINED; Genomic_DNA.
DR EMBL; U46094; AAC50439.1; JOINED; Genomic_DNA.
DR EMBL; U46095; AAC50439.1; JOINED; Genomic_DNA.
DR EMBL; U46096; AAC50439.1; JOINED; Genomic_DNA.
DR EMBL; U46097; AAC50439.1; JOINED; Genomic_DNA.
DR EMBL; U46098; AAC50439.1; JOINED; Genomic_DNA.
DR EMBL; U46099; AAC50439.1; JOINED; Genomic_DNA.
DR EMBL; U46100; AAC50439.1; JOINED; Genomic_DNA.
DR EMBL; U46101; AAC50439.1; JOINED; Genomic_DNA.
DR EMBL; U46102; AAC50439.1; JOINED; Genomic_DNA.
DR EMBL; U46103; AAC50439.1; JOINED; Genomic_DNA.
DR EMBL; U46104; AAC50439.1; JOINED; Genomic_DNA.
DR EMBL; U46105; AAC50439.1; JOINED; Genomic_DNA.
DR EMBL; U46106; AAC50439.1; JOINED; Genomic_DNA.
DR EMBL; U46107; AAC50439.1; JOINED; Genomic_DNA.
DR EMBL; U46108; AAC50439.1; JOINED; Genomic_DNA.
DR EMBL; U46109; AAC50439.1; JOINED; Genomic_DNA.
DR EMBL; U46110; AAC50439.1; JOINED; Genomic_DNA.
DR EMBL; U46111; AAC50439.1; JOINED; Genomic_DNA.
DR EMBL; U46112; AAC50439.1; JOINED; Genomic_DNA.
DR EMBL; U46113; AAC50439.1; JOINED; Genomic_DNA.
DR EMBL; U46114; AAC50439.1; JOINED; Genomic_DNA.
DR EMBL; U46115; AAC50439.1; JOINED; Genomic_DNA.
DR EMBL; AB209871; BAD93108.1; ALT_INIT; mRNA.
DR EMBL; AC004695; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092502; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC096919; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC098482; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC103587; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC103921; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC104849; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC105939; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471055; EAW65397.1; -; Genomic_DNA.
DR EMBL; BC140904; AAI40905.1; -; mRNA.
DR EMBL; BC144110; AAI44111.1; -; mRNA.
DR EMBL; CR749269; CAH18125.1; -; mRNA.
DR EMBL; X54132; CAA38067.1; -; mRNA.
DR CCDS; CCDS2895.1; -. [P23470-1]
DR PIR; A48148; A48148.
DR RefSeq; NP_002832.3; NM_002841.3. [P23470-1]
DR RefSeq; XP_005265410.1; XM_005265353.3.
DR PDB; 2H4V; X-ray; 1.55 A; A/B=831-1127.
DR PDB; 2HY3; X-ray; 2.60 A; A/B=820-1130.
DR PDB; 2NLK; X-ray; 2.40 A; A=827-1445.
DR PDB; 2PBN; X-ray; 1.70 A; A=820-1130.
DR PDB; 3JXH; X-ray; 1.70 A; C=56-320.
DR PDB; 3QCB; X-ray; 2.10 A; A/B=825-1128.
DR PDB; 3QCC; X-ray; 2.10 A; A/B=825-1128.
DR PDB; 3QCD; X-ray; 1.80 A; A=825-1128.
DR PDB; 3QCE; X-ray; 2.10 A; A/B=825-1128.
DR PDB; 3QCF; X-ray; 2.50 A; A/B=825-1128.
DR PDB; 3QCG; X-ray; 2.05 A; A=825-1128.
DR PDB; 3QCH; X-ray; 2.40 A; A=825-1128.
DR PDB; 3QCI; X-ray; 2.27 A; A=825-1128.
DR PDB; 3QCJ; X-ray; 2.26 A; A=825-1128.
DR PDB; 3QCK; X-ray; 2.05 A; A=825-1128.
DR PDB; 3QCL; X-ray; 2.40 A; A=825-1128.
DR PDB; 3QCM; X-ray; 2.40 A; A/B=825-1128.
DR PDB; 3QCN; X-ray; 2.41 A; A=825-1128.
DR PDB; 5E5R; X-ray; 2.60 A; A/C=56-320.
DR PDBsum; 2H4V; -.
DR PDBsum; 2HY3; -.
DR PDBsum; 2NLK; -.
DR PDBsum; 2PBN; -.
DR PDBsum; 3JXH; -.
DR PDBsum; 3QCB; -.
DR PDBsum; 3QCC; -.
DR PDBsum; 3QCD; -.
DR PDBsum; 3QCE; -.
DR PDBsum; 3QCF; -.
DR PDBsum; 3QCG; -.
DR PDBsum; 3QCH; -.
DR PDBsum; 3QCI; -.
DR PDBsum; 3QCJ; -.
DR PDBsum; 3QCK; -.
DR PDBsum; 3QCL; -.
DR PDBsum; 3QCM; -.
DR PDBsum; 3QCN; -.
DR PDBsum; 5E5R; -.
DR AlphaFoldDB; P23470; -.
DR SMR; P23470; -.
DR BioGRID; 111757; 100.
DR IntAct; P23470; 66.
DR MINT; P23470; -.
DR STRING; 9606.ENSP00000418112; -.
DR BindingDB; P23470; -.
DR ChEMBL; CHEMBL4905; -.
DR GuidetoPHARMACOLOGY; 1856; -.
DR DEPOD; PTPRG; -.
DR GlyConnect; 1970; 14 N-Linked glycans (6 sites).
DR GlyGen; P23470; 14 sites, 14 N-linked glycans (6 sites), 3 O-linked glycans (3 sites).
DR iPTMnet; P23470; -.
DR PhosphoSitePlus; P23470; -.
DR SwissPalm; P23470; -.
DR BioMuta; PTPRG; -.
DR DMDM; 229463033; -.
DR EPD; P23470; -.
DR jPOST; P23470; -.
DR MassIVE; P23470; -.
DR MaxQB; P23470; -.
DR PaxDb; P23470; -.
DR PeptideAtlas; P23470; -.
DR PRIDE; P23470; -.
DR ProteomicsDB; 54110; -. [P23470-1]
DR ProteomicsDB; 54111; -. [P23470-2]
DR Antibodypedia; 31706; 137 antibodies from 27 providers.
DR DNASU; 5793; -.
DR Ensembl; ENST00000295874.14; ENSP00000295874.10; ENSG00000144724.20. [P23470-2]
DR Ensembl; ENST00000474889.6; ENSP00000418112.1; ENSG00000144724.20. [P23470-1]
DR GeneID; 5793; -.
DR KEGG; hsa:5793; -.
DR MANE-Select; ENST00000474889.6; ENSP00000418112.1; NM_002841.4; NP_002832.3.
DR UCSC; uc003dlb.4; human. [P23470-1]
DR CTD; 5793; -.
DR DisGeNET; 5793; -.
DR GeneCards; PTPRG; -.
DR HGNC; HGNC:9671; PTPRG.
DR HPA; ENSG00000144724; Low tissue specificity.
DR MIM; 176886; gene.
DR neXtProt; NX_P23470; -.
DR OpenTargets; ENSG00000144724; -.
DR PharmGKB; PA34016; -.
DR VEuPathDB; HostDB:ENSG00000144724; -.
DR eggNOG; KOG0382; Eukaryota.
DR eggNOG; KOG0789; Eukaryota.
DR GeneTree; ENSGT00940000155048; -.
DR InParanoid; P23470; -.
DR OMA; NIHACYT; -.
DR OrthoDB; 251520at2759; -.
DR PhylomeDB; P23470; -.
DR TreeFam; TF351978; -.
DR BRENDA; 3.1.3.48; 2681.
DR PathwayCommons; P23470; -.
DR SignaLink; P23470; -.
DR SIGNOR; P23470; -.
DR BioGRID-ORCS; 5793; 10 hits in 1069 CRISPR screens.
DR ChiTaRS; PTPRG; human.
DR EvolutionaryTrace; P23470; -.
DR GeneWiki; PTPRG; -.
DR GenomeRNAi; 5793; -.
DR Pharos; P23470; Tchem.
DR PRO; PR:P23470; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P23470; protein.
DR Bgee; ENSG00000144724; Expressed in calcaneal tendon and 184 other tissues.
DR Genevisible; P23470; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:UniProtKB.
DR GO; GO:0005001; F:transmembrane receptor protein tyrosine phosphatase activity; TAS:ProtInc.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0010633; P:negative regulation of epithelial cell migration; IMP:UniProtKB.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IEA:Ensembl.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; TAS:ProtInc.
DR CDD; cd03122; alpha_CARP_receptor_like; 1.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.10.200.10; -; 1.
DR Gene3D; 3.90.190.10; -; 2.
DR InterPro; IPR041887; Alpha_CARP_receptor-type.
DR InterPro; IPR001148; CA_dom.
DR InterPro; IPR036398; CA_dom_sf.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
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; PF00194; Carb_anhydrase; 1.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF00102; Y_phosphatase; 2.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM01057; Carb_anhydrase; 1.
DR SMART; SM00060; FN3; 1.
DR SMART; SM00194; PTPc; 2.
DR SMART; SM00404; PTPc_motif; 2.
DR SUPFAM; SSF49265; SSF49265; 1.
DR SUPFAM; SSF51069; SSF51069; 1.
DR SUPFAM; SSF52799; SSF52799; 2.
DR PROSITE; PS51144; ALPHA_CA_2; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
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; Disulfide bond; Glycoprotein;
KW Hydrolase; Membrane; Phosphoprotein; Protein phosphatase;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT CHAIN 20..1445
FT /note="Receptor-type tyrosine-protein phosphatase gamma"
FT /id="PRO_0000025441"
FT TOPO_DOM 20..736
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 737..762
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 763..1445
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 58..321
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT DOMAIN 349..448
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 848..1119
FT /note="Tyrosine-protein phosphatase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT DOMAIN 1150..1410
FT /note="Tyrosine-protein phosphatase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 461..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..589
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..615
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..636
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..710
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1060
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT ECO:0000255|PROSITE-ProRule:PRU10044"
FT BINDING 1028
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1060..1066
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1104
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 1351
FT /note="Ancestral active site"
FT MOD_RES 1182
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 359
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 444
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 619
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 631
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 722
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 78..261
FT /evidence="ECO:0000269|PubMed:20133774"
FT VAR_SEQ 764..792
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_024353"
FT VARIANT 92
FT /note="Y -> H (in dbSNP:rs62620047)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:8833149"
FT /id="VAR_070892"
FT VARIANT 574
FT /note="G -> S (in dbSNP:rs2292245)"
FT /id="VAR_020301"
FT VARIANT 639
FT /note="Q -> R (in dbSNP:rs9870460)"
FT /id="VAR_031562"
FT MUTAGEN 958
FT /note="R->E: Loss of dimerization; when associated with E-
FT 960."
FT /evidence="ECO:0000269|PubMed:19167335"
FT MUTAGEN 960
FT /note="K->E: Loss of dimerization; when associated with E-
FT 958."
FT /evidence="ECO:0000269|PubMed:19167335"
FT MUTAGEN 1305
FT /note="D->K: Loss of dimerization; when associated with K-
FT 1306."
FT /evidence="ECO:0000269|PubMed:19167335"
FT MUTAGEN 1306
FT /note="D->K: Loss of dimerization; when associated with K-
FT 1305."
FT /evidence="ECO:0000269|PubMed:19167335"
FT CONFLICT 80
FT /note="G -> S (in Ref. 1; AAA60224)"
FT /evidence="ECO:0000305"
FT CONFLICT 549
FT /note="A -> V (in Ref. 2; AAC50439)"
FT /evidence="ECO:0000305"
FT CONFLICT 756
FT /note="I -> T (in Ref. 2; AAC50439)"
FT /evidence="ECO:0000305"
FT CONFLICT 805
FT /note="S -> R (in Ref. 7; CAH18125)"
FT /evidence="ECO:0000305"
FT CONFLICT 1316
FT /note="C -> Y (in Ref. 7; CAH18125)"
FT /evidence="ECO:0000305"
FT CONFLICT 1407
FT /note="M -> R (in Ref. 1; AAA60224 and 2; AAC50439)"
FT /evidence="ECO:0000305"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:3JXH"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:3JXH"
FT HELIX 71..74
FT /evidence="ECO:0007829|PDB:3JXH"
FT HELIX 76..79
FT /evidence="ECO:0007829|PDB:3JXH"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:5E5R"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:3JXH"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:3JXH"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:3JXH"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:3JXH"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:3JXH"
FT STRAND 143..152
FT /evidence="ECO:0007829|PDB:3JXH"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:3JXH"
FT STRAND 171..179
FT /evidence="ECO:0007829|PDB:3JXH"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:3JXH"
FT HELIX 187..192
FT /evidence="ECO:0007829|PDB:3JXH"
FT STRAND 197..209
FT /evidence="ECO:0007829|PDB:3JXH"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:3JXH"
FT HELIX 215..223
FT /evidence="ECO:0007829|PDB:3JXH"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:3JXH"
FT HELIX 238..241
FT /evidence="ECO:0007829|PDB:3JXH"
FT STRAND 249..254
FT /evidence="ECO:0007829|PDB:3JXH"
FT STRAND 265..272
FT /evidence="ECO:0007829|PDB:3JXH"
FT STRAND 274..277
FT /evidence="ECO:0007829|PDB:3JXH"
FT HELIX 278..285
FT /evidence="ECO:0007829|PDB:3JXH"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:3JXH"
FT STRAND 299..301
FT /evidence="ECO:0007829|PDB:3JXH"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:5E5R"
FT HELIX 831..861
FT /evidence="ECO:0007829|PDB:2H4V"
FT TURN 867..870
FT /evidence="ECO:0007829|PDB:2H4V"
FT HELIX 872..877
FT /evidence="ECO:0007829|PDB:2H4V"
FT HELIX 887..889
FT /evidence="ECO:0007829|PDB:2H4V"
FT STRAND 890..892
FT /evidence="ECO:0007829|PDB:2H4V"
FT TURN 899..901
FT /evidence="ECO:0007829|PDB:2PBN"
FT HELIX 902..905
FT /evidence="ECO:0007829|PDB:2PBN"
FT STRAND 906..912
FT /evidence="ECO:0007829|PDB:2H4V"
FT STRAND 915..917
FT /evidence="ECO:0007829|PDB:3QCJ"
FT STRAND 921..924
FT /evidence="ECO:0007829|PDB:2H4V"
FT HELIX 929..931
FT /evidence="ECO:0007829|PDB:2H4V"
FT HELIX 932..942
FT /evidence="ECO:0007829|PDB:2H4V"
FT STRAND 946..949
FT /evidence="ECO:0007829|PDB:2H4V"
FT STRAND 953..955
FT /evidence="ECO:0007829|PDB:2H4V"
FT STRAND 967..973
FT /evidence="ECO:0007829|PDB:2H4V"
FT STRAND 976..985
FT /evidence="ECO:0007829|PDB:2H4V"
FT STRAND 987..998
FT /evidence="ECO:0007829|PDB:2H4V"
FT STRAND 1016..1023
FT /evidence="ECO:0007829|PDB:2H4V"
FT STRAND 1028..1031
FT /evidence="ECO:0007829|PDB:2H4V"
FT HELIX 1036..1047
FT /evidence="ECO:0007829|PDB:2H4V"
FT STRAND 1056..1064
FT /evidence="ECO:0007829|PDB:2H4V"
FT HELIX 1065..1082
FT /evidence="ECO:0007829|PDB:2H4V"
FT STRAND 1084..1086
FT /evidence="ECO:0007829|PDB:2PBN"
FT HELIX 1088..1095
FT /evidence="ECO:0007829|PDB:2H4V"
FT TURN 1096..1098
FT /evidence="ECO:0007829|PDB:2H4V"
FT HELIX 1106..1121
FT /evidence="ECO:0007829|PDB:2H4V"
FT HELIX 1129..1131
FT /evidence="ECO:0007829|PDB:2NLK"
FT HELIX 1132..1139
FT /evidence="ECO:0007829|PDB:2NLK"
FT HELIX 1149..1157
FT /evidence="ECO:0007829|PDB:2NLK"
FT STRAND 1172..1174
FT /evidence="ECO:0007829|PDB:2NLK"
FT STRAND 1207..1211
FT /evidence="ECO:0007829|PDB:2NLK"
FT STRAND 1219..1224
FT /evidence="ECO:0007829|PDB:2NLK"
FT HELIX 1228..1230
FT /evidence="ECO:0007829|PDB:2NLK"
FT HELIX 1231..1241
FT /evidence="ECO:0007829|PDB:2NLK"
FT STRAND 1245..1248
FT /evidence="ECO:0007829|PDB:2NLK"
FT STRAND 1270..1272
FT /evidence="ECO:0007829|PDB:2NLK"
FT STRAND 1275..1286
FT /evidence="ECO:0007829|PDB:2NLK"
FT STRAND 1292..1305
FT /evidence="ECO:0007829|PDB:2NLK"
FT STRAND 1308..1315
FT /evidence="ECO:0007829|PDB:2NLK"
FT STRAND 1318..1320
FT /evidence="ECO:0007829|PDB:2NLK"
FT HELIX 1326..1328
FT /evidence="ECO:0007829|PDB:2NLK"
FT HELIX 1329..1340
FT /evidence="ECO:0007829|PDB:2NLK"
FT STRAND 1347..1354
FT /evidence="ECO:0007829|PDB:2NLK"
FT HELIX 1356..1374
FT /evidence="ECO:0007829|PDB:2NLK"
FT STRAND 1375..1377
FT /evidence="ECO:0007829|PDB:2NLK"
FT HELIX 1379..1389
FT /evidence="ECO:0007829|PDB:2NLK"
FT HELIX 1397..1408
FT /evidence="ECO:0007829|PDB:2NLK"
SQ SEQUENCE 1445 AA; 162003 MW; A48A007BA14082BC CRC64;
MRRLLEPCWW ILFLKITSSV LHYVVCFPAL TEGYVGALHE NRHGSAVQIR RRKASGDPYW
AYSGAYGPEH WVTSSVSCGG RHQSPIDILD QYARVGEEYQ ELQLDGFDNE SSNKTWMKNT
GKTVAILLKD DYFVSGAGLP GRFKAEKVEF HWGHSNGSAG SEHSINGRRF PVEMQIFFYN
PDDFDSFQTA ISENRIIGAM AIFFQVSPRD NSALDPIIHG LKGVVHHEKE TFLDPFVLRD
LLPASLGSYY RYTGSLTTPP CSEIVEWIVF RRPVPISYHQ LEAFYSIFTT EQQDHVKSVE
YLRNNFRPQQ RLHDRVVSKS AVRDSWNHDM TDFLENPLGT EASKVCSSPP IHMKVQPLNQ
TALQVSWSQP ETIYHPPIMN YMISYSWTKN EDEKEKTFTK DSDKDLKATI SHVSPDSLYL
FRVQAVCRND MRSDFSQTML FQANTTRIFQ GTRIVKTGVP TASPASSADM APISSGSSTW
TSSGIPFSFV SMATGMGPSS SGSQATVASV VTSTLLAGLG FGGGGISSFP STVWPTRLPT
AASASKQAAR PVLATTEALA SPGPDGDSSP TKDGEGTEEG EKDEKSESED GEREHEEDGE
KDSEKKEKSG VTHAAEERNQ TEPSPTPSSP NRTAEGGHQT IPGHEQDHTA VPTDQTGGRR
DAGPGLDPDM VTSTQVPPTA TEEQYAGSDP KRPEMPSKKP MSRGDRFSED SRFITVNPAE
KNTSGMISRP APGRMEWIIP LIVVSALTFV CLILLIAVLV YWRGCNKIKS KGFPRRFREV
PSSGERGEKG SRKCFQTAHF YVEDSSSPRV VPNESIPIIP IPDDMEAIPV KQFVKHIGEL
YSNNQHGFSE DFEEVQRCTA DMNITAEHSN HPENKHKNRY INILAYDHSR VKLRPLPGKD
SKHSDYINAN YVDGYNKAKA YIATQGPLKS TFEDFWRMIW EQNTGIIVMI TNLVEKGRRK
CDQYWPTENS EEYGNIIVTL KSTKIHACYT VRRFSIRNTK VKKGQKGNPK GRQNERVVIQ
YHYTQWPDMG VPEYALPVLT FVRRSSAARM PETGPVLVHC SAGVGRTGTY IVIDSMLQQI
KDKSTVNVLG FLKHIRTQRN YLVQTEEQYI FIHDALLEAI LGKETEVSSN QLHSYVNSIL
IPGVGGKTRL EKQFKLVTQC NAKYVECFSA QKECNKEKNR NSSVVPSERA RVGLAPLPGM
KGTDYINASY IMGYYRSNEF IITQHPLPHT TKDFWRMIWD HNAQIIVMLP DNQSLAEDEF
VYWPSREESM NCEAFTVTLI SKDRLCLSNE EQIIIHDFIL EATQDDYVLE VRHFQCPKWP
NPDAPISSTF ELINVIKEEA LTRDGPTIVH DEYGAVSAGM LCALTTLSQQ LENENAVDVF
QVAKMINLMR PGVFTDIEQY QFIYKAMLSL VSTKENGNGP MTVDKNGAVL IADESDPAES
MESLV
