PTPRT_HUMAN
ID PTPRT_HUMAN Reviewed; 1441 AA.
AC O14522; A8E4R6; O43655; O75664; Q5W0X9; Q5W0Y1; Q9BR24; Q9BR28; Q9H0Y8;
AC Q9NTL1; Q9NU72; Q9UBD2; Q9UJL7;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 6.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Receptor-type tyrosine-protein phosphatase T;
DE Short=R-PTP-T;
DE EC=3.1.3.48;
DE AltName: Full=Receptor-type tyrosine-protein phosphatase rho;
DE Short=RPTP-rho;
DE Flags: Precursor;
GN Name=PTPRT; Synonyms=KIAA0283;
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), CHARACTERIZATION, AND VARIANT
RP PRO-29.
RX PubMed=9602027; DOI=10.1016/s0169-328x(98)00014-x;
RA McAndrew P.E., Frostholm A., White R.A., Rotter A., Burghes A.H.M.;
RT "Identification and characterization of RPTP rho, a novel RPTP mu/kappa-
RT like receptor protein tyrosine phosphatase whose expression is restricted
RT to the central nervous system.";
RL Brain Res. Mol. Brain Res. 56:9-21(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT PRO-29.
RC TISSUE=Brain;
RX PubMed=9179496; DOI=10.1093/dnares/4.1.53;
RA Ohara O., Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N.,
RA Nomura N.;
RT "Construction and characterization of human brain cDNA libraries suitable
RT for analysis of cDNA clones encoding relatively large proteins.";
RL DNA Res. 4:53-59(1997).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT PRO-29.
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 [5]
RP ALTERNATIVE SPLICING.
RX PubMed=11423001; DOI=10.1186/1471-2164-2-1;
RA Besco J.A., Frostholm A., Popesco M.C., Burghes A.H.M., Rotter A.;
RT "Genomic organization and alternative splicing of the human and mouse
RT RPTPrho genes.";
RL BMC Genomics 2:1-1(2001).
RN [6]
RP ERRATUM OF PUBMED:11423001.
RX PubMed=11814386; DOI=10.1186/1471-2164-2-5;
RA Besco J.A., Frostholm A., Popesco M.C., Burghes A.H.M., Rotter A.;
RL BMC Genomics 2:5-5(2001).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 868-1151.
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 [8]
RP VARIANTS SER-74; THR-209; THR-218; SER-248; HIS-280; VAL-395; PHE-412;
RP CYS-453; LYS-510; MET-605; GLY-648; THR-707; VAL-707; PRO-708; ILE-771;
RP GLY-905; LYS-965; PRO-1096; ILE-1106; TRP-1190; LEU-1237; MET-1247;
RP LEU-1324; PHE-1329 AND MET-1346, AND TISSUE SPECIFICITY.
RX PubMed=15155950; DOI=10.1126/science.1096096;
RA Wang Z., Shen D., Parsons D.W., Bardelli A., Sager J., Szabo S., Ptak J.,
RA Silliman N., Peters B.A., van der Heijden M.S., Parmigiani G., Yan H.,
RA Wang T.-L., Riggins G., Powell S.M., Willson J.K.V., Markowitz S.,
RA Kinzler K.W., Vogelstein B., Velculescu V.E.;
RT "Mutational analysis of the tyrosine phosphatome in colorectal cancers.";
RL Science 304:1164-1166(2004).
RN [9]
RP VARIANT [LARGE SCALE ANALYSIS] LEU-1213.
RX PubMed=18987736; DOI=10.1038/nature07485;
RA Ley T.J., Mardis E.R., Ding L., Fulton B., McLellan M.D., Chen K.,
RA Dooling D., Dunford-Shore B.H., McGrath S., Hickenbotham M., Cook L.,
RA Abbott R., Larson D.E., Koboldt D.C., Pohl C., Smith S., Hawkins A.,
RA Abbott S., Locke D., Hillier L.W., Miner T., Fulton L., Magrini V.,
RA Wylie T., Glasscock J., Conyers J., Sander N., Shi X., Osborne J.R.,
RA Minx P., Gordon D., Chinwalla A., Zhao Y., Ries R.E., Payton J.E.,
RA Westervelt P., Tomasson M.H., Watson M., Baty J., Ivanovich J., Heath S.,
RA Shannon W.D., Nagarajan R., Walter M.J., Link D.C., Graubert T.A.,
RA DiPersio J.F., Wilson R.K.;
RT "DNA sequencing of a cytogenetically normal acute myeloid leukaemia
RT genome.";
RL Nature 456:66-72(2008).
RN [10]
RP VARIANT MET-1346.
RX PubMed=24123876; DOI=10.1136/jmedgenet-2013-101644;
RA Schuurs-Hoeijmakers J.H., Vulto-van Silfhout A.T., Vissers L.E.,
RA van de Vondervoort I.I., van Bon B.W., de Ligt J., Gilissen C.,
RA Hehir-Kwa J.Y., Neveling K., del Rosario M., Hira G., Reitano S.,
RA Vitello A., Failla P., Greco D., Fichera M., Galesi O., Kleefstra T.,
RA Greally M.T., Ockeloen C.W., Willemsen M.H., Bongers E.M., Janssen I.M.,
RA Pfundt R., Veltman J.A., Romano C., Willemsen M.A., van Bokhoven H.,
RA Brunner H.G., de Vries B.B., de Brouwer A.P.;
RT "Identification of pathogenic gene variants in small families with
RT intellectually disabled siblings by exome sequencing.";
RL J. Med. Genet. 50:802-811(2013).
CC -!- FUNCTION: May be involved in both signal transduction and cellular
CC adhesion in the CNS.
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 -!- INTERACTION:
CC O14522; P62993: GRB2; NbExp=2; IntAct=EBI-728180, EBI-401755;
CC O14522; Q16849: PTPRN; NbExp=3; IntAct=EBI-728180, EBI-728153;
CC O14522; Q99K10: Nlgn1; Xeno; NbExp=2; IntAct=EBI-728180, EBI-775037;
CC O14522; Q69ZK9: Nlgn2; Xeno; NbExp=2; IntAct=EBI-728180, EBI-775065;
CC O14522; Q9CS84: Nrxn1; Xeno; NbExp=2; IntAct=EBI-728180, EBI-399696;
CC O14522; Q6P9K9: Nrxn3; Xeno; NbExp=2; IntAct=EBI-728180, EBI-7281557;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=3;
CC IsoId=O14522-3; Sequence=Displayed;
CC Name=1;
CC IsoId=O14522-1; Sequence=VSP_040385, VSP_040386;
CC -!- TISSUE SPECIFICITY: Expressed in colon, lung, heart and testis, as well
CC as in fetal and adult brain. Not detected in muscle and peripheral
CC blood leukocytes. {ECO:0000269|PubMed:15155950}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 2B subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA22952.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF043644; AAD09421.2; -; mRNA.
DR EMBL; AB006621; BAA22952.2; ALT_INIT; mRNA.
DR EMBL; AL021395; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL022239; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL024473; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL031656; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL035459; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL049812; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL121763; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL136461; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z93942; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL031676; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL035666; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL109826; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL117374; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL359695; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC153300; AAI53301.1; -; mRNA.
DR CCDS; CCDS42874.1; -. [O14522-3]
DR RefSeq; NP_008981.4; NM_007050.5. [O14522-3]
DR RefSeq; NP_573400.3; NM_133170.3.
DR PDB; 2OOQ; X-ray; 1.80 A; A/B=868-1151.
DR PDBsum; 2OOQ; -.
DR AlphaFoldDB; O14522; -.
DR SMR; O14522; -.
DR BioGRID; 116296; 9.
DR DIP; DIP-33967N; -.
DR IntAct; O14522; 21.
DR MINT; O14522; -.
DR STRING; 9606.ENSP00000362294; -.
DR DEPOD; PTPRT; -.
DR GlyGen; O14522; 10 sites.
DR iPTMnet; O14522; -.
DR PhosphoSitePlus; O14522; -.
DR BioMuta; PTPRT; -.
DR EPD; O14522; -.
DR jPOST; O14522; -.
DR MassIVE; O14522; -.
DR MaxQB; O14522; -.
DR PaxDb; O14522; -.
DR PeptideAtlas; O14522; -.
DR PRIDE; O14522; -.
DR ProteomicsDB; 48065; -. [O14522-3]
DR ProteomicsDB; 48066; -. [O14522-1]
DR Antibodypedia; 2780; 110 antibodies from 32 providers.
DR DNASU; 11122; -.
DR Ensembl; ENST00000373187.6; ENSP00000362283.1; ENSG00000196090.13. [O14522-3]
DR Ensembl; ENST00000373193.7; ENSP00000362289.4; ENSG00000196090.13. [O14522-1]
DR GeneID; 11122; -.
DR KEGG; hsa:11122; -.
DR MANE-Select; ENST00000373187.6; ENSP00000362283.1; NM_007050.6; NP_008981.4.
DR UCSC; uc002xkg.4; human. [O14522-3]
DR CTD; 11122; -.
DR DisGeNET; 11122; -.
DR GeneCards; PTPRT; -.
DR HGNC; HGNC:9682; PTPRT.
DR HPA; ENSG00000196090; Tissue enhanced (brain, fallopian tube).
DR MIM; 608712; gene.
DR neXtProt; NX_O14522; -.
DR OpenTargets; ENSG00000196090; -.
DR PharmGKB; PA34027; -.
DR VEuPathDB; HostDB:ENSG00000196090; -.
DR eggNOG; KOG4228; Eukaryota.
DR GeneTree; ENSGT00940000155326; -.
DR HOGENOM; CLU_001645_0_0_1; -.
DR InParanoid; O14522; -.
DR OrthoDB; 411281at2759; -.
DR PhylomeDB; O14522; -.
DR TreeFam; TF312900; -.
DR BRENDA; 3.1.3.48; 2681.
DR PathwayCommons; O14522; -.
DR SignaLink; O14522; -.
DR SIGNOR; O14522; -.
DR BioGRID-ORCS; 11122; 13 hits in 1066 CRISPR screens.
DR ChiTaRS; PTPRT; human.
DR EvolutionaryTrace; O14522; -.
DR GeneWiki; PTPRT; -.
DR GenomeRNAi; 11122; -.
DR Pharos; O14522; Tbio.
DR PRO; PR:O14522; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; O14522; protein.
DR Bgee; ENSG00000196090; Expressed in Brodmann (1909) area 10 and 93 other tissues.
DR ExpressionAtlas; O14522; baseline and differential.
DR Genevisible; O14522; HS.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0051393; F:alpha-actinin binding; IEA:Ensembl.
DR GO; GO:0045294; F:alpha-catenin binding; IDA:UniProtKB.
DR GO; GO:0008013; F:beta-catenin binding; IPI:UniProtKB.
DR GO; GO:0045296; F:cadherin binding; IPI:UniProtKB.
DR GO; GO:0070097; F:delta-catenin binding; IPI:UniProtKB.
DR GO; GO:0045295; F:gamma-catenin binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:ARUK-UCL.
DR GO; GO:0019903; F:protein phosphatase binding; IPI:ARUK-UCL.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IMP:UniProtKB.
DR GO; GO:0097677; F:STAT family protein binding; IPI:ARUK-UCL.
DR GO; GO:0016790; F:thiolester hydrolase activity; IEA:Ensembl.
DR GO; GO:0005001; F:transmembrane receptor protein tyrosine phosphatase activity; IDA:ARUK-UCL.
DR GO; GO:0007155; P:cell adhesion; NAS:UniProtKB.
DR GO; GO:0071354; P:cellular response to interleukin-6; IDA:ARUK-UCL.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IDA:UniProtKB.
DR GO; GO:0030336; P:negative regulation of cell migration; IMP:ARUK-UCL.
DR GO; GO:1904893; P:negative regulation of receptor signaling pathway via STAT; IDA:ARUK-UCL.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IDA:ARUK-UCL.
DR GO; GO:1990264; P:peptidyl-tyrosine dephosphorylation involved in inactivation of protein kinase activity; IDA:ARUK-UCL.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:UniProtKB.
DR GO; GO:0007165; P:signal transduction; NAS:UniProtKB.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IMP:UniProtKB.
DR CDD; cd00063; FN3; 3.
DR CDD; cd06263; MAM; 1.
DR Gene3D; 2.60.40.10; -; 4.
DR Gene3D; 3.90.190.10; -; 2.
DR InterPro; IPR013320; ConA-like_dom_sf.
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; IPR000998; MAM_dom.
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; 2.
DR Pfam; PF00629; MAM; 1.
DR Pfam; PF00102; Y_phosphatase; 2.
DR PRINTS; PR00020; MAMDOMAIN.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00060; FN3; 3.
DR SMART; SM00137; MAM; 1.
DR SMART; SM00194; PTPc; 2.
DR SMART; SM00404; PTPc_motif; 2.
DR SUPFAM; SSF48726; SSF48726; 1.
DR SUPFAM; SSF49265; SSF49265; 2.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF52799; SSF52799; 2.
DR PROSITE; PS50853; FN3; 3.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS00740; MAM_1; 1.
DR PROSITE; PS50060; MAM_2; 1.
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; Disulfide bond; Glycoprotein;
KW Hydrolase; Immunoglobulin domain; Membrane; Phosphoprotein;
KW Protein phosphatase; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..1441
FT /note="Receptor-type tyrosine-protein phosphatase T"
FT /id="PRO_0000025463"
FT TOPO_DOM 26..747
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 748..768
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 769..1441
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 30..191
FT /note="MAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT DOMAIN 193..284
FT /note="Ig-like C2-type"
FT DOMAIN 291..384
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 389..483
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 484..590
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 591..726
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 889..1143
FT /note="Tyrosine-protein phosphatase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT DOMAIN 1175..1437
FT /note="Tyrosine-protein phosphatase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 790..839
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..839
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1084
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 1378
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 1052
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1084..1090
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1128
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 1208
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99M80"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 510
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 547
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 601
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 654
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 684
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 213..267
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 725
FT /note="K -> KAPMGSAQVTPGTPLCLLTT (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:9602027"
FT /id="VSP_040385"
FT VAR_SEQ 781
FT /note="L -> LSQR (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:9602027"
FT /id="VSP_040386"
FT VARIANT 29
FT /note="A -> P (in dbSNP:rs2867655)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9179496, ECO:0000269|PubMed:9602027"
FT /id="VAR_028795"
FT VARIANT 74
FT /note="F -> S (in a colorectal cancer)"
FT /evidence="ECO:0000269|PubMed:15155950"
FT /id="VAR_020746"
FT VARIANT 76
FT /note="M -> V (in dbSNP:rs17811401)"
FT /id="VAR_028796"
FT VARIANT 209
FT /note="A -> T (in some colorectal cancers)"
FT /evidence="ECO:0000269|PubMed:15155950"
FT /id="VAR_020747"
FT VARIANT 218
FT /note="K -> T (in a gastric cancer)"
FT /evidence="ECO:0000269|PubMed:15155950"
FT /id="VAR_020748"
FT VARIANT 248
FT /note="F -> S (in a colorectal cancer)"
FT /evidence="ECO:0000269|PubMed:15155950"
FT /id="VAR_020749"
FT VARIANT 280
FT /note="Y -> H (in a colorectal cancer)"
FT /evidence="ECO:0000269|PubMed:15155950"
FT /id="VAR_020750"
FT VARIANT 395
FT /note="I -> V (in a colorectal cancer)"
FT /evidence="ECO:0000269|PubMed:15155950"
FT /id="VAR_020751"
FT VARIANT 412
FT /note="Y -> F (in a colorectal cancer)"
FT /evidence="ECO:0000269|PubMed:15155950"
FT /id="VAR_020752"
FT VARIANT 453
FT /note="R -> C (in a gastric cancer; dbSNP:rs1371429276)"
FT /evidence="ECO:0000269|PubMed:15155950"
FT /id="VAR_020753"
FT VARIANT 510
FT /note="N -> K (in a colorectal cancer; dbSNP:rs749647294)"
FT /evidence="ECO:0000269|PubMed:15155950"
FT /id="VAR_020754"
FT VARIANT 605
FT /note="T -> M (in a colorectal cancer; dbSNP:rs1217327426)"
FT /evidence="ECO:0000269|PubMed:15155950"
FT /id="VAR_020755"
FT VARIANT 648
FT /note="V -> G (in a colorectal cancer)"
FT /evidence="ECO:0000269|PubMed:15155950"
FT /id="VAR_020756"
FT VARIANT 707
FT /note="A -> T (in a colorectal cancer)"
FT /evidence="ECO:0000269|PubMed:15155950"
FT /id="VAR_020757"
FT VARIANT 707
FT /note="A -> V (in a colorectal cancer)"
FT /evidence="ECO:0000269|PubMed:15155950"
FT /id="VAR_020758"
FT VARIANT 708
FT /note="L -> P (in a colorectal cancer)"
FT /evidence="ECO:0000269|PubMed:15155950"
FT /id="VAR_020759"
FT VARIANT 771
FT /note="R -> I (in a lung cancer)"
FT /evidence="ECO:0000269|PubMed:15155950"
FT /id="VAR_020760"
FT VARIANT 905
FT /note="D -> G (in a colorectal cancer)"
FT /evidence="ECO:0000269|PubMed:15155950"
FT /id="VAR_020761"
FT VARIANT 965
FT /note="Q -> K (in a colorectal cancer; reduced phosphatase
FT activity)"
FT /evidence="ECO:0000269|PubMed:15155950"
FT /id="VAR_020762"
FT VARIANT 1096
FT /note="A -> P (in a colorectal cancer)"
FT /evidence="ECO:0000269|PubMed:15155950"
FT /id="VAR_020763"
FT VARIANT 1106
FT /note="N -> I (in a colorectal cancer; reduced phosphatase
FT activity)"
FT /evidence="ECO:0000269|PubMed:15155950"
FT /id="VAR_020764"
FT VARIANT 1190
FT /note="R -> W (in a colorectal cancer; reduced phosphatase
FT activity; dbSNP:rs370873414)"
FT /evidence="ECO:0000269|PubMed:15155950"
FT /id="VAR_020765"
FT VARIANT 1213
FT /note="P -> L (in an acute myeloid leukemia sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:18987736"
FT /id="VAR_054144"
FT VARIANT 1237
FT /note="M -> L (in a colorectal cancer)"
FT /evidence="ECO:0000269|PubMed:15155950"
FT /id="VAR_020766"
FT VARIANT 1247
FT /note="V -> M (in a colorectal cancer; dbSNP:rs761148007)"
FT /evidence="ECO:0000269|PubMed:15155950"
FT /id="VAR_020767"
FT VARIANT 1324
FT /note="R -> L (in a lung cancer; reduced phosphatase
FT activity)"
FT /evidence="ECO:0000269|PubMed:15155950"
FT /id="VAR_020768"
FT VARIANT 1329
FT /note="Y -> F (in a colorectal cancer; dbSNP:rs1568910321)"
FT /evidence="ECO:0000269|PubMed:15155950"
FT /id="VAR_020769"
FT VARIANT 1346
FT /note="T -> M (found in a patient with severe intellectual
FT disability, behavioral problems, microcephaly, congenital
FT cardiac defect and herniation of the abdominal diaphragm;
FT also observed in some colorectal cancers; reduced
FT phosphatase activity; unknown pathological significance;
FT dbSNP:rs199947379)"
FT /evidence="ECO:0000269|PubMed:15155950,
FT ECO:0000269|PubMed:24123876"
FT /id="VAR_020770"
FT CONFLICT 60
FT /note="W -> T (in Ref. 1; AAD09421)"
FT /evidence="ECO:0000305"
FT CONFLICT 375
FT /note="P -> A (in Ref. 1; AAD09421)"
FT /evidence="ECO:0000305"
FT CONFLICT 867
FT /note="P -> L (in Ref. 1; AAD09421)"
FT /evidence="ECO:0000305"
FT HELIX 871..873
FT /evidence="ECO:0007829|PDB:2OOQ"
FT HELIX 874..882
FT /evidence="ECO:0007829|PDB:2OOQ"
FT HELIX 889..895
FT /evidence="ECO:0007829|PDB:2OOQ"
FT TURN 905..908
FT /evidence="ECO:0007829|PDB:2OOQ"
FT HELIX 910..915
FT /evidence="ECO:0007829|PDB:2OOQ"
FT HELIX 925..927
FT /evidence="ECO:0007829|PDB:2OOQ"
FT HELIX 938..941
FT /evidence="ECO:0007829|PDB:2OOQ"
FT STRAND 944..948
FT /evidence="ECO:0007829|PDB:2OOQ"
FT STRAND 951..953
FT /evidence="ECO:0007829|PDB:2OOQ"
FT STRAND 957..960
FT /evidence="ECO:0007829|PDB:2OOQ"
FT TURN 965..967
FT /evidence="ECO:0007829|PDB:2OOQ"
FT HELIX 968..978
FT /evidence="ECO:0007829|PDB:2OOQ"
FT STRAND 982..985
FT /evidence="ECO:0007829|PDB:2OOQ"
FT STRAND 989..991
FT /evidence="ECO:0007829|PDB:2OOQ"
FT STRAND 1003..1009
FT /evidence="ECO:0007829|PDB:2OOQ"
FT STRAND 1011..1020
FT /evidence="ECO:0007829|PDB:2OOQ"
FT STRAND 1022..1033
FT /evidence="ECO:0007829|PDB:2OOQ"
FT STRAND 1040..1047
FT /evidence="ECO:0007829|PDB:2OOQ"
FT HELIX 1060..1072
FT /evidence="ECO:0007829|PDB:2OOQ"
FT STRAND 1080..1083
FT /evidence="ECO:0007829|PDB:2OOQ"
FT STRAND 1085..1088
FT /evidence="ECO:0007829|PDB:2OOQ"
FT HELIX 1089..1107
FT /evidence="ECO:0007829|PDB:2OOQ"
FT STRAND 1108..1110
FT /evidence="ECO:0007829|PDB:2OOQ"
FT HELIX 1112..1122
FT /evidence="ECO:0007829|PDB:2OOQ"
FT HELIX 1130..1145
FT /evidence="ECO:0007829|PDB:2OOQ"
SQ SEQUENCE 1441 AA; 162134 MW; BE60F3DB2CE13539 CRC64;
MASLAALALS LLLRLQLPPL PGARAQSAAG GCSFDEHYSN CGYSVALGTN GFTWEQINTW
EKPMLDQAVP TGSFMMVNSS GRASGQKAHL LLPTLKENDT HCIDFHYYFS SRDRSSPGAL
NVYVKVNGGP QGNPVWNVSG VVTEGWVKAE LAISTFWPHF YQVIFESVSL KGHPGYIAVD
EVRVLAHPCR KAPHFLRLQN VEVNVGQNAT FQCIAGGKWS QHDKLWLQQW NGRDTALMVT
RVVNHRRFSA TVSVADTAQR SVSKYRCVIR SDGGSGVSNY AELIVKEPPT PIAPPELLAV
GATYLWIKPN ANSIIGDGPI ILKEVEYRTT TGTWAETHIV DSPNYKLWHL DPDVEYEIRV
LLTRPGEGGT GPPGPPLTTR TKCADPVHGP QNVEIVDIRA RQLTLQWEPF GYAVTRCHSY
NLTVQYQYVF NQQQYEAEEV IQTSSHYTLR GLRPFMTIRL RLLLSNPEGR MESEELVVQT
EEDVPGAVPL ESIQGGPFEE KIYIQWKPPN ETNGVITLYE INYKAVGSLD PSADLSSQRG
KVFKLRNETH HLFVGLYPGT TYSFTIKAST AKGFGPPVTT RIATKISAPS MPEYDTDTPL
NETDTTITVM LKPAQSRGAP VSVYQLVVKE ERLQKSRRAA DIIECFSVPV SYRNASSLDS
LHYFAAELKP ANLPVTQPFT VGDNKTYNGY WNPPLSPLKS YSIYFQALSK ANGETKINCV
RLATKGASTQ NSNTVEPEKQ VDNTVKMAGV IAGLLMFIII LLGVMLTIKR RRNAYSYSYY
LKLAKKQKET QSGAQREMGP VASADKPTTK LSASRNDEGF SSSSQDVNGF TDGSRGELSQ
PTLTIQTHPY RTCDPVEMSY PRDQFQPAIR VADLLQHITQ MKRGQGYGFK EEYEALPEGQ
TASWDTAKED ENRNKNRYGN IISYDHSRVR LLVLDGDPHS DYINANYIDG YHRPRHYIAT
QGPMQETVKD FWRMIWQENS ASIVMVTNLV EVGRVKCVRY WPDDTEVYGD IKVTLIETEP
LAEYVIRTFT VQKKGYHEIR ELRLFHFTSW PDHGVPCYAT GLLGFVRQVK FLNPPEAGPI
VVHCSAGAGR TGCFIAIDTM LDMAENEGVV DIFNCVRELR AQRVNLVQTE EQYVFVHDAI
LEACLCGNTA IPVCEFRSLY YNISRLDPQT NSSQIKDEFQ TLNIVTPRVR PEDCSIGLLP
RNHDKNRSMD VLPLDRCLPF LISVDGESSN YINAALMDSH KQPAAFVVTQ HPLPNTVADF
WRLVFDYNCS SVVMLNEMDT AQFCMQYWPE KTSGCYGPIQ VEFVSADIDE DIIHRIFRIC
NMARPQDGYR IVQHLQYIGW PAYRDTPPSK RSLLKVVRRL EKWQEQYDGR EGRTVVHCLN
GGGRSGTFCA ICSVCEMIQQ QNIIDVFHIV KTLRNNKSNM VETLEQYKFV YEVALEYLSS
F
