PTPRF_HUMAN
ID PTPRF_HUMAN Reviewed; 1907 AA.
AC P10586; D3DPX6; D3DPX7; Q5T021; Q5T022; Q5W9G2; Q86WS0;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 241.
DE RecName: Full=Receptor-type tyrosine-protein phosphatase F;
DE EC=3.1.3.48;
DE AltName: Full=Leukocyte common antigen related;
DE Short=LAR;
DE Flags: Precursor;
GN Name=PTPRF; Synonyms=LAR;
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).
RC TISSUE=Tonsil;
RX PubMed=2972792; DOI=10.1084/jem.168.5.1523;
RA Streuli M., Krueger N.X., Hall L.R., Schlossman S.F., Saito H.;
RT "A new member of the immunoglobulin superfamily that has a cytoplasmic
RT region homologous to the leukocyte common antigen.";
RL J. Exp. Med. 168:1523-1530(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=15491607; DOI=10.1016/j.jmb.2004.09.028;
RA Homma K., Kikuno R.F., Nagase T., Ohara O., Nishikawa K.;
RT "Alternative splice variants encoding unstable protein domains exist in the
RT human brain.";
RL J. Mol. Biol. 343:1207-1220(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Retinoblastoma;
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 [6]
RP MUTAGENESIS.
RX PubMed=2554325; DOI=10.1073/pnas.86.22.8698;
RA Streuli M., Krueger N.X., Tsai A.Y.M., Saito H.;
RT "A family of receptor-linked protein tyrosine phosphatases in humans and
RT Drosophila.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:8698-8702(1989).
RN [7]
RP MUTAGENESIS.
RX PubMed=1695146; DOI=10.1002/j.1460-2075.1990.tb07415.x;
RA Streuli M., Krueger N.X., Thai T., Tang M., Saito H.;
RT "Distinct functional roles of the two intracellular phosphatase like
RT domains of the receptor-linked protein tyrosine phosphatases LCA and LAR.";
RL EMBO J. 9:2399-2407(1990).
RN [8]
RP INTERACTION WITH INSR.
RX PubMed=8995282; DOI=10.1074/jbc.272.11.7519;
RA Ahmad F., Goldstein B.J.;
RT "Functional association between the insulin receptor and the transmembrane
RT protein-tyrosine phosphatase LAR in intact cells.";
RL J. Biol. Chem. 272:448-457(1997).
RN [9]
RP INTERACTION WITH PPFIA1; PPFIA2 AND PPFIA3.
RX PubMed=9624153; DOI=10.1074/jbc.273.25.15611;
RA Serra-Pages C., Medley Q.G., Tang M., Hart A., Streuli M.;
RT "Liprins, a family of LAR transmembrane protein-tyrosine phosphatase-
RT interacting proteins.";
RL J. Biol. Chem. 273:15611-15620(1998).
RN [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-966.
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 GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-966.
RC TISSUE=Leukemic T-cell;
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP FUNCTION IN EPHA2 DEPHOSPHORYLATION.
RX PubMed=23358419; DOI=10.1128/mcb.01708-12;
RA Lee H., Bennett A.M.;
RT "Receptor protein tyrosine phosphatase-receptor tyrosine kinase substrate
RT screen identifies EphA2 as a target for LAR in cell migration.";
RL Mol. Cell. Biol. 33:1430-1441(2013).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1305, 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 [15]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1334-1897, FUNCTION, AND
RP MUTAGENESIS OF CYS-1548.
RX PubMed=10338209; DOI=10.1016/s0092-8674(00)80755-2;
RA Nam H.J., Poy F., Krueger N.X., Saito H., Frederick C.A.;
RT "Crystal structure of the tandem phosphatase domains of RPTP LAR.";
RL Cell 97:449-457(1999).
RN [16]
RP STRUCTURE BY NMR OF 319-415 AND 596-1010.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structures of FN3 domains of human receptor-type tyrosine-protein
RT phosphatase F.";
RL Submitted (AUG-2007) to the PDB data bank.
RN [17]
RP INVOLVEMENT IN BNAH2.
RX PubMed=24781087; DOI=10.1007/s00439-014-1445-1;
RA Borck G., de Vries L., Wu H.J., Smirin-Yosef P., Nurnberg G., Lagovsky I.,
RA Ishida L.H., Thierry P., Wieczorek D., Nurnberg P., Foley J., Kubisch C.,
RA Basel-Vanagaite L.;
RT "Homozygous truncating PTPRF mutation causes athelia.";
RL Hum. Genet. 133:1041-1047(2014).
CC -!- FUNCTION: Possible cell adhesion receptor. It possesses an intrinsic
CC protein tyrosine phosphatase activity (PTPase) and dephosphorylates
CC EPHA2 regulating its activity.
CC -!- FUNCTION: The first PTPase domain has enzymatic activity, while the
CC second one seems to affect the substrate specificity of the first one.
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: Interacts with GRIP1 (By similarity). Interacts with PPFIA1,
CC PPFIA2 and PPFIA3. Interacts with INSR. {ECO:0000250,
CC ECO:0000269|PubMed:8995282, ECO:0000269|PubMed:9624153}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P10586-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P10586-2; Sequence=VSP_036617;
CC -!- DISEASE: Aplasia or hypoplasia of the breasts and/or nipples 2 (BNAH2)
CC [MIM:616001]: A group of congenital deformities encompassing total
CC absence of breasts and nipple (amastia), absence of the nipple
CC (athelia), and absence of the mammary gland (amazia).
CC {ECO:0000269|PubMed:24781087}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 2A subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD66835.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA68754.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Y00815; CAA68754.1; ALT_INIT; mRNA.
DR EMBL; AB177857; BAD66835.1; ALT_INIT; mRNA.
DR EMBL; AC092815; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL583862; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX07086.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07087.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07088.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07089.1; -; Genomic_DNA.
DR EMBL; BC048768; AAH48768.1; -; mRNA.
DR CCDS; CCDS489.2; -. [P10586-1]
DR CCDS; CCDS490.2; -. [P10586-2]
DR PIR; S03841; TDHULK.
DR RefSeq; NP_002831.2; NM_002840.4. [P10586-1]
DR RefSeq; NP_569707.2; NM_130440.3. [P10586-2]
DR PDB; 1LAR; X-ray; 2.00 A; A/B=1333-1907.
DR PDB; 2DJU; NMR; -; A=319-411.
DR PDB; 2DN7; NMR; -; A=821-914.
DR PDB; 2EDX; NMR; -; A=596-716.
DR PDB; 2EDY; NMR; -; A=915-1010.
DR PDB; 2YD5; X-ray; 2.20 A; A=29-231.
DR PDB; 2YD8; X-ray; 2.05 A; A=29-231.
DR PDB; 4N5U; X-ray; 1.46 A; A=601-705.
DR PDB; 6KR4; X-ray; 2.85 A; A/B/C/D=1332-1907.
DR PDB; 6TPT; X-ray; 3.20 A; A=512-706.
DR PDB; 6TPU; X-ray; 1.55 A; A/B=513-706.
DR PDB; 6TPV; X-ray; 1.80 A; A/B=319-512.
DR PDB; 6TPW; X-ray; 2.90 A; A=319-706.
DR PDBsum; 1LAR; -.
DR PDBsum; 2DJU; -.
DR PDBsum; 2DN7; -.
DR PDBsum; 2EDX; -.
DR PDBsum; 2EDY; -.
DR PDBsum; 2YD5; -.
DR PDBsum; 2YD8; -.
DR PDBsum; 4N5U; -.
DR PDBsum; 6KR4; -.
DR PDBsum; 6TPT; -.
DR PDBsum; 6TPU; -.
DR PDBsum; 6TPV; -.
DR PDBsum; 6TPW; -.
DR AlphaFoldDB; P10586; -.
DR SMR; P10586; -.
DR BioGRID; 111756; 236.
DR IntAct; P10586; 48.
DR MINT; P10586; -.
DR STRING; 9606.ENSP00000353030; -.
DR BindingDB; P10586; -.
DR ChEMBL; CHEMBL3521; -.
DR GuidetoPHARMACOLOGY; 1855; -.
DR DEPOD; PTPRF; -.
DR GlyConnect; 1708; 21 N-Linked glycans (4 sites).
DR GlyGen; P10586; 7 sites, 21 N-linked glycans (4 sites).
DR iPTMnet; P10586; -.
DR PhosphoSitePlus; P10586; -.
DR SwissPalm; P10586; -.
DR BioMuta; PTPRF; -.
DR DMDM; 226709091; -.
DR EPD; P10586; -.
DR jPOST; P10586; -.
DR MassIVE; P10586; -.
DR MaxQB; P10586; -.
DR PaxDb; P10586; -.
DR PeptideAtlas; P10586; -.
DR PRIDE; P10586; -.
DR ProteomicsDB; 52612; -. [P10586-1]
DR ProteomicsDB; 52613; -. [P10586-2]
DR ABCD; P10586; 7 sequenced antibodies.
DR Antibodypedia; 2499; 325 antibodies from 32 providers.
DR DNASU; 5792; -.
DR Ensembl; ENST00000359947.9; ENSP00000353030.4; ENSG00000142949.17. [P10586-1]
DR Ensembl; ENST00000438120.5; ENSP00000398822.1; ENSG00000142949.17. [P10586-2]
DR GeneID; 5792; -.
DR KEGG; hsa:5792; -.
DR MANE-Select; ENST00000359947.9; ENSP00000353030.4; NM_002840.5; NP_002831.2.
DR UCSC; uc001cjr.4; human. [P10586-1]
DR CTD; 5792; -.
DR DisGeNET; 5792; -.
DR GeneCards; PTPRF; -.
DR HGNC; HGNC:9670; PTPRF.
DR HPA; ENSG00000142949; Low tissue specificity.
DR MalaCards; PTPRF; -.
DR MIM; 179590; gene.
DR MIM; 616001; phenotype.
DR neXtProt; NX_P10586; -.
DR OpenTargets; ENSG00000142949; -.
DR Orphanet; 180188; Isolated congenital breast hypoplasia/aplasia.
DR PharmGKB; PA34015; -.
DR VEuPathDB; HostDB:ENSG00000142949; -.
DR eggNOG; KOG4228; Eukaryota.
DR GeneTree; ENSGT00940000155060; -.
DR HOGENOM; CLU_001645_4_0_1; -.
DR InParanoid; P10586; -.
DR OMA; SSRRWEN; -.
DR OrthoDB; 220353at2759; -.
DR PhylomeDB; P10586; -.
DR TreeFam; TF312900; -.
DR BRENDA; 3.1.3.48; 2681.
DR PathwayCommons; P10586; -.
DR Reactome; R-HSA-388844; Receptor-type tyrosine-protein phosphatases.
DR Reactome; R-HSA-8849932; Synaptic adhesion-like molecules.
DR SignaLink; P10586; -.
DR SIGNOR; P10586; -.
DR BioGRID-ORCS; 5792; 8 hits in 1077 CRISPR screens.
DR ChiTaRS; PTPRF; human.
DR EvolutionaryTrace; P10586; -.
DR GeneWiki; PTPRF; -.
DR GenomeRNAi; 5792; -.
DR Pharos; P10586; Tchem.
DR PRO; PR:P10586; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P10586; protein.
DR Bgee; ENSG00000142949; Expressed in gingival epithelium and 198 other tissues.
DR ExpressionAtlas; P10586; baseline and differential.
DR Genevisible; P10586; 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:0043005; C:neuron projection; IEA:Ensembl.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0050839; F:cell adhesion molecule binding; IPI:SynGO-UCL.
DR GO; GO:0035373; F:chondroitin sulfate proteoglycan binding; IEA:Ensembl.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0005001; F:transmembrane receptor protein tyrosine phosphatase activity; TAS:ProtInc.
DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR GO; GO:0016477; P:cell migration; IMP:UniProtKB.
DR GO; GO:1900121; P:negative regulation of receptor binding; IMP:UniProtKB.
DR GO; GO:0031102; P:neuron projection regeneration; IEA:Ensembl.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IMP:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR GO; GO:0048679; P:regulation of axon regeneration; IEA:Ensembl.
DR GO; GO:0099560; P:synaptic membrane adhesion; IDA:SynGO.
DR GO; GO:0007185; P:transmembrane receptor protein tyrosine phosphatase signaling pathway; TAS:ProtInc.
DR CDD; cd00063; FN3; 8.
DR Gene3D; 2.60.40.10; -; 11.
DR Gene3D; 3.90.190.10; -; 2.
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; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
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; 7.
DR Pfam; PF07679; I-set; 3.
DR Pfam; PF00102; Y_phosphatase; 2.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00060; FN3; 8.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 3.
DR SMART; SM00194; PTPc; 2.
DR SMART; SM00404; PTPc_motif; 2.
DR SUPFAM; SSF48726; SSF48726; 3.
DR SUPFAM; SSF49265; SSF49265; 5.
DR SUPFAM; SSF52799; SSF52799; 2.
DR PROSITE; PS50853; FN3; 8.
DR PROSITE; PS50835; IG_LIKE; 3.
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 adhesion; Disulfide bond;
KW Glycoprotein; Heparin-binding; Hydrolase; Immunoglobulin domain; Membrane;
KW Phosphoprotein; Protein phosphatase; Receptor; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..1907
FT /note="Receptor-type tyrosine-protein phosphatase F"
FT /id="PRO_0000025432"
FT TOPO_DOM 30..1263
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1264..1284
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1285..1907
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 33..123
FT /note="Ig-like C2-type 1"
FT DOMAIN 135..224
FT /note="Ig-like C2-type 2"
FT DOMAIN 232..314
FT /note="Ig-like C2-type 3"
FT DOMAIN 321..411
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 416..510
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 514..604
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 609..706
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 711..819
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 820..914
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 918..1010
FT /note="Fibronectin type-III 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1014..1098
FT /note="Fibronectin type-III 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1352..1607
FT /note="Tyrosine-protein phosphatase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT DOMAIN 1639..1898
FT /note="Tyrosine-protein phosphatase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 398..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 693..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1548
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000305"
FT ACT_SITE 1839
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 68..77
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250"
FT BINDING 1516
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1548..1554
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1592
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 1305
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 721
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 966
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19349973"
FT DISULFID 54..107
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 156..207
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 253..298
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 772..780
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:15491607"
FT /id="VSP_036617"
FT VARIANT 412
FT /note="A -> V (in dbSNP:rs1065775)"
FT /id="VAR_054766"
FT VARIANT 450
FT /note="Y -> C (in dbSNP:rs3748796)"
FT /id="VAR_020299"
FT VARIANT 562
FT /note="D -> N (in dbSNP:rs3748800)"
FT /id="VAR_020300"
FT MUTAGEN 1548
FT /note="C->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10338209"
FT CONFLICT 646
FT /note="Y -> H (in Ref. 1; CAA68754)"
FT /evidence="ECO:0000305"
FT CONFLICT 1421
FT /note="I -> T (in Ref. 5; AAH48768)"
FT /evidence="ECO:0000305"
FT STRAND 31..37
FT /evidence="ECO:0007829|PDB:2YD8"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:2YD8"
FT STRAND 50..60
FT /evidence="ECO:0007829|PDB:2YD8"
FT STRAND 63..68
FT /evidence="ECO:0007829|PDB:2YD8"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:2YD8"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:2YD8"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:2YD8"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:2YD8"
FT HELIX 98..101
FT /evidence="ECO:0007829|PDB:2YD8"
FT STRAND 103..111
FT /evidence="ECO:0007829|PDB:2YD8"
FT STRAND 114..125
FT /evidence="ECO:0007829|PDB:2YD8"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:2YD8"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:2YD8"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:2YD8"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:2YD8"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:2YD8"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:2YD8"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:2YD8"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:2YD8"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:2YD8"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:2YD8"
FT STRAND 203..211
FT /evidence="ECO:0007829|PDB:2YD8"
FT STRAND 214..217
FT /evidence="ECO:0007829|PDB:2YD8"
FT STRAND 221..226
FT /evidence="ECO:0007829|PDB:2YD8"
FT STRAND 323..330
FT /evidence="ECO:0007829|PDB:6TPV"
FT STRAND 335..340
FT /evidence="ECO:0007829|PDB:6TPV"
FT STRAND 349..356
FT /evidence="ECO:0007829|PDB:6TPV"
FT STRAND 364..369
FT /evidence="ECO:0007829|PDB:6TPV"
FT STRAND 371..376
FT /evidence="ECO:0007829|PDB:6TPV"
FT STRAND 384..392
FT /evidence="ECO:0007829|PDB:6TPV"
FT STRAND 397..400
FT /evidence="ECO:0007829|PDB:6TPW"
FT STRAND 404..407
FT /evidence="ECO:0007829|PDB:6TPV"
FT STRAND 418..428
FT /evidence="ECO:0007829|PDB:6TPV"
FT STRAND 430..435
FT /evidence="ECO:0007829|PDB:6TPV"
FT STRAND 444..453
FT /evidence="ECO:0007829|PDB:6TPV"
FT HELIX 459..461
FT /evidence="ECO:0007829|PDB:6TPV"
FT STRAND 462..467
FT /evidence="ECO:0007829|PDB:6TPV"
FT STRAND 469..475
FT /evidence="ECO:0007829|PDB:6TPV"
FT STRAND 483..494
FT /evidence="ECO:0007829|PDB:6TPV"
FT STRAND 503..506
FT /evidence="ECO:0007829|PDB:6TPV"
FT STRAND 519..522
FT /evidence="ECO:0007829|PDB:6TPU"
FT STRAND 524..526
FT /evidence="ECO:0007829|PDB:6TPU"
FT STRAND 528..531
FT /evidence="ECO:0007829|PDB:6TPU"
FT STRAND 540..549
FT /evidence="ECO:0007829|PDB:6TPU"
FT HELIX 550..552
FT /evidence="ECO:0007829|PDB:6TPU"
FT STRAND 556..561
FT /evidence="ECO:0007829|PDB:6TPU"
FT STRAND 565..569
FT /evidence="ECO:0007829|PDB:6TPU"
FT STRAND 577..586
FT /evidence="ECO:0007829|PDB:6TPU"
FT STRAND 597..600
FT /evidence="ECO:0007829|PDB:6TPU"
FT STRAND 611..619
FT /evidence="ECO:0007829|PDB:4N5U"
FT STRAND 622..628
FT /evidence="ECO:0007829|PDB:4N5U"
FT HELIX 632..634
FT /evidence="ECO:0007829|PDB:4N5U"
FT STRAND 639..652
FT /evidence="ECO:0007829|PDB:4N5U"
FT STRAND 657..663
FT /evidence="ECO:0007829|PDB:4N5U"
FT STRAND 667..671
FT /evidence="ECO:0007829|PDB:4N5U"
FT STRAND 679..690
FT /evidence="ECO:0007829|PDB:4N5U"
FT STRAND 692..695
FT /evidence="ECO:0007829|PDB:4N5U"
FT STRAND 699..702
FT /evidence="ECO:0007829|PDB:4N5U"
FT STRAND 825..830
FT /evidence="ECO:0007829|PDB:2DN7"
FT STRAND 835..841
FT /evidence="ECO:0007829|PDB:2DN7"
FT STRAND 852..859
FT /evidence="ECO:0007829|PDB:2DN7"
FT STRAND 866..871
FT /evidence="ECO:0007829|PDB:2DN7"
FT STRAND 876..880
FT /evidence="ECO:0007829|PDB:2DN7"
FT STRAND 887..896
FT /evidence="ECO:0007829|PDB:2DN7"
FT STRAND 899..909
FT /evidence="ECO:0007829|PDB:2DN7"
FT STRAND 920..923
FT /evidence="ECO:0007829|PDB:2EDY"
FT STRAND 925..927
FT /evidence="ECO:0007829|PDB:2EDY"
FT STRAND 935..937
FT /evidence="ECO:0007829|PDB:2EDY"
FT STRAND 950..957
FT /evidence="ECO:0007829|PDB:2EDY"
FT STRAND 963..971
FT /evidence="ECO:0007829|PDB:2EDY"
FT STRAND 984..987
FT /evidence="ECO:0007829|PDB:2EDY"
FT HELIX 1334..1344
FT /evidence="ECO:0007829|PDB:1LAR"
FT TURN 1347..1349
FT /evidence="ECO:0007829|PDB:1LAR"
FT HELIX 1350..1358
FT /evidence="ECO:0007829|PDB:1LAR"
FT HELIX 1368..1371
FT /evidence="ECO:0007829|PDB:1LAR"
FT TURN 1373..1375
FT /evidence="ECO:0007829|PDB:1LAR"
FT HELIX 1376..1378
FT /evidence="ECO:0007829|PDB:1LAR"
FT TURN 1388..1390
FT /evidence="ECO:0007829|PDB:1LAR"
FT TURN 1401..1404
FT /evidence="ECO:0007829|PDB:1LAR"
FT STRAND 1407..1413
FT /evidence="ECO:0007829|PDB:1LAR"
FT STRAND 1416..1423
FT /evidence="ECO:0007829|PDB:1LAR"
FT TURN 1428..1430
FT /evidence="ECO:0007829|PDB:1LAR"
FT HELIX 1431..1440
FT /evidence="ECO:0007829|PDB:1LAR"
FT STRAND 1445..1448
FT /evidence="ECO:0007829|PDB:1LAR"
FT STRAND 1452..1454
FT /evidence="ECO:0007829|PDB:1LAR"
FT STRAND 1466..1472
FT /evidence="ECO:0007829|PDB:1LAR"
FT STRAND 1475..1484
FT /evidence="ECO:0007829|PDB:1LAR"
FT STRAND 1486..1497
FT /evidence="ECO:0007829|PDB:1LAR"
FT STRAND 1503..1511
FT /evidence="ECO:0007829|PDB:1LAR"
FT STRAND 1516..1518
FT /evidence="ECO:0007829|PDB:1LAR"
FT HELIX 1524..1536
FT /evidence="ECO:0007829|PDB:1LAR"
FT STRAND 1544..1553
FT /evidence="ECO:0007829|PDB:1LAR"
FT HELIX 1554..1571
FT /evidence="ECO:0007829|PDB:1LAR"
FT STRAND 1572..1574
FT /evidence="ECO:0007829|PDB:6KR4"
FT HELIX 1576..1584
FT /evidence="ECO:0007829|PDB:1LAR"
FT HELIX 1594..1610
FT /evidence="ECO:0007829|PDB:1LAR"
FT HELIX 1617..1619
FT /evidence="ECO:0007829|PDB:1LAR"
FT HELIX 1620..1627
FT /evidence="ECO:0007829|PDB:1LAR"
FT HELIX 1638..1644
FT /evidence="ECO:0007829|PDB:1LAR"
FT TURN 1645..1647
FT /evidence="ECO:0007829|PDB:1LAR"
FT TURN 1657..1660
FT /evidence="ECO:0007829|PDB:1LAR"
FT HELIX 1662..1667
FT /evidence="ECO:0007829|PDB:1LAR"
FT TURN 1677..1679
FT /evidence="ECO:0007829|PDB:1LAR"
FT TURN 1690..1693
FT /evidence="ECO:0007829|PDB:1LAR"
FT STRAND 1696..1700
FT /evidence="ECO:0007829|PDB:1LAR"
FT STRAND 1703..1705
FT /evidence="ECO:0007829|PDB:1LAR"
FT STRAND 1709..1712
FT /evidence="ECO:0007829|PDB:1LAR"
FT HELIX 1717..1719
FT /evidence="ECO:0007829|PDB:1LAR"
FT HELIX 1720..1729
FT /evidence="ECO:0007829|PDB:1LAR"
FT STRAND 1734..1737
FT /evidence="ECO:0007829|PDB:1LAR"
FT STRAND 1741..1743
FT /evidence="ECO:0007829|PDB:1LAR"
FT STRAND 1746..1749
FT /evidence="ECO:0007829|PDB:1LAR"
FT STRAND 1755..1757
FT /evidence="ECO:0007829|PDB:1LAR"
FT STRAND 1759..1761
FT /evidence="ECO:0007829|PDB:1LAR"
FT STRAND 1764..1773
FT /evidence="ECO:0007829|PDB:1LAR"
FT STRAND 1775..1786
FT /evidence="ECO:0007829|PDB:1LAR"
FT TURN 1787..1789
FT /evidence="ECO:0007829|PDB:1LAR"
FT STRAND 1792..1800
FT /evidence="ECO:0007829|PDB:1LAR"
FT STRAND 1805..1807
FT /evidence="ECO:0007829|PDB:1LAR"
FT HELIX 1813..1828
FT /evidence="ECO:0007829|PDB:1LAR"
FT STRAND 1835..1844
FT /evidence="ECO:0007829|PDB:1LAR"
FT HELIX 1845..1862
FT /evidence="ECO:0007829|PDB:1LAR"
FT STRAND 1863..1865
FT /evidence="ECO:0007829|PDB:1LAR"
FT HELIX 1867..1874
FT /evidence="ECO:0007829|PDB:1LAR"
FT TURN 1875..1877
FT /evidence="ECO:0007829|PDB:1LAR"
FT HELIX 1885..1900
FT /evidence="ECO:0007829|PDB:1LAR"
SQ SEQUENCE 1907 AA; 212879 MW; 4A7C14A2090EA88F CRC64;
MAPEPAPGRT MVPLVPALVM LGLVAGAHGD SKPVFIKVPE DQTGLSGGVA SFVCQATGEP
KPRITWMKKG KKVSSQRFEV IEFDDGAGSV LRIQPLRVQR DEAIYECTAT NSLGEINTSA
KLSVLEEEQL PPGFPSIDMG PQLKVVEKAR TATMLCAAGG NPDPEISWFK DFLPVDPATS
NGRIKQLRSG ALQIESSEES DQGKYECVAT NSAGTRYSAP ANLYVRVRRV APRFSIPPSS
QEVMPGGSVN LTCVAVGAPM PYVKWMMGAE ELTKEDEMPV GRNVLELSNV VRSANYTCVA
ISSLGMIEAT AQVTVKALPK PPIDLVVTET TATSVTLTWD SGNSEPVTYY GIQYRAAGTE
GPFQEVDGVA TTRYSIGGLS PFSEYAFRVL AVNSIGRGPP SEAVRARTGE QAPSSPPRRV
QARMLSASTM LVQWEPPEEP NGLVRGYRVY YTPDSRRPPN AWHKHNTDAG LLTTVGSLLP
GITYSLRVLA FTAVGDGPPS PTIQVKTQQG VPAQPADFQA EVESDTRIQL SWLLPPQERI
IMYELVYWAA EDEDQQHKVT FDPTSSYTLE DLKPDTLYRF QLAARSDMGV GVFTPTIEAR
TAQSTPSAPP QKVMCVSMGS TTVRVSWVPP PADSRNGVIT QYSVAYEAVD GEDRGRHVVD
GISREHSSWD LVGLEKWTEY RVWVRAHTDV GPGPESSPVL VRTDEDVPSG PPRKVEVEPL
NSTAVHVYWK LPVPSKQHGQ IRGYQVTYVR LENGEPRGLP IIQDVMLAEA QWRPEESEDY
ETTISGLTPE TTYSVTVAAY TTKGDGARSK PKIVTTTGAV PGRPTMMIST TAMNTALLQW
HPPKELPGEL LGYRLQYCRA DEARPNTIDF GKDDQHFTVT GLHKGTTYIF RLAAKNRAGL
GEEFEKEIRT PEDLPSGFPQ NLHVTGLTTS TTELAWDPPV LAERNGRIIS YTVVFRDINS
QQELQNITTD TRFTLTGLKP DTTYDIKVRA WTSKGSGPLS PSIQSRTMPV EQVFAKNFRV
AAAMKTSVLL SWEVPDSYKS AVPFKILYNG QSVEVDGHSM RKLIADLQPN TEYSFVLMNR
GSSAGGLQHL VSIRTAPDLL PHKPLPASAY IEDGRFDLSM PHVQDPSLVR WFYIVVVPID
RVGGSMLTPR WSTPEELELD ELLEAIEQGG EEQRRRRRQA ERLKPYVAAQ LDVLPETFTL
GDKKNYRGFY NRPLSPDLSY QCFVLASLKE PMDQKRYASS PYSDEIVVQV TPAQQQEEPE
MLWVTGPVLA VILIILIVIA ILLFKRKRTH SPSSKDEQSI GLKDSLLAHS SDPVEMRRLN
YQTPGMRDHP PIPITDLADN IERLKANDGL KFSQEYESID PGQQFTWENS NLEVNKPKNR
YANVIAYDHS RVILTSIDGV PGSDYINANY IDGYRKQNAY IATQGPLPET MGDFWRMVWE
QRTATVVMMT RLEEKSRVKC DQYWPARGTE TCGLIQVTLL DTVELATYTV RTFALHKSGS
SEKRELRQFQ FMAWPDHGVP EYPTPILAFL RRVKACNPLD AGPMVVHCSA GVGRTGCFIV
IDAMLERMKH EKTVDIYGHV TCMRSQRNYM VQTEDQYVFI HEALLEAATC GHTEVPARNL
YAHIQKLGQV PPGESVTAME LEFKLLASSK AHTSRFISAN LPCNKFKNRL VNIMPYELTR
VCLQPIRGVE GSDYINASFL DGYRQQKAYI ATQGPLAEST EDFWRMLWEH NSTIIVMLTK
LREMGREKCH QYWPAERSAR YQYFVVDPMA EYNMPQYILR EFKVTDARDG QSRTIRQFQF
TDWPEQGVPK TGEGFIDFIG QVHKTKEQFG QDGPITVHCS AGVGRTGVFI TLSIVLERMR
YEGVVDMFQT VKTLRTQRPA MVQTEDQYQL CYRAALEYLG SFDHYAT
