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 27-MAR-2024, entry version 250. 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}; 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; 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; 248. DR IntAct; P10586; 50. 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 GlyCosmos; P10586; 7 sites, 21 glycans. DR GlyGen; P10586; 8 sites, 21 N-linked glycans (4 sites), 1 O-linked glycan (1 site). 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; 9606-ENSP00000353030; -. DR PeptideAtlas; P10586; -. DR ProteomicsDB; 52612; -. [P10586-1] DR ProteomicsDB; 52613; -. [P10586-2] DR Pumba; P10586; -. DR ABCD; P10586; 7 sequenced antibodies. DR Antibodypedia; 2499; 376 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 AGR; HGNC:9670; -. 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; YWAAENE; -. DR OrthoDB; 2875525at2759; -. 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-77387; Insulin receptor recycling. DR Reactome; R-HSA-8849932; Synaptic adhesion-like molecules. DR SignaLink; P10586; -. DR SIGNOR; P10586; -. DR BioGRID-ORCS; 5792; 10 hits in 1172 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 200 other cell types or tissues. DR ExpressionAtlas; P10586; baseline and differential. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. 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: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 CDD; cd05738; IgI_2_RPTP_IIa_LAR_like; 1. DR CDD; cd05739; IgI_3_RPTP_IIa_LAR_like; 1. DR CDD; cd14629; R-PTP-F-2; 1. DR CDD; cd14626; R-PTPc-F-1; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 11. DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 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 PANTHER; PTHR46957; CYTOKINE RECEPTOR; 1. DR PANTHER; PTHR46957:SF7; PROTEIN-TYROSINE-PHOSPHATASE; 1. DR Pfam; PF00041; fn3; 7. DR Pfam; PF07679; I-set; 3. DR Pfam; PF00102; Y_phosphatase; 2. DR PRINTS; PR00014; FNTYPEIII. 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; SSF52799; (Phosphotyrosine protein) phosphatases II; 2. DR SUPFAM; SSF49265; Fibronectin type III; 5. DR SUPFAM; SSF48726; Immunoglobulin; 3. 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. DR Genevisible; P10586; HS. 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 //