PTPRK_HUMAN
ID PTPRK_HUMAN Reviewed; 1439 AA.
AC Q15262; B2RTQ8; B7ZMG0; Q14763; Q5TG10; Q5TG11;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=Receptor-type tyrosine-protein phosphatase kappa;
DE Short=Protein-tyrosine phosphatase kappa;
DE Short=R-PTP-kappa;
DE EC=3.1.3.48;
DE Flags: Precursor;
GN Name=PTPRK; Synonyms=PTPK;
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=8663237; DOI=10.1074/jbc.271.28.16712;
RA Fuchs M., Mueller T., Lerch M., Ullrich A.;
RT "Association of human protein-tyrosine phosphatase kappa with members of
RT the armadillo family.";
RL J. Biol. Chem. 271:16712-16719(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Foreskin;
RX PubMed=9047348; DOI=10.1016/s0378-1119(96)00684-1;
RA Yang Y., Gil M.C., Choi E.Y., Park S.H., Pyun K.H., Ha H.;
RT "Molecular cloning and chromosomal localization of a human gene homologous
RT to the murine R-PTP-kappa, a receptor-type protein tyrosine phosphatase.";
RL Gene 186:77-82(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
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] (ISOFORMS 3 AND 4).
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 [6]
RP FUNCTION IN EGFR REGULATION.
RX PubMed=19836242; DOI=10.1016/j.cub.2009.09.048;
RA Tarcic G., Boguslavsky S.K., Wakim J., Kiuchi T., Liu A., Reinitz F.,
RA Nathanson D., Takahashi T., Mischel P.S., Ng T., Yarden Y.;
RT "An unbiased screen identifies DEP-1 tumor suppressor as a phosphatase
RT controlling EGFR endocytosis.";
RL Curr. Biol. 19:1788-1798(2009).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-416.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-416.
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 [9]
RP IDENTIFICATION BY 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 [10]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 865-1154.
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).
CC -!- FUNCTION: Regulation of processes involving cell contact and adhesion
CC such as growth control, tumor invasion, and metastasis. Negative
CC regulator of EGFR signaling pathway. Forms complexes with beta-catenin
CC and gamma-catenin/plakoglobin. Beta-catenin may be a substrate for the
CC catalytic activity of PTPRK/PTP-kappa. {ECO:0000269|PubMed:19836242}.
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 Q15262; P04626: ERBB2; NbExp=2; IntAct=EBI-474052, EBI-641062;
CC Q15262; P28300: LOX; NbExp=4; IntAct=EBI-474052, EBI-3893481;
CC Q15262; Q02763: TEK; NbExp=2; IntAct=EBI-474052, EBI-2257090;
CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction. Cell membrane;
CC Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q15262-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15262-2; Sequence=VSP_024819;
CC Name=3;
CC IsoId=Q15262-3; Sequence=VSP_024819, VSP_042049;
CC Name=4;
CC IsoId=Q15262-4; Sequence=VSP_024819, VSP_054480, VSP_042049;
CC -!- TISSUE SPECIFICITY: High levels in lung, brain and colon; less in
CC liver, pancreas, stomach, kidney, placenta and mammary carcinoma.
CC -!- PTM: This protein undergoes proteolytic processing.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 2B subfamily. {ECO:0000305}.
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DR EMBL; Z70660; CAA94519.1; -; mRNA.
DR EMBL; L77886; AAC37599.1; -; mRNA.
DR EMBL; AL035470; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL034349; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL590006; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL451073; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL357621; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL035465; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL035594; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW48086.1; -; Genomic_DNA.
DR EMBL; BC140775; AAI40776.1; -; mRNA.
DR EMBL; BC144512; AAI44513.1; -; mRNA.
DR EMBL; BC144513; AAI44514.1; -; mRNA.
DR CCDS; CCDS47473.1; -. [Q15262-3]
DR CCDS; CCDS5137.1; -. [Q15262-2]
DR CCDS; CCDS75517.1; -. [Q15262-1]
DR CCDS; CCDS78179.1; -. [Q15262-4]
DR PIR; JC6312; JC6312.
DR RefSeq; NP_001129120.1; NM_001135648.2. [Q15262-3]
DR RefSeq; NP_001278910.1; NM_001291981.1. [Q15262-4]
DR RefSeq; NP_001278913.1; NM_001291984.1. [Q15262-1]
DR RefSeq; NP_002835.2; NM_002844.3. [Q15262-2]
DR PDB; 2C7S; X-ray; 1.95 A; A=865-1154.
DR PDBsum; 2C7S; -.
DR AlphaFoldDB; Q15262; -.
DR SMR; Q15262; -.
DR BioGRID; 111760; 173.
DR IntAct; Q15262; 106.
DR MINT; Q15262; -.
DR STRING; 9606.ENSP00000357196; -.
DR DEPOD; PTPRK; -.
DR GlyConnect; 1709; 31 N-Linked glycans (6 sites).
DR GlyGen; Q15262; 13 sites, 31 N-linked glycans (6 sites).
DR iPTMnet; Q15262; -.
DR PhosphoSitePlus; Q15262; -.
DR BioMuta; PTPRK; -.
DR DMDM; 146345496; -.
DR EPD; Q15262; -.
DR jPOST; Q15262; -.
DR MassIVE; Q15262; -.
DR MaxQB; Q15262; -.
DR PaxDb; Q15262; -.
DR PeptideAtlas; Q15262; -.
DR PRIDE; Q15262; -.
DR ProteomicsDB; 60503; -. [Q15262-1]
DR ProteomicsDB; 60504; -. [Q15262-2]
DR ProteomicsDB; 60505; -. [Q15262-3]
DR ProteomicsDB; 7258; -.
DR Antibodypedia; 32782; 57 antibodies from 20 providers.
DR DNASU; 5796; -.
DR Ensembl; ENST00000368213.9; ENSP00000357196.5; ENSG00000152894.15. [Q15262-3]
DR Ensembl; ENST00000368215.7; ENSP00000357198.3; ENSG00000152894.15. [Q15262-1]
DR Ensembl; ENST00000368226.9; ENSP00000357209.4; ENSG00000152894.15. [Q15262-2]
DR Ensembl; ENST00000532331.5; ENSP00000432973.1; ENSG00000152894.15. [Q15262-4]
DR Ensembl; ENST00000618215.3; ENSP00000484742.2; ENSG00000273993.4. [Q15262-3]
DR Ensembl; ENST00000618924.4; ENSP00000483766.2; ENSG00000273993.4. [Q15262-2]
DR Ensembl; ENST00000619256.4; ENSP00000477791.2; ENSG00000273993.4. [Q15262-4]
DR Ensembl; ENST00000628183.2; ENSP00000486442.1; ENSG00000273993.4. [Q15262-1]
DR GeneID; 5796; -.
DR KEGG; hsa:5796; -.
DR MANE-Select; ENST00000368226.9; ENSP00000357209.4; NM_002844.4; NP_002835.2. [Q15262-2]
DR UCSC; uc003qbj.4; human. [Q15262-1]
DR CTD; 5796; -.
DR DisGeNET; 5796; -.
DR GeneCards; PTPRK; -.
DR HGNC; HGNC:9674; PTPRK.
DR HPA; ENSG00000152894; Low tissue specificity.
DR MIM; 602545; gene.
DR neXtProt; NX_Q15262; -.
DR OpenTargets; ENSG00000152894; -.
DR PharmGKB; PA34019; -.
DR VEuPathDB; HostDB:ENSG00000152894; -.
DR eggNOG; KOG4228; Eukaryota.
DR GeneTree; ENSGT00940000156249; -.
DR InParanoid; Q15262; -.
DR OrthoDB; 411281at2759; -.
DR PhylomeDB; Q15262; -.
DR TreeFam; TF312900; -.
DR BRENDA; 3.1.3.48; 2681.
DR PathwayCommons; Q15262; -.
DR Reactome; R-HSA-182971; EGFR downregulation.
DR SignaLink; Q15262; -.
DR SIGNOR; Q15262; -.
DR BioGRID-ORCS; 5796; 11 hits in 1082 CRISPR screens.
DR ChiTaRS; PTPRK; human.
DR EvolutionaryTrace; Q15262; -.
DR GeneWiki; PTPRK; -.
DR GenomeRNAi; 5796; -.
DR Pharos; Q15262; Tbio.
DR PRO; PR:Q15262; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q15262; protein.
DR Bgee; ENSG00000152894; Expressed in corpus callosum and 107 other tissues.
DR ExpressionAtlas; Q15262; baseline and differential.
DR Genevisible; Q15262; HS.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0031256; C:leading edge membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0008013; F:beta-catenin binding; IPI:UniProtKB.
DR GO; GO:0045295; F:gamma-catenin binding; IPI:UniProtKB.
DR GO; GO:0019901; F:protein kinase 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; NAS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IMP:UniProtKB.
DR GO; GO:0016477; P:cell migration; IMP:UniProtKB.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; IDA:UniProtKB.
DR GO; GO:0034644; P:cellular response to UV; IDA:UniProtKB.
DR GO; GO:0048041; P:focal adhesion assembly; IMP:UniProtKB.
DR GO; GO:0045786; P:negative regulation of cell cycle; IDA:UniProtKB.
DR GO; GO:0030336; P:negative regulation of cell migration; IDA:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:0010839; P:negative regulation of keratinocyte proliferation; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:UniProtKB.
DR GO; GO:0034394; P:protein localization to cell surface; IDA:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IDA:UniProtKB.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IDA:UniProtKB.
DR CDD; cd00063; FN3; 2.
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; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
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; PF07679; I-set; 1.
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; SM00409; IG; 1.
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; Cell junction; Cell membrane;
KW Disulfide bond; Glycoprotein; Hydrolase; Immunoglobulin domain; Membrane;
KW Phosphoprotein; Protein phosphatase; Receptor; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..1439
FT /note="Receptor-type tyrosine-protein phosphatase kappa"
FT /id="PRO_0000025446"
FT TOPO_DOM 27..752
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 753..774
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 775..1439
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 31..194
FT /note="MAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT DOMAIN 196..281
FT /note="Ig-like C2-type"
FT DOMAIN 294..389
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 392..488
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 491..595
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 597..680
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 887..1141
FT /note="Tyrosine-protein phosphatase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT DOMAIN 1173..1435
FT /note="Tyrosine-protein phosphatase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT ACT_SITE 1082
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 1376
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 1050
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1082..1088
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1126
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 643..644
FT /note="Cleavage"
FT /evidence="ECO:0000305"
FT MOD_RES 856
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35822"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 416
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:19349973"
FT CARBOHYD 424
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 436
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 462
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 552
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 586
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 590
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 607
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 690
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 216..270
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 732
FT /note="A -> AA (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9047348"
FT /id="VSP_024819"
FT VAR_SEQ 831
FT /note="Y -> LPNDPLVPTAVLVPITD (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054480"
FT VAR_SEQ 946
FT /note="I -> IDIWLYR (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042049"
FT CONFLICT 9
FT /note="L -> V (in Ref. 2; AAC37599)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="T -> S (in Ref. 1; CAA94519)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="A -> P (in Ref. 2; AAC37599)"
FT /evidence="ECO:0000305"
FT CONFLICT 422
FT /note="T -> S (in Ref. 2; AAC37599)"
FT /evidence="ECO:0000305"
FT CONFLICT 672..674
FT /note="AEL -> CRT (in Ref. 2; AAC37599)"
FT /evidence="ECO:0000305"
FT CONFLICT 715
FT /note="S -> T (in Ref. 2; AAC37599)"
FT /evidence="ECO:0000305"
FT CONFLICT 1366
FT /note="E -> K (in Ref. 2; AAC37599)"
FT /evidence="ECO:0000305"
FT HELIX 869..871
FT /evidence="ECO:0007829|PDB:2C7S"
FT HELIX 872..879
FT /evidence="ECO:0007829|PDB:2C7S"
FT STRAND 883..885
FT /evidence="ECO:0007829|PDB:2C7S"
FT HELIX 887..892
FT /evidence="ECO:0007829|PDB:2C7S"
FT HELIX 903..906
FT /evidence="ECO:0007829|PDB:2C7S"
FT HELIX 908..913
FT /evidence="ECO:0007829|PDB:2C7S"
FT HELIX 923..925
FT /evidence="ECO:0007829|PDB:2C7S"
FT HELIX 936..939
FT /evidence="ECO:0007829|PDB:2C7S"
FT STRAND 942..948
FT /evidence="ECO:0007829|PDB:2C7S"
FT STRAND 951..958
FT /evidence="ECO:0007829|PDB:2C7S"
FT HELIX 963..965
FT /evidence="ECO:0007829|PDB:2C7S"
FT HELIX 966..976
FT /evidence="ECO:0007829|PDB:2C7S"
FT STRAND 980..983
FT /evidence="ECO:0007829|PDB:2C7S"
FT STRAND 987..989
FT /evidence="ECO:0007829|PDB:2C7S"
FT STRAND 1001..1006
FT /evidence="ECO:0007829|PDB:2C7S"
FT STRAND 1009..1018
FT /evidence="ECO:0007829|PDB:2C7S"
FT STRAND 1020..1031
FT /evidence="ECO:0007829|PDB:2C7S"
FT STRAND 1038..1045
FT /evidence="ECO:0007829|PDB:2C7S"
FT STRAND 1050..1053
FT /evidence="ECO:0007829|PDB:2C7S"
FT HELIX 1058..1070
FT /evidence="ECO:0007829|PDB:2C7S"
FT STRAND 1078..1081
FT /evidence="ECO:0007829|PDB:2C7S"
FT STRAND 1083..1086
FT /evidence="ECO:0007829|PDB:2C7S"
FT HELIX 1087..1105
FT /evidence="ECO:0007829|PDB:2C7S"
FT STRAND 1106..1108
FT /evidence="ECO:0007829|PDB:2C7S"
FT HELIX 1110..1120
FT /evidence="ECO:0007829|PDB:2C7S"
FT HELIX 1128..1144
FT /evidence="ECO:0007829|PDB:2C7S"
FT TURN 1150..1153
FT /evidence="ECO:0007829|PDB:2C7S"
SQ SEQUENCE 1439 AA; 162102 MW; EE1EA6EA3CCA31ED CRC64;
MDTTAAAALP AFVALLLLSP WPLLGSAQGQ FSAGGCTFDD GPGACDYHQD LYDDFEWVHV
SAQEPHYLPP EMPQGSYMIV DSSDHDPGEK ARLQLPTMKE NDTHCIDFSY LLYSQKGLNP
GTLNILVRVN KGPLANPIWN VTGFTGRDWL RAELAVSTFW PNEYQVIFEA EVSGGRSGYI
AIDDIQVLSY PCDKSPHFLR LGDVEVNAGQ NATFQCIATG RDAVHNKLWL QRRNGEDIPV
AQTKNINHRR FAASFRLQEV TKTDQDLYRC VTQSERGSGV SNFAQLIVRE PPRPIAPPQL
LGVGPTYLLI QLNANSIIGD GPIILKEVEY RMTSGSWTET HAVNAPTYKL WHLDPDTEYE
IRVLLTRPGE GGTGLPGPPL ITRTKCAEPM RTPKTLKIAE IQARRIAVDW ESLGYNITRC
HTFNVTICYH YFRGHNESKA DCLDMDPKAP QHVVNHLPPY TNVSLKMILT NPEGRKESEE
TIIQTDEDVP GPVPVKSLQG TSFENKIFLN WKEPLDPNGI ITQYEISYSS IRSFDPAVPV
AGPPQTVSNL WNSTHHVFMH LHPGTTYQFF IRASTVKGFG PATAINVTTN ISAPTLPDYE
GVDASLNETA TTITVLLRPA QAKGAPISAY QIVVEELHPH RTKREAGAME CYQVPVTYQN
AMSGGAPYYF AAELPPGNLP EPAPFTVGDN RTYQGFWNPP LAPRKGYNIY FQAMSSVEKE
TKTQCVRIAT KAATEEPEVI PDPAKQTDRV VKIAGISAGI LVFILLLLVV ILIVKKSKLA
KKRKDAMGNT RQEMTHMVNA MDRSYADQST LHAEDPLSIT FMDQHNFSPR YENHSATAES
SRLLDVPRYL CEGTESPYQT GQLHPAIRVA DLLQHINLMK TSDSYGFKEE YESFFEGQSA
SWDVAKKDQN RAKNRYGNII AYDHSRVILQ PVEDDPSSDY INANYIDGYQ RPSHYIATQG
PVHETVYDFW RMIWQEQSAC IVMVTNLVEV GRVKCYKYWP DDTEVYGDFK VTCVEMEPLA
EYVVRTFTLE RRGYNEIREV KQFHFTGWPD HGVPYHATGL LSFIRRVKLS NPPSAGPIVV
HCSAGAGRTG CYIVIDIMLD MAEREGVVDI YNCVKALRSR RINMVQTEEQ YIFIHDAILE
ACLCGETAIP VCEFKAAYFD MIRIDSQTNS SHLKDEFQTL NSVTPRLQAE DCSIACLPRN
HDKNRFMDML PPDRCLPFLI TIDGESSNYI NAALMDSYRQ PAAFIVTQYP LPNTVKDFWR
LVYDYGCTSI VMLNEVDLSQ GCPQYWPEEG MLRYGPIQVE CMSCSMDCDV INRIFRICNL
TRPQEGYLMV QQFQYLGWAS HREVPGSKRS FLKLILQVEK WQEECEEGEG RTIIHCLNGG
GRSGMFCAIG IVVEMVKRQN VVDVFHAVKT LRNSKPNMVE APEQYRFCYD VALEYLESS
