PTN13_HUMAN
ID PTN13_HUMAN Reviewed; 2485 AA.
AC Q12923; B2RTR0; Q15159; Q15263; Q15264; Q15265; Q15674; Q16826; Q8IWH7;
AC Q9NYN9; Q9UDA8;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 227.
DE RecName: Full=Tyrosine-protein phosphatase non-receptor type 13;
DE EC=3.1.3.48 {ECO:0000269|PubMed:15611135, ECO:0000269|PubMed:19307596};
DE AltName: Full=Fas-associated protein-tyrosine phosphatase 1;
DE Short=FAP-1;
DE AltName: Full=PTP-BAS;
DE AltName: Full=Protein-tyrosine phosphatase 1E;
DE Short=PTP-E1;
DE Short=hPTPE1;
DE AltName: Full=Protein-tyrosine phosphatase PTPL1;
GN Name=PTPN13; Synonyms=PNP1, PTP1E, PTPL1;
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 4).
RC TISSUE=Mammary carcinoma;
RX PubMed=8071359; DOI=10.1016/s0021-9258(17)31792-1;
RA Banville D., Ahmad S., Stocco R., Shen S.-H.;
RT "A novel protein-tyrosine phosphatase with homology to both the
RT cytoskeletal proteins of the band 4.1 family and junction-associated
RT guanylate kinases.";
RL J. Biol. Chem. 269:22320-22327(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), AND ALTERNATIVE SPLICING.
RC TISSUE=Leukemia;
RX PubMed=8287977; DOI=10.1016/0014-5793(94)80273-4;
RA Maekawa K., Imagawa N., Nagamatsu M., Harada S.;
RT "Molecular cloning of a novel protein-tyrosine phosphatase containing a
RT membrane-binding domain and GLGF repeats.";
RL FEBS Lett. 337:200-206(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC TISSUE=Fibroblast;
RX PubMed=7929060; DOI=10.1016/s0021-9258(19)51050-x;
RA Saras J., Claesson-Welsh L., Heldin C.-H., Gonez L.J.;
RT "Cloning and characterization of PTPL1, a protein tyrosine phosphatase with
RT similarities to cytoskeletal-associated proteins.";
RL J. Biol. Chem. 269:24082-24089(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1323-1922 (ISOFORM 1).
RC TISSUE=Brain, and Eye;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 1216-2485 (ISOFORMS 1/2/3).
RC TISSUE=Pancreas;
RA Wang H.-Y.;
RL Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1279-1883 (ISOFORM 4).
RC TISSUE=Brain;
RX PubMed=7536343; DOI=10.1126/science.7536343;
RA Sato T., Irie S., Kitada S., Reed J.C.;
RT "FAP-1: a protein tyrosine phosphatase that associates with Fas.";
RL Science 268:411-415(1995).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1323-1821 (ISOFORMS 1/2/3), AND INTERACTION
RP WITH NGFR.
RX PubMed=10544233; DOI=10.1016/s0014-5793(99)01324-1;
RA Irie S., Hachiya T., Rabizadeh S., Maruyama W., Mukai J., Li Y., Reed J.C.,
RA Bredesen D.E., Sato T.A.;
RT "Functional interaction of Fas-associated phosphatase-1 (FAP-1) with
RT p75(NTR) and their effect on NF-kappaB activation.";
RL FEBS Lett. 460:191-198(1999).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2298-2414.
RC TISSUE=Leukemia;
RX PubMed=8483328;
RA Honda H., Shibuya M., Chiba S., Yazaki Y., Hirai H.;
RT "Identification of novel protein-tyrosine phosphatases in a human leukemia
RT cell line, F-36P.";
RL Leukemia 7:742-746(1993).
RN [9]
RP INTERACTION WITH ARHGAP29.
RX PubMed=9305890; DOI=10.1074/jbc.272.39.24333;
RA Saras J., Franzen P., Aspenstroem P., Hellman U., Gonez L.J., Heldin C.-H.;
RT "A novel GTPase-activating protein for Rho interacts with a PDZ domain of
RT the protein-tyrosine phosphatase PTPL1.";
RL J. Biol. Chem. 272:24333-24338(1997).
RN [10]
RP INTERACTION WITH TRIP6.
RX PubMed=10400701; DOI=10.1074/jbc.274.29.20679;
RA Murthy K.K., Clark K., Fortin Y., Shen S.-H., Banville D.;
RT "ZRP-1, a zyxin-related protein, interacts with the second PDZ domain of
RT the cytosolic protein tyrosine phosphatase hPTP1E.";
RL J. Biol. Chem. 274:20679-20687(1999).
RN [11]
RP INTERACTION TRIP6, AND SUBCELLULAR LOCATION.
RX PubMed=10826496; DOI=10.1078/s0171-9335(04)70031-x;
RA Cuppen E., van Ham M., Wansink D.G., de Leeuw A., Wieringa B., Hendriks W.;
RT "The zyxin-related protein TRIP6 interacts with PDZ motifs in the adaptor
RT protein RIL and the protein tyrosine phosphatase PTP-BL.";
RL Eur. J. Cell Biol. 79:283-293(2000).
RN [12]
RP INTERACTION WITH PKN2, AND SUBCELLULAR LOCATION.
RX PubMed=11356191; DOI=10.1016/s0014-5793(01)02401-2;
RA Gross C., Heumann R., Erdmann K.S.;
RT "The protein kinase C-related kinase PRK2 interacts with the protein
RT tyrosine phosphatase PTP-BL via a novel PDZ domain binding motif.";
RL FEBS Lett. 496:101-104(2001).
RN [13]
RP INTERACTION WITH PLEKHA1 AND PLEKHA2.
RX PubMed=14516276; DOI=10.1042/bj20031154;
RA Kimber W.A., Deak M., Prescott A.R., Alessi D.R.;
RT "Interaction of the protein tyrosine phosphatase PTPL1 with the
RT PtdIns(3,4)P2-binding adaptor protein TAPP1.";
RL Biochem. J. 376:525-535(2003).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [15]
RP CATALYTIC ACTIVITY, AND INTERACTION WITH PDLIM4.
RX PubMed=19307596; DOI=10.1083/jcb.200810155;
RA Zhang Y., Tu Y., Zhao J., Chen K., Wu C.;
RT "Reversion-induced LIM interaction with Src reveals a novel Src
RT inactivation cycle.";
RL J. Cell Biol. 184:785-792(2009).
RN [16]
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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1029 AND SER-1033, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240; SER-890; SER-908 AND
RP SER-1085, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [19]
RP FUNCTION, AND INTERACTION WITH FBXL2 AND PIK3R2.
RX PubMed=23604317; DOI=10.1038/ncb2731;
RA Kuchay S., Duan S., Schenkein E., Peschiaroli A., Saraf A., Florens L.,
RA Washburn M.P., Pagano M.;
RT "FBXL2- and PTPL1-mediated degradation of p110-free p85beta regulatory
RT subunit controls the PI(3)K signalling cascade.";
RL Nat. Cell Biol. 15:472-480(2013).
RN [20]
RP IDENTIFICATION IN A COMPLEX WITH ENTR1 AND GIT1, AND INTERACTION WITH
RP ENTR1.
RX PubMed=23108400; DOI=10.1038/onc.2012.485;
RA Hagemann N., Ackermann N., Christmann J., Brier S., Yu F., Erdmann K.S.;
RT "The serologically defined colon cancer antigen-3 interacts with the
RT protein tyrosine phosphatase PTPN13 and is involved in the regulation of
RT cytokinesis.";
RL Oncogene 32:4602-4613(2013).
RN [21]
RP TISSUE SPECIFICITY.
RX PubMed=29043977; DOI=10.7554/elife.27356;
RA Mishra A., Oules B., Pisco A.O., Ly T., Liakath-Ali K., Walko G.,
RA Viswanathan P., Tihy M., Nijjher J., Dunn S.J., Lamond A.I., Watt F.M.;
RT "A protein phosphatase network controls the temporal and spatial dynamics
RT of differentiation commitment in human epidermis.";
RL Elife 6:0-0(2017).
RN [22]
RP STRUCTURE BY NMR OF 1361-1456 UNCOMPLEXED AND IN COMPLEX WITH THE
RP C-TERMINUS OF TNFRSF6.
RX PubMed=10704206; DOI=10.1021/bi991913c;
RA Kozlov G., Gehring K., Ekiel I.;
RT "Solution structure of the PDZ2 domain from human phosphatase hPTP1E and
RT its interactions with C-terminal peptides from the Fas receptor.";
RL Biochemistry 39:2572-2580(2000).
RN [23]
RP STRUCTURE BY NMR OF 1361-1456 IN COMPLEX WITH THE C-TERMINUS OF THE GUANINE
RP NUCLEOTIDE EXCHANGE FACTOR RA-GEF-2.
RX PubMed=12095257; DOI=10.1016/s0022-2836(02)00544-2;
RA Kozlov G., Banville D., Gehring K., Ekiel I.;
RT "Solution structure of the PDZ2 domain from cytosolic human phosphatase
RT hPTP1E complexed with a peptide reveals contribution of the beta2-beta3
RT loop to PDZ domain-ligand interactions.";
RL J. Mol. Biol. 320:813-820(2002).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 2163-2477, FUNCTION, CATALYTIC
RP ACTIVITY, MUTAGENESIS OF ASP-2154; ARG-2205; GLN-2221; MET-2307; CYS-2408;
RP ARG-2444; HIS-2448; GLY-2449 AND GLU-2474, AND CHARACTERIZATION OF VARIANT
RP VAL-2458.
RX PubMed=15611135; DOI=10.1074/jbc.m412211200;
RA Villa F., Deak M., Bloomberg G.B., Alessi D.R., van Aalten D.M.;
RT "Crystal structure of the PTPL1/FAP-1 human tyrosine phosphatase mutated in
RT colorectal cancer: evidence for a second phosphotyrosine substrate
RT recognition pocket.";
RL J. Biol. Chem. 280:8180-8187(2005).
RN [25]
RP VARIANTS PRO-1419 AND MET-1522.
RX PubMed=12436199; DOI=10.1007/s100380200094;
RA Yoshida S., Harada H., Nagai H., Fukino K., Teramoto A., Emi M.;
RT "Head-to-head juxtaposition of Fas-associated phosphatase-1 (FAP-1) and c-
RT Jun NH2-terminal kinase 3 (JNK3) genes: genomic structure and seven
RT polymorphisms of the FAP-1 gene.";
RL J. Hum. Genet. 47:614-619(2002).
CC -!- FUNCTION: Tyrosine phosphatase which regulates negatively FAS-induced
CC apoptosis and NGFR-mediated pro-apoptotic signaling (PubMed:15611135).
CC May regulate phosphoinositide 3-kinase (PI3K) signaling through
CC dephosphorylation of PIK3R2 (PubMed:23604317).
CC {ECO:0000269|PubMed:15611135, ECO:0000269|PubMed:23604317}.
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;
CC Evidence={ECO:0000269|PubMed:15611135, ECO:0000269|PubMed:19307596};
CC -!- SUBUNIT: Interacts (via the first PDZ domain) with PLEKHA1 and PLEKHA2
CC (PubMed:14516276). Interacts (via the second PDZ domain) with TNFRSF6
CC (Fas receptor) (via C-terminus) (PubMed:10704206). Interacts (via the
CC second PDZ domain) with TRIP6 (via the third LIM domain and C-terminus)
CC (PubMed:10826496, PubMed:10400701). Interacts (via the third PDZ
CC domain) with NGFR (via C-terminal SVP motif) and PKN2 (via C-terminus)
CC (PubMed:10544233, PubMed:11356191). Interacts (via the second or fourth
CC PDZ domains) with PDLIM4 (via C-terminus only or via combined C-
CC terminus and LIM domain, but not LIM domain only). Found in a complex
CC with PDLIM4 and TRIP6 (By similarity). Interacts with PDLIM4; this
CC interaction results in dephosphorylation of SRC 'Tyr-419' by this
CC protein leading to its inactivation (PubMed:19307596). Interacts with
CC BRD7 (By similarity). Interacts with RAPGEF6 (PubMed:12095257).
CC Interacts with ARHGAP29 (PubMed:9305890). Interacts with PIK3R2;
CC dephosphorylates PIK3R2 (PubMed:23604317). Interacts with FBXL2
CC (PubMed:23604317). Interacts (via the FERM domain) with ENTR1
CC (PubMed:23108400). Found in a complex with ENTR1, PTPN13 and GIT1
CC (PubMed:23108400). {ECO:0000250|UniProtKB:Q64512,
CC ECO:0000269|PubMed:10400701, ECO:0000269|PubMed:10544233,
CC ECO:0000269|PubMed:10704206, ECO:0000269|PubMed:10826496,
CC ECO:0000269|PubMed:11356191, ECO:0000269|PubMed:12095257,
CC ECO:0000269|PubMed:14516276, ECO:0000269|PubMed:19307596,
CC ECO:0000269|PubMed:23108400, ECO:0000269|PubMed:23604317,
CC ECO:0000269|PubMed:9305890}.
CC -!- INTERACTION:
CC Q12923; P25445: FAS; NbExp=3; IntAct=EBI-355227, EBI-494743;
CC Q12923; Q9BUL8: PDCD10; NbExp=3; IntAct=EBI-355227, EBI-740195;
CC Q12923; Q8TEU7: RAPGEF6; NbExp=4; IntAct=EBI-355227, EBI-2693017;
CC Q12923; Q13501: SQSTM1; NbExp=2; IntAct=EBI-355227, EBI-307104;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:11356191}. Nucleus {ECO:0000269|PubMed:10826496,
CC ECO:0000269|PubMed:11356191}. Cell projection, lamellipodium
CC {ECO:0000269|PubMed:11356191}. Note=Colocalizes with F-actin
CC (PubMed:10826496). Colocalizes with PKN2 in lamellipodia-like
CC structure, regions of large actin turnover (PubMed:11356191).
CC {ECO:0000269|PubMed:10826496, ECO:0000269|PubMed:11356191}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q12923-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q12923-2; Sequence=VSP_000496;
CC Name=3;
CC IsoId=Q12923-3; Sequence=VSP_000497;
CC Name=4;
CC IsoId=Q12923-4; Sequence=VSP_007921;
CC -!- TISSUE SPECIFICITY: Expressed in keratinocytes (at protein level)
CC (PubMed:29043977). Present in most tissues with the exception of the
CC liver and skeletal muscle. Most abundant in lung, kidney and fetal
CC brain. {ECO:0000269|PubMed:29043977}.
CC -!- MISCELLANEOUS: [Isoform 4]: May be due to a competing donor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH39610.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/PTPN13ID41912ch4q21.html";
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; U12128; AAB60339.1; -; mRNA.
DR EMBL; D21209; BAA04750.1; -; mRNA.
DR EMBL; D21210; BAA04751.1; -; mRNA.
DR EMBL; D21211; BAA04752.1; -; mRNA.
DR EMBL; X80289; CAA56563.1; -; mRNA.
DR EMBL; BC039610; AAH39610.1; ALT_SEQ; mRNA.
DR EMBL; BC140777; AAI40778.1; -; mRNA.
DR EMBL; X79676; CAA56124.1; -; mRNA.
DR EMBL; L34583; AAC41755.1; -; mRNA.
DR EMBL; AF233323; AAF63474.1; -; mRNA.
DR CCDS; CCDS47093.1; -. [Q12923-4]
DR CCDS; CCDS47094.1; -. [Q12923-1]
DR CCDS; CCDS47095.1; -. [Q12923-3]
DR CCDS; CCDS47096.1; -. [Q12923-2]
DR PIR; A54971; A54971.
DR PIR; I67629; I67629.
DR PIR; I67630; I67630.
DR RefSeq; NP_006255.1; NM_006264.2. [Q12923-3]
DR RefSeq; NP_542414.1; NM_080683.2. [Q12923-1]
DR RefSeq; NP_542415.1; NM_080684.2. [Q12923-2]
DR RefSeq; NP_542416.1; NM_080685.2. [Q12923-4]
DR PDB; 1D5G; NMR; -; A=1361-1456.
DR PDB; 1Q7X; NMR; -; A=1358-1459.
DR PDB; 1WCH; X-ray; 1.85 A; A=2163-2477.
DR PDB; 2M0Z; NMR; -; A=1361-1456.
DR PDB; 2M10; NMR; -; A=1361-1456.
DR PDB; 3LNX; X-ray; 1.64 A; A/B/C/D/E/F=1361-1456.
DR PDB; 3LNY; X-ray; 1.30 A; A=1361-1456.
DR PDB; 3PDZ; NMR; -; A=1361-1456.
DR PDB; 5GLJ; X-ray; 1.60 A; A/B/C/D=1086-1178.
DR PDBsum; 1D5G; -.
DR PDBsum; 1Q7X; -.
DR PDBsum; 1WCH; -.
DR PDBsum; 2M0Z; -.
DR PDBsum; 2M10; -.
DR PDBsum; 3LNX; -.
DR PDBsum; 3LNY; -.
DR PDBsum; 3PDZ; -.
DR PDBsum; 5GLJ; -.
DR AlphaFoldDB; Q12923; -.
DR SMR; Q12923; -.
DR BioGRID; 111747; 133.
DR DIP; DIP-40449N; -.
DR ELM; Q12923; -.
DR IntAct; Q12923; 40.
DR MINT; Q12923; -.
DR STRING; 9606.ENSP00000394794; -.
DR BindingDB; Q12923; -.
DR ChEMBL; CHEMBL2976; -.
DR DEPOD; PTPN13; -.
DR GlyGen; Q12923; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q12923; -.
DR PhosphoSitePlus; Q12923; -.
DR BioMuta; PTPN13; -.
DR DMDM; 12643716; -.
DR EPD; Q12923; -.
DR jPOST; Q12923; -.
DR MassIVE; Q12923; -.
DR MaxQB; Q12923; -.
DR PaxDb; Q12923; -.
DR PeptideAtlas; Q12923; -.
DR PRIDE; Q12923; -.
DR ProteomicsDB; 59027; -. [Q12923-1]
DR ProteomicsDB; 59028; -. [Q12923-2]
DR ProteomicsDB; 59029; -. [Q12923-3]
DR ProteomicsDB; 59030; -. [Q12923-4]
DR Antibodypedia; 3696; 214 antibodies from 30 providers.
DR DNASU; 5783; -.
DR Ensembl; ENST00000316707.10; ENSP00000322675.6; ENSG00000163629.13. [Q12923-2]
DR Ensembl; ENST00000411767.7; ENSP00000407249.2; ENSG00000163629.13. [Q12923-1]
DR Ensembl; ENST00000427191.6; ENSP00000408368.2; ENSG00000163629.13. [Q12923-3]
DR Ensembl; ENST00000436978.5; ENSP00000394794.1; ENSG00000163629.13. [Q12923-4]
DR Ensembl; ENST00000511467.1; ENSP00000426626.1; ENSG00000163629.13. [Q12923-4]
DR GeneID; 5783; -.
DR KEGG; hsa:5783; -.
DR MANE-Select; ENST00000411767.7; ENSP00000407249.2; NM_080683.3; NP_542414.1.
DR UCSC; uc003hpy.4; human. [Q12923-1]
DR CTD; 5783; -.
DR DisGeNET; 5783; -.
DR GeneCards; PTPN13; -.
DR HGNC; HGNC:9646; PTPN13.
DR HPA; ENSG00000163629; Tissue enhanced (retina).
DR MIM; 600267; gene.
DR neXtProt; NX_Q12923; -.
DR OpenTargets; ENSG00000163629; -.
DR PharmGKB; PA33988; -.
DR VEuPathDB; HostDB:ENSG00000163629; -.
DR eggNOG; KOG0792; Eukaryota.
DR GeneTree; ENSGT00940000155133; -.
DR HOGENOM; CLU_000906_0_0_1; -.
DR InParanoid; Q12923; -.
DR OMA; ESPPHTI; -.
DR OrthoDB; 411281at2759; -.
DR PhylomeDB; Q12923; -.
DR TreeFam; TF315388; -.
DR BRENDA; 3.1.3.48; 2681.
DR PathwayCommons; Q12923; -.
DR Reactome; R-HSA-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-HSA-9008059; Interleukin-37 signaling.
DR Reactome; R-HSA-9696264; RND3 GTPase cycle.
DR Reactome; R-HSA-9696270; RND2 GTPase cycle.
DR Reactome; R-HSA-9696273; RND1 GTPase cycle.
DR SignaLink; Q12923; -.
DR SIGNOR; Q12923; -.
DR BioGRID-ORCS; 5783; 11 hits in 1076 CRISPR screens.
DR ChiTaRS; PTPN13; human.
DR EvolutionaryTrace; Q12923; -.
DR GeneWiki; PTPN13; -.
DR GenomeRNAi; 5783; -.
DR Pharos; Q12923; Tchem.
DR PRO; PR:Q12923; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q12923; protein.
DR Bgee; ENSG00000163629; Expressed in mucosa of paranasal sinus and 205 other tissues.
DR ExpressionAtlas; Q12923; baseline and differential.
DR Genevisible; Q12923; HS.
DR GO; GO:0044297; C:cell body; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0036312; F:phosphatidylinositol 3-kinase regulatory subunit binding; IPI:UniProtKB.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:UniProtKB.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:UniProtKB.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IMP:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:UniProtKB.
DR GO; GO:0014066; P:regulation of phosphatidylinositol 3-kinase signaling; IDA:UniProtKB.
DR CDD; cd14473; FERM_B-lobe; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.30.42.10; -; 5.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR000299; FERM_domain.
DR InterPro; IPR018979; FERM_N.
DR InterPro; IPR018980; FERM_PH-like_C.
DR InterPro; IPR011019; KIND_dom.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR012153; PTPN13.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR Pfam; PF09380; FERM_C; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF09379; FERM_N; 1.
DR Pfam; PF00595; PDZ; 5.
DR Pfam; PF00102; Y_phosphatase; 1.
DR PIRSF; PIRSF000933; Tyr-Ptase_nr13; 1.
DR PRINTS; PR00935; BAND41.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00295; B41; 1.
DR SMART; SM01196; FERM_C; 1.
DR SMART; SM00750; KIND; 1.
DR SMART; SM00228; PDZ; 5.
DR SMART; SM00194; PTPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF47031; SSF47031; 1.
DR SUPFAM; SSF50156; SSF50156; 5.
DR SUPFAM; SSF52799; SSF52799; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50057; FERM_3; 1.
DR PROSITE; PS51377; KIND; 1.
DR PROSITE; PS50106; PDZ; 5.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell projection; Coiled coil;
KW Cytoplasm; Cytoskeleton; Hydrolase; Nucleus; Phosphoprotein;
KW Protein phosphatase; Reference proteome; Repeat.
FT CHAIN 1..2485
FT /note="Tyrosine-protein phosphatase non-receptor type 13"
FT /id="PRO_0000219435"
FT DOMAIN 3..190
FT /note="KIND"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00709"
FT DOMAIN 572..872
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT DOMAIN 1093..1178
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1368..1452
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1501..1588
FT /note="PDZ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1788..1868
FT /note="PDZ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1882..1965
FT /note="PDZ 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 2213..2467
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 186..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 947..975
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 995..1049
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1227..1258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1273..1362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1608..1665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1715..1751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1971..1996
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2408..2414
FT /note="Substrate"
FT COILED 469..504
FT /evidence="ECO:0000255"
FT COMPBIAS 447..467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 953..969
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1007..1030
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1031..1045
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1273..1309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1310..1324
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1325..1359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1608..1630
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1631..1648
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1649..1665
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1735..1751
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2408
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000305"
FT BINDING 2378
FT /ligand="substrate"
FT BINDING 2408..2414
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 2452
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64512"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64512"
FT MOD_RES 890
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 897
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64512"
FT MOD_RES 908
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 911
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64512"
FT MOD_RES 914
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64512"
FT MOD_RES 1029
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1033
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1085
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 884..1074
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8287977"
FT /id="VSP_000496"
FT VAR_SEQ 1056..1074
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:7929060, ECO:0000303|PubMed:8287977"
FT /id="VSP_000497"
FT VAR_SEQ 1383
FT /note="T -> TVLFDK (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:7536343,
FT ECO:0000303|PubMed:8071359"
FT /id="VSP_007921"
FT VARIANT 1356
FT /note="F -> L (in dbSNP:rs10033029)"
FT /id="VAR_048359"
FT VARIANT 1419
FT /note="L -> P (in dbSNP:rs749353184)"
FT /evidence="ECO:0000269|PubMed:12436199"
FT /id="VAR_016200"
FT VARIANT 1522
FT /note="I -> M (in dbSNP:rs2230600)"
FT /evidence="ECO:0000269|PubMed:12436199"
FT /id="VAR_016201"
FT VARIANT 1625
FT /note="E -> K (in dbSNP:rs12500797)"
FT /id="VAR_024373"
FT VARIANT 1744
FT /note="S -> P (in dbSNP:rs17012064)"
FT /id="VAR_048360"
FT VARIANT 2081
FT /note="Y -> D (in dbSNP:rs989902)"
FT /id="VAR_024374"
FT VARIANT 2458
FT /note="I -> V (no effect on substrate affinity;
FT dbSNP:rs34226837)"
FT /evidence="ECO:0000269|PubMed:15611135"
FT /id="VAR_048361"
FT MUTAGEN 2154
FT /note="D->H: No effect on substrate affinity."
FT /evidence="ECO:0000269|PubMed:15611135"
FT MUTAGEN 2205
FT /note="R->W: No effect on substrate affinity."
FT /evidence="ECO:0000269|PubMed:15611135"
FT MUTAGEN 2221
FT /note="Q->M: Reduces substrate affinity 2 fold."
FT /evidence="ECO:0000269|PubMed:15611135"
FT MUTAGEN 2307
FT /note="M->T: Reduces substrate affinity 7 fold."
FT /evidence="ECO:0000269|PubMed:15611135"
FT MUTAGEN 2408
FT /note="C->S: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:15611135"
FT MUTAGEN 2444
FT /note="R->E: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:15611135"
FT MUTAGEN 2444
FT /note="R->K: Reduces substrate affinity 7 fold."
FT /evidence="ECO:0000269|PubMed:15611135"
FT MUTAGEN 2444
FT /note="R->Q: Strongly decreases catalytic activity."
FT /evidence="ECO:0000269|PubMed:15611135"
FT MUTAGEN 2448
FT /note="H->A: Reduces substrate affinity 2 fold."
FT /evidence="ECO:0000269|PubMed:15611135"
FT MUTAGEN 2449
FT /note="G->V: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:15611135"
FT MUTAGEN 2474
FT /note="E->D: No effect on substrate affinity."
FT /evidence="ECO:0000269|PubMed:15611135"
FT CONFLICT 1134..1135
FT /note="LD -> FH (in Ref. 3; CAA56563)"
FT /evidence="ECO:0000305"
FT CONFLICT 1216..1229
FT /note="KDHHWSRGTLRHIS -> DLSRSHCHVYLAHL (in Ref. 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 1238..1239
FT /note="GL -> A (in Ref. 5; CAA56124)"
FT /evidence="ECO:0000305"
FT CONFLICT 1357
FT /note="S -> P (in Ref. 5; CAA56124)"
FT /evidence="ECO:0000305"
FT CONFLICT 1362..1363
FT /note="KP -> RS (in Ref. 5; CAA56124)"
FT /evidence="ECO:0000305"
FT CONFLICT 1538
FT /note="P -> A (in Ref. 3; CAA56563)"
FT /evidence="ECO:0000305"
FT CONFLICT 1649
FT /note="R -> K (in Ref. 5; CAA56124)"
FT /evidence="ECO:0000305"
FT CONFLICT 1698..1714
FT /note="KSQEDTICTMFYYPQKI -> RVKKIPFVPCFTILRKR (in Ref. 5;
FT CAA56124)"
FT /evidence="ECO:0000305"
FT CONFLICT 1797
FT /note="G -> A (in Ref. 3; CAA56563)"
FT /evidence="ECO:0000305"
FT CONFLICT 1856..1857
FT /note="AA -> G (in Ref. 5; CAA56124)"
FT /evidence="ECO:0000305"
FT CONFLICT 2069
FT /note="A -> S (in Ref. 5; CAA56124)"
FT /evidence="ECO:0000305"
FT CONFLICT 2206..2210
FT /note="GLLDQ -> VARS (in Ref. 5; CAA56124)"
FT /evidence="ECO:0000305"
FT STRAND 1090..1097
FT /evidence="ECO:0007829|PDB:5GLJ"
FT TURN 1100..1102
FT /evidence="ECO:0007829|PDB:5GLJ"
FT STRAND 1105..1109
FT /evidence="ECO:0007829|PDB:5GLJ"
FT STRAND 1122..1126
FT /evidence="ECO:0007829|PDB:5GLJ"
FT HELIX 1131..1135
FT /evidence="ECO:0007829|PDB:5GLJ"
FT STRAND 1143..1147
FT /evidence="ECO:0007829|PDB:5GLJ"
FT HELIX 1157..1166
FT /evidence="ECO:0007829|PDB:5GLJ"
FT STRAND 1169..1177
FT /evidence="ECO:0007829|PDB:5GLJ"
FT STRAND 1366..1372
FT /evidence="ECO:0007829|PDB:3LNY"
FT STRAND 1374..1377
FT /evidence="ECO:0007829|PDB:1D5G"
FT STRAND 1379..1384
FT /evidence="ECO:0007829|PDB:3LNY"
FT STRAND 1385..1387
FT /evidence="ECO:0007829|PDB:2M0Z"
FT STRAND 1388..1390
FT /evidence="ECO:0007829|PDB:3LNY"
FT HELIX 1391..1393
FT /evidence="ECO:0007829|PDB:3LNY"
FT STRAND 1395..1400
FT /evidence="ECO:0007829|PDB:3LNY"
FT HELIX 1405..1409
FT /evidence="ECO:0007829|PDB:3LNY"
FT STRAND 1417..1421
FT /evidence="ECO:0007829|PDB:3LNY"
FT HELIX 1431..1439
FT /evidence="ECO:0007829|PDB:3LNY"
FT STRAND 1443..1450
FT /evidence="ECO:0007829|PDB:3LNY"
FT HELIX 2175..2179
FT /evidence="ECO:0007829|PDB:1WCH"
FT STRAND 2188..2190
FT /evidence="ECO:0007829|PDB:1WCH"
FT HELIX 2194..2209
FT /evidence="ECO:0007829|PDB:1WCH"
FT HELIX 2212..2220
FT /evidence="ECO:0007829|PDB:1WCH"
FT HELIX 2231..2233
FT /evidence="ECO:0007829|PDB:1WCH"
FT HELIX 2235..2238
FT /evidence="ECO:0007829|PDB:1WCH"
FT TURN 2257..2260
FT /evidence="ECO:0007829|PDB:1WCH"
FT STRAND 2264..2272
FT /evidence="ECO:0007829|PDB:1WCH"
FT STRAND 2275..2282
FT /evidence="ECO:0007829|PDB:1WCH"
FT HELIX 2287..2289
FT /evidence="ECO:0007829|PDB:1WCH"
FT HELIX 2290..2299
FT /evidence="ECO:0007829|PDB:1WCH"
FT STRAND 2304..2307
FT /evidence="ECO:0007829|PDB:1WCH"
FT STRAND 2311..2313
FT /evidence="ECO:0007829|PDB:1WCH"
FT STRAND 2331..2346
FT /evidence="ECO:0007829|PDB:1WCH"
FT STRAND 2348..2359
FT /evidence="ECO:0007829|PDB:1WCH"
FT TURN 2360..2363
FT /evidence="ECO:0007829|PDB:1WCH"
FT STRAND 2364..2373
FT /evidence="ECO:0007829|PDB:1WCH"
FT HELIX 2385..2398
FT /evidence="ECO:0007829|PDB:1WCH"
FT STRAND 2404..2407
FT /evidence="ECO:0007829|PDB:1WCH"
FT STRAND 2409..2412
FT /evidence="ECO:0007829|PDB:1WCH"
FT HELIX 2413..2429
FT /evidence="ECO:0007829|PDB:1WCH"
FT HELIX 2436..2444
FT /evidence="ECO:0007829|PDB:1WCH"
FT HELIX 2454..2475
FT /evidence="ECO:0007829|PDB:1WCH"
SQ SEQUENCE 2485 AA; 276906 MW; 8D1B31597C66962B CRC64;
MHVSLAEALE VRGGPLQEEE IWAVLNQSAE SLQELFRKVS LADPAALGFI ISPWSLLLLP
SGSVSFTDEN ISNQDLRAFT APEVLQNQSL TSLSDVEKIH IYSLGMTLYW GADYEVPQSQ
PIKLGDHLNS ILLGMCEDVI YARVSVRTVL DACSAHIRNS NCAPSFSYVK HLVKLVLGNL
SGTDQLSCNS EQKPDRSQAI RDRLRGKGLP TGRSSTSDVL DIQKPPLSHQ TFLNKGLSKS
MGFLSIKDTQ DENYFKDILS DNSGREDSEN TFSPYQFKTS GPEKKPIPGI DVLSKKKIWA
SSMDLLCTAD RDFSSGETAT YRRCHPEAVT VRTSTTPRKK EARYSDGSIA LDIFGPQKMD
PIYHTRELPT SSAISSALDR IRERQKKLQV LREAMNVEEP VRRYKTYHGD VFSTSSESPS
IISSESDFRQ VRRSEASKRF ESSSGLPGVD ETLSQGQSQR PSRQYETPFE GNLINQEIML
KRQEEELMQL QAKMALRQSR LSLYPGDTIK ASMLDITRDP LREIALETAM TQRKLRNFFG
PEFVKMTIEP FISLDLPRSI LTKKGKNEDN RRKVNIMLLN GQRLELTCDT KTICKDVFDM
VVAHIGLVEH HLFALATLKD NEYFFVDPDL KLTKVAPEGW KEEPKKKTKA TVNFTLFFRI
KFFMDDVSLI QHTLTCHQYY LQLRKDILEE RMHCDDETSL LLASLALQAE YGDYQPEVHG
VSYFRMEHYL PARVMEKLDL SYIKEELPKL HNTYVGASEK ETELEFLKVC QRLTEYGVHF
HRVHPEKKSQ TGILLGVCSK GVLVFEVHNG VRTLVLRFPW RETKKISFSK KKITLQNTSD
GIKHGFQTDN SKICQYLLHL CSYQHKFQLQ MRARQSNQDA QDIERASFRS LNLQAESVRG
FNMGRAISTG SLASSTLNKL AVRPLSVQAE ILKRLSCSEL SLYQPLQNSS KEKNDKASWE
EKPREMSKSY HDLSQASLYP HRKNVIVNME PPPQTVAELV GKPSHQMSRS DAESLAGVTK
LNNSKSVASL NRSPERRKHE SDSSSIEDPG QAYVLGMTMH SSGNSSSQVP LKENDVLHKR
WSIVSSPERE ITLVNLKKDA KYGLGFQIIG GEKMGRLDLG IFISSVAPGG PADLDGCLKP
GDRLISVNSV SLEGVSHHAA IEILQNAPED VTLVISQPKE KISKVPSTPV HLTNEMKNYM
KKSSYMQDSA IDSSSKDHHW SRGTLRHISE NSFGPSGGLR EGSLSSQDSR TESASLSQSQ
VNGFFASHLG DQTWQESQHG SPSPSVISKA TEKETFTDSN QSKTKKPGIS DVTDYSDRGD
SDMDEATYSS SQDHQTPKQE SSSSVNTSNK MNFKTFSSSP PKPGDIFEVE LAKNDNSLGI
SVTGGVNTSV RHGGIYVKAV IPQGAAESDG RIHKGDRVLA VNGVSLEGAT HKQAVETLRN
TGQVVHLLLE KGQSPTSKEH VPVTPQCTLS DQNAQGQGPE KVKKTTQVKD YSFVTEENTF
EVKLFKNSSG LGFSFSREDN LIPEQINASI VRVKKLFPGQ PAAESGKIDV GDVILKVNGA
SLKGLSQQEV ISALRGTAPE VFLLLCRPPP GVLPEIDTAL LTPLQSPAQV LPNSSKDSSQ
PSCVEQSTSS DENEMSDKSK KQCKSPSRRD SYSDSSGSGE DDLVTAPANI SNSTWSSALH
QTLSNMVSQA QSHHEAPKSQ EDTICTMFYY PQKIPNKPEF EDSNPSPLPP DMAPGQSYQP
QSESASSSSM DKYHIHHISE PTRQENWTPL KNDLENHLED FELEVELLIT LIKSEKGSLG
FTVTKGNQRI GCYVHDVIQD PAKSDGRLKP GDRLIKVNDT DVTNMTHTDA VNLLRAASKT
VRLVIGRVLE LPRIPMLPHL LPDITLTCNK EELGFSLCGG HDSLYQVVYI SDINPRSVAA
IEGNLQLLDV IHYVNGVSTQ GMTLEEVNRA LDMSLPSLVL KATRNDLPVV PSSKRSAVSA
PKSTKGNGSY SVGSCSQPAL TPNDSFSTVA GEEINEISYP KGKCSTYQIK GSPNLTLPKE
SYIQEDDIYD DSQEAEVIQS LLDVVDEEAQ NLLNENNAAG YSCGPGTLKM NGKLSEERTE
DTDCDGSPLP EYFTEATKMN GCEEYCEEKV KSESLIQKPQ EKKTDDDEIT WGNDELPIER
TNHEDSDKDH SFLTNDELAV LPVVKVLPSG KYTGANLKSV IRVLRGLLDQ GIPSKELENL
QELKPLDQCL IGQTKENRRK NRYKNILPYD ATRVPLGDEG GYINASFIKI PVGKEEFVYI
ACQGPLPTTV GDFWQMIWEQ KSTVIAMMTQ EVEGEKIKCQ RYWPNILGKT TMVSNRLRLA
LVRMQQLKGF VVRAMTLEDI QTREVRHISH LNFTAWPDHD TPSQPDDLLT FISYMRHIHR
SGPIITHCSA GIGRSGTLIC IDVVLGLISQ DLDFDISDLV RCMRLQRHGM VQTEDQYIFC
YQVILYVLTR LQAEEEQKQQ PQLLK
