PTPRS_RAT
ID PTPRS_RAT Reviewed; 1907 AA.
AC Q64605; Q07808; Q3KRE9; Q64621; Q64675;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Receptor-type tyrosine-protein phosphatase S;
DE Short=R-PTP-S;
DE EC=3.1.3.48 {ECO:0000269|PubMed:8068021};
DE AltName: Full=Leukocyte common antigen-related protein-tyrosine phosphatase 2;
DE Short=LAR-PTP2 {ECO:0000303|PubMed:8068021};
DE AltName: Full=Receptor-type tyrosine-protein phosphatase sigma;
DE Short=R-PTP-sigma;
DE Flags: Precursor;
GN Name=Ptprs;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), CATALYTIC ACTIVITY, FUNCTION, AND
RP TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=8068021; DOI=10.1042/bj3020039;
RA Zhang W.-R., Hashimoto N., Ahmad F., Ding W., Goldstein B.J.;
RT "Molecular cloning and expression of a unique receptor-like protein-
RT tyrosine-phosphatase in the leucocyte-common-antigen-related phosphate
RT family.";
RL Biochem. J. 302:39-47(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Prostate;
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 [3]
RP INTERACTION WITH NTRK1 AND NTRK3.
RX PubMed=17967490; DOI=10.1016/j.bbamcr.2007.06.008;
RA Faux C., Hawadle M., Nixon J., Wallace A., Lee S., Murray S., Stoker A.;
RT "PTPsigma binds and dephosphorylates neurotrophin receptors and can
RT suppress NGF-dependent neurite outgrowth from sensory neurons.";
RL Biochim. Biophys. Acta 1773:1689-1700(2007).
RN [4]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=22519304; DOI=10.1111/j.1471-4159.2012.07762.x;
RA Horn K.E., Xu B., Gobert D., Hamam B.N., Thompson K.M., Wu C.L.,
RA Bouchard J.F., Uetani N., Racine R.J., Tremblay M.L., Ruthazer E.S.,
RA Chapman C.A., Kennedy T.E.;
RT "Receptor protein tyrosine phosphatase sigma regulates synapse structure,
RT function and plasticity.";
RL J. Neurochem. 122:147-161(2012).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1328-1614.
RX PubMed=18058037; DOI=10.1007/s10969-007-9036-1;
RA Almo S.C., Bonanno J.B., Sauder J.M., Emtage S., Dilorenzo T.P.,
RA Malashkevich V., Wasserman S.R., Swaminathan S., Eswaramoorthy S.,
RA Agarwal R., Kumaran D., Madegowda M., Ragumani S., Patskovsky Y.,
RA Alvarado J., Ramagopal U.A., Faber-Barata J., Chance M.R., Sali A.,
RA Fiser A., Zhang Z.Y., Lawrence D.S., Burley S.K.;
RT "Structural genomics of protein phosphatases.";
RL J. Struct. Funct. Genomics 8:121-140(2007).
CC -!- FUNCTION: Cell surface receptor that binds to glycosaminoglycans,
CC including chondroitin sulfate proteoglycans and heparan sulfate
CC proteoglycans. Binding to chondroitin sulfate and heparan sulfate
CC proteoglycans has opposite effects on PTPRS oligomerization and
CC regulation of neurite outgrowth. Contributes to the inhibition of
CC neurite and axonal outgrowth by chondroitin sulfate proteoglycans, also
CC after nerve transection. Plays a role in stimulating neurite outgrowth
CC in response to the heparan sulfate proteoglycan GPC2. Required for
CC normal brain development, especially for normal development of the
CC pituitary gland and the olfactory bulb (By similarity). Functions as
CC tyrosine phosphatase (PubMed:8068021). Mediates dephosphorylation of
CC NTRK1, NTRK2 and NTRK3 (By similarity). Plays a role in down-regulation
CC of signaling cascades that lead to the activation of Akt and MAP
CC kinases. Down-regulates TLR9-mediated activation of NF-kappa-B, as well
CC as production of TNF, interferon alpha and interferon beta (By
CC similarity). {ECO:0000250|UniProtKB:B0V2N1,
CC ECO:0000250|UniProtKB:F1NWE3, ECO:0000269|PubMed:8068021}.
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, ECO:0000269|PubMed:8068021};
CC -!- SUBUNIT: Binding to large heparan sulfate proteoglycan structures
CC promotes oligomerization. Binding to chondroitin sulfate proteoglycan
CC does not lead to oligomerization (By similarity). Interacts (via Ig-
CC like domains) with NTRK1 and NTRK3, but does not form detectable
CC complexes with NTRK2 (PubMed:17967490). Interacts with PPFIA1, PPFIA2
CC and PPFIA3 (By similarity). {ECO:0000250|UniProtKB:B0V2N1,
CC ECO:0000250|UniProtKB:Q13332, ECO:0000269|PubMed:17967490}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22519304};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:B0V2N1}.
CC Cell projection, axon {ECO:0000250|UniProtKB:B0V2N1}. Perikaryon
CC {ECO:0000250|UniProtKB:B0V2N1}. Cytoplasmic vesicle, secretory vesicle,
CC synaptic vesicle membrane {ECO:0000269|PubMed:22519304}. Synapse,
CC synaptosome {ECO:0000269|PubMed:22519304}. Postsynaptic density
CC {ECO:0000269|PubMed:22519304}. Cell projection, neuron projection
CC {ECO:0000250|UniProtKB:B0V2N1}. Cell projection, growth cone
CC {ECO:0000250|UniProtKB:B0V2N1}. Note=Is rapidly internalized when
CC dendritic cells are stimulated with the TLR9 ligand cytidine-phosphate-
CC guanosine (CpG). Detected in a punctate pattern along neurites and axon
CC growth cones. {ECO:0000250|UniProtKB:B0V2N1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q64605-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q64605-2; Sequence=VSP_026932;
CC -!- TISSUE SPECIFICITY: Detected in brain neocortex (at protein level)
CC (PubMed:22519304). Detected in heart, testis and liver
CC (PubMed:8068021). Detected at lower levels in skeletal muscle, brain,
CC spleen and kidney (PubMed:8068021). {ECO:0000269|PubMed:22519304,
CC ECO:0000269|PubMed:8068021}.
CC -!- PTM: A cleavage occurs, separating the extracellular domain from the
CC transmembrane segment. This process called 'ectodomain shedding' is
CC thought to be involved in receptor desensitization, signal transduction
CC and/or membrane localization (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 2A subfamily. {ECO:0000305}.
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DR EMBL; L11587; AAC37656.1; -; mRNA.
DR EMBL; BC105753; AAI05754.1; -; mRNA.
DR PIR; I58148; I58148.
DR PIR; S46217; S46217.
DR RefSeq; NP_062013.1; NM_019140.2. [Q64605-2]
DR PDB; 2NV5; X-ray; 2.00 A; A/B/C=1328-1614.
DR PDBsum; 2NV5; -.
DR AlphaFoldDB; Q64605; -.
DR SMR; Q64605; -.
DR BioGRID; 247561; 3.
DR STRING; 10116.ENSRNOP00000065227; -.
DR GlyGen; Q64605; 4 sites.
DR iPTMnet; Q64605; -.
DR PhosphoSitePlus; Q64605; -.
DR PaxDb; Q64605; -.
DR PRIDE; Q64605; -.
DR ABCD; Q64605; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000073991; ENSRNOP00000065227; ENSRNOG00000047247. [Q64605-2]
DR Ensembl; ENSRNOT00000103214; ENSRNOP00000084874; ENSRNOG00000047247. [Q64605-1]
DR GeneID; 25529; -.
DR KEGG; rno:25529; -.
DR CTD; 5802; -.
DR RGD; 3452; Ptprs.
DR eggNOG; KOG4228; Eukaryota.
DR GeneTree; ENSGT00940000153617; -.
DR InParanoid; Q64605; -.
DR OrthoDB; 220353at2759; -.
DR PhylomeDB; Q64605; -.
DR Reactome; R-RNO-388844; Receptor-type tyrosine-protein phosphatases.
DR Reactome; R-RNO-8849932; Synaptic adhesion-like molecules.
DR EvolutionaryTrace; Q64605; -.
DR PRO; PR:Q64605; -.
DR Proteomes; UP000002494; Chromosome 9.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IDA:UniProtKB.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IDA:SynGO.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; IDA:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:RGD.
DR GO; GO:0035374; F:chondroitin sulfate binding; ISS:UniProtKB.
DR GO; GO:0043395; F:heparan sulfate proteoglycan binding; ISS:UniProtKB.
DR GO; GO:0008201; F:heparin binding; ISS:UniProtKB.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; ISO:RGD.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:RGD.
DR GO; GO:0021549; P:cerebellum development; ISO:RGD.
DR GO; GO:0021987; P:cerebral cortex development; ISO:RGD.
DR GO; GO:0022038; P:corpus callosum development; ISO:RGD.
DR GO; GO:0090557; P:establishment of endothelial intestinal barrier; ISO:RGD.
DR GO; GO:0021766; P:hippocampus development; ISO:RGD.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:RGD.
DR GO; GO:0030517; P:negative regulation of axon extension; ISS:UniProtKB.
DR GO; GO:0048681; P:negative regulation of axon regeneration; ISS:UniProtKB.
DR GO; GO:0048671; P:negative regulation of collateral sprouting; ISS:UniProtKB.
DR GO; GO:0061000; P:negative regulation of dendritic spine development; ISS:UniProtKB.
DR GO; GO:0032687; P:negative regulation of interferon-alpha production; ISO:RGD.
DR GO; GO:0032688; P:negative regulation of interferon-beta production; ISO:RGD.
DR GO; GO:0010977; P:negative regulation of neuron projection development; ISS:UniProtKB.
DR GO; GO:0034164; P:negative regulation of toll-like receptor 9 signaling pathway; ISO:RGD.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; ISO:RGD.
DR GO; GO:0006470; P:protein dephosphorylation; ISO:RGD.
DR GO; GO:0099151; P:regulation of postsynaptic density assembly; IDA:SynGO.
DR GO; GO:1905606; P:regulation of presynapse assembly; IDA:SynGO.
DR GO; GO:0021510; P:spinal cord development; ISO:RGD.
DR GO; GO:0050808; P:synapse organization; ISO:RGD.
DR GO; GO:0099560; P:synaptic membrane adhesion; IDA:SynGO.
DR CDD; cd00063; FN3; 7.
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; 6.
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; Cell membrane;
KW Cell projection; Cytoplasmic vesicle; Disulfide bond; Glycoprotein;
KW Heparin-binding; Hydrolase; Immunoglobulin domain; Membrane;
KW Protein phosphatase; Receptor; Reference proteome; Repeat; Signal; Synapse;
KW Synaptosome; Transmembrane; Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..1907
FT /note="Receptor-type tyrosine-protein phosphatase S"
FT /id="PRO_5000142153"
FT TOPO_DOM 30..1257
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1258..1278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1279..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..603
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 608..705
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 710..809
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 810..906
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 907..1008
FT /note="Fibronectin type-III 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1011..1095
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 68..72
FT /note="Important for binding to glycosaminoglycan chains"
FT /evidence="ECO:0000250|UniProtKB:B0V2N1"
FT REGION 691..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1286..1313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1548
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 1839
FT /note="Phosphocysteine intermediate"
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 SITE 1172..1173
FT /note="Cleavage"
FT /evidence="ECO:0000250"
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 720
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 916
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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 624..668
FT /note="VSWRPPPPETHNGALVGYSVRYRPLGSEDPDPKEVNNIPPTTTQI -> I
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8068021"
FT /id="VSP_026932"
FT CONFLICT 597
FT /note="R -> C (in Ref. 1; AAC37656)"
FT /evidence="ECO:0000305"
FT CONFLICT 753
FT /note="A -> T (in Ref. 1; AAC37656)"
FT /evidence="ECO:0000305"
FT CONFLICT 913
FT /note="A -> P (in Ref. 1; AAC37656)"
FT /evidence="ECO:0000305"
FT CONFLICT 934
FT /note="R -> G (in Ref. 1; AAC37656)"
FT /evidence="ECO:0000305"
FT CONFLICT 950
FT /note="A -> T (in Ref. 1; AAC37656)"
FT /evidence="ECO:0000305"
FT HELIX 1334..1336
FT /evidence="ECO:0007829|PDB:2NV5"
FT HELIX 1337..1358
FT /evidence="ECO:0007829|PDB:2NV5"
FT HELIX 1369..1371
FT /evidence="ECO:0007829|PDB:2NV5"
FT TURN 1373..1375
FT /evidence="ECO:0007829|PDB:2NV5"
FT HELIX 1376..1378
FT /evidence="ECO:0007829|PDB:2NV5"
FT HELIX 1388..1390
FT /evidence="ECO:0007829|PDB:2NV5"
FT STRAND 1391..1393
FT /evidence="ECO:0007829|PDB:2NV5"
FT TURN 1401..1404
FT /evidence="ECO:0007829|PDB:2NV5"
FT STRAND 1405..1413
FT /evidence="ECO:0007829|PDB:2NV5"
FT STRAND 1416..1423
FT /evidence="ECO:0007829|PDB:2NV5"
FT HELIX 1428..1430
FT /evidence="ECO:0007829|PDB:2NV5"
FT HELIX 1431..1440
FT /evidence="ECO:0007829|PDB:2NV5"
FT STRAND 1445..1448
FT /evidence="ECO:0007829|PDB:2NV5"
FT STRAND 1452..1454
FT /evidence="ECO:0007829|PDB:2NV5"
FT STRAND 1457..1460
FT /evidence="ECO:0007829|PDB:2NV5"
FT STRAND 1466..1472
FT /evidence="ECO:0007829|PDB:2NV5"
FT STRAND 1475..1484
FT /evidence="ECO:0007829|PDB:2NV5"
FT STRAND 1486..1497
FT /evidence="ECO:0007829|PDB:2NV5"
FT STRAND 1504..1511
FT /evidence="ECO:0007829|PDB:2NV5"
FT STRAND 1516..1519
FT /evidence="ECO:0007829|PDB:2NV5"
FT HELIX 1524..1536
FT /evidence="ECO:0007829|PDB:2NV5"
FT STRAND 1544..1553
FT /evidence="ECO:0007829|PDB:2NV5"
FT HELIX 1554..1571
FT /evidence="ECO:0007829|PDB:2NV5"
FT STRAND 1572..1574
FT /evidence="ECO:0007829|PDB:2NV5"
FT HELIX 1576..1584
FT /evidence="ECO:0007829|PDB:2NV5"
FT HELIX 1594..1608
FT /evidence="ECO:0007829|PDB:2NV5"
SQ SEQUENCE 1907 AA; 211931 MW; 5CD377A88377CDA4 CRC64;
MAPTWRPSVV SVVGPVGLFL VLLARGCLAE EPPRFIREPK DQIGVSGGVA SFVCQATGDP
KPRVTWNKKG KKVNSQRFET IDFDESSGAV LRIQPLRTPR DENVYECVAQ NSVGEITVHA
KLTVLREDQL PPGFPNIDMG PQLKVVERTR TATMLCAASG NPDPEITWFK DFLPVDPSAS
NGRIKQLRSG ALQIESSEET DQGKYECVAT NSAGVRYSSP ANLYVRVRRV APRFSILPMS
HEIMPGGNVN ITCVAVGSPM PYVKWMQGAE DLTPEDDMPV GRNVLELTDV KDSANYTCVA
MSSLGVIEAV AQITVKSLPK APGTPVVTEN TATSITVTWD SGNPDPVSYY VIEYKSKSQD
GPYQIKEDIT TTRYSIGGLS PNSEYEIWVS AVNSIGQGPP SESVVTRTGE QAPASAPRNV
QARMLSATTM IVQWEEPVEP NGLIRGYRVY YTMEPEHPVG NWQKHNVDDS LLTTVGSLLE
DETYTVRVLA FTSVGDGPLS DPIQVKTQQG VPGQPMNLRA EAKSETSIGL SWSAPRQESV
IKYELLFREG DRGREVGRTF DPTTAFVVED LKPNTEYAFR LAARSPQGLG AFTAVVRQRT
LQAKPSAPPQ DVKCTSLRST AILVSWRPPP PETHNGALVG YSVRYRPLGS EDPDPKEVNN
IPPTTTQILL EALEKWTEYR VTAVAYTEVG PGPESSPVVV RTDEDVPSAP PRKVEAEALN
ATAIRVLWRS PTPGRQHGQI RGYQVHYVRM EGAEARGPPR IKDIMLADAQ EMVITNLQPE
TAYSITVAAY TMKGDGARSK PKVVVTKGAV LGRPTLSVQQ TPEGSLLARW EPPADAAEDP
VLGYRLQFGR EDAAPATLEL AAWERRFAAP AHKGATYVFR LAARGRAGLG EEASAALSIP
EDAPRGFPQI LGAAGNVSAG SVILRWLPPV PAERNGAIIK YTVSVREAGA PGPATETELA
AAAQPGAETA LTLQGLRPET AYELRVRAHT RRGPGPFSPP LRYRLARDPV SPKNFKVKMI
MKTSVLLSWE FPDNYNSPTP YKIQYNGLTL DVDGRTTKKL ITHLKPHTFY NFVLTNRGSS
LGGLQQTVTA RTAFNMLSGK PSVAPKPDND GSIVVYLPDG QSPVTVQNYF IVMVPLRKSR
GGQFPILLGS PEDMDLEELI QDLSRLQRRS LRHSRQLEVP RPYIAARFSI LPAVFHPGNQ
KQYGGFDNRG LEPGHRYVLF VLAVLQKNEP TFAASPFSDP FQLDNPDPQP IVDGEEGLIW
VIGPVLAVVF IICIVIAILL YKNKPDSKRK DSEPRTKCLL NNADLAPHHP KDPVEMRRIN
FQTPGMLSHP PIPITDMAEH MERLKANDSL KLSQEYESID PGQQFTWEHS NLEANKPKNR
YANVIAYDHS RVILQPLEGI MGSDYINANY VDGYRRQNAY IATQGPLPET FGDFWRMVWE
QRSATVVMMT RLEEKSRVKC DQYWPNRGTE TYGFIQVTLL DTMELATFCV RTFSLHKNGS
SEKREVRHFQ FTAWPDHGVP EYPTPFLAFL RRVKTCNPPD AGPVVVHCSA GVGRTGCFIV
IDAMLERIRT EKTVDVYGHV TLMRSQRNYM VQTEDQYSFI HEALLEAVGC GNTEVPARSL
YTYIQKLAQV EPGEHVTGME LEFKRLASSK AHTSRFITAS LPCNKFKNRL VNILPYESSR
VCLQPIRGVE GSDYINASFI DGYRQQKAYI ATQGPLAETT EDFWRALWEN NSTIVVMLTK
LREMGREKCH QYWPAERSAR YQYFVVDPMA EYNMPQYILR EFKVTDARDG QSRTVRQFQF
TDWPEQGAPK SGEGFIDFIG QVHKTKEQFG QDGPISVHCS AGVGRTGVFI TLSIVLERMR
YEGVVDIFQT VKVLRTQRPA MVQTEDEYQF CFQAALEYLG SFDHYAT
