PTPRF_MOUSE
ID PTPRF_MOUSE Reviewed; 1898 AA.
AC A2A8L5; Q6PG86; Q9EQ17;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 134.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Thymus;
RX PubMed=11241288;
RX DOI=10.1002/1521-4141(200103)31:3<832::aid-immu832>3.0.co;2-d;
RA Terszowski G., Jankowski A., Hendriks W.J.A.J., Rolink A.G., Kisielow P.;
RT "Within the hemopoietic system, LAR phosphatase is a T cell lineage-
RT specific adhesion receptor-like protein whose phosphatase activity appears
RT dispensable for T cell development, repertoire selection and function.";
RL Eur. J. Immunol. 31:832-840(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 370-1898.
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-721; ASN-941 AND ASN-960.
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 30-226, HEPARIN-BINDING REGION,
RP AND DISULFIDE BONDS.
RX PubMed=21402080; DOI=10.1016/j.jmb.2011.03.013;
RA Biersmith B.H., Hammel M., Geisbrecht E.R., Bouyain S.;
RT "The immunoglobulin-like domains 1 and 2 of the protein tyrosine
RT phosphatase LAR adopt an unusual horseshoe-like conformation.";
RL J. Mol. Biol. 408:616-627(2011).
CC -!- FUNCTION: Possible cell adhesion receptor. It possesses an intrinsic
CC protein tyrosine phosphatase activity (PTPase) and dephosphorylates
CC EPHA2 regulating its activity (By similarity). {ECO:0000250}.
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. Interacts with PPFIA1, PPFIA2 and
CC PPFIA3. Interacts with PTPRF. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in the cell of the T lineage but not in
CC cells of any other hemopoietic lineage. {ECO:0000269|PubMed:11241288}.
CC -!- DOMAIN: The first PTPase domain has enzymatic activity, while the
CC second one seems to affect the substrate specificity of the first one.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 2A subfamily. {ECO:0000305}.
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DR EMBL; AF300943; AAG40194.1; -; mRNA.
DR EMBL; AL626764; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL807774; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC057166; AAH57166.1; -; mRNA.
DR CCDS; CCDS18546.1; -.
DR RefSeq; NP_035343.2; NM_011213.2.
DR PDB; 3PXH; X-ray; 2.00 A; A=30-226.
DR PDB; 6X39; X-ray; 1.70 A; A=709-812.
DR PDBsum; 3PXH; -.
DR PDBsum; 6X39; -.
DR AlphaFoldDB; A2A8L5; -.
DR SMR; A2A8L5; -.
DR BioGRID; 202497; 18.
DR IntAct; A2A8L5; 3.
DR MINT; A2A8L5; -.
DR STRING; 10090.ENSMUSP00000039368; -.
DR GlyConnect; 2669; 2 N-Linked glycans (3 sites).
DR GlyGen; A2A8L5; 7 sites, 2 N-linked glycans (3 sites).
DR iPTMnet; A2A8L5; -.
DR PhosphoSitePlus; A2A8L5; -.
DR SwissPalm; A2A8L5; -.
DR CPTAC; non-CPTAC-3600; -.
DR EPD; A2A8L5; -.
DR jPOST; A2A8L5; -.
DR MaxQB; A2A8L5; -.
DR PaxDb; A2A8L5; -.
DR PeptideAtlas; A2A8L5; -.
DR PRIDE; A2A8L5; -.
DR ProteomicsDB; 301976; -.
DR ABCD; A2A8L5; 2 sequenced antibodies.
DR Antibodypedia; 2499; 325 antibodies from 32 providers.
DR DNASU; 19268; -.
DR Ensembl; ENSMUST00000049074; ENSMUSP00000039368; ENSMUSG00000033295.
DR GeneID; 19268; -.
DR KEGG; mmu:19268; -.
DR UCSC; uc008ujq.1; mouse.
DR CTD; 5792; -.
DR MGI; MGI:102695; Ptprf.
DR VEuPathDB; HostDB:ENSMUSG00000033295; -.
DR eggNOG; KOG4228; Eukaryota.
DR GeneTree; ENSGT00940000155060; -.
DR HOGENOM; CLU_001645_4_0_1; -.
DR InParanoid; A2A8L5; -.
DR OMA; SSRRWEN; -.
DR OrthoDB; 220353at2759; -.
DR PhylomeDB; A2A8L5; -.
DR TreeFam; TF312900; -.
DR Reactome; R-MMU-388844; Receptor-type tyrosine-protein phosphatases.
DR Reactome; R-MMU-8849932; Synaptic adhesion-like molecules.
DR BioGRID-ORCS; 19268; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Ptprf; mouse.
DR PRO; PR:A2A8L5; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; A2A8L5; protein.
DR Bgee; ENSMUSG00000033295; Expressed in metanephric ureteric bud and 252 other tissues.
DR ExpressionAtlas; A2A8L5; baseline and differential.
DR Genevisible; A2A8L5; MM.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0060076; C:excitatory synapse; ISO:MGI.
DR GO; GO:0030426; C:growth cone; ISO:MGI.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; IDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISO:MGI.
DR GO; GO:0035373; F:chondroitin sulfate proteoglycan binding; IPI:MGI.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0005158; F:insulin receptor binding; ISO:MGI.
DR GO; GO:0042301; F:phosphate ion binding; ISO:MGI.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:MGI.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:MGI.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; ISO:MGI.
DR GO; GO:0005001; F:transmembrane receptor protein tyrosine phosphatase activity; ISO:MGI.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0031345; P:negative regulation of cell projection organization; ISO:MGI.
DR GO; GO:0001960; P:negative regulation of cytokine-mediated signaling pathway; ISO:MGI.
DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; ISO:MGI.
DR GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; ISO:MGI.
DR GO; GO:0051387; P:negative regulation of neurotrophin TRK receptor signaling pathway; ISO:MGI.
DR GO; GO:1900121; P:negative regulation of receptor binding; ISS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; ISO:MGI.
DR GO; GO:0031102; P:neuron projection regeneration; IMP:MGI.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0050775; P:positive regulation of dendrite morphogenesis; ISO:MGI.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISO:MGI.
DR GO; GO:0006470; P:protein dephosphorylation; ISO:MGI.
DR GO; GO:0048679; P:regulation of axon regeneration; IMP:MGI.
DR GO; GO:0010975; P:regulation of neuron projection development; IMP:MGI.
DR GO; GO:0099175; P:regulation of postsynapse organization; ISO:MGI.
DR GO; GO:0050803; P:regulation of synapse structure or activity; ISO:MGI.
DR GO; GO:0099560; P:synaptic membrane adhesion; ISO:MGI.
DR CDD; cd00063; FN3; 8.
DR Gene3D; 2.60.40.10; -; 11.
DR Gene3D; 3.90.190.10; -; 2.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR Pfam; PF00041; fn3; 7.
DR Pfam; PF07679; I-set; 3.
DR Pfam; PF00102; Y_phosphatase; 2.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00060; FN3; 8.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 3.
DR SMART; SM00194; PTPc; 2.
DR SMART; SM00404; PTPc_motif; 2.
DR SUPFAM; SSF48726; SSF48726; 3.
DR SUPFAM; SSF49265; SSF49265; 5.
DR SUPFAM; SSF52799; SSF52799; 2.
DR PROSITE; PS50853; FN3; 8.
DR PROSITE; PS50835; IG_LIKE; 3.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 2.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Disulfide bond; Glycoprotein; Heparin-binding;
KW Hydrolase; Immunoglobulin domain; Membrane; Phosphoprotein;
KW Protein phosphatase; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..1898
FT /note="Receptor-type tyrosine-protein phosphatase F"
FT /id="PRO_0000370193"
FT TOPO_DOM 30..1254
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1255..1275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1276..1898
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..810
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 811..904
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 909..1001
FT /note="Fibronectin type-III 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1005..1089
FT /note="Fibronectin type-III 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1343..1598
FT /note="Tyrosine-protein phosphatase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT DOMAIN 1630..1889
FT /note="Tyrosine-protein phosphatase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 693..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1539
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 1830
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 68..77
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT BINDING 1507
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1539..1545
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1583
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 1296
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10586"
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:0000269|PubMed:19349973"
FT CARBOHYD 941
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 957
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 960
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT DISULFID 54..107
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:21402080"
FT DISULFID 156..207
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:21402080"
FT DISULFID 253..298
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 47
FT /note="G -> E (in Ref. 1; AAG40194)"
FT /evidence="ECO:0000305"
FT CONFLICT 482
FT /note="I -> V (in Ref. 1; AAG40194)"
FT /evidence="ECO:0000305"
FT CONFLICT 514..515
FT /note="QP -> RS (in Ref. 1; AAG40194)"
FT /evidence="ECO:0000305"
FT CONFLICT 579
FT /note="H -> R (in Ref. 1; AAG40194)"
FT /evidence="ECO:0000305"
FT CONFLICT 1006
FT /note="A -> T (in Ref. 1; AAG40194)"
FT /evidence="ECO:0000305"
FT CONFLICT 1184
FT /note="V -> A (in Ref. 3; AAH57166)"
FT /evidence="ECO:0000305"
FT CONFLICT 1374
FT /note="N -> D (in Ref. 1; AAG40194)"
FT /evidence="ECO:0000305"
FT STRAND 31..37
FT /evidence="ECO:0007829|PDB:3PXH"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:3PXH"
FT STRAND 50..60
FT /evidence="ECO:0007829|PDB:3PXH"
FT STRAND 63..68
FT /evidence="ECO:0007829|PDB:3PXH"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:3PXH"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:3PXH"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:3PXH"
FT HELIX 98..101
FT /evidence="ECO:0007829|PDB:3PXH"
FT STRAND 103..110
FT /evidence="ECO:0007829|PDB:3PXH"
FT STRAND 115..125
FT /evidence="ECO:0007829|PDB:3PXH"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:3PXH"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:3PXH"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:3PXH"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:3PXH"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:3PXH"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:3PXH"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:3PXH"
FT STRAND 180..186
FT /evidence="ECO:0007829|PDB:3PXH"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:3PXH"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:3PXH"
FT STRAND 203..211
FT /evidence="ECO:0007829|PDB:3PXH"
FT STRAND 214..217
FT /evidence="ECO:0007829|PDB:3PXH"
FT STRAND 221..225
FT /evidence="ECO:0007829|PDB:3PXH"
FT STRAND 713..721
FT /evidence="ECO:0007829|PDB:6X39"
FT STRAND 724..730
FT /evidence="ECO:0007829|PDB:6X39"
FT STRAND 741..752
FT /evidence="ECO:0007829|PDB:6X39"
FT STRAND 755..765
FT /evidence="ECO:0007829|PDB:6X39"
FT STRAND 772..775
FT /evidence="ECO:0007829|PDB:6X39"
FT STRAND 783..792
FT /evidence="ECO:0007829|PDB:6X39"
FT STRAND 803..806
FT /evidence="ECO:0007829|PDB:6X39"
SQ SEQUENCE 1898 AA; 211489 MW; 903FF6814F0BC914 CRC64;
MAPEPAPGRR MVPLVPALVM LGLMAGAHGD SKPVFVKVPE DQTGLSGGVA SFVCQATGEP
KPRITWMKKG KKVSSQRFEV IEFDDGAGSV LRIQPLRVQR DEAIYECTAT NSLGEINTSA
KLSVLEEDQL PSGFPTIDMG PQLKVVEKGR TATMLCAAGG NPDPEISWFK DFLPVDPAAS
NGRIKQLRSG ALQIESSEES DQGKYECVAT NSAGTRYSAP ANLYVRVRRV APRFSIPPSS
QEVMPGGSVN LTCVAVGAPM PYVKWMMGAE ELTKEDEMPV GRNVLELSNV MRSANYTCVA
ISSLGMIEAT AQVTVKALPK PPIDLVVTET TATSVTLTWD SGNTEPVSFY GIQYRAAGTD
GPFQEVDGVA STRYSIGGLS PFSEYAFRVL AVNSIGRGPP SEAVRARTGE QAPSSPPRRV
QARMLSASTM LVQWEPPEEP NGLVRGYRVY YTPDSRRPLS AWHKHNTDAG LLTTVGSLLP
GITYSLRVLA FTAVGDGPPS PTIQVKTQQG VPAQPADFQA NAESDTRIQL SWLLPPQERI
VKYELVYWAA EDEGQQHKVT FDPTSSYTLE DLKPDTLYHF QLAARSDLGV GVFTPTVEAR
TAQSTPSAPP QKVTCVSTGS TTVRVSWVPP PADSRNGIIT QYSVAYEAVD GEDRKRHVVD
GISREHSSWD LLGLEKWTEY RVWVRAHTDV GPGPESSPVL VRTDEDVPSG PPRKVEVEPL
NSTAVHVSWK LPVPNKQHGQ IRGYQVTYVR LENGEPRGQP IIQDVMLAEA QETTISGLTP
ETTYSITVAA YTTKGDGARS KPKVVTTTGA VPGRPTMMVS TTAMHTALLQ WHPPKELPGE
LLGYRLQYRR ADEARPNTID FGKDDQHFTV TGLHKGATYV FRLAAKNRAG PGEEFEKEIT
TPEDVPSGFP QNLRVTGLTT STTELTWDPP VLAERNGHIT NYTVVYRDIN SQLELQNVTN
DTHLTLLGLK PDTTYDIKVR AHTSKGAGPL SPSIQSRTMP VEQVFAKNFR VAAAMKTSVL
LSWEVPDSYK SAVPFKILYN GQSVEVDGHS MRKLIADLQP NTEYSFVLMN RGSSAGGLQH
LVSIRTAPDL LPQKPLPASA FIEDGRFSLS MPQVQDPSLV RWFYIVVVPI DRVGGNLLAP
RWNTPEELEL DELLEAIEQG EEKQRRRRRQ AERLKPYVAA QVDVLPDTFT LGDKKSYRGF
YNRPLSPDLS YQCFVLASLK EPMDQKRYAS SPYSDEIVVQ VTPAQQQEEP EMLWVTGPVL
AVILIILIVI AILLFKRKRT HSPSSKDEQS IGLKDSLLAH SSDPVEMRRL NYQTPGMRDH
PPIPITDLAD NIERLKANDG LKFSQEYESI DPGQQFTWEN SNSEVNKPKN RYANVIAYDH
SRVLLTSIDG VPGSDYINAN YIDGYRKQNA YIATQGPLPE TMGDFWRMVW EQRTATVVMM
TRLEEKSRVK CDQYWPVRGT ETYGLIQVTL VDTVELATYT MRTFALHKSG SSEKRELRQF
QFMAWPDHGV PEYPTPILAF LRRVKACNPL DAGPMVVHCS AGVGRTGCFI VIDAMLERMK
HEKTVDIYGH VTCMRSQRNY MVQTEDQYVF IHEALLEAAM CGHTEVLARN LYAHIQKLGQ
VPPGESVTAM ELEFKLLANS KAHTSRFVSA NLPCNKFKNR LVNIMPYELT RVCLQPIRGV
EGSDYINASF LDGYRQQKAY IATQGPLAES TEDFWRMLWE HNSTIIVMLT KLREMGREKC
HQYWPAERSA RYQYFVVDPM AEYNMPQYIL REFKVTDARD GQSRTIRQFQ FTDWPEQGVP
KTGEGFIDFI GQVHKTKEQF GQDGPITVHC SAGVGRTGVF ITLSIVLERM RYEGVVDMFQ
TVKTLRTQRP AMVQTEDQYQ LCYRAALEYL GSFDHYAT
