ID PTPRF_HUMAN Reviewed; 1907 AA.
AC P10586; D3DPX6; D3DPX7; Q5T021; Q5T022; Q5W9G2; Q86WS0;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 2.
DT 01-MAY-2013, entry version 162.
DE RecName: Full=Receptor-type tyrosine-protein phosphatase F;
DE EC=3.1.3.48;
DE AltName: Full=Leukocyte common antigen related;
DE Short=LAR;
DE Flags: Precursor;
GN Name=PTPRF; Synonyms=LAR;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Tonsil;
RX PubMed=2972792; DOI=10.1084/jem.168.5.1523;
RA Streuli M., Krueger N.X., Hall L.R., Schlossman S.F., Saito H.;
RT "A new member of the immunoglobulin superfamily that has a cytoplasmic
RT region homologous to the leukocyte common antigen.";
RL J. Exp. Med. 168:1523-1530(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=15491607; DOI=10.1016/j.jmb.2004.09.028;
RA Homma K., Kikuno R.F., Nagase T., Ohara O., Nishikawa K.;
RT "Alternative splice variants encoding unstable protein domains exist
RT in the human brain.";
RL J. Mol. Biol. 343:1207-1220(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Retinoblastoma;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP MUTAGENESIS.
RX PubMed=2554325; DOI=10.1073/pnas.86.22.8698;
RA Streuli M., Krueger N.X., Tsai A.Y.M., Saito H.;
RT "A family of receptor-linked protein tyrosine phosphatases in humans
RT and Drosophila.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:8698-8702(1989).
RN [7]
RP MUTAGENESIS.
RX PubMed=1695146;
RA Streuli M., Krueger N.X., Thai T., Tang M., Saito H.;
RT "Distinct functional roles of the two intracellular phosphatase like
RT domains of the receptor-linked protein tyrosine phosphatases LCA and
RT LAR.";
RL EMBO J. 9:2399-2407(1990).
RN [8]
RP INTERACTION WITH INSR.
RX PubMed=8995282; DOI=10.1074/jbc.272.11.7519;
RA Ahmad F., Goldstein B.J.;
RT "Functional association between the insulin receptor and the
RT transmembrane protein-tyrosine phosphatase LAR in intact cells.";
RL J. Biol. Chem. 272:448-457(1997).
RN [9]
RP INTERACTION WITH PPFIA1; PPFIA2 AND PPFIA3.
RX PubMed=9624153; DOI=10.1074/jbc.273.25.15611;
RA Serra-Pages C., Medley Q.G., Tang M., Hart A., Streuli M.;
RT "Liprins, a family of LAR transmembrane protein-tyrosine phosphatase-
RT interacting proteins.";
RL J. Biol. Chem. 273:15611-15620(1998).
RN [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-966, AND MASS
RP SPECTROMETRY.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
RA Moore R.J., Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-959 AND ASN-966, AND MASS
RP SPECTROMETRY.
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-
RT linked cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1334-1897, FUNCTION, AND
RP MUTAGENESIS OF CYS-1548.
RX PubMed=10338209; DOI=10.1016/S0092-8674(00)80755-2;
RA Nam H.J., Poy F., Krueger N.X., Saito H., Frederick C.A.;
RT "Crystal structure of the tandem phosphatase domains of RPTP LAR.";
RL Cell 97:449-457(1999).
RN [14]
RP STRUCTURE BY NMR OF 319-415 AND 596-1010.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structures of FN3 domains of human receptor-type tyrosine-
RT protein phosphatase F.";
RL Submitted (AUG-2007) to the PDB data bank.
CC -!- FUNCTION: Possible cell adhesion receptor. It possesses an
CC intrinsic protein tyrosine phosphatase activity (PTPase).
CC -!- FUNCTION: The first PTPase domain has enzymatic activity, while
CC the second one seems to affect the substrate specificity of the
CC first one.
CC -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC tyrosine + phosphate.
CC -!- SUBUNIT: Interacts with GRIP1 (By similarity). Interacts with
CC PPFIA1, PPFIA2 and PPFIA3. Interacts with INSR.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P10586-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P10586-2; Sequence=VSP_036617;
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 2A subfamily.
CC -!- SIMILARITY: Contains 8 fibronectin type-III domains.
CC -!- SIMILARITY: Contains 3 Ig-like C2-type (immunoglobulin-like)
CC domains.
CC -!- SIMILARITY: Contains 2 tyrosine-protein phosphatase domains.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD66835.1; Type=Erroneous initiation;
CC Sequence=CAA68754.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; Y00815; CAA68754.1; ALT_INIT; mRNA.
DR EMBL; AB177857; BAD66835.1; ALT_INIT; mRNA.
DR EMBL; AL583862; CAI14894.1; -; Genomic_DNA.
DR EMBL; AC092815; CAI14894.1; JOINED; Genomic_DNA.
DR EMBL; AL583862; CAI14895.1; -; Genomic_DNA.
DR EMBL; AC092815; CAI14895.1; JOINED; Genomic_DNA.
DR EMBL; CH471059; EAX07086.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07087.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07088.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07089.1; -; Genomic_DNA.
DR EMBL; BC048768; AAH48768.1; -; mRNA.
DR IPI; IPI00107831; -.
DR IPI; IPI00465186; -.
DR PIR; S03841; TDHULK.
DR RefSeq; NP_002831.2; NM_002840.3.
DR RefSeq; NP_569707.2; NM_130440.2.
DR UniGene; Hs.272062; -.
DR PDB; 1LAR; X-ray; 2.00 A; A/B=1334-1897.
DR PDB; 2DJU; NMR; -; A=319-411.
DR PDB; 2DN7; NMR; -; A=821-914.
DR PDB; 2EDX; NMR; -; A=596-716.
DR PDB; 2EDY; NMR; -; A=915-1010.
DR PDB; 2YD5; X-ray; 2.20 A; A=29-231.
DR PDB; 2YD8; X-ray; 2.05 A; A=29-231.
DR PDBsum; 1LAR; -.
DR PDBsum; 2DJU; -.
DR PDBsum; 2DN7; -.
DR PDBsum; 2EDX; -.
DR PDBsum; 2EDY; -.
DR PDBsum; 2YD5; -.
DR PDBsum; 2YD8; -.
DR ProteinModelPortal; P10586; -.
DR MINT; MINT-1189049; -.
DR STRING; 9606.ENSP00000353030; -.
DR PhosphoSite; P10586; -.
DR DMDM; 226709091; -.
DR PaxDb; P10586; -.
DR PRIDE; P10586; -.
DR DNASU; 5792; -.
DR Ensembl; ENST00000359947; ENSP00000353030; ENSG00000142949.
DR Ensembl; ENST00000372413; ENSP00000361490; ENSG00000142949.
DR Ensembl; ENST00000372414; ENSP00000361491; ENSG00000142949.
DR Ensembl; ENST00000438120; ENSP00000398822; ENSG00000142949.
DR GeneID; 5792; -.
DR KEGG; hsa:5792; -.
DR UCSC; uc001cjr.3; human.
DR UCSC; uc001cjs.3; human.
DR CTD; 5792; -.
DR GeneCards; GC01P043990; -.
DR HGNC; HGNC:9670; PTPRF.
DR HPA; HPA012710; -.
DR MIM; 179590; gene.
DR neXtProt; NX_P10586; -.
DR PharmGKB; PA34015; -.
DR eggNOG; COG5599; -.
DR HOVERGEN; HBG053758; -.
DR InParanoid; P10586; -.
DR KO; K05695; -.
DR OMA; FTPTIEA; -.
DR OrthoDB; EOG4BG8V3; -.
DR BindingDB; P10586; -.
DR ChEMBL; CHEMBL3521; -.
DR ChiTaRS; PTPRF; human.
DR EvolutionaryTrace; P10586; -.
DR GenomeRNAi; 5792; -.
DR NextBio; 22550; -.
DR PMAP-CutDB; Q5T022; -.
DR ArrayExpress; P10586; -.
DR Bgee; P10586; -.
DR CleanEx; HS_PTPRF; -.
DR Genevestigator; P10586; -.
DR GermOnline; ENSG00000142949; Homo sapiens.
DR GO; GO:0005887; C:integral to plasma membrane; TAS:ProtInc.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0005001; F:transmembrane receptor protein tyrosine phosphatase activity; TAS:ProtInc.
DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR GO; GO:0007185; P:transmembrane receptor protein tyrosine phosphatase signaling pathway; TAS:ProtInc.
DR Gene3D; 2.60.40.10; -; 10.
DR InterPro; IPR003961; Fibronectin_type3.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR000387; Tyr/Dual-sp_Pase.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR000242; Tyr_Pase_rcpt/non-rcpt.
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; SM00408; IGc2; 3.
DR SMART; SM00194; PTPc; 2.
DR SUPFAM; SSF49265; FN_III-like; 8.
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; Complete proteome;
KW Disulfide bond; Glycoprotein; Heparin-binding; Hydrolase;
KW Immunoglobulin domain; Membrane; Polymorphism; Protein phosphatase;
KW Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1 29 Potential.
FT CHAIN 30 1907 Receptor-type tyrosine-protein
FT phosphatase F.
FT /FTId=PRO_0000025432.
FT TOPO_DOM 30 1263 Extracellular (Potential).
FT TRANSMEM 1264 1284 Helical; (Potential).
FT TOPO_DOM 1285 1907 Cytoplasmic (Potential).
FT DOMAIN 33 123 Ig-like C2-type 1.
FT DOMAIN 135 224 Ig-like C2-type 2.
FT DOMAIN 232 314 Ig-like C2-type 3.
FT DOMAIN 319 407 Fibronectin type-III 1.
FT DOMAIN 413 506 Fibronectin type-III 2.
FT DOMAIN 512 602 Fibronectin type-III 3.
FT DOMAIN 606 703 Fibronectin type-III 4.
FT DOMAIN 708 815 Fibronectin type-III 5.
FT DOMAIN 817 910 Fibronectin type-III 6.
FT DOMAIN 915 1008 Fibronectin type-III 7.
FT DOMAIN 1011 1095 Fibronectin type-III 8.
FT DOMAIN 1352 1607 Tyrosine-protein phosphatase 1.
FT DOMAIN 1639 1898 Tyrosine-protein phosphatase 2.
FT REGION 68 77 Heparin-binding (By similarity).
FT REGION 1548 1554 Substrate binding (By similarity).
FT ACT_SITE 1548 1548 Phosphocysteine intermediate (Probable).
FT ACT_SITE 1839 1839 Phosphocysteine intermediate (By
FT similarity).
FT BINDING 1516 1516 Substrate (By similarity).
FT BINDING 1592 1592 Substrate (By similarity).
FT CARBOHYD 117 117 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 250 250 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 295 295 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 721 721 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 959 959 N-linked (GlcNAc...).
FT CARBOHYD 966 966 N-linked (GlcNAc...).
FT DISULFID 54 107 By similarity.
FT DISULFID 156 207 By similarity.
FT DISULFID 253 298 By similarity.
FT VAR_SEQ 772 780 Missing (in isoform 2).
FT /FTId=VSP_036617.
FT VARIANT 412 412 A -> V (in dbSNP:rs1065775).
FT /FTId=VAR_054766.
FT VARIANT 450 450 Y -> C (in dbSNP:rs3748796).
FT /FTId=VAR_020299.
FT VARIANT 562 562 D -> N (in dbSNP:rs3748800).
FT /FTId=VAR_020300.
FT MUTAGEN 1548 1548 C->S: Loss of activity.
FT CONFLICT 646 646 Y -> H (in Ref. 1; CAA68754).
FT CONFLICT 1421 1421 I -> T (in Ref. 5; AAH48768).
FT STRAND 31 37
FT STRAND 42 45
FT STRAND 50 60
FT STRAND 63 68
FT TURN 75 77
FT STRAND 78 83
FT HELIX 84 86
FT STRAND 88 93
FT HELIX 98 101
FT STRAND 103 111
FT STRAND 114 125
FT HELIX 127 129
FT STRAND 136 139
FT STRAND 144 147
FT STRAND 152 154
FT STRAND 157 159
FT STRAND 165 170
FT HELIX 177 179
FT STRAND 183 186
FT STRAND 192 194
FT HELIX 199 201
FT STRAND 203 211
FT STRAND 214 217
FT STRAND 221 226
FT STRAND 323 331
FT STRAND 334 340
FT STRAND 348 356
FT STRAND 371 378
FT STRAND 384 392
FT STRAND 404 407
FT STRAND 610 616
FT STRAND 618 628
FT STRAND 639 652
FT STRAND 657 659
FT STRAND 667 673
FT STRAND 679 688
FT STRAND 699 702
FT STRAND 825 830
FT STRAND 835 841
FT STRAND 852 859
FT STRAND 866 871
FT STRAND 876 880
FT STRAND 887 896
FT STRAND 899 909
FT STRAND 920 923
FT STRAND 925 927
FT STRAND 935 937
FT STRAND 950 957
FT STRAND 963 971
FT STRAND 984 987
FT HELIX 1334 1344
FT TURN 1347 1349
FT HELIX 1350 1358
FT HELIX 1368 1371
FT TURN 1373 1375
FT HELIX 1376 1378
FT TURN 1388 1390
FT TURN 1401 1404
FT STRAND 1407 1413
FT STRAND 1416 1423
FT TURN 1428 1430
FT HELIX 1431 1440
FT STRAND 1445 1448
FT STRAND 1452 1454
FT STRAND 1466 1472
FT STRAND 1475 1484
FT STRAND 1486 1497
FT STRAND 1503 1511
FT STRAND 1516 1518
FT HELIX 1524 1536
FT STRAND 1544 1553
FT HELIX 1554 1571
FT HELIX 1576 1584
FT HELIX 1594 1610
FT HELIX 1617 1619
FT HELIX 1620 1627
FT HELIX 1638 1644
FT TURN 1645 1647
FT TURN 1657 1660
FT HELIX 1662 1667
FT TURN 1677 1679
FT TURN 1690 1693
FT STRAND 1696 1700
FT STRAND 1703 1705
FT STRAND 1709 1712
FT HELIX 1717 1719
FT HELIX 1720 1729
FT STRAND 1734 1737
FT STRAND 1741 1743
FT STRAND 1746 1749
FT STRAND 1755 1757
FT STRAND 1759 1761
FT STRAND 1764 1773
FT STRAND 1775 1786
FT TURN 1787 1789
FT STRAND 1792 1800
FT STRAND 1805 1807
FT HELIX 1813 1828
FT STRAND 1835 1844
FT HELIX 1845 1862
FT STRAND 1863 1865
FT HELIX 1867 1874
FT TURN 1875 1877
FT HELIX 1885 1897
SQ SEQUENCE 1907 AA; 212879 MW; 4A7C14A2090EA88F CRC64;
MAPEPAPGRT MVPLVPALVM LGLVAGAHGD SKPVFIKVPE DQTGLSGGVA SFVCQATGEP
KPRITWMKKG KKVSSQRFEV IEFDDGAGSV LRIQPLRVQR DEAIYECTAT NSLGEINTSA
KLSVLEEEQL PPGFPSIDMG PQLKVVEKAR TATMLCAAGG NPDPEISWFK DFLPVDPATS
NGRIKQLRSG ALQIESSEES DQGKYECVAT NSAGTRYSAP ANLYVRVRRV APRFSIPPSS
QEVMPGGSVN LTCVAVGAPM PYVKWMMGAE ELTKEDEMPV GRNVLELSNV VRSANYTCVA
ISSLGMIEAT AQVTVKALPK PPIDLVVTET TATSVTLTWD SGNSEPVTYY GIQYRAAGTE
GPFQEVDGVA TTRYSIGGLS PFSEYAFRVL AVNSIGRGPP SEAVRARTGE QAPSSPPRRV
QARMLSASTM LVQWEPPEEP NGLVRGYRVY YTPDSRRPPN AWHKHNTDAG LLTTVGSLLP
GITYSLRVLA FTAVGDGPPS PTIQVKTQQG VPAQPADFQA EVESDTRIQL SWLLPPQERI
IMYELVYWAA EDEDQQHKVT FDPTSSYTLE DLKPDTLYRF QLAARSDMGV GVFTPTIEAR
TAQSTPSAPP QKVMCVSMGS TTVRVSWVPP PADSRNGVIT QYSVAYEAVD GEDRGRHVVD
GISREHSSWD LVGLEKWTEY RVWVRAHTDV GPGPESSPVL VRTDEDVPSG PPRKVEVEPL
NSTAVHVYWK LPVPSKQHGQ IRGYQVTYVR LENGEPRGLP IIQDVMLAEA QWRPEESEDY
ETTISGLTPE TTYSVTVAAY TTKGDGARSK PKIVTTTGAV PGRPTMMIST TAMNTALLQW
HPPKELPGEL LGYRLQYCRA DEARPNTIDF GKDDQHFTVT GLHKGTTYIF RLAAKNRAGL
GEEFEKEIRT PEDLPSGFPQ NLHVTGLTTS TTELAWDPPV LAERNGRIIS YTVVFRDINS
QQELQNITTD TRFTLTGLKP DTTYDIKVRA WTSKGSGPLS PSIQSRTMPV EQVFAKNFRV
AAAMKTSVLL SWEVPDSYKS AVPFKILYNG QSVEVDGHSM RKLIADLQPN TEYSFVLMNR
GSSAGGLQHL VSIRTAPDLL PHKPLPASAY IEDGRFDLSM PHVQDPSLVR WFYIVVVPID
RVGGSMLTPR WSTPEELELD ELLEAIEQGG EEQRRRRRQA ERLKPYVAAQ LDVLPETFTL
GDKKNYRGFY NRPLSPDLSY QCFVLASLKE PMDQKRYASS PYSDEIVVQV TPAQQQEEPE
MLWVTGPVLA VILIILIVIA ILLFKRKRTH SPSSKDEQSI GLKDSLLAHS SDPVEMRRLN
YQTPGMRDHP PIPITDLADN IERLKANDGL KFSQEYESID PGQQFTWENS NLEVNKPKNR
YANVIAYDHS RVILTSIDGV PGSDYINANY IDGYRKQNAY IATQGPLPET MGDFWRMVWE
QRTATVVMMT RLEEKSRVKC DQYWPARGTE TCGLIQVTLL DTVELATYTV RTFALHKSGS
SEKRELRQFQ FMAWPDHGVP EYPTPILAFL RRVKACNPLD AGPMVVHCSA GVGRTGCFIV
IDAMLERMKH EKTVDIYGHV TCMRSQRNYM VQTEDQYVFI HEALLEAATC GHTEVPARNL
YAHIQKLGQV PPGESVTAME LEFKLLASSK AHTSRFISAN LPCNKFKNRL VNIMPYELTR
VCLQPIRGVE GSDYINASFL DGYRQQKAYI ATQGPLAEST EDFWRMLWEH NSTIIVMLTK
LREMGREKCH QYWPAERSAR YQYFVVDPMA EYNMPQYILR EFKVTDARDG QSRTIRQFQF
TDWPEQGVPK TGEGFIDFIG QVHKTKEQFG QDGPITVHCS AGVGRTGVFI TLSIVLERMR
YEGVVDMFQT VKTLRTQRPA MVQTEDQYQL CYRAALEYLG SFDHYAT
//
