ID PTN4_HUMAN Reviewed; 926 AA. AC P29074; B2RBV8; Q9UDA7; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 1. DT 07-OCT-2020, entry version 190. DE RecName: Full=Tyrosine-protein phosphatase non-receptor type 4; DE EC=3.1.3.48; DE AltName: Full=Protein-tyrosine phosphatase MEG1; DE Short=MEG; DE Short=PTPase-MEG1; GN Name=PTPN4; 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]. RX PubMed=1648233; DOI=10.1073/pnas.88.13.5867; RA Gu M., York J.D., Warshawsky I., Majerus P.W.; RT "Identification, cloning, and expression of a cytosolic megakaryocyte RT protein-tyrosine-phosphatase with sequence homology to cytoskeletal protein RT 4.1."; RL Proc. Natl. Acad. Sci. U.S.A. 88:5867-5871(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Colon; 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 NUCLEOTIDE SEQUENCE [MRNA] OF 745-858. 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 [5] RP SUBCELLULAR LOCATION, PHOSPHORYLATION, AND CLEAVAGE. RX PubMed=8910369; DOI=10.1074/jbc.271.44.27751; RA Gu M., Majerus P.W.; RT "The properties of the protein tyrosine phosphatase PTPMEG."; RL J. Biol. Chem. 271:27751-27759(1996). RN [6] RP FUNCTION. RX PubMed=25825441; DOI=10.4049/jimmunol.1402183; RA Huai W., Song H., Wang L., Li B., Zhao J., Han L., Gao C., Jiang G., RA Zhang L., Zhao W.; RT "Phosphatase PTPN4 preferentially inhibits TRIF-dependent TLR4 pathway by RT dephosphorylating TRAM."; RL J. Immunol. 194:4458-4465(2015). RN [7] RP STRUCTURE BY NMR OF 507-612. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of PDZ domain of protein tyrosine phosphatase, non- RT receptor type 4."; RL Submitted (NOV-2005) to the PDB data bank. RN [8] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ATTENUATED RABIES RP VIRUS PROTEIN G (MICROBIAL INFECTION). RX PubMed=20086240; DOI=10.1126/scisignal.2000510; RA Prehaud C., Wolff N., Terrien E., Lafage M., Megret F., Babault N., RA Cordier F., Tan G.S., Maitrepierre E., Menager P., Chopy D., Hoos S., RA England P., Delepierre M., Schnell M.J., Buc H., Lafon M.; RT "Attenuation of rabies virulence: takeover by the cytoplasmic domain of its RT envelope protein."; RL Sci. Signal. 3:RA5-RA5(2010). RN [9] RP X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) OF 499-604, INTERACTION WITH MAPK12, RP AND FUNCTION. RX PubMed=27246854; DOI=10.1074/jbc.m115.707208; RA Maisonneuve P., Caillet-Saguy C., Vaney M.C., Bibi-Zainab E., Sawyer K., RA Raynal B., Haouz A., Delepierre M., Lafon M., Cordier F., Wolff N.; RT "Molecular Basis of the Interaction of the Human Protein Tyrosine RT Phosphatase Non-receptor Type 4 (PTPN4) with the Mitogen-activated Protein RT Kinase p38gamma."; RL J. Biol. Chem. 291:16699-16708(2016). CC -!- FUNCTION: Phosphatase that plays a role in immunity, learning, synaptic CC plasticity or cell homeostasis (PubMed:25825441, PubMed:27246854). CC Regulates neuronal cell homeostasis by protecting neurons against CC apoptosis (PubMed:20086240). Negatively regulates TLR4-induced CC interferon beta production by dephosphorylating adapter TICAM2 and CC inhibiting subsequent TRAM-TRIF interaction (PubMed:25825441). CC Dephosphorylates also the immunoreceptor tyrosine-based activation CC motifs/ITAMs of the TCR zeta subunit and thereby negatively regulates CC TCR-mediated signaling pathway (By similarity). May act at junctions CC between the membrane and the cytoskeleton. {ECO:0000250, CC ECO:0000250|UniProtKB:Q9WU22, ECO:0000269|PubMed:20086240, CC ECO:0000269|PubMed:25825441, ECO:0000269|PubMed:27246854}. 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 MAPK12 (via C-terminus); this interaction CC abolishes PTPN4 catalytic autoinhibition and thus activates the CC phosphatase activity. {ECO:0000269|PubMed:27246854}. CC -!- SUBUNIT: (Microbial infection) Interacts with attenuated rabies virus CC protein G; this interaction is required for virally-induced apoptosis. CC {ECO:0000269|PubMed:20086240}. CC -!- INTERACTION: CC P29074; P46108: CRK; NbExp=3; IntAct=EBI-710431, EBI-886; CC P29074; Q92993: KAT5; NbExp=2; IntAct=EBI-710431, EBI-399080; CC P29074; P53778: MAPK12; NbExp=2; IntAct=EBI-710431, EBI-602406; CC P29074; P16333: NCK1; NbExp=3; IntAct=EBI-710431, EBI-389883; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8910369}; CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side CC {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:8910369}. CC Cytoplasm {ECO:0000269|PubMed:20086240, ECO:0000269|PubMed:8910369}. CC -!- PTM: Highly phosphorylated on serine and threonine residues but not on CC tyrosines. {ECO:0000269|PubMed:8910369}. CC -!- PTM: Cleaved and activated by calpain I/CAPN1. CC {ECO:0000269|PubMed:8910369}. CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non- CC receptor class subfamily. {ECO:0000305}. 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; M68941; AAA36530.1; -; mRNA. DR EMBL; AK314836; BAG37355.1; -; mRNA. DR EMBL; BC010674; AAH10674.1; -; mRNA. DR CCDS; CCDS2129.1; -. DR PIR; A41105; A41105. DR RefSeq; NP_002821.1; NM_002830.3. DR RefSeq; XP_016860089.1; XM_017004600.1. DR PDB; 2CS5; NMR; -; A=507-612. DR PDB; 2I75; X-ray; 2.45 A; A=611-926. DR PDB; 2VPH; X-ray; 1.90 A; A/B=513-606. DR PDB; 3NFK; X-ray; 1.43 A; A/B=499-604. DR PDB; 3NFL; X-ray; 1.91 A; A/B/C/D=499-604. DR PDB; 5EYZ; X-ray; 2.09 A; A/B/C/D=499-604. DR PDB; 5EZ0; X-ray; 2.35 A; A/B/C/D=499-604. DR PDBsum; 2CS5; -. DR PDBsum; 2I75; -. DR PDBsum; 2VPH; -. DR PDBsum; 3NFK; -. DR PDBsum; 3NFL; -. DR PDBsum; 5EYZ; -. DR PDBsum; 5EZ0; -. DR BMRB; P29074; -. DR SMR; P29074; -. DR BioGRID; 111741; 44. DR DIP; DIP-34634N; -. DR IntAct; P29074; 29. DR MINT; P29074; -. DR STRING; 9606.ENSP00000263708; -. DR BindingDB; P29074; -. DR ChEMBL; CHEMBL3165; -. DR DrugBank; DB00630; Alendronic acid. DR DEPOD; PTPN4; -. DR iPTMnet; P29074; -. DR PhosphoSitePlus; P29074; -. DR BioMuta; PTPN4; -. DR DMDM; 131531; -. DR EPD; P29074; -. DR jPOST; P29074; -. DR MassIVE; P29074; -. DR PaxDb; P29074; -. DR PeptideAtlas; P29074; -. DR PRIDE; P29074; -. DR ProteomicsDB; 54516; -. DR Antibodypedia; 18333; 131 antibodies. DR DNASU; 5775; -. DR Ensembl; ENST00000263708; ENSP00000263708; ENSG00000088179. DR GeneID; 5775; -. DR KEGG; hsa:5775; -. DR UCSC; uc002tmf.3; human. DR CTD; 5775; -. DR DisGeNET; 5775; -. DR EuPathDB; HostDB:ENSG00000088179.8; -. DR GeneCards; PTPN4; -. DR HGNC; HGNC:9656; PTPN4. DR HPA; ENSG00000088179; Low tissue specificity. DR MIM; 176878; gene. DR neXtProt; NX_P29074; -. DR OpenTargets; ENSG00000088179; -. DR PharmGKB; PA34000; -. DR eggNOG; KOG0792; Eukaryota. DR GeneTree; ENSGT00940000157211; -. DR HOGENOM; CLU_001645_7_0_1; -. DR InParanoid; P29074; -. DR KO; K18037; -. DR OMA; SHNNGKP; -. DR OrthoDB; 96595at2759; -. DR PhylomeDB; P29074; -. DR TreeFam; TF315900; -. DR BRENDA; 3.1.3.48; 2681. DR PathwayCommons; P29074; -. DR Reactome; R-HSA-166016; Toll Like Receptor 4 (TLR4) Cascade. DR Reactome; R-HSA-9008059; Interleukin-37 signaling. DR Reactome; R-HSA-9022699; MECP2 regulates neuronal receptors and channels. DR BioGRID-ORCS; 5775; 6 hits in 871 CRISPR screens. DR ChiTaRS; PTPN4; human. DR EvolutionaryTrace; P29074; -. DR GeneWiki; PTPN4; -. DR GenomeRNAi; 5775; -. DR Pharos; P29074; Tbio. DR PRO; PR:P29074; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; P29074; protein. DR Bgee; ENSG00000088179; Expressed in corpus callosum and 233 other tissues. DR ExpressionAtlas; P29074; baseline and differential. DR Genevisible; P29074; HS. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:UniProtKB. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro. DR GO; GO:0004726; F:non-membrane spanning protein tyrosine phosphatase activity; TAS:ProtInc. DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central. DR GO; GO:0071345; P:cellular response to cytokine stimulus; TAS:Reactome. DR GO; GO:0006470; P:protein dephosphorylation; TAS:ProtInc. DR CDD; cd14473; FERM_B-lobe; 1. DR CDD; cd13189; FERM_C_PTPN4_PTPN3_like; 1. DR Gene3D; 1.20.80.10; -; 1. DR Gene3D; 2.30.29.30; -; 1. DR Gene3D; 2.30.42.10; -; 1. DR Gene3D; 3.90.190.10; -; 1. DR IDEAL; IID00656; -. DR InterPro; IPR019749; Band_41_domain. DR InterPro; IPR014847; FERM-adjacent. DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf. DR InterPro; IPR035963; FERM_2. DR InterPro; IPR019748; FERM_central. DR InterPro; IPR019747; FERM_CS. DR InterPro; IPR000299; FERM_domain. DR InterPro; IPR018979; FERM_N. DR InterPro; IPR018980; FERM_PH-like_C. 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; PTPase_domain. DR InterPro; IPR041783; PTPN3/4_FERM_C. DR InterPro; IPR016130; Tyr_Pase_AS. DR InterPro; IPR003595; Tyr_Pase_cat. DR InterPro; IPR012151; Tyr_Pase_non-rcpt_typ-3/4. DR InterPro; IPR000387; TYR_PHOSPHATASE_dom. DR InterPro; IPR029071; Ubiquitin-like_domsf. DR Pfam; PF08736; FA; 1. DR Pfam; PF09380; FERM_C; 1. DR Pfam; PF00373; FERM_M; 1. DR Pfam; PF09379; FERM_N; 1. DR Pfam; PF00595; PDZ; 1. DR Pfam; PF00102; Y_phosphatase; 1. DR PIRSF; PIRSF000927; Tyr-Ptase_nr3; 1. DR PRINTS; PR00935; BAND41. DR PRINTS; PR00700; PRTYPHPHTASE. DR SMART; SM00295; B41; 1. DR SMART; SM01195; FA; 1. DR SMART; SM01196; FERM_C; 1. DR SMART; SM00228; PDZ; 1. DR SMART; SM00194; PTPc; 1. DR SMART; SM00404; PTPc_motif; 1. DR SUPFAM; SSF47031; SSF47031; 1. DR SUPFAM; SSF50156; SSF50156; 1. DR SUPFAM; SSF52799; SSF52799; 1. DR SUPFAM; SSF54236; SSF54236; 1. DR PROSITE; PS00660; FERM_1; 1. DR PROSITE; PS00661; FERM_2; 1. DR PROSITE; PS50057; FERM_3; 1. DR PROSITE; PS50106; PDZ; 1. DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1. DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1. DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Cytoplasm; Cytoskeleton; Hydrolase; Membrane; KW Phosphoprotein; Polymorphism; Protein phosphatase; Reference proteome. FT CHAIN 1..926 FT /note="Tyrosine-protein phosphatase non-receptor type 4" FT /id="PRO_0000219434" FT DOMAIN 29..312 FT /note="FERM" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084" FT DOMAIN 517..589 FT /note="PDZ" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143" FT DOMAIN 655..911 FT /note="Tyrosine-protein phosphatase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160" FT REGION 852..858 FT /note="Substrate binding" FT /evidence="ECO:0000250" FT ACT_SITE 852 FT /note="Phosphocysteine intermediate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160, FT ECO:0000255|PROSITE-ProRule:PRU10044" FT BINDING 820 FT /note="Substrate" FT /evidence="ECO:0000250" FT BINDING 896 FT /note="Substrate" FT /evidence="ECO:0000250" FT MOD_RES 474 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9WU22" FT VARIANT 924 FT /note="T -> S (in dbSNP:rs3189128)" FT /id="VAR_061033" FT CONFLICT 131 FT /note="K -> E (in Ref. 2; BAG37355)" FT /evidence="ECO:0000305" FT CONFLICT 772 FT /note="G -> K (in Ref. 4; no nucleotide entry)" FT /evidence="ECO:0000305" FT CONFLICT 863 FT /note="I -> V (in Ref. 2; BAG37355)" FT /evidence="ECO:0000305" FT STRAND 516..520 FT /evidence="ECO:0000244|PDB:3NFK" FT STRAND 524..526 FT /evidence="ECO:0000244|PDB:2CS5" FT STRAND 530..535 FT /evidence="ECO:0000244|PDB:3NFK" FT HELIX 536..538 FT /evidence="ECO:0000244|PDB:3NFK" FT STRAND 540..547 FT /evidence="ECO:0000244|PDB:3NFK" FT STRAND 549..551 FT /evidence="ECO:0000244|PDB:2CS5" FT HELIX 552..555 FT /evidence="ECO:0000244|PDB:3NFK" FT STRAND 556..558 FT /evidence="ECO:0000244|PDB:3NFK" FT STRAND 565..569 FT /evidence="ECO:0000244|PDB:3NFK" FT HELIX 579..587 FT /evidence="ECO:0000244|PDB:3NFK" FT HELIX 589..591 FT /evidence="ECO:0000244|PDB:3NFK" FT STRAND 596..602 FT /evidence="ECO:0000244|PDB:3NFK" FT STRAND 605..609 FT /evidence="ECO:0000244|PDB:2VPH" FT HELIX 639..651 FT /evidence="ECO:0000244|PDB:2I75" FT HELIX 654..661 FT /evidence="ECO:0000244|PDB:2I75" FT TURN 677..679 FT /evidence="ECO:0000244|PDB:2I75" FT HELIX 680..682 FT /evidence="ECO:0000244|PDB:2I75" FT HELIX 692..694 FT /evidence="ECO:0000244|PDB:2I75" FT STRAND 695..697 FT /evidence="ECO:0000244|PDB:2I75" FT STRAND 704..713 FT /evidence="ECO:0000244|PDB:2I75" FT STRAND 720..726 FT /evidence="ECO:0000244|PDB:2I75" FT HELIX 731..733 FT /evidence="ECO:0000244|PDB:2I75" FT HELIX 734..743 FT /evidence="ECO:0000244|PDB:2I75" FT STRAND 748..751 FT /evidence="ECO:0000244|PDB:2I75" FT STRAND 755..757 FT /evidence="ECO:0000244|PDB:2I75" FT STRAND 773..776 FT /evidence="ECO:0000244|PDB:2I75" FT STRAND 779..783 FT /evidence="ECO:0000244|PDB:2I75" FT STRAND 790..801 FT /evidence="ECO:0000244|PDB:2I75" FT TURN 802..805 FT /evidence="ECO:0000244|PDB:2I75" FT STRAND 806..815 FT /evidence="ECO:0000244|PDB:2I75" FT STRAND 820..823 FT /evidence="ECO:0000244|PDB:2I75" FT HELIX 828..841 FT /evidence="ECO:0000244|PDB:2I75" FT STRAND 848..851 FT /evidence="ECO:0000244|PDB:2I75" FT STRAND 853..857 FT /evidence="ECO:0000244|PDB:2I75" FT HELIX 858..873 FT /evidence="ECO:0000244|PDB:2I75" FT HELIX 880..888 FT /evidence="ECO:0000244|PDB:2I75" FT HELIX 898..911 FT /evidence="ECO:0000244|PDB:2I75" SQ SEQUENCE 926 AA; 105911 MW; 4DAC6A87A675CFB0 CRC64; MTSRFRLPAG RTYNVRASEL ARDRQHTEVV CNILLLDNTV QAFKVNKHDQ GQVLLDVVFK HLDLTEQDYF GLQLADDSTD NPRWLDPNKP IRKQLKRGSP YSLNFRVKFF VSDPNKLQEE YTRYQYFLQI KQDILTGRLP CPSNTAALLA SFAVQSELGD YDQSENLSGY LSDYSFIPNQ PQDFEKEIAK LHQQHIGLSP AEAEFNYLNT ARTLELYGVE FHYARDQSNN EIMIGVMSGG ILIYKNRVRM NTFPWLKIVK ISFKCKQFFI QLRKELHESR ETLLGFNMVN YRACKNLWKA CVEHHTFFRL DRPLPPQKNF FAHYFTLGSK FRYCGRTEVQ SVQYGKEKAN KDRVFARSPS KPLARKLMDW EVVSRNSISD DRLETQSLPS RSPPGTPNHR NSTFTQEGTR LRPSSVGHLV DHMVHTSPSE VFVNQRSPSS TQANSIVLES SPSQETPGDG KPPALPPKQS KKNSWNQIHY SHSQQDLESH INETFDIPSS PEKPTPNGGI PHDNLVLIRM KPDENGRFGF NVKGGYDQKM PVIVSRVAPG TPADLCVPRL NEGDQVVLIN GRDIAEHTHD QVVLFIKASC ERHSGELMLL VRPNAVYDVV EEKLENEPDF QYIPEKAPLD SVHQDDHSLR ESMIQLAEGL ITGTVLTQFD QLYRKKPGMT MSCAKLPQNI SKNRYRDISP YDATRVILKG NEDYINANYI NMEIPSSSII NQYIACQGPL PHTCTDFWQM TWEQGSSMVV MLTTQVERGR VKCHQYWPEP TGSSSYGCYQ VTCHSEEGNT AYIFRKMTLF NQEKNESRPL TQIQYIAWPD HGVPDDSSDF LDFVCHVRNK RAGKEEPVVV HCSAGIGRTG VLITMETAMC LIECNQPVYP LDIVRTMRDQ RAMMIQTPSQ YRFVCEAILK VYEEGFVKPL TTSTNK //