MTMR2_MOUSE
ID MTMR2_MOUSE Reviewed; 643 AA.
AC Q9Z2D1; B8JJF4; Q8VHA7;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Myotubularin-related protein 2;
DE AltName: Full=Phosphatidylinositol-3,5-bisphosphate 3-phosphatase;
DE EC=3.1.3.95 {ECO:0000269|PubMed:12045210, ECO:0000269|PubMed:16399794};
DE AltName: Full=Phosphatidylinositol-3-phosphate phosphatase;
DE EC=3.1.3.64 {ECO:0000269|PubMed:12045210, ECO:0000269|PubMed:16399794};
GN Name=Mtmr2;
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].
RA Bolino A., Marigo V., Loader J., Romio L., Leoni A., Di Duca M., Cinti R.,
RA Feltri M.L., Wrabetz L., Ravazzolo R., Monaco A.P.;
RT "Molecular characterization and expression analysis of Mtmr2, mouse homolog
RT of MTMR2, the myotubularin-related 2 gene, mutated in CMT4B.";
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
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 GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-225.
RX PubMed=9736772; DOI=10.1093/hmg/7.11.1703;
RA Laporte J., Blondeau F., Buj-Bello A., Tentler D., Kretz C., Dahl N.,
RA Mandel J.-L.;
RT "Characterization of the myotubularin dual specificity phosphatase gene
RT family from yeast to human.";
RL Hum. Mol. Genet. 7:1703-1712(1998).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF GLY-103, AND TISSUE
RP SPECIFICITY.
RX PubMed=12045210; DOI=10.1093/hmg/11.13.1569;
RA Berger P., Bonneick S., Willi S., Wymann M., Suter U.;
RT "Loss of phosphatase activity in myotubularin-related protein 2 is
RT associated with Charcot-Marie-Tooth disease type 4B1.";
RL Hum. Mol. Genet. 11:1569-1579(2002).
RN [6]
RP SUBCELLULAR LOCATION, MUTAGENESIS OF GLY-103 AND CYS-417, SUBUNIT, AND
RP DOMAIN.
RX PubMed=14530412; DOI=10.1073/pnas.2132732100;
RA Berger P., Schaffitzel C., Berger I., Ban N., Suter U.;
RT "Membrane association of myotubularin-related protein 2 is mediated by a
RT pleckstrin homology-GRAM domain and a coiled-coil dimerization module.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:12177-12182(2003).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, INTERACTION WITH SBF2,
RP SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP CYS-417 AND 589-PRO--VAL-643.
RX PubMed=16399794; DOI=10.1093/hmg/ddi473;
RA Berger P., Berger I., Schaffitzel C., Tersar K., Volkmer B., Suter U.;
RT "Multi-level regulation of myotubularin-related protein-2 phosphatase
RT activity by myotubularin-related protein-13/set-binding factor-2.";
RL Hum. Mol. Genet. 15:569-579(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-9 AND SER-58, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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 [10]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF 589-PRO--VAL-643.
RX PubMed=23297362; DOI=10.1093/hmg/dds562;
RA Ng A.A., Logan A.M., Schmidt E.J., Robinson F.L.;
RT "The CMT4B disease-causing phosphatases Mtmr2 and Mtmr13 localize to the
RT Schwann cell cytoplasm and endomembrane compartments, where they depend
RT upon each other to achieve wild-type levels of protein expression.";
RL Hum. Mol. Genet. 22:1493-1506(2013).
CC -!- FUNCTION: Phosphatase that acts on lipids with a phosphoinositol
CC headgroup (PubMed:12045210, PubMed:16399794). Has phosphatase activity
CC towards pho sphatidylinositol 3-phosphate and phosphatidylinositol 3,5-
CC bisphosphate (PubMed:12045210, PubMed:16399794). Binds
CC phosphatidylinositol 4-phosphate, phosphatidylinositol 5-phosphate,
CC phosphatidylinositol 3,5-bisphosphate and phosphatidylinositol 3,4,5-
CC trisphosphate (PubMed:12045210, PubMed:16399794). Stabilizes
CC SBF2/MTMR13 at the membranes (PubMed:23297362). Specifically in
CC peripheral nerves, stabilizes SBF2/MTMR13 protein (PubMed:23297362).
CC {ECO:0000269|PubMed:12045210, ECO:0000269|PubMed:16399794,
CC ECO:0000269|PubMed:23297362}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-
CC phosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol) + phosphate; Xref=Rhea:RHEA:12316, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57880, ChEBI:CHEBI:58088; EC=3.1.3.64;
CC Evidence={ECO:0000269|PubMed:12045210, ECO:0000269|PubMed:16399794};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-
CC bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-5-phosphate) + phosphate; Xref=Rhea:RHEA:39019,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57795,
CC ChEBI:CHEBI:57923; EC=3.1.3.95;
CC Evidence={ECO:0000269|PubMed:12045210, ECO:0000269|PubMed:16399794};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dioctanoyl-sn-glycero-3-phospho-(1-D-myo-inositol-3-
CC phosphate) + H2O = 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-
CC inositol) + phosphate; Xref=Rhea:RHEA:42328, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:65221, ChEBI:CHEBI:78934;
CC Evidence={ECO:0000250|UniProtKB:Q13614};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-
CC bisphosphate) + H2O = 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-5-phosphate) + phosphate; Xref=Rhea:RHEA:45632,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:78911,
CC ChEBI:CHEBI:85342; Evidence={ECO:0000250|UniProtKB:Q13614};
CC -!- ACTIVITY REGULATION: Interaction with SBF1/MTMR5 increases phosphatase
CC activity (By similarity). Increases SBF2/MTMR13 catalytic activity
CC towards phosphatidylinositol 3,5-bisphosphate and to a lesser extent
CC towards phosphatidylinositol 3-phosphate (PubMed:16399794).
CC {ECO:0000250|UniProtKB:Q13614, ECO:0000269|PubMed:16399794}.
CC -!- SUBUNIT: Homodimer (via coiled-coil domain) (PubMed:14530412,
CC PubMed:16399794). Heterotetramer consisting of one MTMR2 dimer and one
CC SBF2/MTMR13 dimer (PubMed:16399794). Heterodimer with SBF1/MTMR5 (By
CC similarity). Heterodimer with MTMR12 (By similarity).
CC {ECO:0000250|UniProtKB:Q13614, ECO:0000269|PubMed:14530412,
CC ECO:0000269|PubMed:16399794}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14530412,
CC ECO:0000269|PubMed:16399794, ECO:0000269|PubMed:23297362}. Early
CC endosome membrane {ECO:0000250|UniProtKB:Q13614}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:Q13614}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:14530412}. Cell projection, axon
CC {ECO:0000269|PubMed:23297362}. Endosome membrane
CC {ECO:0000269|PubMed:23297362}; Peripheral membrane protein
CC {ECO:0000305}. Note=Partly associated with membranes (PubMed:14530412,
CC PubMed:23297362). Localizes to vacuoles in hypo-osmotic conditions
CC (PubMed:16399794). {ECO:0000269|PubMed:14530412,
CC ECO:0000269|PubMed:16399794, ECO:0000269|PubMed:23297362}.
CC -!- TISSUE SPECIFICITY: Expressed in sciatic nerve and in Schwann cells (at
CC protein level) (PubMed:16399794, PubMed:23297362). Detected in adult
CC dorsal root ganglia, neurons of the central nervous system, motor
CC neurons, cell soma and neurites of sensory neurons, olfactory bulb,
CC cerebellum and hippocampus (PubMed:12045210).
CC {ECO:0000269|PubMed:12045210, ECO:0000269|PubMed:16399794,
CC ECO:0000269|PubMed:23297362}.
CC -!- DEVELOPMENTAL STAGE: In 16.5 dpc embryos, expressed in forebrain,
CC dorsal root ganglia, trigeminal ganglia, kidney, adrenal gland and
CC lung. {ECO:0000269|PubMed:12045210}.
CC -!- DOMAIN: The coiled-coil domain mediates homodimerization
CC (PubMed:14530412). Also mediates interaction with SBF1/MTMR5 and
CC SBF2/MTMR13 (By similarity). {ECO:0000250|UniProtKB:Q13614,
CC ECO:0000269|PubMed:14530412}.
CC -!- DOMAIN: The GRAM domain mediates binding to phosphatidylinositol 4-
CC phosphate, phosphatidylinositol 5-phosphate, phosphatidylinositol 3,5-
CC biphosphate and phosphatidylinositol 3,4,5-trisphosphate.
CC {ECO:0000269|PubMed:14530412}.
CC -!- PTM: Phosphorylation at Ser-58 decreases MTMR2 localization to
CC endocytic vesicular structures. {ECO:0000250|UniProtKB:Q13614}.
CC -!- DISRUPTION PHENOTYPE: SBF2/MTMR13 protein levels are decreased in
CC sciatic nerves but not in the brain or in fibroblasts.
CC {ECO:0000269|PubMed:23297362}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class myotubularin subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC80002.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY055832; AAL14198.1; -; mRNA.
DR EMBL; CT010488; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466522; EDL24975.1; -; Genomic_DNA.
DR EMBL; AF073880; AAC80002.1; ALT_INIT; mRNA.
DR CCDS; CCDS22818.3; -.
DR RefSeq; NP_076347.3; NM_023858.3.
DR AlphaFoldDB; Q9Z2D1; -.
DR SMR; Q9Z2D1; -.
DR BioGRID; 218525; 11.
DR IntAct; Q9Z2D1; 5.
DR STRING; 10090.ENSMUSP00000034396; -.
DR iPTMnet; Q9Z2D1; -.
DR PhosphoSitePlus; Q9Z2D1; -.
DR SwissPalm; Q9Z2D1; -.
DR EPD; Q9Z2D1; -.
DR jPOST; Q9Z2D1; -.
DR MaxQB; Q9Z2D1; -.
DR PaxDb; Q9Z2D1; -.
DR PeptideAtlas; Q9Z2D1; -.
DR PRIDE; Q9Z2D1; -.
DR ProteomicsDB; 290069; -.
DR Antibodypedia; 31676; 267 antibodies from 29 providers.
DR DNASU; 77116; -.
DR Ensembl; ENSMUST00000034396; ENSMUSP00000034396; ENSMUSG00000031918.
DR GeneID; 77116; -.
DR KEGG; mmu:77116; -.
DR UCSC; uc009odz.2; mouse.
DR CTD; 8898; -.
DR MGI; MGI:1924366; Mtmr2.
DR VEuPathDB; HostDB:ENSMUSG00000031918; -.
DR eggNOG; KOG4471; Eukaryota.
DR GeneTree; ENSGT00940000153669; -.
DR InParanoid; Q9Z2D1; -.
DR OMA; ESYAICD; -.
DR OrthoDB; 824298at2759; -.
DR PhylomeDB; Q9Z2D1; -.
DR TreeFam; TF315197; -.
DR BRENDA; 3.1.3.95; 3474.
DR Reactome; R-MMU-1483248; Synthesis of PIPs at the ER membrane.
DR Reactome; R-MMU-1660516; Synthesis of PIPs at the early endosome membrane.
DR Reactome; R-MMU-1660517; Synthesis of PIPs at the late endosome membrane.
DR BioGRID-ORCS; 77116; 6 hits in 74 CRISPR screens.
DR ChiTaRS; Mtmr2; mouse.
DR PRO; PR:Q9Z2D1; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9Z2D1; protein.
DR Bgee; ENSMUSG00000031918; Expressed in humerus cartilage element and 201 other tissues.
DR ExpressionAtlas; Q9Z2D1; baseline and differential.
DR Genevisible; Q9Z2D1; MM.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0097060; C:synaptic membrane; ISO:MGI.
DR GO; GO:0008021; C:synaptic vesicle; ISO:MGI.
DR GO; GO:0005774; C:vacuolar membrane; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0052866; F:phosphatidylinositol phosphate phosphatase activity; IMP:MGI.
DR GO; GO:0052629; F:phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity; ISS:UniProtKB.
DR GO; GO:0004438; F:phosphatidylinositol-3-phosphatase activity; ISS:UniProtKB.
DR GO; GO:0097062; P:dendritic spine maintenance; ISO:MGI.
DR GO; GO:0016311; P:dephosphorylation; IDA:MGI.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IDA:MGI.
DR GO; GO:0032288; P:myelin assembly; IMP:MGI.
DR GO; GO:0042552; P:myelination; IGI:MGI.
DR GO; GO:0045806; P:negative regulation of endocytosis; ISO:MGI.
DR GO; GO:0090394; P:negative regulation of excitatory postsynaptic potential; ISO:MGI.
DR GO; GO:0031642; P:negative regulation of myelination; IMP:MGI.
DR GO; GO:2000645; P:negative regulation of receptor catabolic process; ISO:MGI.
DR GO; GO:0002091; P:negative regulation of receptor internalization; ISO:MGI.
DR GO; GO:0048666; P:neuron development; IGI:MGI.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IDA:MGI.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; IMP:MGI.
DR GO; GO:2000643; P:positive regulation of early endosome to late endosome transport; ISO:MGI.
DR GO; GO:0060304; P:regulation of phosphatidylinositol dephosphorylation; ISO:MGI.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR004182; GRAM.
DR InterPro; IPR010569; Myotubularin-like_Pase_dom.
DR InterPro; IPR030564; Myotubularin_fam.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR PANTHER; PTHR10807; PTHR10807; 1.
DR Pfam; PF02893; GRAM; 1.
DR Pfam; PF06602; Myotub-related; 1.
DR SMART; SM00568; GRAM; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
PE 1: Evidence at protein level;
KW Cell projection; Coiled coil; Cytoplasm; Endosome; Hydrolase;
KW Lipid metabolism; Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..643
FT /note="Myotubularin-related protein 2"
FT /id="PRO_0000094935"
FT DOMAIN 68..139
FT /note="GRAM"
FT /evidence="ECO:0000255"
FT DOMAIN 205..580
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00669"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 593..627
FT /evidence="ECO:0000269|PubMed:14530412"
FT COMPBIAS 20..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..643
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 417
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q13614"
FT BINDING 330..333
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q13614"
FT BINDING 355..356
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q13614"
FT BINDING 417..423
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q13614"
FT BINDING 463
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q13614"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MUTAGEN 103
FT /note="G->E: Severely impaired interaction with membranes
FT and strongly reduced catalytic activity."
FT /evidence="ECO:0000269|PubMed:12045210,
FT ECO:0000269|PubMed:14530412"
FT MUTAGEN 417
FT /note="C->A: Loss of activity. Does not affect the
FT interaction with SBF2/MTMR13."
FT /evidence="ECO:0000269|PubMed:14530412,
FT ECO:0000269|PubMed:16399794"
FT MUTAGEN 589..643
FT /note="Missing: Loss of interaction with SBF2/MTMR13 which
FT results in a decrease in SBF2/MTMR13 localization to
FT membranes."
FT /evidence="ECO:0000269|PubMed:16399794,
FT ECO:0000269|PubMed:23297362"
SQ SEQUENCE 643 AA; 73232 MW; FD4E43867CBB9864 CRC64;
MEKSSSCESL GAQLPAARLP SEDSLSSAST SHSENSVHTK SASAISSDSI STSADNFSPD
LRVLREANKL AEMEEPALLP GENIKDMAKD VTYICPFTGA VRGTLTVTSY RLYFKSMERD
PPFVLDASLG VISRVEKIGG ASSRGENSYG LETVCKDIRN LRFAHKPEGR TRRSIFENLM
KYAFPVSNGL PLFAFEYKEV FPENGWKLYD PLLEYRRQGI PNESWRITKI NERYELCDTY
PALLVVPANI PDEELKRVAS FRSRGRIPVL SWIHPESQAT VTRCSQPMVG VSGKRSKEDE
KYLQAIMDSN AQSHKIFIFD ARPSVNAVAN KAKGGGYESE DAYQNAELVF LDIHNIHVMR
ESLRKLKEIV YPTIEETHWL SNLESTHWLE HIKLILAGAL RIADKVESGK TSVVVHCSDG
WDRTAQLTSL AMLMLDGYYR TIRGFEVLVE KEWLSFGHRF QLRVGHGDKN HADADRSPVF
LQFIDCVWQM TRQFPTAFEF NEYFLITILD HLYSCLFGTF LCNSEQQRGK ENLPKKTVSL
WSYINSQLED FTNPLYGSYS NHVLYPVASM RHLELWVGYY IRWNPRMKPQ EPIHSRYKEL
LAKRAELQRK VEELQREISN RSTSSSERAS SPAQCVTPVQ TVV
