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 24-JAN-2024, entry version 174. 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, RC Pancreas, 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}; 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; 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 GlyGen; Q9Z2D1; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9Z2D1; -. DR PhosphoSitePlus; Q9Z2D1; -. DR SwissPalm; Q9Z2D1; -. DR EPD; Q9Z2D1; -. DR jPOST; Q9Z2D1; -. DR MaxQB; Q9Z2D1; -. DR PaxDb; 10090-ENSMUSP00000034396; -. DR PeptideAtlas; Q9Z2D1; -. DR ProteomicsDB; 290069; -. DR Pumba; Q9Z2D1; -. DR Antibodypedia; 31676; 299 antibodies from 29 providers. DR DNASU; 77116; -. DR Ensembl; ENSMUST00000034396.14; ENSMUSP00000034396.8; ENSMUSG00000031918.17. DR GeneID; 77116; -. DR KEGG; mmu:77116; -. DR UCSC; uc009odz.2; mouse. DR AGR; MGI:1924366; -. DR CTD; 8898; -. DR MGI; MGI:1924366; Mtmr2. DR VEuPathDB; HostDB:ENSMUSG00000031918; -. DR eggNOG; KOG4471; Eukaryota. DR GeneTree; ENSGT00940000153669; -. DR InParanoid; Q9Z2D1; -. DR OMA; WRATKIN; -. DR OrthoDB; 5474662at2759; -. 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 79 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 204 other cell types or tissues. DR ExpressionAtlas; Q9Z2D1; baseline and differential. 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:0016020; C:membrane; IBA:GO_Central. 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-phosphate 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: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 CDD; cd14590; PTP-MTMR2; 1. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 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; MYOTUBULARIN-RELATED; 1. DR PANTHER; PTHR10807:SF42; MYOTUBULARIN-RELATED PROTEIN 2; 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; (Phosphotyrosine protein) phosphatases II; 1. DR SUPFAM; SSF50729; PH domain-like; 1. DR PROSITE; PS51339; PPASE_MYOTUBULARIN; 1. DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1. DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1. DR Genevisible; Q9Z2D1; MM. 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 //