MTMR3_CAEEL
ID MTMR3_CAEEL Reviewed; 1006 AA.
AC Q22712; A8NBE6; Q9U360; Q9XTK4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Myotubularin-related protein 3;
DE Short=ceMTM3;
DE EC=3.1.3.48 {ECO:0000250|UniProtKB:Q13615};
DE AltName: Full=Myotubularin homologous protein 1;
DE Short=ceMTMH1;
DE AltName: Full=Phosphatidylinositol-3,5-bisphosphate 3-phosphatase;
DE EC=3.1.3.95 {ECO:0000269|PubMed:18393358, ECO:0000269|PubMed:25124690};
DE AltName: Full=Phosphatidylinositol-3-phosphate phosphatase;
DE EC=3.1.3.64 {ECO:0000269|PubMed:18393358, ECO:0000269|PubMed:25124690};
GN Name=mtm-3 {ECO:0000312|WormBase:T24A11.1a};
GN ORFNames=T24A11.1 {ECO:0000312|WormBase:T24A11.1a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), FUNCTION, CATALYTIC ACTIVITY,
RP PHOSPHATIDYLINOSITOL 3-PHOSPHATE-BINDING, ACTIVITY REGULATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=18393358; DOI=10.1002/jcb.21752;
RA Ma J., Zeng F., Ho W.T., Teng L., Li Q., Fu X., Zhao Z.J.;
RT "Characterization and functional studies of a FYVE domain-containing
RT phosphatase in C. elegans.";
RL J. Cell. Biochem. 104:1843-1852(2008).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=12788949; DOI=10.1074/jbc.m303259200;
RA Xue Y., Fares H., Grant B., Li Z., Rose A.M., Clark S.G., Skolnik E.Y.;
RT "Genetic analysis of the myotubularin family of phosphatases in
RT Caenorhabditis elegans.";
RL J. Biol. Chem. 278:34380-34386(2003).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, ACTIVE SITE, AND MUTAGENESIS OF 67-LEU--LEU-1006.
RX PubMed=25124690; DOI=10.15252/embr.201438618;
RA Wu Y., Cheng S., Zhao H., Zou W., Yoshina S., Mitani S., Zhang H., Wang X.;
RT "PI3P phosphatase activity is required for autophagosome maturation and
RT autolysosome formation.";
RL EMBO Rep. 15:973-981(2014).
CC -!- FUNCTION: Preferentially dephosphorylates phosphatidylinositol 3-
CC phosphate (PI3P), and has some activity towards phosphatidylinositol
CC 3,5-bisphosphate (PI35P) (PubMed:18393358, PubMed:25124690). May also
CC dephosphorylate proteins phosphorylated on Ser, Thr, and Tyr residues
CC (By similarity). Positively regulates autophagy and is recruited to
CC autophagosomes by PI3P where it catalyzes PI3P turnover to promote
CC autophagosome maturation (PubMed:25124690). Thought to have a role in
CC maintenance of muscle function (PubMed:18393358). Involved in
CC locomotion and lifespan determination (PubMed:18393358).
CC {ECO:0000250|UniProtKB:Q13615, ECO:0000269|PubMed:18393358,
CC ECO:0000269|PubMed:25124690}.
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;
CC Evidence={ECO:0000250|UniProtKB:Q13615, ECO:0000255|PROSITE-
CC ProRule:PRU10044};
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:18393358, ECO:0000269|PubMed:25124690};
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:18393358, ECO:0000269|PubMed:25124690};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-3-
CC phosphate) + H2O = 1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-
CC inositol) + phosphate; Xref=Rhea:RHEA:45640, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:72835, ChEBI:CHEBI:78995;
CC Evidence={ECO:0000250|UniProtKB:Q13615};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-
CC phosphate) + H2O = 1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-5-phosphate) + phosphate; Xref=Rhea:RHEA:45636,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:78994,
CC ChEBI:CHEBI:84968; Evidence={ECO:0000250|UniProtKB:Q13615};
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:Q13615};
CC -!- ACTIVITY REGULATION: Inhibited by sodium vanadate and peroxide.
CC {ECO:0000269|PubMed:18393358}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25124690}. Membrane
CC {ECO:0000250|UniProtKB:Q13615}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q13615}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:T24A11.1a};
CC IsoId=Q22712-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:T24A11.1b};
CC IsoId=Q22712-2; Sequence=VSP_035035, VSP_035036, VSP_035037;
CC -!- TISSUE SPECIFICITY: Expressed in the body wall muscle and in eggs
CC (PubMed:18393358). Expressed in head neurons (PubMed:12788949).
CC Expressed in the intestine (PubMed:18393358, PubMed:25124690).
CC Expressed in pharyngeal cells, vulval muscle cells and cells of the
CC tail region (PubMed:25124690). {ECO:0000269|PubMed:12788949,
CC ECO:0000269|PubMed:18393358, ECO:0000269|PubMed:25124690}.
CC -!- DEVELOPMENTAL STAGE: Expressed in most cells during embryogenesis
CC (PubMed:25124690). Expressed most strongly in the egg with expression
CC present in L1 but reducing through to L3 where it is very weak. No
CC expression was found in L4. Strong expression is also seen in egg-
CC laying adults and post-reproductive adults.
CC {ECO:0000269|PubMed:18393358, ECO:0000269|PubMed:25124690}.
CC -!- DOMAIN: Interacts with phosphatidylinositol 3-phosphate (PI3P) via the
CC FYVE-type domain. {ECO:0000269|PubMed:18393358}.
CC -!- DISRUPTION PHENOTYPE: Worms exhibit a 2-fold increase in PI3P, sluggish
CC body movement with progressive deterioration and defects in gestation.
CC {ECO:0000269|PubMed:18393358}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class myotubularin subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC78763.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF031519; AAC78763.1; ALT_FRAME; mRNA.
DR EMBL; DQ988041; ABK59970.1; -; mRNA.
DR EMBL; BX284603; CAA88884.2; -; Genomic_DNA.
DR EMBL; BX284603; CAB61017.2; -; Genomic_DNA.
DR PIR; T25215; T25215.
DR RefSeq; NP_001022794.2; NM_001027623.5. [Q22712-1]
DR RefSeq; NP_497766.3; NM_065365.6. [Q22712-2]
DR AlphaFoldDB; Q22712; -.
DR SMR; Q22712; -.
DR BioGRID; 40728; 3.
DR STRING; 6239.T24A11.1a; -.
DR EPD; Q22712; -.
DR PaxDb; Q22712; -.
DR PeptideAtlas; Q22712; -.
DR EnsemblMetazoa; T24A11.1a.1; T24A11.1a.1; WBGene00003476. [Q22712-1]
DR EnsemblMetazoa; T24A11.1b.1; T24A11.1b.1; WBGene00003476. [Q22712-2]
DR EnsemblMetazoa; T24A11.1b.2; T24A11.1b.2; WBGene00003476. [Q22712-2]
DR GeneID; 175490; -.
DR KEGG; cel:CELE_T24A11.1; -.
DR UCSC; T24A11.1b; c. elegans.
DR CTD; 175490; -.
DR WormBase; T24A11.1a; CE28087; WBGene00003476; mtm-3. [Q22712-1]
DR WormBase; T24A11.1b; CE42568; WBGene00003476; mtm-3. [Q22712-2]
DR eggNOG; KOG1089; Eukaryota.
DR GeneTree; ENSGT00940000172447; -.
DR InParanoid; Q22712; -.
DR OMA; FENTEYY; -.
DR OrthoDB; 824298at2759; -.
DR PhylomeDB; Q22712; -.
DR Reactome; R-CEL-1632852; Macroautophagy.
DR Reactome; R-CEL-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-CEL-1660516; Synthesis of PIPs at the early endosome membrane.
DR Reactome; R-CEL-1660517; Synthesis of PIPs at the late endosome membrane.
DR Reactome; R-CEL-2173788; Downregulation of TGF-beta receptor signaling.
DR PRO; PR:Q22712; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00003476; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0019898; C:extrinsic component of membrane; ISS:UniProtKB.
DR GO; GO:0016312; F:inositol bisphosphate phosphatase activity; IDA:WormBase.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0034594; F:phosphatidylinositol trisphosphate phosphatase activity; IDA:WormBase.
DR GO; GO:0052629; F:phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity; IDA:UniProtKB.
DR GO; GO:0004438; F:phosphatidylinositol-3-phosphatase activity; IDA:UniProtKB.
DR GO; GO:0019903; F:protein phosphatase binding; IBA:GO_Central.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:WormBase.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IDA:WormBase.
DR GO; GO:0040011; P:locomotion; IMP:WormBase.
DR GO; GO:1901075; P:negative regulation of engulfment of apoptotic cell; IGI:WormBase.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; ISS:UniProtKB.
DR GO; GO:1901098; P:positive regulation of autophagosome maturation; IMP:UniProtKB.
DR GO; GO:0010508; P:positive regulation of autophagy; IMP:UniProtKB.
DR GO; GO:0045807; P:positive regulation of endocytosis; IMP:WormBase.
DR GO; GO:0010506; P:regulation of autophagy; IBA:GO_Central.
DR GO; GO:0046662; P:regulation of oviposition; IMP:WormBase.
DR GO; GO:0042594; P:response to starvation; IMP:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR010569; Myotubularin-like_Pase_dom.
DR InterPro; IPR030564; Myotubularin_fam.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10807; PTHR10807; 2.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF06602; Myotub-related; 1.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Developmental protein; Hydrolase;
KW Lipid metabolism; Lipid-binding; Membrane; Metal-binding;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..1006
FT /note="Myotubularin-related protein 3"
FT /id="PRO_0000094947"
FT DOMAIN 224..630
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00669"
FT ZN_FING 818..883
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 641..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 886..1006
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..705
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..925
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 930..953
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 954..970
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 984..998
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 463
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10044,
FT ECO:0000269|PubMed:25124690"
FT BINDING 377..380
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q13614"
FT BINDING 402..403
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q13614"
FT BINDING 463..469
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q13614"
FT BINDING 509
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 824
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 827
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 845
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 848
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 853
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 856
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 875
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 878
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT VAR_SEQ 41..44
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000303|PubMed:18393358"
FT /id="VSP_035035"
FT VAR_SEQ 891..965
FT /note="SSSTTTTSSSTKIENDSNVPGLDNNSDNVSENVSENAIPDIIVEEKEAEDPI
FT KEAESPSKETKCPKTLRNFISFS -> RATSLSEMSSFDSFGPSSPPASSTSSSSLNML
FT ASMSPTRPQPIPISCKSSSNSISSPRPSPGEFSRHSSTQAVKG (in isoform b)"
FT /evidence="ECO:0000303|PubMed:18393358"
FT /id="VSP_035036"
FT VAR_SEQ 966..1006
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000303|PubMed:18393358"
FT /id="VSP_035037"
FT MUTAGEN 67..1006
FT /note="Missing: In tm4475; viable but display 36% embryonic
FT lethality and 45% larval arrest. Reduces survival of L1
FT larvae in nutrient-deprived conditions. Defective
FT autophagosome maturation and degradation of autophagic
FT protein aggregates."
FT /evidence="ECO:0000269|PubMed:25124690"
FT MUTAGEN 463
FT /note="C->S: Abolished phosphatase activity towards
FT phosphatidylinositol 3-phosphate (PI3P)
FT phosphatidylinositol 3,5-bisphosphate (PI35P)."
FT /evidence="ECO:0000269|PubMed:25124690"
SQ SEQUENCE 1006 AA; 113614 MW; BEFC03296E74DB1A CRC64;
MTVTSSAAID IGGGGGGRRS DRLDSDRTSE DMSFIASPAN ESFQIGASFV DVQNESSGSI
DTATATLHEL NYTFGMPPVT EESENMPQNY ETVVELLPGE ERAPINKLTE FPIEGGSLFV
TNFRIVVILK DKEVEEALRF LVFPLQDIEQ IDLAIPAFIH LSLKIGRMFT ICFKTAEDAA
LVHKILYTAF QRLNRPISSI YTSRPQDWTS KNTDNPMQSL NAFAWKFSEA VDELDRDGKL
PSWLLRADSV AQEITHIDFN RLGMSEHFQI SSVNENFEVC PTYPEKIIVP KGITDDDIRK
GAPYRSIGRF PAVIWRCRKT RAVLMRSSQP QVGILSWRNP TDEKIIEEAV KASRIEGEEK
KQFIIMDARG YTSAFANRAR SGGFENTEYY QQAKLEFLGL PNIHAVRGSF NNVRTMLHNL
GPNEQLLTSL QTTGWLLNLS NLLVNAANCA DHLSKGHSVL VHCSDGWDRT TQVTTLAKIM
LDEYYRTVKG FEELIRRDWI AFGHKLYDRQ LVAFGNWGTS DERSPVFLQF LEAVRHLQRE
QPTLFQFTHA YLIKLAKHAY SGLFGSFLFN SHKERREAME KCKGTLVDIW RFIGPHNEEY
VNQSFDEHYT GAVKPVNVSV INLRVWHEVF ADEEEHYTQI FSPKEERPLS GCTTPMNTST
STNLVKSKSS ESINSLNVDG SAKESSQQHP TCSTTPSDNT NSLPMSTSFI QQSLYQPKVR
GVAAIDRDGV IRFEDDEQAM LRKKNKLRAE EIRRKDEKIE ELRRRAVLDT NKVSPGQRQS
YSESDVETTG TLERVMSDVS MVDPVNELPH FKPNTTWEGE SGHCAYCKKE FNKLSVYVED
RQHHCRNCGR VVCEDCSKNR FSVIEEGKSV QKRACDSCYD SMHETDLKLS SSSTTTTSSS
TKIENDSNVP GLDNNSDNVS ENVSENAIPD IIVEEKEAED PIKEAESPSK ETKCPKTLRN
FISFSPKSSM RKNKVHSRDP LKSIDEGSSS QQAESDDVLD VNEQPL
