PPN1_YEAST
ID PPN1_YEAST Reviewed; 674 AA.
AC Q04119; D6VT77;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Endopolyphosphatase {ECO:0000303|PubMed:11447286};
DE EC=3.6.1.10 {ECO:0000269|PubMed:15792812};
DE AltName: Full=Deoxyadenosine triphosphate phosphohydrolase {ECO:0000303|Ref.16};
DE Short=dATP phosphohydrolase {ECO:0000303|Ref.16};
DE EC=3.6.1.- {ECO:0000269|Ref.16};
DE AltName: Full=Exopolyphosphatase;
DE EC=3.6.1.11 {ECO:0000269|PubMed:15170373};
DE AltName: Full=Phosphate metabolism protein 5 {ECO:0000303|PubMed:11102525};
DE Flags: Precursor;
GN Name=PPN1 {ECO:0000303|PubMed:11447286};
GN Synonyms=PHM5 {ECO:0000303|PubMed:11102525};
GN OrderedLocusNames=YDR452W {ECO:0000312|SGD:S000002860}; ORFNames=D9461.37;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 184-212, FUNCTION,
RP AND PROTEOLYTIC PROCESSING.
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=11447286; DOI=10.1073/pnas.151269398;
RA Sethuraman A., Rao N.N., Kornberg A.;
RT "The endopolyphosphatase gene: essential in Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:8542-8547(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP PROTEIN SEQUENCE OF 84-95 AND 381-384, FUNCTION, CATALYTIC ACTIVITY,
RP GLYCOSYLATION, PROTEOLYTIC PROCESSING, AND MUTAGENESIS OF ASN-11; ASN-505
RP AND ASN-511.
RX PubMed=15792812; DOI=10.1016/j.febslet.2005.02.032;
RA Shi X., Kornberg A.;
RT "Endopolyphosphatase in Saccharomyces cerevisiae undergoes post-
RT translational activations to produce short-chain polyphosphates.";
RL FEBS Lett. 579:2014-2018(2005).
RN [5]
RP PROTEIN SEQUENCE OF 97-126; 184-198; 243-258; 320-334 AND 580-605, AND
RP SUBCELLULAR LOCATION.
RX PubMed=17009950; DOI=10.1134/s0006297906090045;
RA Andreeva N.A., Kulakovskaya T.V., Kulaev I.S.;
RT "High molecular mass exopolyphosphatase from the cytosol of the yeast
RT Saccharomyces cerevisiae is encoded by the PPN1 gene.";
RL Biochemistry (Mosc.) 71:975-977(2006).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, COFACTOR, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=8900207; DOI=10.1074/jbc.271.43.27146;
RA Kumble K.D., Kornberg A.;
RT "Endopolyphosphatases for long chain inorganic polyphosphate in yeast and
RT mammals.";
RL J. Biol. Chem. 271:27146-27151(1996).
RN [7]
RP FUNCTION.
RX PubMed=11102525; DOI=10.1091/mbc.11.12.4309;
RA Ogawa N., DeRisi J.L., Brown P.O.;
RT "New components of a system for phosphate accumulation and polyphosphate
RT metabolism in Saccharomyces cerevisiae revealed by genomic expression
RT analysis.";
RL Mol. Biol. Cell 11:4309-4321(2000).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, UBIQUITINATION
RP AT LYS-6, AND MUTAGENESIS OF LYS-6.
RX PubMed=11566881; DOI=10.1093/emboj/20.18.5176;
RA Reggiori F., Pelham H.R.B.;
RT "Sorting of proteins into multivesicular bodies: ubiquitin-dependent and
RT -independent targeting.";
RL EMBO J. 20:5176-5186(2001).
RN [9]
RP SUBCELLULAR LOCATION, AND ROLE OF UBIQUITINATION.
RX PubMed=11788821; DOI=10.1038/ncb743;
RA Reggiori F., Pelham H.R.B.;
RT "A transmembrane ubiquitin ligase required to sort membrane proteins into
RT multivesicular bodies.";
RL Nat. Cell Biol. 4:117-123(2002).
RN [10]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [11]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [12]
RP FUNCTION.
RX PubMed=15342119; DOI=10.1016/j.bbagen.2004.06.004;
RA Lichko L., Kulakovskaya T., Kulaev I.;
RT "Inactivation of endopolyphosphatase gene PPN1 results in inhibition of
RT expression of exopolyphosphatase PPX1 and high-molecular-mass
RT exopolyphosphatase not encoded by PPX1 in Saccharomyces cerevisiae.";
RL Biochim. Biophys. Acta 1674:98-102(2004).
RN [13]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=15170373; DOI=10.1023/b:biry.0000026193.44046.29;
RA Andreeva N.A., Kulakovskaya T.V., Kulaev I.S.;
RT "Purification and properties of exopolyphosphatase from the cytosol of
RT Saccharomyces cerevisiae not encoded by the PPX1 gene.";
RL Biochemistry (Mosc.) 69:387-393(2004).
RN [14]
RP SUBCELLULAR LOCATION, AND ROLE OF UBIQUITINATION.
RX PubMed=15086787; DOI=10.1111/j.1398-9219.2004.00183.x;
RA Morvan J., Froissard M., Haguenauer-Tsapis R., Urban-Grimal D.;
RT "The ubiquitin ligase Rsp5p is required for modification and sorting of
RT membrane proteins into multivesicular bodies.";
RL Traffic 5:383-392(2004).
RN [15]
RP COFACTOR.
RX PubMed=25742176; DOI=10.1371/journal.pone.0119594;
RA Andreeva N., Trilisenko L., Eldarov M., Kulakovskaya T.;
RT "Polyphosphatase PPN1 of Saccharomyces cerevisiae: switching of
RT exopolyphosphatase and endopolyphosphatase activities.";
RL PLoS ONE 10:E0119594-E0119594(2015).
RN [16]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX DOI=10.4236/aer.2016.44013;
RA Andreeva N., Trilisenko L., Eldarov M., Kulakovskaya T.;
RT "Polyphosphatase PPN1 of Saccharomyces cerevisiae is a deoxyadenosine
RT triphosphate phosphohydrolase.";
RL Adv. Enzyme Res. 4:144-151(2016).
CC -!- FUNCTION: Catalyzes the hydrolysis of inorganic polyphosphate (polyP)
CC chains of many hundreds of phosphate residues into shorter lengths both
CC by cleaving phosphate from the chain end and by fragmenting long-chain
CC polymers into shorter ones. The limited digestion products are 1 and 3
CC P(i) residues (PubMed:11102525, PubMed:11447286, PubMed:15170373,
CC PubMed:15342119, PubMed:15792812, PubMed:8900207, Ref.16). Also
CC releases phosphate from dATP. dATP phosphohydrolase activity is about
CC 7-fold lower than the exopolyphosphatase activity (Ref.16).
CC {ECO:0000269|PubMed:11102525, ECO:0000269|PubMed:11447286,
CC ECO:0000269|PubMed:15170373, ECO:0000269|PubMed:15342119,
CC ECO:0000269|PubMed:15792812, ECO:0000269|PubMed:8900207,
CC ECO:0000269|Ref.16}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[phosphate](n+1) + n H2O = n H(+) + (n+1) phosphate;
CC Xref=Rhea:RHEA:22452, Rhea:RHEA-COMP:14280, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16838, ChEBI:CHEBI:43474; EC=3.6.1.10;
CC Evidence={ECO:0000269|PubMed:15792812};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[phosphate](n) + H2O = [phosphate](n-1) + H(+) + phosphate;
CC Xref=Rhea:RHEA:21528, Rhea:RHEA-COMP:9859, Rhea:RHEA-COMP:14279,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16838,
CC ChEBI:CHEBI:43474; EC=3.6.1.11;
CC Evidence={ECO:0000269|PubMed:15170373};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dATP + H2O = dADP + H(+) + phosphate; Xref=Rhea:RHEA:51908,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57667, ChEBI:CHEBI:61404; Evidence={ECO:0000269|Ref.16};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:8900207};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:8900207};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|Ref.16};
CC Note=Divalent metal cations. Exopolyphosphatase activity is predominant
CC in the presence of Co(2+), while endopolyphosphatase activity is
CC predominant in the presence of Mg(2+) (PubMed:8900207,
CC PubMed:25742176). Co(2+) is more effective than Mn(2+) for dATP
CC phosphohydrolase activity (Ref.16). {ECO:0000269|PubMed:25742176,
CC ECO:0000269|PubMed:8900207, ECO:0000269|Ref.16};
CC -!- ACTIVITY REGULATION: Inhibited by heparin and EDTA.
CC {ECO:0000269|PubMed:15170373}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=185 nM for polyP(750) {ECO:0000269|PubMed:8900207};
CC KM=3.5 uM for polyP(208) {ECO:0000269|PubMed:15170373};
CC KM=75 uM for polyP(15) {ECO:0000269|PubMed:15170373};
CC KM=1100 uM for polyP(3) {ECO:0000269|PubMed:15170373};
CC KM=0.88 mM for dATP {ECO:0000269|Ref.16};
CC pH dependence:
CC Optimum pH is about 7.5. {ECO:0000269|PubMed:8900207};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:15792812}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:11566881,
CC ECO:0000269|PubMed:11788821, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:15086787, ECO:0000269|PubMed:8900207}; Single-pass
CC type II membrane protein {ECO:0000269|PubMed:11566881,
CC ECO:0000269|PubMed:11788821, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:15086787, ECO:0000269|PubMed:8900207}. Cytoplasm
CC {ECO:0000269|PubMed:17009950}. Note=The cytoplasmic form appears in the
CC cytosol during the transition of cells from stationary growth phase to
CC new budding on glucose addition and phosphate excess.
CC {ECO:0000269|PubMed:17009950}.
CC -!- DOMAIN: The transmembrane domain contains polar residues that mediate
CC the recognition by TUL1. {ECO:0000269|PubMed:11566881}.
CC -!- PTM: Processing by proteases in the vacuole is required for activation.
CC {ECO:0000305|PubMed:11447286}.
CC -!- PTM: Ubiquitinated. Ubiquitination mediates sorting into internal
CC vesicles in late endosomes. TUL1 and RSP5 are required for
CC ubiquitination. Other cytoplasmic Lys residues than Lys-6 may also be
CC ubiquitinated. {ECO:0000269|PubMed:11566881}.
CC -!- PTM: N-glycosylated (Probable). N-glycosylation is essential for the
CC protease-mediated maturation. {ECO:0000269|PubMed:15792812,
CC ECO:0000305}.
CC -!- MISCELLANEOUS: Inactivation of PPN1 leads to the inhibition of
CC expression of both exopolyphosphatase PPX1 and high-molecular-mass
CC exopolyphosphatase not encoded by PPX1.
CC -!- MISCELLANEOUS: Present with 319 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the endopolyphosphatase PPN1 family.
CC {ECO:0000305}.
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DR EMBL; AF322107; AAG37278.1; -; Genomic_DNA.
DR EMBL; U33007; AAB64872.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12287.1; -; Genomic_DNA.
DR PIR; S69731; S69731.
DR RefSeq; NP_010740.3; NM_001180760.3.
DR AlphaFoldDB; Q04119; -.
DR SMR; Q04119; -.
DR BioGRID; 32507; 69.
DR DIP; DIP-2584N; -.
DR IntAct; Q04119; 13.
DR MINT; Q04119; -.
DR STRING; 4932.YDR452W; -.
DR iPTMnet; Q04119; -.
DR MaxQB; Q04119; -.
DR PaxDb; Q04119; -.
DR PRIDE; Q04119; -.
DR EnsemblFungi; YDR452W_mRNA; YDR452W; YDR452W.
DR GeneID; 852063; -.
DR KEGG; sce:YDR452W; -.
DR SGD; S000002860; PPN1.
DR VEuPathDB; FungiDB:YDR452W; -.
DR eggNOG; KOG3770; Eukaryota.
DR GeneTree; ENSGT00950000183182; -.
DR HOGENOM; CLU_013424_1_0_1; -.
DR InParanoid; Q04119; -.
DR OMA; MKAILMG; -.
DR BioCyc; YEAST:G3O-29983-MON; -.
DR BRENDA; 3.6.1.10; 984.
DR BRENDA; 3.6.1.11; 984.
DR PRO; PR:Q04119; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q04119; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IMP:SGD.
DR GO; GO:0000298; F:endopolyphosphatase activity; IDA:SGD.
DR GO; GO:0004309; F:exopolyphosphatase activity; IDA:SGD.
DR GO; GO:0016787; F:hydrolase activity; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006798; P:polyphosphate catabolic process; IDA:SGD.
DR GO; GO:0006797; P:polyphosphate metabolic process; IDA:SGD.
DR CDD; cd00842; MPP_ASMase; 1.
DR InterPro; IPR041805; ASMase/PPN1_MPP.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR012358; EndopolyPtase_N1.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR Pfam; PF00149; Metallophos; 1.
DR PIRSF; PIRSF027093; EndopolyPtase_N1; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Glycoprotein; Hydrolase;
KW Isopeptide bond; Membrane; Metal-binding; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix; Ubl conjugation;
KW Vacuole; Zymogen.
FT PROPEP 1..83
FT /note="Removed in mature form"
FT /evidence="ECO:0000269|PubMed:15792812"
FT /id="PRO_0000022089"
FT CHAIN 84..384
FT /note="Endopolyphosphatase"
FT /id="PRO_0000022090"
FT PROPEP 385..674
FT /note="Removed in mature form"
FT /evidence="ECO:0000269|PubMed:15792812"
FT /id="PRO_0000022091"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 22..42
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..674
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT REGION 384..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 505
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 511
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CROSSLNK 6
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000305|PubMed:11566881"
FT MUTAGEN 6
FT /note="K->R,G: Causes accumulation in vacuoles and
FT abolishes sorting into internal vesicles in late
FT endosomes."
FT /evidence="ECO:0000269|PubMed:11566881"
FT MUTAGEN 11
FT /note="N->A: Abolishes enzyme activity; when associated
FT with A-505 and A-511."
FT /evidence="ECO:0000269|PubMed:15792812"
FT MUTAGEN 505
FT /note="N->A: Abolishes enzyme activity; when associated
FT with A-11 and A-511."
FT /evidence="ECO:0000269|PubMed:15792812"
FT MUTAGEN 511
FT /note="N->A: Abolishes enzyme activity; when associated
FT with A-11 and A-505."
FT /evidence="ECO:0000269|PubMed:15792812"
SQ SEQUENCE 674 AA; 78344 MW; EEC78BC7568098B3 CRC64;
MVVVGKSEVR NVSMSRPKKK SLIAILSTCV LFFLVFIIGA KFQYVSVFSK FLDDRGDNES
LQLLNDIEFT RLGLTPREPV IIKDVKTGKE RKLHGRFLHI TDIHPDPYYV EGSSIDAVCH
TGKPSKKKDV APKFGKAMSG CDSPVILMEE TLRWIKENLR DKIDFVIWTG DNIRHDNDRK
HPRTEAQIFD MNNIVADKMT ELFSAGNEED PRDFDVSVIP SLGNNDVFPH NMFALGPTLQ
TREYYRIWKN FVPQQQQRTF DRSASFLTEV IPGKLAVLSI NTLYLFKANP LVDNCNSKKE
PGYQLLLWFG YVLEELRSRG MKVWLSGHVP PIAKNFDQSC YDKFTLWTHE YRDIIIGGLY
GHMNIDHFIP TDGKKARKSL LKAMEQSTRV QQGEDSNEED EETELNRILD HAMAAKEVFL
MGAKPSNKEA YMNTVRDTYY RKVWNKLERV DEKNVENEKK KKEKKDKKKK KPITRKELIE
RYSIVNIGGS VIPTFNPSFR IWEYNITDIV NDSNFAVSEY KPWDEFFESL NKIMEDSLLE
DEMDSSNIEV GINREKMGEK KNKKKKKNDK TMPIEMPDKY ELGPAYVPQL FTPTRFVQFY
ADLEKINQEL HNSFVESKDI FRYEIEYTSD EKPYSMDSLT VGSYLDLAGR LYENKPAWEK
YVEWSFASSG YKDD
