CHS5_YEAST
ID CHS5_YEAST Reviewed; 671 AA.
AC Q12114; D6VYX2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Chitin biosynthesis protein CHS5;
DE AltName: Full=Protein CAL3;
GN Name=CHS5; Synonyms=CAL3; OrderedLocusNames=YLR330W; ORFNames=L8543.18;
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], AND FUNCTION.
RC STRAIN=S288c / GRF88;
RX PubMed=9111317; DOI=10.1128/mcb.17.5.2485;
RA Santos B., Duran A., Valdivieso M.H.;
RT "CHS5, a gene involved in chitin synthesis and mating in Saccharomyces
RT cerevisiae.";
RL Mol. Cell. Biol. 17:2485-2496(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(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 FUNCTION.
RX PubMed=8197125; DOI=10.1073/pnas.91.11.4727;
RA Choi W.-J., Sburlati A., Cabib E.;
RT "Chitin synthase 3 from yeast has zymogenic properties that depend on both
RT the CAL1 and the CAL3 genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:4727-4730(1994).
RN [5]
RP DOMAIN FIBRONECTIN TYPE-III.
RX PubMed=8994808; DOI=10.1016/s0960-9822(02)70765-3;
RA Bateman A., Chothia C.;
RT "Fibronectin type III domains in yeast detected by a hidden Markov model.";
RL Curr. Biol. 6:1544-1546(1996).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=9008706; DOI=10.1083/jcb.136.1.95;
RA Santos B., Snyder M.;
RT "Targeting of chitin synthase 3 to polarized growth sites in yeast requires
RT Chs5p and Myo2p.";
RL J. Cell Biol. 136:95-110(1997).
RN [7]
RP FUNCTION.
RX PubMed=12912901; DOI=10.1128/ec.2.4.821-825.2003;
RA Santos B., Snyder M.;
RT "Specific protein targeting during cell differentiation: polarized
RT localization of Fus1p during mating depends on Chs5p in Saccharomyces
RT cerevisiae.";
RL Eukaryot. Cell 2:821-825(2003).
RN [8]
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 [9]
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 [10]
RP FUNCTION.
RX PubMed=15715908; DOI=10.1186/1471-2156-6-8;
RA Lesage G., Shapiro J., Specht C.A., Sdicu A.-M., Menard P., Hussein S.,
RA Tong A.H.Y., Boone C., Bussey H.;
RT "An interactional network of genes involved in chitin synthesis in
RT Saccharomyces cerevisiae.";
RL BMC Genet. 6:8-8(2005).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ARF1; BCH1; BCH2; BUD7;
RP CHS3 AND CHS6, AND DOMAIN.
RX PubMed=16498409; DOI=10.1038/sj.emboj.7601007;
RA Trautwein M., Schindler C., Gauss R., Dengjel J., Hartmann E., Spang A.;
RT "Arf1p, Chs5p and the ChAPs are required for export of specialized cargo
RT from the Golgi.";
RL EMBO J. 25:943-954(2006).
RN [12]
RP FUNCTION.
RX PubMed=16818716; DOI=10.1083/jcb.200602049;
RA Lam K.K.Y., Davey M., Sun B., Roth A.F., Davis N.G., Conibear E.;
RT "Palmitoylation by the DHHC protein Pfa4 regulates the ER exit of Chs3.";
RL J. Cell Biol. 174:19-25(2006).
RN [13]
RP FUNCTION, IDENTIFICATION IN THE CHS5/6 COMPLEX, INTERACTION WITH ARF1, AND
RP SUBCELLULAR LOCATION.
RX PubMed=17000877; DOI=10.1083/jcb.200605106;
RA Wang C.-W., Hamamoto S., Orci L., Schekman R.;
RT "Exomer: a coat complex for transport of select membrane proteins from the
RT trans-Golgi network to the plasma membrane in yeast.";
RL J. Cell Biol. 174:973-983(2006).
RN [14]
RP FUNCTION, IDENTIFICATION IN THE CHS5/6 COMPLEX, AND INTERACTION WITH CHS3.
RX PubMed=16855022; DOI=10.1091/mbc.e06-03-0210;
RA Sanchatjate S., Schekman R.;
RT "Chs5/6 complex: a multiprotein complex that interacts with and conveys
RT chitin synthase III from the trans-Golgi network to the cell surface.";
RL Mol. Biol. Cell 17:4157-4166(2006).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-590, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338; SER-362; SER-573 AND
RP SER-590, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-305; SER-338; SER-365;
RP SER-383; SER-384; SER-579 AND SER-590, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [18]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-584, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [19]
RP DISRUPTION PHENOTYPE.
RX PubMed=28346351; DOI=10.3390/ijms18040702;
RA Gohlke S., Muthukrishnan S., Merzendorfer H.;
RT "In Vitro and In Vivo Studies on the Structural Organization of Chs3 from
RT Saccharomyces cerevisiae.";
RL Int. J. Mol. Sci. 18:0-0(2017).
CC -!- FUNCTION: Component of the CHS5/6 complex which mediates export of
CC specific cargo proteins, including chitin synthase CHS3. Also involved
CC in targeting FUS1 to sites of polarized growth.
CC {ECO:0000269|PubMed:12912901, ECO:0000269|PubMed:15715908,
CC ECO:0000269|PubMed:16498409, ECO:0000269|PubMed:16818716,
CC ECO:0000269|PubMed:16855022, ECO:0000269|PubMed:17000877,
CC ECO:0000269|PubMed:8197125, ECO:0000269|PubMed:9111317}.
CC -!- SUBUNIT: Component of the CHS5/6 complex composed of the 4 CHAPS
CC proteins BCH1, BCH2, BUD7, and CHS6 as well as at least CHS5 and GTP-
CC bound ARF1. The complex interacts with the cargo protein CHS3.
CC {ECO:0000269|PubMed:16498409, ECO:0000269|PubMed:16855022,
CC ECO:0000269|PubMed:17000877}.
CC -!- INTERACTION:
CC Q12114; P11076: ARF1; NbExp=5; IntAct=EBI-4640, EBI-2816;
CC Q12114; Q05029: BCH1; NbExp=17; IntAct=EBI-4640, EBI-27508;
CC Q12114; P36122: BCH2; NbExp=7; IntAct=EBI-4640, EBI-26374;
CC Q12114; Q08754: BUD7; NbExp=10; IntAct=EBI-4640, EBI-32770;
CC Q12114; P40955: CHS6; NbExp=17; IntAct=EBI-4640, EBI-4649;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16498409,
CC ECO:0000269|PubMed:17000877, ECO:0000269|PubMed:9008706}; Peripheral
CC membrane protein {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:16498409, ECO:0000269|PubMed:17000877,
CC ECO:0000269|PubMed:9008706}. Note=Trans-Golgi network location requires
CC interaction with myristoylated GTP-bound ARF1 for the recruitment to
CC the membranes.
CC -!- DISRUPTION PHENOTYPE: Abolishes CHS3 localization to the bud neck and
CC plasma membrane, with increased protein localization to intracellular
CC vesicles. {ECO:0000269|PubMed:28346351}.
CC -!- MISCELLANEOUS: Present with 172 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the CHS5 family. {ECO:0000305}.
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DR EMBL; Z49198; CAA89059.1; -; Genomic_DNA.
DR EMBL; U20618; AAB64526.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09638.1; -; Genomic_DNA.
DR PIR; S53407; S53407.
DR RefSeq; NP_013434.1; NM_001182219.1.
DR PDB; 4IN3; X-ray; 2.94 A; A/C=1-77.
DR PDB; 4WJW; X-ray; 2.59 A; A=1-77.
DR PDB; 4YG8; X-ray; 2.75 A; A=50-299.
DR PDBsum; 4IN3; -.
DR PDBsum; 4WJW; -.
DR PDBsum; 4YG8; -.
DR AlphaFoldDB; Q12114; -.
DR SMR; Q12114; -.
DR BioGRID; 31594; 459.
DR ComplexPortal; CPX-1719; Exomer complex.
DR DIP; DIP-8073N; -.
DR IntAct; Q12114; 42.
DR MINT; Q12114; -.
DR STRING; 4932.YLR330W; -.
DR iPTMnet; Q12114; -.
DR MaxQB; Q12114; -.
DR PaxDb; Q12114; -.
DR PRIDE; Q12114; -.
DR EnsemblFungi; YLR330W_mRNA; YLR330W; YLR330W.
DR GeneID; 851041; -.
DR KEGG; sce:YLR330W; -.
DR SGD; S000004322; CHS5.
DR VEuPathDB; FungiDB:YLR330W; -.
DR eggNOG; KOG1181; Eukaryota.
DR HOGENOM; CLU_019904_3_0_1; -.
DR InParanoid; Q12114; -.
DR OMA; TPYEFQL; -.
DR BioCyc; YEAST:YLR330W-MON; -.
DR PRO; PR:Q12114; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q12114; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0034044; C:exomer complex; IDA:SGD.
DR GO; GO:0043332; C:mating projection tip; HDA:SGD.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0031267; F:small GTPase binding; IPI:SGD.
DR GO; GO:0030476; P:ascospore wall assembly; IMP:SGD.
DR GO; GO:0006039; P:cell wall chitin catabolic process; IMP:SGD.
DR GO; GO:0000282; P:cellular bud site selection; IMP:SGD.
DR GO; GO:0000747; P:conjugation with cellular fusion; IMP:SGD.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; IMP:SGD.
DR GO; GO:0015031; P:protein transport; IC:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:SGD.
DR CDD; cd13945; Chs5_N; 1.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.40.50.10190; -; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR031673; Chs5_N.
DR InterPro; IPR031669; Fn3_2.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF16892; CHS5_N; 1.
DR Pfam; PF16893; fn3_2; 1.
DR SMART; SM00292; BRCT; 1.
DR SMART; SM00060; FN3; 1.
DR SUPFAM; SSF49265; SSF49265; 1.
DR SUPFAM; SSF52113; SSF52113; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS50853; FN3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Golgi apparatus; Isopeptide bond; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Transport; Ubl conjugation.
FT CHAIN 1..671
FT /note="Chitin biosynthesis protein CHS5"
FT /id="PRO_0000089661"
FT DOMAIN 78..168
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 166..262
FT /note="BRCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT REGION 280..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..304
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..464
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..482
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..525
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..571
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..600
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..671
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 305
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 338
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 573
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 579
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 590
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT CROSSLNK 584
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT STRAND 4..13
FT /evidence="ECO:0007829|PDB:4IN3"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:4WJW"
FT STRAND 27..31
FT /evidence="ECO:0007829|PDB:4IN3"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:4WJW"
FT STRAND 44..53
FT /evidence="ECO:0007829|PDB:4IN3"
FT HELIX 57..74
FT /evidence="ECO:0007829|PDB:4WJW"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:4YG8"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:4YG8"
FT STRAND 108..117
FT /evidence="ECO:0007829|PDB:4YG8"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:4YG8"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:4YG8"
FT STRAND 142..151
FT /evidence="ECO:0007829|PDB:4YG8"
FT STRAND 154..164
FT /evidence="ECO:0007829|PDB:4YG8"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:4YG8"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:4YG8"
FT HELIX 189..198
FT /evidence="ECO:0007829|PDB:4YG8"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:4YG8"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:4YG8"
FT HELIX 227..234
FT /evidence="ECO:0007829|PDB:4YG8"
FT HELIX 243..250
FT /evidence="ECO:0007829|PDB:4YG8"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:4YG8"
FT HELIX 266..272
FT /evidence="ECO:0007829|PDB:4YG8"
FT HELIX 279..284
FT /evidence="ECO:0007829|PDB:4YG8"
SQ SEQUENCE 671 AA; 73639 MW; FA92741B862814C2 CRC64;
MSSVDVLLTV GKLDASLALL TTQDHHVIEF PTVLLPENVK AGSIIKMQVS QNLEEEKKQR
NHFKSIQAKI LEKYGTHKPE SPVLKIVNVT QTSCVLAWDP LKLGSAKLKS LILYRKGIRS
MVIPNPFKVT TTKISGLSVD TPYEFQLKLI TTSGTLWSEK VILRTHKMTD MSGITVCLGP
LDPLKEISDL QISQCLSHIG ARPLQRHVAI DTTHFVCNDL DNEESNEELI RAKHNNIPIV
RPEWVRACEV EKRIVGVRGF YLDADQSILK NYTFPPVNEE ELSYSKENEP VAEVADENKM
PEDTTDVEQV ASPNDNESNP SEAKEQGEKS GHETAPVSPV EDPLHASTAL ENETTIETVN
PSVRSLKSEP VGTPNIEENK ADSSAEAVVE EPNEAVAESS PNEEATGQKS EDTDTHSNEQ
ADNGFVQTEE VAENNITTES AGENNEPADD AAMEFGRPEA EIETPEVNES IEDANEPAED
SNEPVEDSNK PVKDSNKPVE DSNKPVEDSN KPVEDSNKPV EDANEPVEDT SEPVEDAGEP
VQETNEFTTD IASPRHQEED IELEAEPKDA TESVAVEPSN EDVKPEEKGS EAEDDINNVS
KEAASGESTT HQKTEASASL ESSAVTEEQE TTEAEVNTDD VLSTKEAKKN TGNSNSNKKK
NKKNKKKGKK K
