VATE_YEAST
ID VATE_YEAST Reviewed; 233 AA.
AC P22203; D6W328;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=V-type proton ATPase subunit E;
DE Short=V-ATPase subunit E;
DE AltName: Full=V-ATPase 27 kDa subunit;
DE AltName: Full=Vacuolar proton pump subunit E;
GN Name=VMA4 {ECO:0000303|PubMed:9660816}; Synonyms=VAT5;
GN OrderedLocusNames=YOR332W; ORFNames=O6241;
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], FUNCTION, AND SUBUNIT.
RX PubMed=2145285; DOI=10.1016/s0021-9258(17)44787-9;
RA Foury F.;
RT "The 31-kDa polypeptide is an essential subunit of the vacuolar ATPase in
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 265:18554-18560(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8896263;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<999::aid-yea976>3.0.co;2-e;
RA Parle-McDermott A.G., Hand N.J., Goulding S.E., Wolfe K.H.;
RT "Sequence of 29 kb around the PDR10 locus on the right arm of Saccharomyces
RT cerevisiae chromosome XV: similarity to part of chromosome I.";
RL Yeast 12:999-1004(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [4]
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 [5]
RP PROTEIN SEQUENCE OF 2-26; 39-63; 69-77; 86-131; 145-158; 167-181 AND
RP 197-227, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RA Bienvenut W.V., Peters C.;
RL Submitted (MAY-2005) to UniProtKB.
RN [6]
RP PROTEIN SEQUENCE OF 209-219, FUNCTION, AND SUBUNIT.
RX PubMed=8416931; DOI=10.1016/s0021-9258(18)54138-7;
RA Ho M.N., Hill K.J., Lindorfer M.A., Stevens T.H.;
RT "Isolation of vacuolar membrane H(+)-ATPase-deficient yeast mutants; the
RT VMA5 and VMA4 genes are essential for assembly and activity of the vacuolar
RT H(+)-ATPase.";
RL J. Biol. Chem. 268:221-227(1993).
RN [7]
RP HOMODIMERIZATION.
RX PubMed=8626613; DOI=10.1074/jbc.271.17.10397;
RA Tomashek J.J., Sonnenburg J.L., Artimovich J.M., Klionsky D.J.;
RT "Resolution of subunit interactions and cytoplasmic subcomplexes of the
RT yeast vacuolar proton-translocating ATPase.";
RL J. Biol. Chem. 271:10397-10404(1996).
RN [8]
RP MUTAGENESIS OF ASP-145.
RX PubMed=9660816; DOI=10.1074/jbc.273.29.18470;
RA Zhang J.W., Parra K.J., Liu J., Kane P.M.;
RT "Characterization of a temperature-sensitive yeast vacuolar ATPase mutant
RT with defects in actin distribution and bud morphology.";
RL J. Biol. Chem. 273:18470-18480(1998).
RN [9]
RP INTERACTION WITH RAV1 AND RAV2.
RX PubMed=11283612; DOI=10.1038/35070067;
RA Seol J.H., Shevchenko A., Shevchenko A., Deshaies R.J.;
RT "Skp1 forms multiple protein complexes, including RAVE, a regulator of V-
RT ATPase assembly.";
RL Nat. Cell Biol. 3:384-391(2001).
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 INTERACTION WITH VMA5 AND VMA10.
RX PubMed=15751969; DOI=10.1021/bi048402x;
RA Jones R.P.O., Durose L.J., Findlay J.B.C., Harrison M.A.;
RT "Defined sites of interaction between subunits E (Vma4p), C (Vma5p), and G
RT (Vma10p) within the stator structure of the vacuolar H(+)-ATPase.";
RL Biochemistry 44:3933-3941(2005).
RN [13]
RP ERRATUM OF PUBMED:15751969.
RX DOI=10.1021/bi058022r;
RA Jones R.P.O., Durose L.J., Findlay J.B.C., Harrison M.A.;
RL Biochemistry 44:11924-11924(2005).
RN [14]
RP MUTAGENESIS OF SER-2; THR-6; THR-9; SER-78; TYR-160; THR-202; LYS-230 AND
RP ASP-233.
RX PubMed=15718227; DOI=10.1074/jbc.m412567200;
RA Owegi M.A., Carenbauer A.L., Wick N.M., Brown J.F., Terhune K.L.,
RA Bilbo S.A., Weaver R.S., Shircliff R., Newcomb N., Parra-Belky K.J.;
RT "Mutational analysis of the stator subunit E of the yeast V-ATPase.";
RL J. Biol. Chem. 280:18393-18402(2005).
RN [15]
RP IDENTIFICATION IN THE V-ATPASE COMPLEX, MASS SPECTROMETRY, AND CLEAVAGE OF
RP INITIATOR METHIONINE.
RX PubMed=18055462; DOI=10.1074/jbc.m707924200;
RA Kitagawa N., Mazon H., Heck A.J.R., Wilkens S.;
RT "Stoichiometry of the peripheral stalk subunits E and G of yeast V1-ATPase
RT determined by mass spectrometry.";
RL J. Biol. Chem. 283:3329-3337(2008).
RN [16]
RP 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 ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [18] {ECO:0007744|PDB:3J9T, ECO:0007744|PDB:3J9U, ECO:0007744|PDB:3J9V}
RP STRUCTURE BY ELECTRON MICROSCOPY (6.90 ANGSTROMS), AND IDENTIFICATION IN
RP THE V-ATPASE COMPLEX.
RX PubMed=25971514; DOI=10.1038/nature14365;
RA Zhao J., Benlekbir S., Rubinstein J.L.;
RT "Electron cryomicroscopy observation of rotational states in a eukaryotic
RT V-ATPase.";
RL Nature 521:241-245(2015).
RN [19] {ECO:0007744|PDB:5BW9, ECO:0007744|PDB:5D80}
RP X-RAY CRYSTALLOGRAPHY (6.20 ANGSTROMS), AND IDENTIFICATION IN THE V-ATPASE
RP COMPLEX.
RX PubMed=27295975; DOI=10.15252/embj.201593447;
RA Oot R.A., Kane P.M., Berry E.A., Wilkens S.;
RT "Crystal structure of yeast V1-ATPase in the autoinhibited state.";
RL EMBO J. 35:1694-1706(2016).
CC -!- FUNCTION: Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase),
CC a multisubunit enzyme composed of a peripheral complex (V1) that
CC hydrolyzes ATP and a membrane integral complex (V0) that translocates
CC protons (PubMed:8416931). V-ATPase is responsible for acidifying and
CC maintaining the pH of intracellular compartments (PubMed:8416931,
CC PubMed:2145285). {ECO:0000269|PubMed:2145285,
CC ECO:0000269|PubMed:8416931}.
CC -!- SUBUNIT: Homodimer (PubMed:8626613). V-ATPase is a heteromultimeric
CC enzyme composed of a peripheral catalytic V1 complex (components A to
CC H) attached to an integral membrane V0 proton pore complex (components:
CC a, c, c', c'', d, e, f and VOA1) (PubMed:2145285, PubMed:8416931,
CC PubMed:25971514, PubMed:18055462, PubMed:27295975). Interacts with
CC VMA5; the interaction is direct (PubMed:15751969). Interacts with
CC VMA10; the interaction is direct (PubMed:15751969). Interacts with RAV1
CC and RAV2 components of the RAVE complex, which are essential for the
CC stability and assembly of V-ATPase (PubMed:11283612).
CC {ECO:0000269|PubMed:11283612, ECO:0000269|PubMed:15751969,
CC ECO:0000269|PubMed:18055462, ECO:0000269|PubMed:2145285,
CC ECO:0000269|PubMed:25971514, ECO:0000269|PubMed:27295975,
CC ECO:0000269|PubMed:8416931, ECO:0000269|PubMed:8626613}.
CC -!- INTERACTION:
CC P22203; P47104: RAV1; NbExp=3; IntAct=EBI-20268, EBI-25471;
CC P22203; P48836: VMA10; NbExp=4; IntAct=EBI-20268, EBI-20276;
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:14562095};
CC Peripheral membrane protein {ECO:0000269|PubMed:14562095}; Cytoplasmic
CC side {ECO:0000305}.
CC -!- MASS SPECTROMETRY: Mass=26387.3; Mass_error=4.5; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:18055462};
CC -!- MISCELLANEOUS: Present with 16134 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the V-ATPase E subunit family. {ECO:0000305}.
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DR EMBL; M60663; AAA35209.1; -; Genomic_DNA.
DR EMBL; Z49821; CAA89978.1; -; Genomic_DNA.
DR EMBL; Z75239; CAA99654.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11094.1; -; Genomic_DNA.
DR PIR; S62063; S62063.
DR RefSeq; NP_014977.3; NM_001183752.3.
DR PDB; 2KZ9; NMR; -; A=1-69.
DR PDB; 3J9T; EM; 6.90 A; G/I/K=1-233.
DR PDB; 3J9U; EM; 7.60 A; G/I/K=1-233.
DR PDB; 3J9V; EM; 8.30 A; G/I/K=1-233.
DR PDB; 4DL0; X-ray; 2.90 A; E/J=1-233.
DR PDB; 4EFA; X-ray; 2.82 A; E=1-233.
DR PDB; 5BW9; X-ray; 7.00 A; I/K/M/i/k/m=1-233.
DR PDB; 5D80; X-ray; 6.20 A; I/K/M/i/k/m=1-233.
DR PDB; 5VOX; EM; 6.80 A; G/I/K=1-233.
DR PDB; 5VOY; EM; 7.90 A; G/I/K=1-233.
DR PDB; 5VOZ; EM; 7.60 A; G/I/K=1-233.
DR PDB; 6O7V; EM; 6.60 A; G/I/K=1-233.
DR PDB; 6O7W; EM; 7.00 A; G/I/K=1-233.
DR PDB; 6O7X; EM; 8.70 A; G/I/K=1-233.
DR PDB; 7FDA; EM; 4.20 A; G/I/K=1-233.
DR PDB; 7FDB; EM; 4.80 A; G/I/K=1-233.
DR PDB; 7FDC; EM; 6.60 A; G/I/K=1-233.
DR PDB; 7FDE; EM; 3.80 A; G/I/K=1-233.
DR PDBsum; 2KZ9; -.
DR PDBsum; 3J9T; -.
DR PDBsum; 3J9U; -.
DR PDBsum; 3J9V; -.
DR PDBsum; 4DL0; -.
DR PDBsum; 4EFA; -.
DR PDBsum; 5BW9; -.
DR PDBsum; 5D80; -.
DR PDBsum; 5VOX; -.
DR PDBsum; 5VOY; -.
DR PDBsum; 5VOZ; -.
DR PDBsum; 6O7V; -.
DR PDBsum; 6O7W; -.
DR PDBsum; 6O7X; -.
DR PDBsum; 7FDA; -.
DR PDBsum; 7FDB; -.
DR PDBsum; 7FDC; -.
DR PDBsum; 7FDE; -.
DR AlphaFoldDB; P22203; -.
DR BMRB; P22203; -.
DR SMR; P22203; -.
DR BioGRID; 34716; 101.
DR ComplexPortal; CPX-1192; Vacuolar proton translocating ATPase complex, Golgi variant.
DR ComplexPortal; CPX-1193; Vacuolar proton translocating ATPase complex, vacuole variant.
DR DIP; DIP-4595N; -.
DR IntAct; P22203; 26.
DR STRING; 4932.YOR332W; -.
DR TCDB; 3.A.2.2.3; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR iPTMnet; P22203; -.
DR SWISS-2DPAGE; P22203; -.
DR MaxQB; P22203; -.
DR PaxDb; P22203; -.
DR PRIDE; P22203; -.
DR TopDownProteomics; P22203; -.
DR EnsemblFungi; YOR332W_mRNA; YOR332W; YOR332W.
DR GeneID; 854509; -.
DR KEGG; sce:YOR332W; -.
DR SGD; S000005859; VMA4.
DR VEuPathDB; FungiDB:YOR332W; -.
DR eggNOG; KOG1664; Eukaryota.
DR GeneTree; ENSGT00390000002730; -.
DR HOGENOM; CLU_073641_0_0_1; -.
DR InParanoid; P22203; -.
DR OMA; AIDTQYE; -.
DR BioCyc; YEAST:G3O-33808-MON; -.
DR Reactome; R-SCE-1222556; ROS and RNS production in phagocytes.
DR Reactome; R-SCE-77387; Insulin receptor recycling.
DR Reactome; R-SCE-917977; Transferrin endocytosis and recycling.
DR Reactome; R-SCE-9639288; Amino acids regulate mTORC1.
DR PRO; PR:P22203; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P22203; protein.
DR GO; GO:0010008; C:endosome membrane; IC:ComplexPortal.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR GO; GO:0000139; C:Golgi membrane; IC:ComplexPortal.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0033176; C:proton-transporting V-type ATPase complex; IPI:ComplexPortal.
DR GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IPI:ComplexPortal.
DR GO; GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; IDA:UniProtKB.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IBA:GO_Central.
DR GO; GO:0048388; P:endosomal lumen acidification; IC:ComplexPortal.
DR GO; GO:0061795; P:Golgi lumen acidification; IC:ComplexPortal.
DR GO; GO:1902600; P:proton transmembrane transport; IDA:ComplexPortal.
DR GO; GO:0007035; P:vacuolar acidification; TAS:SGD.
DR Gene3D; 3.30.2320.30; -; 1.
DR HAMAP; MF_00311; ATP_synth_E_arch; 1.
DR InterPro; IPR038495; ATPase_E_C.
DR InterPro; IPR002842; ATPase_V1_Esu.
DR PANTHER; PTHR45715; PTHR45715; 1.
DR Pfam; PF01991; vATP-synt_E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Coiled coil; Direct protein sequencing;
KW Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW Transport; Vacuole.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:18055462, ECO:0000269|Ref.5,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..233
FT /note="V-type proton ATPase subunit E"
FT /id="PRO_0000117310"
FT REGION 8..20
FT /note="Interaction with VMA5"
FT /evidence="ECO:0000269|PubMed:15751969"
FT REGION 19..38
FT /note="Interaction with VMA10"
FT /evidence="ECO:0000269|PubMed:15751969"
FT COILED 15..45
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:22814378"
FT MUTAGEN 2
FT /note="S->A: Reduces ATPase activity by 11%."
FT /evidence="ECO:0000269|PubMed:15718227"
FT MUTAGEN 6
FT /note="T->A: Reduces ATPase activity by 73%."
FT /evidence="ECO:0000269|PubMed:15718227"
FT MUTAGEN 9
FT /note="T->A: Increases ATPase activity 1.4-fold."
FT /evidence="ECO:0000269|PubMed:15718227"
FT MUTAGEN 78
FT /note="S->A: Reduces ATPase activity by 88%. Prevents
FT assembly of V1 subunits at the membrane."
FT /evidence="ECO:0000269|PubMed:15718227"
FT MUTAGEN 145
FT /note="D->G: In VMA4-1; is rapidly degraded at 37 degrees
FT Celsius."
FT /evidence="ECO:0000269|PubMed:9660816"
FT MUTAGEN 160
FT /note="Y->A: Reduces ATPase activity by 22%."
FT /evidence="ECO:0000269|PubMed:15718227"
FT MUTAGEN 202
FT /note="T->A: Increases ATPase activity 2.1-fold by
FT increasing Vmax for ATP hydrolysis 2-fold. Reduces ATPase
FT activity by 90% and produces structurally aberrant V-ATPase
FT complexes; when associated with A-233."
FT /evidence="ECO:0000269|PubMed:15718227"
FT MUTAGEN 230
FT /note="K->A: Increases ATPase activity 1.3-fold."
FT /evidence="ECO:0000269|PubMed:15718227"
FT MUTAGEN 233
FT /note="D->A: Reduces ATPase activity by 74%. Reduces ATPase
FT activity by 90% and produces structurally aberrant V-ATPase
FT complexes; when associated with A-202."
FT /evidence="ECO:0000269|PubMed:15718227"
FT CONFLICT 97..98
FT /note="DG -> ER (in Ref. 1; AAA35209)"
FT /evidence="ECO:0000305"
FT HELIX 10..111
FT /evidence="ECO:0007829|PDB:4EFA"
FT HELIX 114..132
FT /evidence="ECO:0007829|PDB:4EFA"
FT STRAND 135..141
FT /evidence="ECO:0007829|PDB:4EFA"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:4EFA"
FT HELIX 146..149
FT /evidence="ECO:0007829|PDB:4EFA"
FT HELIX 153..163
FT /evidence="ECO:0007829|PDB:4EFA"
FT TURN 164..166
FT /evidence="ECO:0007829|PDB:4EFA"
FT STRAND 171..174
FT /evidence="ECO:0007829|PDB:4EFA"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:4EFA"
FT STRAND 185..191
FT /evidence="ECO:0007829|PDB:4EFA"
FT STRAND 198..202
FT /evidence="ECO:0007829|PDB:4EFA"
FT HELIX 203..222
FT /evidence="ECO:0007829|PDB:4EFA"
SQ SEQUENCE 233 AA; 26471 MW; 7AC5169FF7E5A39C CRC64;
MSSAITALTP NQVNDELNKM QAFIRKEAEE KAKEIQLKAD QEYEIEKTNI VRNETNNIDG
NFKSKLKKAM LSQQITKSTI ANKMRLKVLS AREQSLDGIF EETKEKLSGI ANNRDEYKPI
LQSLIVEALL KLLEPKAIVK ALERDVDLIE SMKDDIMREY GEKAQRAPLE EIVISNDYLN
KDLVSGGVVV SNASDKIEIN NTLEERLKLL SEEALPAIRL ELYGPSKTRK FFD
