ID   VPP2_YEAST              Reviewed;         890 AA.
AC   P37296; D6VZM9;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   27-MAR-2024, entry version 209.
DE   RecName: Full=V-type proton ATPase subunit a, Golgi isoform;
DE            Short=V-ATPase a 2 subunit;
DE   AltName: Full=Similar to VPH1 protein 1;
DE   AltName: Full=V-ATPase 101 kDa subunit;
DE   AltName: Full=V-ATPase subunit AC115;
DE   AltName: Full=Vacuolar proton translocating ATPase subunit a 2;
GN   Name=STV1; OrderedLocusNames=YMR054W; ORFNames=YM9796.07;
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, SUBUNIT, AND SUBCELLULAR
RP   LOCATION.
RC   STRAIN=ATCC 26109 / X2180;
RX   PubMed=7514599; DOI=10.1016/s0021-9258(17)36755-8;
RA   Manolson M.F., Wu B., Proteau D., Taillon B.E., Roberts B.T., Hoyt M.A.,
RA   Jones E.W.;
RT   "STV1 gene encodes functional homologue of 95-kDa yeast vacuolar H(+)-
RT   ATPase subunit Vph1p.";
RL   J. Biol. Chem. 269:14064-14074(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169872;
RA   Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA   Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA   Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA   Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL   Nature 387:90-93(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, AND SUBUNIT.
RX   PubMed=11278748; DOI=10.1074/jbc.m010790200;
RA   Kawasaki-Nishi S., Nishi T., Forgac M.;
RT   "Yeast V-ATPase complexes containing different isoforms of the 100-kDa a-
RT   subunit differ in coupling efficiency and in vivo dissociation.";
RL   J. Biol. Chem. 276:17941-17948(2001).
RN   [5]
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   [6]
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   [7]
RP   TOPOLOGY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 208353 / W303-1A;
RX   PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA   Kim H., Melen K., Oesterberg M., von Heijne G.;
RT   "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223, 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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223, AND IDENTIFICATION BY
RP   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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223 AND SER-228, AND
RP   IDENTIFICATION BY MASS 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   [11]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [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).
CC   -!- FUNCTION: Subunit of the V0 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:7514599, PubMed:11278748). V-ATPase is responsible for
CC       acidifying and maintaining the pH of intracellular compartments
CC       (PubMed:11278748, PubMed:7514599). Is present only in Golgi- and
CC       endosome-residing V-ATPase complexes; enzymes containing this subunit
CC       have a 4-fold lower ratio of proton transport to ATP hydrolysis than
CC       complexes containing the vacuolar isoform and do not dissociate V1 and
CC       V0 in response to glucose depletion (PubMed:11278748, PubMed:7514599).
CC       {ECO:0000269|PubMed:11278748, ECO:0000269|PubMed:7514599}.
CC   -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a peripheral
CC       catalytic V1 complex (components A to H) attached to an integral
CC       membrane V0 proton pore complex (components: a, c, c', c'', d, e, f and
CC       VOA1). {ECO:0000269|PubMed:11278748, ECO:0000269|PubMed:7514599}.
CC   -!- INTERACTION:
CC       P37296; P32366: VMA6; NbExp=2; IntAct=EBI-18479, EBI-20201;
CC   -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:7514599};
CC       Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane
CC       {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:7514599}; Multi-pass
CC       membrane protein {ECO:0000255}.
CC   -!- PTM: Glycosylated.
CC   -!- MISCELLANEOUS: Present with 1084 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the V-ATPase 116 kDa subunit family.
CC       {ECO:0000305}.
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DR   EMBL; U06465; AAA20596.1; -; Genomic_DNA.
DR   EMBL; Z49703; CAA89764.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA09953.1; -; Genomic_DNA.
DR   PIR; S54554; S54554.
DR   RefSeq; NP_013770.1; NM_001182552.1.
DR   PDB; 6O7U; EM; 3.10 A; a=1-890.
DR   PDB; 6O7V; EM; 6.60 A; a=1-890.
DR   PDB; 6O7W; EM; 7.00 A; a=1-890.
DR   PDB; 6O7X; EM; 8.70 A; a=1-890.
DR   PDBsum; 6O7U; -.
DR   PDBsum; 6O7V; -.
DR   PDBsum; 6O7W; -.
DR   PDBsum; 6O7X; -.
DR   AlphaFoldDB; P37296; -.
DR   BMRB; P37296; -.
DR   EMDB; EMD-0645; -.
DR   EMDB; EMD-0646; -.
DR   EMDB; EMD-0647; -.
DR   EMDB; EMD-0648; -.
DR   SMR; P37296; -.
DR   BioGRID; 35230; 152.
DR   ComplexPortal; CPX-1192; Vacuolar proton translocating ATPase complex, Golgi variant.
DR   DIP; DIP-4450N; -.
DR   IntAct; P37296; 2.
DR   MINT; P37296; -.
DR   STRING; 4932.YMR054W; -.
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; P37296; -.
DR   MaxQB; P37296; -.
DR   PaxDb; 4932-YMR054W; -.
DR   PeptideAtlas; P37296; -.
DR   EnsemblFungi; YMR054W_mRNA; YMR054W; YMR054W.
DR   GeneID; 855076; -.
DR   KEGG; sce:YMR054W; -.
DR   AGR; SGD:S000004658; -.
DR   SGD; S000004658; STV1.
DR   VEuPathDB; FungiDB:YMR054W; -.
DR   eggNOG; KOG2189; Eukaryota.
DR   GeneTree; ENSGT00950000182881; -.
DR   HOGENOM; CLU_005230_0_0_1; -.
DR   InParanoid; P37296; -.
DR   OMA; TYVQLYI; -.
DR   OrthoDB; 1967517at2759; -.
DR   BioCyc; YEAST:G3O-32759-MONOMER; -.
DR   Reactome; R-SCE-1222556; ROS and RNS production in phagocytes.
DR   Reactome; R-SCE-6798695; Neutrophil degranulation.
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   BioGRID-ORCS; 855076; 2 hits in 10 CRISPR screens.
DR   PRO; PR:P37296; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; P37296; Protein.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IBA:GO_Central.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:SGD.
DR   GO; GO:0000139; C:Golgi membrane; NAS:ComplexPortal.
DR   GO; GO:0005770; C:late endosome; IDA:SGD.
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; IBA:GO_Central.
DR   GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; IDA:SGD.
DR   GO; GO:0051117; F:ATPase binding; IBA:GO_Central.
DR   GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IDA:SGD.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR   GO; GO:0048388; P:endosomal lumen acidification; NAS:ComplexPortal.
DR   GO; GO:0061795; P:Golgi lumen acidification; NAS:ComplexPortal.
DR   GO; GO:1902600; P:proton transmembrane transport; IDA:ComplexPortal.
DR   GO; GO:0007035; P:vacuolar acidification; IMP:SGD.
DR   InterPro; IPR002490; V-ATPase_116kDa_su.
DR   InterPro; IPR026028; V-type_ATPase_116kDa_su_euka.
DR   PANTHER; PTHR11629:SF59; V-TYPE PROTON ATPASE SUBUNIT A, GOLGI ISOFORM; 1.
DR   PANTHER; PTHR11629; VACUOLAR PROTON ATPASES; 1.
DR   Pfam; PF01496; V_ATPase_I; 1.
DR   PIRSF; PIRSF001293; ATP6V0A1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Coiled coil; Endosome; Glycoprotein;
KW   Golgi apparatus; Hydrogen ion transport; Ion transport; Membrane;
KW   Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..890
FT                   /note="V-type proton ATPase subunit a, Golgi isoform"
FT                   /id="PRO_0000119225"
FT   TOPO_DOM        1..450
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        451..469
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        470..471
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        472..488
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        489..502
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        503..532
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        533..580
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        581..600
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        601..618
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        619..639
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        640..682
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        683..702
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        703..779
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        780..804
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        805..828
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        829..867
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        868..890
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   COILED          113..154
FT                   /evidence="ECO:0000255"
FT   COILED          297..347
FT                   /evidence="ECO:0000255"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   MOD_RES         223
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT   MOD_RES         228
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   CONFLICT        805
FT                   /note="Q -> E (in Ref. 1; AAA20596)"
FT                   /evidence="ECO:0000305"
FT   STRAND          7..9
FT                   /evidence="ECO:0007829|PDB:6O7U"
FT   STRAND          16..24
FT                   /evidence="ECO:0007829|PDB:6O7U"
FT   HELIX           25..35
FT                   /evidence="ECO:0007829|PDB:6O7U"
FT   STRAND          49..55
FT                   /evidence="ECO:0007829|PDB:6O7U"
FT   HELIX           58..77
FT                   /evidence="ECO:0007829|PDB:6O7U"
FT   HELIX           113..117
FT                   /evidence="ECO:0007829|PDB:6O7U"
FT   HELIX           119..163
FT                   /evidence="ECO:0007829|PDB:6O7U"
FT   STRAND          241..245
FT                   /evidence="ECO:0007829|PDB:6O7U"
FT   HELIX           246..248
FT                   /evidence="ECO:0007829|PDB:6O7U"
FT   HELIX           249..259
FT                   /evidence="ECO:0007829|PDB:6O7U"
FT   STRAND          267..270
FT                   /evidence="ECO:0007829|PDB:6O7U"
FT   STRAND          284..288
FT                   /evidence="ECO:0007829|PDB:6O7U"
FT   STRAND          293..296
FT                   /evidence="ECO:0007829|PDB:6O7U"
FT   HELIX           297..304
FT                   /evidence="ECO:0007829|PDB:6O7U"
FT   TURN            305..308
FT                   /evidence="ECO:0007829|PDB:6O7U"
FT   TURN            318..320
FT                   /evidence="ECO:0007829|PDB:6O7U"
FT   HELIX           321..351
FT                   /evidence="ECO:0007829|PDB:6O7U"
FT   HELIX           354..371
FT                   /evidence="ECO:0007829|PDB:6O7U"
FT   STRAND          378..386
FT                   /evidence="ECO:0007829|PDB:6O7U"
FT   HELIX           389..391
FT                   /evidence="ECO:0007829|PDB:6O7U"
FT   HELIX           392..405
FT                   /evidence="ECO:0007829|PDB:6O7U"
FT   TURN            431..433
FT                   /evidence="ECO:0007829|PDB:6O7U"
FT   HELIX           434..443
FT                   /evidence="ECO:0007829|PDB:6O7U"
FT   TURN            453..456
FT                   /evidence="ECO:0007829|PDB:6O7U"
FT   HELIX           457..468
FT                   /evidence="ECO:0007829|PDB:6O7U"
FT   HELIX           472..487
FT                   /evidence="ECO:0007829|PDB:6O7U"
FT   HELIX           489..493
FT                   /evidence="ECO:0007829|PDB:6O7U"
FT   HELIX           499..506
FT                   /evidence="ECO:0007829|PDB:6O7U"
FT   HELIX           508..524
FT                   /evidence="ECO:0007829|PDB:6O7U"
FT   STRAND          528..530
FT                   /evidence="ECO:0007829|PDB:6O7U"
FT   STRAND          539..541
FT                   /evidence="ECO:0007829|PDB:6O7U"
FT   STRAND          561..564
FT                   /evidence="ECO:0007829|PDB:6O7U"
FT   HELIX           566..568
FT                   /evidence="ECO:0007829|PDB:6O7U"
FT   HELIX           574..597
FT                   /evidence="ECO:0007829|PDB:6O7U"
FT   HELIX           599..607
FT                   /evidence="ECO:0007829|PDB:6O7U"
FT   HELIX           611..625
FT                   /evidence="ECO:0007829|PDB:6O7U"
FT   TURN            626..628
FT                   /evidence="ECO:0007829|PDB:6O7U"
FT   HELIX           629..641
FT                   /evidence="ECO:0007829|PDB:6O7U"
FT   STRAND          644..647
FT                   /evidence="ECO:0007829|PDB:6O7U"
FT   HELIX           655..663
FT                   /evidence="ECO:0007829|PDB:6O7U"
FT   HELIX           676..688
FT                   /evidence="ECO:0007829|PDB:6O7U"
FT   HELIX           690..702
FT                   /evidence="ECO:0007829|PDB:6O7U"
FT   HELIX           704..706
FT                   /evidence="ECO:0007829|PDB:6O7U"
FT   HELIX           768..790
FT                   /evidence="ECO:0007829|PDB:6O7U"
FT   TURN            791..794
FT                   /evidence="ECO:0007829|PDB:6O7U"
FT   HELIX           795..814
FT                   /evidence="ECO:0007829|PDB:6O7U"
FT   STRAND          816..818
FT                   /evidence="ECO:0007829|PDB:6O7U"
FT   STRAND          821..823
FT                   /evidence="ECO:0007829|PDB:6O7U"
FT   HELIX           827..846
FT                   /evidence="ECO:0007829|PDB:6O7U"
FT   HELIX           847..851
FT                   /evidence="ECO:0007829|PDB:6O7U"
FT   HELIX           853..865
FT                   /evidence="ECO:0007829|PDB:6O7U"
FT   TURN            866..871
FT                   /evidence="ECO:0007829|PDB:6O7U"
FT   HELIX           885..887
FT                   /evidence="ECO:0007829|PDB:6O7U"
SQ   SEQUENCE   890 AA;  101661 MW;  7CA12E37C1E42C67 CRC64;
     MNQEEAIFRS ADMTYVQLYI PLEVIREVTF LLGKMSVFMV MDLNKDLTAF QRGYVNQLRR
     FDEVERMVGF LNEVVEKHAA ETWKYILHID DEGNDIAQPD MADLINTMEP LSLENVNDMV
     KEITDCESRA RQLDESLDSL RSKLNDLLEQ RQVIFECSKF IEVNPGIAGR ATNPEIEQEE
     RDVDEFRMTP DDISETLSDA FSFDDETPQD RGALGNDLTR NQSVEDLSFL EQGYQHRYMI
     TGSIRRTKVD ILNRILWRLL RGNLIFQNFP IEEPLLEGKE KVEKDCFIIF THGETLLKKV
     KRVIDSLNGK IVSLNTRSSE LVDTLNRQID DLQRILDTTE QTLHTELLVI HDQLPVWSAM
     TKREKYVYTT LNKFQQESQG LIAEGWVPST ELIHLQDSLK DYIETLGSEY STVFNVILTN
     KLPPTYHRTN KFTQAFQSIV DAYGIATYKE INAGLATVVT FPFMFAIMFG DMGHGFILFL
     MALFLVLNER KFGAMHRDEI FDMAFTGRYV LLLMGAFSVY TGLLYNDIFS KSMTIFKSGW
     QWPSTFRKGE SIEAKKTGVY PFGLDFAWHG TDNGLLFSNS YKMKLSILMG YAHMTYSFMF
     SYINYRAKNS KVDIIGNFIP GLVFMQSIFG YLSWAIVYKW SKDWIKDDKP APGLLNMLIN
     MFLAPGTIDD QLYSGQAKLQ VVLLLAALVC VPWLLLYKPL TLRRLNKNGG GGRPHGYQSV
     GNIEHEEQIA QQRHSAEGFQ GMIISDVASV ADSINESVGG GEQGPFNFGD VMIHQVIHTI
     EFCLNCISHT ASYLRLWALS LAHAQLSSVL WDMTISNAFS SKNSGSPLAV MKVVFLFAMW
     FVLTVCILVF MEGTSAMLHA LRLHWVEAMS KFFEGEGYAY EPFSFRAIIE
//