PMA1_YEAST
ID PMA1_YEAST Reviewed; 918 AA.
AC P05030; D6VUC9;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 224.
DE RecName: Full=Plasma membrane ATPase 1;
DE EC=7.1.2.1;
DE AltName: Full=Proton pump 1;
GN Name=PMA1; OrderedLocusNames=YGL008C;
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].
RX PubMed=3005867; DOI=10.1038/319689a0;
RA Serrano R., Kielland-Brandt M.C., Fink G.R.;
RT "Yeast plasma membrane ATPase is essential for growth and has homology with
RT (Na+ + K+), K+- and Ca2+-ATPases.";
RL Nature 319:689-693(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(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 556-566.
RX PubMed=2136852; DOI=10.1016/s0021-9258(19)40013-6;
RA Davis C.B., Smith K.E., Campbell B.N. Jr., Hammes G.G.;
RT "The ATP binding site of the yeast plasma membrane proton-translocating
RT ATPase.";
RL J. Biol. Chem. 265:1300-1305(1990).
RN [5]
RP MUTAGENESIS OF GLU-129; ASP-200; GLU-233; ARG-271; PRO-335; ASP-378;
RP LYS-474; ASP-534; ASP-560; ASP-638 AND ASN-848.
RX PubMed=2901955; DOI=10.1002/j.1460-2075.1988.tb03010.x;
RA Portillo F., Serrano R.;
RT "Dissection of functional domains of the yeast proton-pumping ATPase by
RT directed mutagenesis.";
RL EMBO J. 7:1793-1798(1988).
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 UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-555, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=14557538; DOI=10.1073/pnas.2135500100;
RA Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.;
RT "A subset of membrane-associated proteins is ubiquitinated in response to
RT mutations in the endoplasmic reticulum degradation machinery.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003).
RN [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-911; THR-912 AND THR-918, AND
RP IDENTIFICATION BY 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61, 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 [11]
RP PRION IDENTIFICATION, AND INTERACTION WITH STD1.
RX PubMed=19797769; DOI=10.1101/gad.1839109;
RA Brown J.C., Lindquist S.;
RT "A heritable switch in carbon source utilization driven by an unusual yeast
RT prion.";
RL Genes Dev. 23:2320-2332(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-175; SER-911 AND THR-912, 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 [13]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-252, 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 [14]
RP INTERACTION WITH EXP1.
RX PubMed=28727280; DOI=10.1111/tra.12503;
RA Geva Y., Crissman J., Arakel E.C., Gomez-Navarro N., Chuartzman S.G.,
RA Stahmer K.R., Schwappach B., Miller E.A., Schuldiner M.;
RT "Two novel effectors of trafficking and maturation of the yeast plasma
RT membrane H+ -ATPase.";
RL Traffic 18:672-682(2017).
CC -!- FUNCTION: The plasma membrane ATPase of plants and fungi is a hydrogen
CC ion pump. The proton gradient it generates drives the active transport
CC of nutrients by H(+)-symport. The resulting external acidification
CC and/or internal alkinization may mediate growth responses.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H(+)(in) + H2O = ADP + 2 H(+)(out) + phosphate;
CC Xref=Rhea:RHEA:20852, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.1;
CC -!- SUBUNIT: Interacts with its cargot receptor EXP1 for its transport
CC within the cell and maturation. {ECO:0000269|PubMed:28727280}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- PTM: Phosphorylated on multiple Ser and Thr residues.
CC -!- MISCELLANEOUS: The prion state [GAR+] is provoked by the interaction of
CC the two proteins STD1 and PMA1. It involves a complex between a small
CC fraction of the cellular complement of PMA1, and STD1, a much lower-
CC abundance protein, and it is transmissible by non-Mendelian,
CC cytoplasmic inheritance. [GAR+] makes cells resistant to the glucose-
CC associated repression of alternative carbon sources. In contrast to
CC other prion forms, [GAR+] cannot be cured by GdnHCl or by inactivation
CC of the molecular chaperone HSP104. {ECO:0000305|PubMed:19797769}.
CC -!- MISCELLANEOUS: There are two plasma membrane ATPases in yeast. This is
CC the major isoform.
CC -!- MISCELLANEOUS: Present with 1260000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIIA subfamily. {ECO:0000305}.
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DR EMBL; X03534; CAA27237.1; -; Genomic_DNA.
DR EMBL; Z72530; CAA96708.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08090.1; -; Genomic_DNA.
DR PIR; S64010; PXBY1P.
DR RefSeq; NP_011507.1; NM_001180873.1.
DR PDB; 7VH5; EM; 3.20 A; A/B/C/D/E/F=1-918.
DR PDB; 7VH6; EM; 3.80 A; A/B/C/D/E/F=1-918.
DR PDBsum; 7VH5; -.
DR PDBsum; 7VH6; -.
DR AlphaFoldDB; P05030; -.
DR SMR; P05030; -.
DR BioGRID; 33238; 804.
DR DIP; DIP-2537N; -.
DR IntAct; P05030; 23.
DR MINT; P05030; -.
DR STRING; 4932.YGL008C; -.
DR TCDB; 3.A.3.3.6; the p-type atpase (p-atpase) superfamily.
DR CarbonylDB; P05030; -.
DR iPTMnet; P05030; -.
DR MaxQB; P05030; -.
DR PaxDb; P05030; -.
DR PRIDE; P05030; -.
DR EnsemblFungi; YGL008C_mRNA; YGL008C; YGL008C.
DR GeneID; 852876; -.
DR KEGG; sce:YGL008C; -.
DR SGD; S000002976; PMA1.
DR VEuPathDB; FungiDB:YGL008C; -.
DR eggNOG; KOG0205; Eukaryota.
DR GeneTree; ENSGT00940000176570; -.
DR HOGENOM; CLU_002360_6_0_1; -.
DR InParanoid; P05030; -.
DR OMA; FTIFGWF; -.
DR BioCyc; MetaCyc:G3O-30531-MON; -.
DR BioCyc; YEAST:G3O-30531-MON; -.
DR BRENDA; 7.1.2.1; 984.
DR SABIO-RK; P05030; -.
DR PRO; PR:P05030; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P05030; protein.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0032126; C:eisosome; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0045121; C:membrane raft; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015662; F:P-type ion transporter activity; IBA:GO_Central.
DR GO; GO:0008553; F:P-type proton-exporting transporter activity; IDA:SGD.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR GO; GO:1904263; P:positive regulation of TORC1 signaling; IMP:SGD.
DR GO; GO:1902906; P:proteasome storage granule assembly; IMP:SGD.
DR GO; GO:0120029; P:proton export across plasma membrane; IEA:InterPro.
DR GO; GO:1902600; P:proton transmembrane transport; IDA:SGD.
DR GO; GO:0051453; P:regulation of intracellular pH; IBA:GO_Central.
DR GO; GO:0055085; P:transmembrane transport; IDA:SGD.
DR CDD; cd02076; P-type_ATPase_H; 1.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006534; P-type_ATPase_IIIA.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR PRINTS; PR00120; HATPASE.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01647; ATPase-IIIA_H; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 3.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amyloid; ATP-binding; Cell membrane;
KW Direct protein sequencing; Hydrogen ion transport; Ion transport;
KW Isopeptide bond; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Prion; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix; Transport; Ubl conjugation.
FT CHAIN 1..918
FT /note="Plasma membrane ATPase 1"
FT /id="PRO_0000046271"
FT TOPO_DOM 1..115
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 137..140
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..160
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 161..291
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..313
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 314..325
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 326..347
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 348..719
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 720..738
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 739..754
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 755..774
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 775..824
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 825..845
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 846..857
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 858..874
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 875..918
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..61
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 378
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 634
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 638
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 175
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 911
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 912
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 918
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT CROSSLNK 252
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 555
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:14557538"
FT MUTAGEN 129
FT /note="E->L,Q: Normal activity."
FT /evidence="ECO:0000269|PubMed:2901955"
FT MUTAGEN 200
FT /note="D->N: Activity reduced to 23%."
FT /evidence="ECO:0000269|PubMed:2901955"
FT MUTAGEN 233
FT /note="E->Q: Activity reduced to 33%."
FT /evidence="ECO:0000269|PubMed:2901955"
FT MUTAGEN 271
FT /note="R->T: Normal activity."
FT /evidence="ECO:0000269|PubMed:2901955"
FT MUTAGEN 335
FT /note="P->A: Activity reduced to 53%."
FT /evidence="ECO:0000269|PubMed:2901955"
FT MUTAGEN 378
FT /note="D->E: Activity reduced to 67%."
FT /evidence="ECO:0000269|PubMed:2901955"
FT MUTAGEN 378
FT /note="D->N: Activity reduced to 73%."
FT /evidence="ECO:0000269|PubMed:2901955"
FT MUTAGEN 378
FT /note="D->T: Activity reduced to 49%."
FT /evidence="ECO:0000269|PubMed:2901955"
FT MUTAGEN 474
FT /note="K->Q: Activity reduced to 19%."
FT /evidence="ECO:0000269|PubMed:2901955"
FT MUTAGEN 534
FT /note="D->N: Activity reduced to 37%."
FT /evidence="ECO:0000269|PubMed:2901955"
FT MUTAGEN 560
FT /note="D->N: Activity reduced to 24%."
FT /evidence="ECO:0000269|PubMed:2901955"
FT MUTAGEN 638
FT /note="D->N: Activity reduced to 24%."
FT /evidence="ECO:0000269|PubMed:2901955"
FT MUTAGEN 848
FT /note="N->D: Normal activity."
FT /evidence="ECO:0000269|PubMed:2901955"
FT HELIX 111..120
FT /evidence="ECO:0007829|PDB:7VH5"
FT HELIX 123..137
FT /evidence="ECO:0007829|PDB:7VH5"
FT HELIX 141..173
FT /evidence="ECO:0007829|PDB:7VH5"
FT STRAND 179..184
FT /evidence="ECO:0007829|PDB:7VH5"
FT STRAND 187..192
FT /evidence="ECO:0007829|PDB:7VH5"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:7VH5"
FT STRAND 198..204
FT /evidence="ECO:0007829|PDB:7VH5"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:7VH5"
FT STRAND 223..226
FT /evidence="ECO:0007829|PDB:7VH5"
FT TURN 229..231
FT /evidence="ECO:0007829|PDB:7VH5"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:7VH5"
FT STRAND 250..253
FT /evidence="ECO:0007829|PDB:7VH5"
FT STRAND 256..260
FT /evidence="ECO:0007829|PDB:7VH5"
FT HELIX 268..279
FT /evidence="ECO:0007829|PDB:7VH5"
FT HELIX 285..314
FT /evidence="ECO:0007829|PDB:7VH5"
FT HELIX 319..333
FT /evidence="ECO:0007829|PDB:7VH5"
FT HELIX 338..355
FT /evidence="ECO:0007829|PDB:7VH5"
FT STRAND 358..362
FT /evidence="ECO:0007829|PDB:7VH5"
FT HELIX 364..370
FT /evidence="ECO:0007829|PDB:7VH5"
FT STRAND 374..378
FT /evidence="ECO:0007829|PDB:7VH5"
FT HELIX 379..383
FT /evidence="ECO:0007829|PDB:7VH5"
FT HELIX 401..410
FT /evidence="ECO:0007829|PDB:7VH5"
FT HELIX 416..418
FT /evidence="ECO:0007829|PDB:7VH5"
FT HELIX 421..427
FT /evidence="ECO:0007829|PDB:7VH5"
FT TURN 435..440
FT /evidence="ECO:0007829|PDB:7VH5"
FT STRAND 445..449
FT /evidence="ECO:0007829|PDB:7VH5"
FT TURN 453..455
FT /evidence="ECO:0007829|PDB:7VH5"
FT STRAND 457..463
FT /evidence="ECO:0007829|PDB:7VH5"
FT STRAND 469..475
FT /evidence="ECO:0007829|PDB:7VH5"
FT HELIX 477..481
FT /evidence="ECO:0007829|PDB:7VH5"
FT STRAND 487..490
FT /evidence="ECO:0007829|PDB:7VH5"
FT HELIX 491..507
FT /evidence="ECO:0007829|PDB:7VH5"
FT STRAND 511..518
FT /evidence="ECO:0007829|PDB:7VH5"
FT STRAND 520..522
FT /evidence="ECO:0007829|PDB:7VH5"
FT STRAND 524..533
FT /evidence="ECO:0007829|PDB:7VH5"
FT HELIX 540..549
FT /evidence="ECO:0007829|PDB:7VH5"
FT STRAND 553..557
FT /evidence="ECO:0007829|PDB:7VH5"
FT HELIX 562..572
FT /evidence="ECO:0007829|PDB:7VH5"
FT STRAND 578..580
FT /evidence="ECO:0007829|PDB:7VH5"
FT HELIX 581..584
FT /evidence="ECO:0007829|PDB:7VH5"
FT STRAND 585..588
FT /evidence="ECO:0007829|PDB:7VH5"
FT HELIX 594..603
FT /evidence="ECO:0007829|PDB:7VH5"
FT STRAND 605..609
FT /evidence="ECO:0007829|PDB:7VH5"
FT HELIX 612..624
FT /evidence="ECO:0007829|PDB:7VH5"
FT STRAND 629..633
FT /evidence="ECO:0007829|PDB:7VH5"
FT HELIX 639..644
FT /evidence="ECO:0007829|PDB:7VH5"
FT STRAND 645..650
FT /evidence="ECO:0007829|PDB:7VH5"
FT HELIX 656..661
FT /evidence="ECO:0007829|PDB:7VH5"
FT STRAND 663..668
FT /evidence="ECO:0007829|PDB:7VH5"
FT HELIX 671..713
FT /evidence="ECO:0007829|PDB:7VH5"
FT HELIX 719..736
FT /evidence="ECO:0007829|PDB:7VH5"
FT HELIX 752..776
FT /evidence="ECO:0007829|PDB:7VH5"
FT HELIX 791..804
FT /evidence="ECO:0007829|PDB:7VH5"
FT HELIX 806..810
FT /evidence="ECO:0007829|PDB:7VH5"
FT STRAND 812..814
FT /evidence="ECO:0007829|PDB:7VH5"
FT TURN 816..818
FT /evidence="ECO:0007829|PDB:7VH5"
FT HELIX 823..842
FT /evidence="ECO:0007829|PDB:7VH5"
FT TURN 843..845
FT /evidence="ECO:0007829|PDB:7VH5"
FT STRAND 846..848
FT /evidence="ECO:0007829|PDB:7VH5"
FT HELIX 852..877
FT /evidence="ECO:0007829|PDB:7VH5"
FT HELIX 880..887
FT /evidence="ECO:0007829|PDB:7VH5"
FT HELIX 897..916
FT /evidence="ECO:0007829|PDB:7VH5"
SQ SEQUENCE 918 AA; 99619 MW; AA1E93966B37E8E1 CRC64;
MTDTSSSSSS SSASSVSAHQ PTQEKPAKTY DDAASESSDD DDIDALIEEL QSNHGVDDED
SDNDGPVAAG EARPVPEEYL QTDPSYGLTS DEVLKRRKKY GLNQMADEKE SLVVKFVMFF
VGPIQFVMEA AAILAAGLSD WVDFGVICGL LMLNAGVGFV QEFQAGSIVD ELKKTLANTA
VVIRDGQLVE IPANEVVPGD ILQLEDGTVI PTDGRIVTED CFLQIDQSAI TGESLAVDKH
YGDQTFSSST VKRGEGFMVV TATGDNTFVG RAAALVNKAA GGQGHFTEVL NGIGIILLVL
VIATLLLVWT ACFYRTNGIV RILRYTLGIT IIGVPVGLPA VVTTTMAVGA AYLAKKQAIV
QKLSAIESLA GVEILCSDKT GTLTKNKLSL HEPYTVEGVS PDDLMLTACL AASRKKKGLD
AIDKAFLKSL KQYPKAKDAL TKYKVLEFHP FDPVSKKVTA VVESPEGERI VCVKGAPLFV
LKTVEEDHPI PEDVHENYEN KVAELASRGF RALGVARKRG EGHWEILGVM PCMDPPRDDT
AQTVSEARHL GLRVKMLTGD AVGIAKETCR QLGLGTNIYN AERLGLGGGG DMPGSELADF
VENADGFAEV FPQHKYRVVE ILQNRGYLVA MTGDGVNDAP SLKKADTGIA VEGATDAARS
AADIVFLAPG LSAIIDALKT SRQIFHRMYS YVVYRIALSL HLEIFLGLWI AILDNSLDID
LIVFIAIFAD VATLAIAYDN APYSPKPVKW NLPRLWGMSI ILGIVLAIGS WITLTTMFLP
KGGIIQNFGA MNGIMFLQIS LTENWLIFIT RAAGPFWSSI PSWQLAGAVF AVDIIATMFT
LFGWWSENWT DIVTVVRVWI WSIGIFCVLG GFYYEMSTSE AFDRLMNGKP MKEKKSTRSV
EDFMAAMQRV STQHEKET
