PMA1_ARATH
ID PMA1_ARATH Reviewed; 949 AA.
AC P20649; O64626;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=ATPase 1, plasma membrane-type {ECO:0000303|PubMed:2521951};
DE EC=7.1.2.1 {ECO:0000305};
DE AltName: Full=Proton pump 1;
GN Name=AHA1 {ECO:0000303|PubMed:2521951};
GN OrderedLocusNames=At2g18960 {ECO:0000312|Araport:AT2G18960};
GN ORFNames=F19F24.16 {ECO:0000312|EMBL:AAC09030.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=2521951; DOI=10.1073/pnas.86.4.1234;
RA Harper J.F., Surowy T.K., Sussman M.R.;
RT "Molecular cloning and sequence of cDNA encoding the plasma membrane proton
RT pump (H+-ATPase) of Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:1234-1238(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP INTERACTION WITH PPI1.
RC STRAIN=cv. Landsberg erecta; TISSUE=Leaf, and Root;
RX PubMed=12182706; DOI=10.1046/j.1365-313x.2002.01373.x;
RA Morandini P., Valera M., Albumi C., Bonza M.C., Giacometti S., Ravera G.,
RA Murgia I., Soave C., De Michelis M.I.;
RT "A novel interaction partner for the C-terminus of Arabidopsis thaliana
RT plasma membrane H+-ATPase (AHA1 isoform): site and mechanism of action on
RT H+-ATPase activity differ from those of 14-3-3 proteins.";
RL Plant J. 31:487-497(2002).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. La-0;
RX PubMed=14506206; DOI=10.1074/mcp.t300006-mcp200;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Large-scale analysis of in vivo phosphorylated membrane proteins by
RT immobilized metal ion affinity chromatography and mass spectrometry.";
RL Mol. Cell. Proteomics 2:1234-1243(2003).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=15308754; DOI=10.1105/tpc.104.023150;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Phosphoproteomics of the Arabidopsis plasma membrane and a new
RT phosphorylation site database.";
RL Plant Cell 16:2394-2405(2004).
RN [8]
RP INTERACTION WITH PPI1.
RX PubMed=16279950; DOI=10.1111/j.1742-4658.2005.04985.x;
RA Viotti C., Luoni L., Morandini P., De Michelis M.I.;
RT "Characterization of the interaction between the plasma membrane H-ATPase
RT of Arabidopsis thaliana and a novel interactor (PPI1).";
RL FEBS J. 272:5864-5871(2005).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Seedling;
RX PubMed=17586839; DOI=10.1074/mcp.m700164-mcp200;
RA Niittylae T., Fuglsang A.T., Palmgren M.G., Frommer W.B., Schulze W.X.;
RT "Temporal analysis of sucrose-induced phosphorylation changes in plasma
RT membrane proteins of Arabidopsis.";
RL Mol. Cell. Proteomics 6:1711-1726(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-948, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-881, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [13]
RP DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX PubMed=20348108; DOI=10.1074/jbc.m110.101733;
RA Haruta M., Burch H.L., Nelson R.B., Barrett-Wilt G., Kline K.G.,
RA Mohsin S.B., Young J.C., Otegui M.S., Sussman M.R.;
RT "Molecular characterization of mutant Arabidopsis plants with reduced
RT plasma membrane proton pump activity.";
RL J. Biol. Chem. 285:17918-17929(2010).
RN [14]
RP ACTIVITY REGULATION.
RC STRAIN=cv. Columbia;
RX PubMed=24858935; DOI=10.1105/tpc.114.126037;
RA Spartz A.K., Ren H., Park M.Y., Grandt K.N., Lee S.H., Murphy A.S.,
RA Sussman M.R., Overvoorde P.J., Gray W.M.;
RT "SAUR inhibition of PP2C-D phosphatases activates plasma membrane H+-
RT ATPases to promote cell expansion in Arabidopsis.";
RL Plant Cell 26:2129-2142(2014).
RN [15]
RP INTERACTION WITH PSY1R.
RX PubMed=25267325; DOI=10.1111/tpj.12680;
RA Fuglsang A.T., Kristensen A., Cuin T.A., Schulze W.X., Persson J.,
RA Thuesen K.H., Ytting C.K., Oehlenschlaeger C.B., Mahmood K.,
RA Sondergaard T.E., Shabala S., Palmgren M.G.;
RT "Receptor kinase-mediated control of primary active proton pumping at the
RT plasma membrane.";
RL Plant J. 80:951-964(2014).
RN [16]
RP FUNCTION, INTERACTION WITH CNGC17 AND PSKR1, AND SUBCELLULAR LOCATION.
RX PubMed=26071421; DOI=10.1105/tpc.15.00306;
RA Ladwig F., Dahlke R.I., Stuehrwohldt N., Hartmann J., Harter K., Sauter M.;
RT "Phytosulfokine regulates growth in Arabidopsis through a response module
RT at the plasma membrane that includes CYCLIC NUCLEOTIDE-GATED CHANNEL17, H+-
RT ATPase, and BAK1.";
RL Plant Cell 27:1718-1729(2015).
CC -!- FUNCTION: The plasma membrane H(+) ATPase of plants and fungi generates
CC a proton gradient that drives the active transport of nutrients by
CC H(+)-symport. The resulting external acidification and/or internal
CC alkinization may mediate growth responses. Forms a functional cation-
CC translocating unit with CNGC17 that is activated by PSKR1/BAK1 and
CC possibly other BAK1/RLK complexes (PubMed:26071421).
CC {ECO:0000269|PubMed:26071421}.
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 Evidence={ECO:0000305};
CC -!- SUBUNIT: Binds to 14-3-3 proteins. The binding is induced by
CC phosphorylation of Thr-948. Binding to 14-3-3 proteins activates the
CC H(+)-ATPase (By similarity). Interacts with PPI1; this interaction
CC promotes ATPase activity. Interacts with PSY1R (PubMed:25267325). Part
CC of a functional complex containing PSKR1, BAK1, CNGC17, and AHA
CC (PubMed:26071421). Interacts with CNGC17 and PSKR1 (PubMed:26071421).
CC Triggered by SAUR9 via the phosphorylation of the C-terminal
CC autoinhibitory domain (PubMed:24858935). {ECO:0000250,
CC ECO:0000269|PubMed:12182706, ECO:0000269|PubMed:16279950,
CC ECO:0000269|PubMed:24858935, ECO:0000269|PubMed:25267325,
CC ECO:0000269|PubMed:26071421}.
CC -!- INTERACTION:
CC P20649; O23144: PPI1; NbExp=7; IntAct=EBI-2354448, EBI-2354477;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26071421,
CC ECO:0000305|PubMed:15308754}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:15308754}.
CC -!- DEVELOPMENTAL STAGE: Expressed on the surface of developing seeds and
CC from 8- to 16-cell stages to the heart stage of embryo development.
CC {ECO:0000269|PubMed:20348108}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype, due to the redudancy with
CC AHA2. Aha1 and aha2 double mutants are embryo lethal.
CC {ECO:0000269|PubMed:20348108}.
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; M24107; AAA32813.1; -; mRNA.
DR EMBL; AC003673; AAC09030.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06832.1; -; Genomic_DNA.
DR EMBL; BT008692; AAP40498.1; -; mRNA.
DR PIR; T01624; PXMUP1.
DR RefSeq; NP_179486.1; NM_127453.4.
DR AlphaFoldDB; P20649; -.
DR SMR; P20649; -.
DR BioGRID; 1770; 15.
DR IntAct; P20649; 4.
DR MINT; P20649; -.
DR STRING; 3702.AT2G18960.1; -.
DR TCDB; 3.A.3.3.7; the p-type atpase (p-atpase) superfamily.
DR iPTMnet; P20649; -.
DR SwissPalm; P20649; -.
DR PaxDb; P20649; -.
DR PRIDE; P20649; -.
DR ProteomicsDB; 234928; -.
DR EnsemblPlants; AT2G18960.1; AT2G18960.1; AT2G18960.
DR GeneID; 816413; -.
DR Gramene; AT2G18960.1; AT2G18960.1; AT2G18960.
DR KEGG; ath:AT2G18960; -.
DR Araport; AT2G18960; -.
DR TAIR; locus:2044450; AT2G18960.
DR eggNOG; KOG0205; Eukaryota.
DR HOGENOM; CLU_002360_6_4_1; -.
DR InParanoid; P20649; -.
DR OrthoDB; 188115at2759; -.
DR PhylomeDB; P20649; -.
DR BioCyc; ARA:AT2G18960-MON; -.
DR BRENDA; 7.1.2.1; 399.
DR PRO; PR:P20649; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; P20649; baseline and differential.
DR Genevisible; P20649; AT.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; ISS:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IMP:TAIR.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
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:UniProtKB.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0120029; P:proton export across plasma membrane; IEA:InterPro.
DR GO; GO:1902600; P:proton transmembrane transport; IDA:UniProtKB.
DR GO; GO:0051453; P:regulation of intracellular pH; IBA:GO_Central.
DR GO; GO:0010119; P:regulation of stomatal movement; IMP:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
DR GO; GO:1990069; P:stomatal opening; IMP:TAIR.
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; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Cell membrane; Hydrogen ion transport;
KW Ion transport; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P19456"
FT CHAIN 2..949
FT /note="ATPase 1, plasma membrane-type"
FT /id="PRO_0000046274"
FT TOPO_DOM 2..61
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..81
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 82..93
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..114
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 115..243
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..264
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 265..273
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..291
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 292..643
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 644..665
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 666..670
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 671..693
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 694..709
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 710..730
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 731..751
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 752..772
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 773..784
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 785..805
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 806..813
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 814..834
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 835..949
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 947..949
FT /note="Interaction with 14-3-3 proteins"
FT /evidence="ECO:0000250"
FT ACT_SITE 329
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 588
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 592
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P19456"
FT MOD_RES 881
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19245862"
FT MOD_RES 899
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19456"
FT MOD_RES 931
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19456"
FT MOD_RES 948
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18433157"
FT CONFLICT 771
FT /note="V -> L (in Ref. 1; AAA32813)"
FT /evidence="ECO:0000305"
FT CONFLICT 778
FT /note="S -> Y (in Ref. 1; AAA32813)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 949 AA; 104224 MW; A613FF6070ECC9F3 CRC64;
MSGLEDIKNE TVDLEKIPIE EVFQQLKCTR EGLTTQEGED RIVIFGPNKL EEKKESKILK
FLGFMWNPLS WVMEAAALMA IALANGDNRP PDWQDFVGII CLLVINSTIS FIEENNAGNA
AAALMAGLAP KTKVLRDGKW SEQEAAILVP GDIVSIKLGD IIPADARLLE GDPLKVDQSA
LTGESLPVTK HPGQEVFSGS TCKQGEIEAV VIATGVHTFF GKAAHLVDST NQVGHFQKVL
TSIGNFCICS IAIGIAIEIV VMYPIQHRKY RDGIDNLLVL LIGGIPIAMP TVLSVTMAIG
SHRLSQQGAI TKRMTAIEEM AGMDVLCSDK TGTLTLNKLS VDKNLVEVFC KGVEKDQVLL
FAAMASRVEN QDAIDAAMVG MLADPKEARA GIREVHFLPF NPVDKRTALT YIDSDGNWHR
VSKGAPEQIL DLANARPDLR KKVLSCIDKY AERGLRSLAV ARQVVPEKTK ESPGGPWEFV
GLLPLFDPPR HDSAETIRRA LNLGVNVKMI TGDQLAIGKE TGRRLGMGTN MYPSAALLGT
DKDSNIASIP VEELIEKADG FAGVFPEHKY EIVKKLQERK HIVGMTGDGV NDAPALKKAD
IGIAVADATD AARGASDIVL TEPGLSVIIS AVLTSRAIFQ RMKNYTIYAV SITIRIVFGF
MLIALIWEFD FSAFMVLIIA ILNDGTIMTI SKDRVKPSPT PDSWKLKEIF ATGIVLGGYQ
AIMSVIFFWA AHKTDFFSDK FGVRSIRDNN DELMGAVYLQ VSIISQALIF VTRSRSWSFV
ERPGALLMIA FVIAQLVATL IAVYADWTFA KVKGIGWGWA GVIWIYSIVT YFPQDILKFA
IRYILSGKAW ASLFDNRTAF TTKKDYGIGE REAQWAQAQR TLHGLQPKED VNIFPEKGSY
RELSEIAEQA KRRAEIARLR ELHTLKGHVE SVAKLKGLDI DTAGHHYTV
