PMA2_ARATH
ID PMA2_ARATH Reviewed; 948 AA.
AC P19456;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=ATPase 2, plasma membrane-type {ECO:0000303|PubMed:2143186};
DE EC=7.1.2.1 {ECO:0000305};
DE AltName: Full=Proton pump 2;
GN Name=AHA2 {ECO:0000303|PubMed:2143186};
GN OrderedLocusNames=At4g30190 {ECO:0000312|Araport:AT4G30190};
GN ORFNames=F9N11.40 {ECO:0000312|EMBL:CAB52463.1};
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 [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=2143186; DOI=10.1016/s0021-9258(18)77391-2;
RA Harper J.F., Manney L., Dewitt N.D., Yoo M.H., Sussman M.R.;
RT "The Arabidopsis thaliana plasma membrane H(+)-ATPase multigene family.
RT Genomic sequence and expression of a third isoform.";
RL J. Biol. Chem. 265:13601-13608(1990).
RN [2]
RP ERRATUM OF PUBMED:2143186.
RA Harper J.F., Manney L., Dewitt N.D., Yoo M.H., Sussman M.R.;
RL J. Biol. Chem. 265:22569-22569(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [4]
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 [5]
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 [6]
RP DOMAIN, AND ACTIVITY REGULATION.
RX PubMed=10353834; DOI=10.1021/bi982482l;
RA Axelsen K.B., Venema K., Jahn T., Baunsgaard L., Palmgren M.G.;
RT "Molecular dissection of the C-terminal regulatory domain of the plant
RT plasma membrane H+-ATPase AHA2: mapping of residues that when altered give
RT rise to an activated enzyme.";
RL Biochemistry 38:7227-7234(1999).
RN [7]
RP PHOSPHORYLATION AT THR-947, AND INTERACTION WITH 14-3-3 PROTEINS.
RX PubMed=10593986; DOI=10.1074/jbc.274.51.36774;
RA Fuglsang A.T., Visconti S., Drumm K., Jahn T., Stensballe A., Mattei B.,
RA Jensen O.N., Aducci P., Palmgren M.G.;
RT "Binding of 14-3-3 protein to the plasma membrane H(+)-ATPase AHA2 involves
RT the three C-terminal residues Tyr(946)-Thr-Val and requires phosphorylation
RT of Thr(947).";
RL J. Biol. Chem. 274:36774-36780(1999).
RN [8]
RP MUTAGENESIS OF ASP-684, AND SUBCELLULAR LOCATION.
RX PubMed=10995773; DOI=10.1074/jbc.m007537200;
RA Buch-Pedersen M.J., Venema K., Serrano R., Palmgren M.G.;
RT "Abolishment of proton pumping and accumulation in the E1P conformational
RT state of a plant plasma membrane H+-ATPase by substitution of a conserved
RT aspartyl residue in transmembrane segment 6.";
RL J. Biol. Chem. 275:39167-39173(2000).
RN [9]
RP REVIEW.
RX PubMed=10748244; DOI=10.1016/s0005-2736(00)00128-0;
RA Morsomme P., Boutry M.;
RT "The plant plasma membrane H(+)-ATPase: structure, function and
RT regulation.";
RL Biochim. Biophys. Acta 1465:1-16(2000).
RN [10]
RP MUTAGENESIS OF ARG-655 AND ASP-684, AND PHOSPHORYLATION.
RX PubMed=12626496; DOI=10.1074/jbc.m212729200;
RA Buch-Pedersen M.J., Palmgren M.G.;
RT "Conserved Asp684 in transmembrane segment M6 of the plant plasma membrane
RT P-type proton pump AHA2 is a molecular determinant of proton
RT translocation.";
RL J. Biol. Chem. 278:17845-17851(2003).
RN [11]
RP FUNCTION.
RX PubMed=12920605; DOI=10.1007/s10265-003-0111-9;
RA Buch-Pedersen M.J., Palmgren M.G.;
RT "Mechanism of proton transport by plant plasma membrane proton ATPases.";
RL J. Plant Res. 116:507-515(2003).
RN [12]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
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 [13]
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 [14]
RP PHOSPHORYLATION AT SER-931, MUTAGENESIS OF SER-904; THR-924; SER-931;
RP THR-942 AND THR-947, TISSUE SPECIFICITY, AND ACTIVITY REGULATION.
RX PubMed=17483306; DOI=10.1105/tpc.105.035626;
RA Fuglsang A.T., Guo Y., Cuin T.A., Qiu Q., Song C., Kristiansen K.A.,
RA Bych K., Schulz A., Shabala S., Schumaker K.S., Palmgren M.G., Zhu J.K.;
RT "Arabidopsis protein kinase PKS5 inhibits the plasma membrane H+ -ATPase by
RT preventing interaction with 14-3-3 protein.";
RL Plant Cell 19:1617-1634(2007).
RN [15]
RP PHOSPHORYLATION AT THR-881; SER-899 AND THR-947.
RX PubMed=17651370; DOI=10.1111/j.1365-313x.2007.03192.x;
RA Nuehse T.S., Bottrill A.R., Jones A.M., Peck S.C.;
RT "Quantitative phosphoproteomic analysis of plasma membrane proteins reveals
RT regulatory mechanisms of plant innate immune responses.";
RL Plant J. 51:931-940(2007).
RN [16]
RP IDENTIFICATION BY 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 [17]
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 [18]
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 [19]
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=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [20]
RP FUNCTION.
RX PubMed=22214817; DOI=10.1104/pp.111.189167;
RA Haruta M., Sussman M.R.;
RT "The effect of a genetically reduced plasma membrane protonmotive force on
RT vegetative growth of Arabidopsis.";
RL Plant Physiol. 158:1158-1171(2012).
RN [21]
RP MUTAGENESIS OF ASN-106.
RX PubMed=23420846; DOI=10.1074/jbc.m112.417345;
RA Ekberg K., Wielandt A.G., Buch-Pedersen M.J., Palmgren M.G.;
RT "A conserved asparagine in a P-type proton pump is required for efficient
RT gating of protons.";
RL J. Biol. Chem. 288:9610-9618(2013).
RN [22]
RP ACTIVITY REGULATION, INTERACTION WITH PP2C67/PP2C-D1, AND PHOSPHORYLATION
RP AT THR-947.
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 [23]
RP FUNCTION, AND PHOSPHORYLATION.
RX PubMed=24492258; DOI=10.1093/pcp/pcu028;
RA Hayashi Y., Takahashi K., Inoue S., Kinoshita T.;
RT "Abscisic acid suppresses hypocotyl elongation by dephosphorylating plasma
RT membrane H(+)-ATPase in Arabidopsis thaliana.";
RL Plant Cell Physiol. 55:845-853(2014).
RN [24]
RP INTERACTION WITH PSY1R, PHOSPHORYLATION AT THR-881, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, MUTAGENESIS OF THR-881, AND ACTIVITY REGULATION.
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 [25]
RP PHOSPHORYLATION AT SER-899, AND ACTIVITY REGULATION.
RC STRAIN=cv. Columbia;
RX PubMed=24458638; DOI=10.1126/science.1244454;
RA Haruta M., Sabat G., Stecker K., Minkoff B.B., Sussman M.R.;
RT "A peptide hormone and its receptor protein kinase regulate plant cell
RT expansion.";
RL Science 343:408-411(2014).
RN [26]
RP ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF
RP LEU-919 AND LEU-922.
RX PubMed=25971968; DOI=10.1074/jbc.m114.617746;
RA Wielandt A.G., Pedersen J.T., Falhof J., Kemmer G.C., Lund A., Ekberg K.,
RA Fuglsang A.T., Pomorski T.G., Buch-Pedersen M.J., Palmgren M.;
RT "Specific Activation of the Plant P-type Plasma Membrane H+-ATPase by
RT Lysophospholipids Depends on the Autoinhibitory N- and C-terminal
RT Domains.";
RL J. Biol. Chem. 290:16281-16291(2015).
RN [27]
RP FUNCTION, AND INDUCTION BY NITRATE.
RX PubMed=25382626; DOI=10.1111/ppl.12305;
RA Mlodzinska E., Klobus G., Christensen M.D., Fuglsang A.T.;
RT "The plasma membrane H(+)-ATPase AHA2 contributes to the root architecture
RT in response to different nitrogen supply.";
RL Physiol. Plantarum 154:270-282(2015).
RN [28]
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).
RN [29]
RP FUNCTION.
RX PubMed=27013734; DOI=10.1126/science.aad6429;
RA Veshaguri S., Christensen S.M., Kemmer G.C., Ghale G., Moeller M.P.,
RA Lohr C., Christensen A.L., Justesen B.H., Joergensen I.L., Schiller J.,
RA Hatzakis N.S., Grabe M., Pomorski T.G., Stamou D.;
RT "Direct observation of proton pumping by a eukaryotic P-type ATPase.";
RL Science 351:1469-1473(2016).
RN [30]
RP PHOSPHORYLATION AT THR-947.
RC STRAIN=cv. Columbia;
RX PubMed=30649552; DOI=10.1093/pcp/pcz005;
RA Minami A., Takahashi K., Inoue S.I., Tada Y., Kinoshita T.;
RT "Brassinosteroid induces phosphorylation of the plasma membrane H+-ATPase
RT during hypocotyl elongation in Arabidopsis thaliana.";
RL Plant Cell Physiol. 60:935-944(2019).
RN [31]
RP X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) OF 1-875.
RX PubMed=18075595; DOI=10.1038/nature06417;
RA Pedersen B.P., Buch-Pedersen M.J., Morth J.P., Palmgren M.G., Nissen P.;
RT "Crystal structure of the plasma membrane proton pump.";
RL Nature 450:1111-1114(2007).
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 (PubMed:10748244, PubMed:12920605, PubMed:27013734). The
CC resulting external acidification and/or internal alkinization may
CC mediate growth responses (PubMed:10748244, PubMed:12920605). Involved
CC in maintaining the membrane potential and delta-pH, together forming
CC the plasma membrane protonmotive force (PMF) required for root and
CC hypocotyl elongation and root tropism (PubMed:22214817,
CC PubMed:24492258). Important for root growth and development during
CC different nitrogen regimes (PubMed:25382626). Forms a functional
CC cation-translocating unit with CNGC17 that is activated by PSKR1/BAK1
CC and possibly other BAK1/RLK complexes (PubMed:26071421).
CC {ECO:0000269|PubMed:12920605, ECO:0000269|PubMed:22214817,
CC ECO:0000269|PubMed:24492258, ECO:0000269|PubMed:25382626,
CC ECO:0000269|PubMed:26071421, ECO:0000269|PubMed:27013734,
CC ECO:0000305|PubMed:10748244}.
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 -!- ACTIVITY REGULATION: Regulated by an auto-inhibitory C-terminal domain
CC that can be displaced by phosphorylation of Thr-947 and the subsequent
CC binding of 14-3-3 proteins (PubMed:10353834). Negatively regulated by
CC PKS5 (PubMed:17483306). PKS5 phosphorylates Ser-931, inhibiting
CC interaction with the activating 14-3-3 protein (PubMed:17483306).
CC Positively regulated by PSY1R (PubMed:25267325). PSY1R phosphorylates
CC Thr-881, situated in the auto-inhibitory region I of the C-terminal
CC domain, causing pump activation (PubMed:25267325). Negatively regulated
CC by the secreted peptide RALF (PubMed:24458638). After specific binding
CC to FERONIA, RALF causes phosphorylation at Ser-899, mediating the
CC inhibition of proton transport (PubMed:24458638). Activated by
CC lysophospholipids, without the involvement of phosphorylation of Thr-
CC 947 (PubMed:25971968). This activation is critically dependent on the
CC single autoinhibitory residue Leu-919 (PubMed:25971968). Repressed by
CC PP2C-D phosphatases (e.g. PP2C67/PP2C-D1 and PP2C64/PP2C-D5) which
CC dephosphorylates Thr-947 (PubMed:24858935). Triggered by SAUR19 via
CC phosphorylation of the C-terminal autoinhibitory domain (e.g. Thr-947),
CC as a result of the inhibition of PP2C67/PP2C-D1 (PubMed:24858935).
CC {ECO:0000269|PubMed:10353834, ECO:0000269|PubMed:10593986,
CC ECO:0000269|PubMed:17483306, ECO:0000269|PubMed:24458638,
CC ECO:0000269|PubMed:24858935, ECO:0000269|PubMed:25267325,
CC ECO:0000269|PubMed:25971968}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.2 mM for ATP {ECO:0000269|PubMed:25971968};
CC Vmax=0.87 umol/min/mg enzyme {ECO:0000269|PubMed:25971968};
CC -!- SUBUNIT: Binds to 14-3-3 proteins (PubMed:10593986). The binding is
CC induced by phosphorylation of Thr-947 and it activates the H(+)-ATPase
CC (PubMed:10593986). Interacts (via the R-domain) with PSY1R (via C-
CC terminus) (PubMed:25267325). Part of a functional complex containing
CC PSKR1, BAK1, CNGC17, and AHA (PubMed:26071421). Interacts with CNGC17
CC and PSKR1 (PubMed:26071421). Interacts with PP2C67/PP2C-D1 at the
CC plasma membrane (PubMed:24858935). {ECO:0000269|PubMed:10593986,
CC ECO:0000269|PubMed:24858935, ECO:0000269|PubMed:25267325,
CC ECO:0000269|PubMed:26071421}.
CC -!- INTERACTION:
CC P19456; O22932: CIPK11; NbExp=3; IntAct=EBI-2293350, EBI-537638;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10995773,
CC ECO:0000269|PubMed:25267325, ECO:0000269|PubMed:26071421,
CC ECO:0000305|PubMed:15308754}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=P19456-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Higher levels in roots than in shoots
CC (PubMed:2143186). Expressed in epidermal and root cortex cells, in
CC phloem, xylem and root hairs (PubMed:17483306). Detected in cotyledons,
CC hypocotyls, roots and root hairs (PubMed:25267325).
CC {ECO:0000269|PubMed:17483306, ECO:0000269|PubMed:2143186,
CC ECO:0000269|PubMed:25267325}.
CC -!- DEVELOPMENTAL STAGE: Expressed on the surface of developing seeds and
CC up to the early globular stage of embryo development.
CC {ECO:0000269|PubMed:20348108}.
CC -!- INDUCTION: Up-regulated by low nitrate conditions.
CC {ECO:0000269|PubMed:25382626}.
CC -!- DOMAIN: The C-terminus contains a R-domain composed of 2 autoinhibitory
CC regions (863-885 and 904-919). {ECO:0000269|PubMed:10353834}.
CC -!- PTM: Phosphorylation at Thr-881 by PSY1R (PubMed:17651370,
CC PubMed:25267325). This phosphorylation activates proton pumping
CC (PubMed:25267325). Decreased phosphorylation in response to flg22
CC elicitation (PubMed:17651370). {ECO:0000269|PubMed:17651370,
CC ECO:0000269|PubMed:25267325}.
CC -!- PTM: Phosphorylation at Ser-899 is specifically induced by RALF1, thus
CC leading to the inhibition of proton transport (PubMed:24458638).
CC Increased phosphorylation in response to flg22 elicitation
CC (PubMed:17651370). {ECO:0000269|PubMed:17651370,
CC ECO:0000269|PubMed:24458638}.
CC -!- PTM: Phosphorylation of Thr-947 induces the binding to 14-3-3 proteins,
CC but phosphorylation of Ser-931 interfers with this binding no matter
CC whether Thr-947 is phosphorylated or not (PubMed:10593986,
CC PubMed:17483306). Decreased phosphorylation in response to flg22
CC elicitation (PubMed:17651370). Phosphorylation of Thr-947 is enhanced
CC by the presence of brassinolide (BL) via the BRI1-BIN2 pathway and
CC prior the trigger of hypocotyl elongation (PubMed:30649552).
CC Inactivated by PP2C67/PP2C-D1-mediated Thr-947 dephosphorylation;
CC SAUR19 inhibits the action of PP2C67/PP2C-D1 and thus promotes the
CC active phosphorylated form (PubMed:24858935).
CC {ECO:0000269|PubMed:10593986, ECO:0000269|PubMed:17483306,
CC ECO:0000269|PubMed:17651370, ECO:0000269|PubMed:24858935,
CC ECO:0000269|PubMed:30649552}.
CC -!- PTM: Abscisic acid induces dephosphorylation of AHA2 in etiolated
CC seedlings, suppressing ATP hydrolysis and hypocotyl elongation.
CC {ECO:0000269|PubMed:24492258}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, due to the redudancy with AHA1. Aha1 and aha2 double
CC mutants are embryo lethal. {ECO:0000269|PubMed:20348108}.
CC -!- MISCELLANEOUS: The catalytic mechanism involves at least four different
CC enzyme conformational states named E1, E1P, E2P, and E2, with the E1P-
CC E2P transition accompanying the transfer of ion across the membrane.
CC E1P and E2P are phosphorylated intermediates.
CC {ECO:0000305|PubMed:10748244}.
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; J05570; AAA32751.1; -; Genomic_DNA.
DR EMBL; AL109796; CAB52463.1; -; Genomic_DNA.
DR EMBL; AL161576; CAB81012.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85731.1; -; Genomic_DNA.
DR EMBL; AY035075; AAK59580.1; -; mRNA.
DR EMBL; BT000781; AAN31920.1; -; mRNA.
DR EMBL; BT001969; AAN71968.1; -; mRNA.
DR PIR; A37116; PXMUP2.
DR RefSeq; NP_194748.1; NM_119165.4. [P19456-1]
DR PDB; 5KSD; X-ray; 3.50 A; A/B=12-844.
DR PDBsum; 5KSD; -.
DR AlphaFoldDB; P19456; -.
DR SMR; P19456; -.
DR BioGRID; 14429; 48.
DR IntAct; P19456; 30.
DR STRING; 3702.AT4G30190.2; -.
DR TCDB; 3.A.3.3.9; the p-type atpase (p-atpase) superfamily.
DR iPTMnet; P19456; -.
DR PaxDb; P19456; -.
DR PRIDE; P19456; -.
DR ProteomicsDB; 236644; -. [P19456-1]
DR EnsemblPlants; AT4G30190.1; AT4G30190.1; AT4G30190. [P19456-1]
DR GeneID; 829142; -.
DR Gramene; AT4G30190.1; AT4G30190.1; AT4G30190. [P19456-1]
DR KEGG; ath:AT4G30190; -.
DR Araport; AT4G30190; -.
DR eggNOG; KOG0205; Eukaryota.
DR HOGENOM; CLU_002360_6_4_1; -.
DR InParanoid; P19456; -.
DR PhylomeDB; P19456; -.
DR BioCyc; ARA:AT4G30190-MON; -.
DR BioCyc; MetaCyc:AT4G30190-MON; -.
DR BRENDA; 7.1.2.1; 399.
DR SABIO-RK; P19456; -.
DR EvolutionaryTrace; P19456; -.
DR PRO; PR:P19456; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P19456; baseline and differential.
DR Genevisible; P19456; AT.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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 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 3D-structure; Acetylation; Alternative splicing; ATP-binding;
KW Cell membrane; Hydrogen ion transport; Ion transport; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..948
FT /note="ATPase 2, plasma membrane-type"
FT /id="PRO_0000046275"
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..948
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 946..948
FT /note="Interaction with 14-3-3 proteins"
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:0007744|PubMed:22223895"
FT MOD_RES 881
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:25267325"
FT MOD_RES 899
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24458638"
FT MOD_RES 931
FT /note="Phosphoserine; by CIPK11"
FT /evidence="ECO:0000269|PubMed:17483306"
FT MOD_RES 947
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:10593986,
FT ECO:0000269|PubMed:24858935, ECO:0000269|PubMed:30649552"
FT MUTAGEN 106
FT /note="N->A,D,K,Q,T: Reduced proton transport."
FT /evidence="ECO:0000269|PubMed:23420846"
FT MUTAGEN 655
FT /note="R->A,D: No effect on ATP affinity, but reduced
FT proton transport."
FT /evidence="ECO:0000269|PubMed:12626496"
FT MUTAGEN 655
FT /note="R->K: No effect on ATP affinity and proton
FT transport."
FT /evidence="ECO:0000269|PubMed:12626496"
FT MUTAGEN 684
FT /note="D->A,V,R: No effect on ATP affinity, but loss of
FT proton transport."
FT /evidence="ECO:0000269|PubMed:12626496"
FT MUTAGEN 684
FT /note="D->E: No effect on ATP affinity, but reduced proton
FT transport."
FT /evidence="ECO:0000269|PubMed:12626496"
FT MUTAGEN 684
FT /note="D->N: Insensitive to the inhibitor vanadate and
FT locked in the E1 conformation. No effect on ATP hydrolysis,
FT but loss of proton transport."
FT /evidence="ECO:0000269|PubMed:10995773,
FT ECO:0000269|PubMed:12626496"
FT MUTAGEN 881
FT /note="T->A: Decreased phosphorylation by PSY1R."
FT /evidence="ECO:0000269|PubMed:25267325"
FT MUTAGEN 881
FT /note="T->D: No effect on 14-3-3 protein binding, but
FT increased activity."
FT /evidence="ECO:0000269|PubMed:25267325"
FT MUTAGEN 904
FT /note="S->A: No effect on phosphorylation."
FT /evidence="ECO:0000269|PubMed:17483306"
FT MUTAGEN 919
FT /note="L->A: Loss of activation by lysophospholipids."
FT /evidence="ECO:0000269|PubMed:25971968"
FT MUTAGEN 922
FT /note="L->A: Increased activation by lysophospholipids."
FT /evidence="ECO:0000269|PubMed:25971968"
FT MUTAGEN 924
FT /note="T->A: No effect on phosphorylation."
FT /evidence="ECO:0000269|PubMed:17483306"
FT MUTAGEN 931
FT /note="S->A: Loss of phosphorylation and increased 14-3-3
FT protein binding."
FT /evidence="ECO:0000269|PubMed:17483306"
FT MUTAGEN 931
FT /note="S->D: Loss of interaction with 14-3-3 protein."
FT /evidence="ECO:0000269|PubMed:17483306"
FT MUTAGEN 942
FT /note="T->A: No effect on phosphorylation."
FT /evidence="ECO:0000269|PubMed:17483306"
FT MUTAGEN 947
FT /note="T->A: No effect on phosphorylation."
FT /evidence="ECO:0000269|PubMed:17483306"
FT HELIX 20..26
FT /evidence="ECO:0007829|PDB:5KSD"
FT HELIX 36..45
FT /evidence="ECO:0007829|PDB:5KSD"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:5KSD"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:5KSD"
FT HELIX 68..83
FT /evidence="ECO:0007829|PDB:5KSD"
FT TURN 84..88
FT /evidence="ECO:0007829|PDB:5KSD"
FT HELIX 90..120
FT /evidence="ECO:0007829|PDB:5KSD"
FT HELIX 122..128
FT /evidence="ECO:0007829|PDB:5KSD"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:5KSD"
FT STRAND 139..144
FT /evidence="ECO:0007829|PDB:5KSD"
FT STRAND 150..156
FT /evidence="ECO:0007829|PDB:5KSD"
FT STRAND 166..172
FT /evidence="ECO:0007829|PDB:5KSD"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:5KSD"
FT TURN 179..182
FT /evidence="ECO:0007829|PDB:5KSD"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:5KSD"
FT STRAND 201..204
FT /evidence="ECO:0007829|PDB:5KSD"
FT STRAND 207..211
FT /evidence="ECO:0007829|PDB:5KSD"
FT TURN 215..217
FT /evidence="ECO:0007829|PDB:5KSD"
FT HELIX 219..223
FT /evidence="ECO:0007829|PDB:5KSD"
FT HELIX 235..254
FT /evidence="ECO:0007829|PDB:5KSD"
FT TURN 255..257
FT /evidence="ECO:0007829|PDB:5KSD"
FT HELIX 258..265
FT /evidence="ECO:0007829|PDB:5KSD"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:5KSD"
FT HELIX 274..284
FT /evidence="ECO:0007829|PDB:5KSD"
FT HELIX 288..307
FT /evidence="ECO:0007829|PDB:5KSD"
FT HELIX 316..322
FT /evidence="ECO:0007829|PDB:5KSD"
FT STRAND 325..329
FT /evidence="ECO:0007829|PDB:5KSD"
FT HELIX 330..334
FT /evidence="ECO:0007829|PDB:5KSD"
FT HELIX 343..345
FT /evidence="ECO:0007829|PDB:5KSD"
FT TURN 355..357
FT /evidence="ECO:0007829|PDB:5KSD"
FT HELIX 358..364
FT /evidence="ECO:0007829|PDB:5KSD"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:5KSD"
FT HELIX 373..381
FT /evidence="ECO:0007829|PDB:5KSD"
FT HELIX 385..389
FT /evidence="ECO:0007829|PDB:5KSD"
FT STRAND 394..398
FT /evidence="ECO:0007829|PDB:5KSD"
FT TURN 402..404
FT /evidence="ECO:0007829|PDB:5KSD"
FT STRAND 406..413
FT /evidence="ECO:0007829|PDB:5KSD"
FT TURN 414..416
FT /evidence="ECO:0007829|PDB:5KSD"
FT STRAND 417..424
FT /evidence="ECO:0007829|PDB:5KSD"
FT HELIX 426..429
FT /evidence="ECO:0007829|PDB:5KSD"
FT TURN 430..434
FT /evidence="ECO:0007829|PDB:5KSD"
FT HELIX 437..453
FT /evidence="ECO:0007829|PDB:5KSD"
FT STRAND 456..464
FT /evidence="ECO:0007829|PDB:5KSD"
FT STRAND 478..486
FT /evidence="ECO:0007829|PDB:5KSD"
FT HELIX 493..502
FT /evidence="ECO:0007829|PDB:5KSD"
FT STRAND 506..510
FT /evidence="ECO:0007829|PDB:5KSD"
FT HELIX 515..525
FT /evidence="ECO:0007829|PDB:5KSD"
FT HELIX 534..537
FT /evidence="ECO:0007829|PDB:5KSD"
FT STRAND 538..542
FT /evidence="ECO:0007829|PDB:5KSD"
FT TURN 546..548
FT /evidence="ECO:0007829|PDB:5KSD"
FT HELIX 551..557
FT /evidence="ECO:0007829|PDB:5KSD"
FT STRAND 559..563
FT /evidence="ECO:0007829|PDB:5KSD"
FT HELIX 566..578
FT /evidence="ECO:0007829|PDB:5KSD"
FT STRAND 583..587
FT /evidence="ECO:0007829|PDB:5KSD"
FT HELIX 590..592
FT /evidence="ECO:0007829|PDB:5KSD"
FT HELIX 593..598
FT /evidence="ECO:0007829|PDB:5KSD"
FT STRAND 599..604
FT /evidence="ECO:0007829|PDB:5KSD"
FT HELIX 610..615
FT /evidence="ECO:0007829|PDB:5KSD"
FT STRAND 617..622
FT /evidence="ECO:0007829|PDB:5KSD"
FT HELIX 625..667
FT /evidence="ECO:0007829|PDB:5KSD"
FT HELIX 673..686
FT /evidence="ECO:0007829|PDB:5KSD"
FT HELIX 687..692
FT /evidence="ECO:0007829|PDB:5KSD"
FT HELIX 706..730
FT /evidence="ECO:0007829|PDB:5KSD"
FT TURN 731..733
FT /evidence="ECO:0007829|PDB:5KSD"
FT HELIX 736..739
FT /evidence="ECO:0007829|PDB:5KSD"
FT HELIX 750..773
FT /evidence="ECO:0007829|PDB:5KSD"
FT TURN 778..780
FT /evidence="ECO:0007829|PDB:5KSD"
FT HELIX 785..804
FT /evidence="ECO:0007829|PDB:5KSD"
FT TURN 808..811
FT /evidence="ECO:0007829|PDB:5KSD"
FT HELIX 817..843
FT /evidence="ECO:0007829|PDB:5KSD"
SQ SEQUENCE 948 AA; 104401 MW; 431F4021E99A3CEC CRC64;
MSSLEDIKNE TVDLEKIPIE EVFQQLKCSR EGLTTQEGED RIQIFGPNKL EEKKESKLLK
FLGFMWNPLS WVMEMAAIMA IALANGDGRP PDWQDFVGII CLLVINSTIS FIEENNAGNA
AAALMAGLAP KTKVLRDGKW SEQEAAILVP GDIVSIKLGD IIPADARLLE GDPLKVDQSA
LTGESLPVTK HPGQEVFSGS TCKQGEIEAV VIATGVHTFF GKAAHLVDST NQVGHFQKVL
TAIGNFCICS IAIGMVIEII VMYPIQRRKY RDGIDNLLVL LIGGIPIAMP TVLSVTMAIG
SHRLSQQGAI TKRMTAIEEM AGMDVLCSDK TGTLTLNKLS VDKNLVEVFC KGVEKDQVLL
FAAMASRVEN QDAIDAAMVG MLADPKEARA GIREVHFLPF NPVDKRTALT YIDGSGNWHR
VSKGAPEQIL ELAKASNDLS KKVLSIIDKY AERGLRSLAV ARQVVPEKTK ESPGAPWEFV
GLLPLFDPPR HDSAETIRRA LNLGVNVKMI TGDQLAIGKE TGRRLGMGTN MYPSSALLGT
HKDANLASIP VEELIEKADG FAGVFPEHKY EIVKKLQERK HIVGMTGDGV NDAPALKKAD
IGIAVADATD AARGASDIVL TEPGLSVIIS AVLTSRAIFQ RMKNYTIYAV SITIRIVFGF
MLIALIWEFD FSAFMVLIIA ILNDGTIMTI SKDRVKPSPT PDSWKLKEIF ATGVVLGGYQ
AIMTVIFFWA AHKTDFFSDT FGVRSIRDNN HELMGAVYLQ VSIISQALIF VTRSRSWSFV
ERPGALLMIA FLIAQLIATL IAVYANWEFA KIRGIGWGWA GVIWLYSIVT YFPLDVFKFA
IRYILSGKAW LNLFENKTAF TMKKDYGKEE REAQWALAQR TLHGLQPKEA VNIFPEKGSY
RELSEIAEQA KRRAEIARLR ELHTLKGHVE SVVKLKGLDI ETPSHYTV
