NHX1_ARATH
ID NHX1_ARATH Reviewed; 538 AA.
AC Q68KI4; O04655; Q8LRL1; Q9ZPK3;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Sodium/hydrogen exchanger 1;
DE AltName: Full=Na(+)/H(+) exchanger 1;
DE Short=NHE-1;
GN Name=NHX1; OrderedLocusNames=At5g27150; ORFNames=T21B4.60;
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], FUNCTION, AND INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=9990049; DOI=10.1073/pnas.96.4.1480;
RA Gaxiola R.A., Rao R., Sherman A., Grisafi P., Alper S.L., Fink G.R.;
RT "The Arabidopsis thaliana proton transporters, AtNhx1 and Avp1, can
RT function in cation detoxification in yeast.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:1480-1485(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=10767428; DOI=10.1016/s0014-5793(00)01412-5;
RA Quintero F.J., Blatt M.R., Pardo J.M.;
RT "Functional conservation between yeast and plant endosomal Na(+)/H(+)
RT antiporters.";
RL FEBS Lett. 471:224-228(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Baek S.H., Kim H.S., Lee Y.T., Lee M.H., Yun S.J.;
RT "Isolation and characterization of a Na(+)/H(+) antiporter gene from
RT Arabidopsis.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Wang D., Zhang J.L., Zhang J.W.;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [6]
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 [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10455050; DOI=10.1126/science.285.5431.1256;
RA Apse M.P., Aharon G.S., Snedden W.A., Blumwald E.;
RT "Salt tolerance conferred by overexpression of a vacuolar Na(+)/H(+)
RT antiport in Arabidopsis.";
RL Science 285:1256-1258(1999).
RN [8]
RP FUNCTION, AND REGULATION.
RX PubMed=10998367; DOI=10.1042/0264-6021:3510241;
RA Darley C.P., van Wuytswinkel O.C.M., van der Woude K., Mager W.H.,
RA de Boer A.H.;
RT "Arabidopsis thaliana and Saccharomyces cerevisiae NHX1 genes encode
RT amiloride sensitive electroneutral Na(+)/H(+) exchangers.";
RL Biochem. J. 351:241-249(2000).
RN [9]
RP FUNCTION, AND BIOTECHNOLOGICAL RELEVANCE.
RX PubMed=11606781; DOI=10.1073/pnas.231476498;
RA Zhang H.-X., Hodson J.N., Williams J.P., Blumwald E.;
RT "Engineering salt-tolerant Brassica plants: characterization of yield and
RT seed oil quality in transgenic plants with increased vacuolar sodium
RT accumulation.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:12832-12836(2001).
RN [10]
RP FUNCTION, AND REGULATION.
RX PubMed=11707435; DOI=10.1074/jbc.m105043200;
RA Venema K., Quintero F.J., Pardo J.M., Donaire J.P.;
RT "The Arabidopsis Na(+)/H(+) exchanger AtNHX1 catalyzes low affinity Na(+)
RT and K(+) transport in reconstituted liposomes.";
RL J. Biol. Chem. 277:2413-2418(2002).
RN [11]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=12047628; DOI=10.1046/j.1365-313x.2002.01309.x;
RA Yokoi S., Quintero F.J., Cubero B., Ruiz M.T., Bressan R.A., Hasegawa P.M.,
RA Pardo J.M.;
RT "Differential expression and function of Arabidopsis thaliana NHX
RT Na(+)/H(+) antiporters in the salt stress response.";
RL Plant J. 30:529-539(2002).
RN [12]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=12369629; DOI=10.1023/a:1019859319617;
RA Shi H., Zhu J.-K.;
RT "Regulation of expression of the vacuolar Na(+)/H(+) antiporter gene AtNHX1
RT by salt stress and abscisic acid.";
RL Plant Mol. Biol. 50:543-550(2002).
RN [13]
RP FUNCTION, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=14535887; DOI=10.1046/j.1365-313x.2003.01871.x;
RA Apse M.P., Sottosanto J.B., Blumwald E.;
RT "Vacuolar cation/H(+) exchange, ion homeostasis, and leaf development are
RT altered in a T-DNA insertional mutant of AtNHX1, the Arabidopsis vacuolar
RT Na(+)/H(+) antiporter.";
RL Plant J. 36:229-239(2003).
RN [14]
RP TOPOLOGY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=14530406; DOI=10.1073/pnas.2034966100;
RA Yamaguchi T., Apse M.P., Shi H., Blumwald E.;
RT "Topological analysis of a plant vacuolar Na(+)/H(+) antiporter reveals a
RT luminal C-terminus that regulates antiporter cation selectivity.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:12510-12515(2003).
RN [15]
RP FUNCTION, AND BIOTECHNOLOGICAL RELEVANCE.
RX PubMed=16179357; DOI=10.1093/pcp/pci201;
RA He C., Yan J., Shen G., Fu L., Holaday A.S., Auld D., Blumwald E.,
RA Zhang H.-X.;
RT "Expression of an Arabidopsis vacuolar sodium/proton antiporter gene in
RT cotton improves photosynthetic performance under salt conditions and
RT increases fiber yield in the field.";
RL Plant Cell Physiol. 46:1848-1854(2005).
RN [16]
RP INTERACTION WITH CML18/CAM15, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP REGULATION.
RX PubMed=16249341; DOI=10.1073/pnas.0504437102;
RA Yamaguchi T., Aharon G.S., Sottosanto J.B., Blumwald E.;
RT "Vacuolar Na(+)/H(+) antiporter cation selectivity is regulated by
RT calmodulin from within the vacuole in a Ca2(+)- and pH-dependent manner.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:16107-16112(2005).
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).
CC -!- FUNCTION: Acts in low affinity electroneutral exchange of protons for
CC cations such as Na(+) or K(+) across membranes. Can also exchange Li(+)
CC and Cs(+) with a lower affinity. Involved in vacuolar ion
CC compartmentalization necessary for cell volume regulation and
CC cytoplasmic Na(+) detoxification. Required during leaves expansion,
CC probably to stimulate epidermal cell expansion. Confers competence to
CC grow in high salinity conditions. {ECO:0000269|PubMed:10455050,
CC ECO:0000269|PubMed:10767428, ECO:0000269|PubMed:10998367,
CC ECO:0000269|PubMed:11606781, ECO:0000269|PubMed:11707435,
CC ECO:0000269|PubMed:14535887, ECO:0000269|PubMed:16179357,
CC ECO:0000269|PubMed:9990049}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(out) + Na(+)(in) = H(+)(in) + Na(+)(out);
CC Xref=Rhea:RHEA:29419, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101;
CC Evidence={ECO:0000269|PubMed:11707435};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(out) + K(+)(in) = H(+)(in) + K(+)(out);
CC Xref=Rhea:RHEA:29467, ChEBI:CHEBI:15378, ChEBI:CHEBI:29103;
CC Evidence={ECO:0000269|PubMed:11707435};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=24 mM for Na(+) (without CML18/CAM15)
CC {ECO:0000269|PubMed:14530406, ECO:0000269|PubMed:16249341};
CC KM=15 mM for Na(+) (in presence of CML18/CAM15)
CC {ECO:0000269|PubMed:14530406, ECO:0000269|PubMed:16249341};
CC KM=12 mM for K(+) (without CML18/CAM15) {ECO:0000269|PubMed:14530406,
CC ECO:0000269|PubMed:16249341};
CC KM=17 mM for K(+) (in presence of CML18/CAM15)
CC {ECO:0000269|PubMed:14530406, ECO:0000269|PubMed:16249341};
CC -!- SUBUNIT: Calcium and pH-dependent interaction with CML18/CAM15
CC (increases when pH decreases, better at pH 5.5 than at pH 7.5).
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:10455050};
CC Multi-pass membrane protein {ECO:0000269|PubMed:10455050}. Endoplasmic
CC reticulum membrane {ECO:0000305|PubMed:10455050}; Multi-pass membrane
CC protein {ECO:0000305|PubMed:10455050}. Golgi apparatus membrane
CC {ECO:0000305|PubMed:10455050}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:10455050}. Note=Tonoplast. Possibly also present in
CC endoplasmic reticulum (ER) and Golgi apparatus.
CC -!- TISSUE SPECIFICITY: Ubiquitous, with higher levels around vascular
CC tissues and guard cells. {ECO:0000269|PubMed:10767428,
CC ECO:0000269|PubMed:12047628, ECO:0000269|PubMed:12369629,
CC ECO:0000269|PubMed:14535887}.
CC -!- DEVELOPMENTAL STAGE: Present in flowers, particularly in petals,
CC stamens and anthers (including pollen). Slightly expressed in
CC developing ovaries, strongly expressed in developing embryos and in
CC siliques outer integuments (mostly in base and tips). During first days
CC after germination, mainly localized in roots, including root tips.
CC Later, ubiquitous except in root tips. {ECO:0000269|PubMed:12369629,
CC ECO:0000269|PubMed:14535887}.
CC -!- INDUCTION: Induced by NaCl, KCl and sorbitol in a ABA-dependent but SOS
CC signaling-independent manner. Also induced by abscisic acid (ABA).
CC {ECO:0000269|PubMed:10767428, ECO:0000269|PubMed:12047628,
CC ECO:0000269|PubMed:12369629, ECO:0000269|PubMed:9990049}.
CC -!- BIOTECHNOLOGY: Transgenic plants of agricultural interest (e.g. cotton,
CC Brassica napus) that overexpress NHX1 have enhanced capability to grow
CC on high saline soils. {ECO:0000269|PubMed:11606781,
CC ECO:0000269|PubMed:16179357}.
CC -!- MISCELLANEOUS: Inhibition of Na(+) transport activity but not of K(+)
CC transport activity is mediated by binding with CML18/CAM15. Inhibited
CC by the diuretic compound amiloride and its analogs ethylisopropyl-
CC amiloride (EIPA), 5-(N-ethyl-N-isopropyl)amiloride (MIA), and benzamil.
CC Also down-regulated by quinine.
CC -!- SIMILARITY: Belongs to the monovalent cation:proton antiporter 1 (CPA1)
CC transporter (TC 2.A.36) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB61069.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF106324; AAD16946.1; -; mRNA.
DR EMBL; AF056190; AAF21755.1; -; mRNA.
DR EMBL; AF510074; AAM34759.1; -; mRNA.
DR EMBL; AY685183; AAT95387.1; -; mRNA.
DR EMBL; AF007271; AAB61069.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED93655.1; -; Genomic_DNA.
DR PIR; T01804; T01804.
DR RefSeq; NP_198067.1; NM_122597.3.
DR AlphaFoldDB; Q68KI4; -.
DR SMR; Q68KI4; -.
DR BioGRID; 18047; 6.
DR IntAct; Q68KI4; 3.
DR STRING; 3702.AT5G27150.1; -.
DR TCDB; 2.A.36.5.1; the monovalent cation:proton antiporter-1 (cpa1) family.
DR iPTMnet; Q68KI4; -.
DR PaxDb; Q68KI4; -.
DR PRIDE; Q68KI4; -.
DR ProteomicsDB; 250532; -.
DR EnsemblPlants; AT5G27150.1; AT5G27150.1; AT5G27150.
DR GeneID; 832773; -.
DR Gramene; AT5G27150.1; AT5G27150.1; AT5G27150.
DR KEGG; ath:AT5G27150; -.
DR Araport; AT5G27150; -.
DR TAIR; locus:2181246; AT5G27150.
DR eggNOG; KOG1965; Eukaryota.
DR HOGENOM; CLU_005912_11_2_1; -.
DR InParanoid; Q68KI4; -.
DR OMA; HYHFNAL; -.
DR OrthoDB; 546232at2759; -.
DR PhylomeDB; Q68KI4; -.
DR PRO; PR:Q68KI4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q68KI4; baseline and differential.
DR Genevisible; Q68KI4; AT.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000325; C:plant-type vacuole; TAS:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005773; C:vacuole; IDA:TAIR.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0015386; F:potassium:proton antiporter activity; IBA:GO_Central.
DR GO; GO:0015385; F:sodium:proton antiporter activity; IDA:TAIR.
DR GO; GO:0048366; P:leaf development; IMP:TAIR.
DR GO; GO:0055075; P:potassium ion homeostasis; IGI:TAIR.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0051453; P:regulation of intracellular pH; IBA:GO_Central.
DR GO; GO:0090333; P:regulation of stomatal closure; IGI:TAIR.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR GO; GO:0098719; P:sodium ion import across plasma membrane; IBA:GO_Central.
DR InterPro; IPR006153; Cation/H_exchanger.
DR InterPro; IPR018422; Cation/H_exchanger_CPA1.
DR InterPro; IPR004709; NaH_exchanger.
DR PANTHER; PTHR10110; PTHR10110; 1.
DR Pfam; PF00999; Na_H_Exchanger; 1.
DR PRINTS; PR01084; NAHEXCHNGR.
DR TIGRFAMs; TIGR00840; b_cpa1; 1.
PE 1: Evidence at protein level;
KW Antiport; Calmodulin-binding; Endoplasmic reticulum; Glycoprotein;
KW Golgi apparatus; Ion transport; Membrane; Potassium; Potassium transport;
KW Reference proteome; Sodium; Sodium transport; Transmembrane;
KW Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..538
FT /note="Sodium/hydrogen exchanger 1"
FT /id="PRO_0000052372"
FT TOPO_DOM 1..19
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 41..45
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 67..73
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 95..106
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 128..146
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT INTRAMEM 147..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT INTRAMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 193..216
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 238..262
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 284..302
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 303..323
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 324..342
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 343..363
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 364..378
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 379..399
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 400..413
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 414..434
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 435..538
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT REGION 496..518
FT /note="Interaction with CML18/CAM15"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 447
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 41
FT /note="E -> K (in Ref. 4; AAT95387)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="G -> S (in Ref. 3; AAM34759)"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="L -> M (in Ref. 3; AAM34759)"
FT /evidence="ECO:0000305"
FT CONFLICT 483
FT /note="R -> Q (in Ref. 4; AAT95387)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 538 AA; 59513 MW; 1189AD6C5C726996 CRC64;
MLDSLVSKLP SLSTSDHASV VALNLFVALL CACIVLGHLL EENRWMNESI TALLIGLGTG
VTILLISKGK SSHLLVFSED LFFIYLLPPI IFNAGFQVKK KQFFRNFVTI MLFGAVGTII
SCTIISLGVT QFFKKLDIGT FDLGDYLAIG AIFAATDSVC TLQVLNQDET PLLYSLVFGE
GVVNDATSVV VFNAIQSFDL THLNHEAAFH LLGNFLYLFL LSTLLGAATG LISAYVIKKL
YFGRHSTDRE VALMMLMAYL SYMLAELFDL SGILTVFFCG IVMSHYTWHN VTESSRITTK
HTFATLSFLA ETFIFLYVGM DALDIDKWRS VSDTPGTSIA VSSILMGLVM VGRAAFVFPL
SFLSNLAKKN QSEKINFNMQ VVIWWSGLMR GAVSMALAYN KFTRAGHTDV RGNAIMITST
ITVCLFSTVV FGMLTKPLIS YLLPHQNATT SMLSDDNTPK SIHIPLLDQD SFIEPSGNHN
VPRPDSIRGF LTRPTRTVHY YWRQFDDSFM RPVFGGRGFV PFVPGSPTER NPPDLSKA
