AMT11_ARATH
ID AMT11_ARATH Reviewed; 501 AA.
AC P54144; Q94C23;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Ammonium transporter 1 member 1;
DE Short=AtAMT1;1;
GN Name=AMT1-1; OrderedLocusNames=At4g13510; ORFNames=T6G15.60;
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].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=8062823; DOI=10.1002/j.1460-2075.1994.tb06652.x;
RA Ninnemann O., Janniaux J.-C., Frommer W.B.;
RT "Identification of a high affinity NH4+ transporter from plants.";
RL EMBO J. 13:3464-3471(1994).
RN [2]
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 [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 TISSUE SPECIFICITY.
RC STRAIN=cv. C24;
RX PubMed=10330477; DOI=10.2307/3870826;
RA Gazzarrini S., Lejay L., Gojon A., Ninnemann O., Frommer W.B.,
RA von Wiren N.;
RT "Three functional transporters for constitutive, diurnally regulated, and
RT starvation-induced uptake of ammonium into Arabidopsis roots.";
RL Plant Cell 11:937-948(1999).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=12427993; DOI=10.1104/pp.102.010843;
RA Kaiser B.N., Rawat S.R., Siddiqi M.Y., Masle J., Glass A.D.M.;
RT "Functional analysis of an Arabidopsis T-DNA 'knockout' of the high-
RT affinity NH4(+) transporter AtAMT1;1.";
RL Plant Physiol. 130:1263-1275(2002).
RN [7]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=12481062; DOI=10.1104/pp.008599;
RA Sohlenkamp C., Wood C.C., Roeb G.W., Udvardi M.K.;
RT "Characterization of Arabidopsis AtAMT2, a high-affinity ammonium
RT transporter of the plasma membrane.";
RL Plant Physiol. 130:1788-1796(2002).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-460, AND IDENTIFICATION BY
RP 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 [9]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-460,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [10]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=16806203; DOI=10.1016/j.febslet.2006.06.026;
RA Wood C.C., Poree F., Dreyer I., Koehler G.J., Udvardi M.K.;
RT "Mechanisms of ammonium transport, accumulation, and retention in ooyctes
RT and yeast cells expressing Arabidopsis AtAMT1;1.";
RL FEBS Lett. 580:3931-3936(2006).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=16917981; DOI=10.1055/s-2006-923877;
RA Mayer M., Ludewig U.;
RT "Role of AMT1;1 in NH4+ acquisition in Arabidopsis thaliana.";
RL Plant Biol. 8:522-528(2006).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=17026539; DOI=10.1111/j.1365-313x.2006.02887.x;
RA Loque D., Yuan L., Kojima S., Gojon A., Wirth J., Gazzarrini S.,
RA Ishiyama K., Takahashi H., von Wiren N.;
RT "Additive contribution of AMT1;1 and AMT1;3 to high-affinity ammonium
RT uptake across the plasma membrane of nitrogen-deficient Arabidopsis
RT roots.";
RL Plant J. 48:522-534(2006).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-460; SER-490 AND SER-492, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17869214; DOI=10.1016/j.bbrc.2007.08.177;
RA Hem S., Rofidal V., Sommerer N., Rossignol M.;
RT "Novel subsets of the Arabidopsis plasmalemma phosphoproteome identify
RT phosphorylation sites in secondary active transporters.";
RL Biochem. Biophys. Res. Commun. 363:375-380(2007).
RN [14]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=17085512; DOI=10.1104/pp.106.088500;
RA Engineer C.B., Kranz R.G.;
RT "Reciprocal leaf and root expression of AtAmt1.1 and root architectural
RT changes in response to nitrogen starvation.";
RL Plant Physiol. 143:236-250(2007).
RN [15]
RP INDUCTION.
RX PubMed=17172286; DOI=10.1104/pp.106.093237;
RA Yuan L., Loque D., Ye F., Frommer W.B., von Wiren N.;
RT "Nitrogen-dependent posttranscriptional regulation of the ammonium
RT transporter AtAMT1;1.";
RL Plant Physiol. 143:732-744(2007).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-475, 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-460, 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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488, AND IDENTIFICATION BY
RP 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 [19]
RP SUBUNIT, AND INTERACTION WITH CEPR2; AT2G28990 AND PAM74.
RX PubMed=21423366; DOI=10.3389/fphys.2010.00024;
RA Lalonde S., Sero A., Pratelli R., Pilot G., Chen J., Sardi M.I.,
RA Parsa S.A., Kim D.Y., Acharya B.R., Stein E.V., Hu H.C., Villiers F.,
RA Takeda K., Yang Y., Han Y.S., Schwacke R., Chiang W., Kato N., Loque D.,
RA Assmann S.M., Kwak J.M., Schroeder J.I., Rhee S.Y., Frommer W.B.;
RT "A membrane protein/signaling protein interaction network for Arabidopsis
RT version AMPv2.";
RL Front. Physiol. 1:24-24(2010).
CC -!- FUNCTION: High affinity ammonium transporter probably involved in
CC ammonium uptake from the soil, long-distance transport to the shoots
CC and re-uptake of apoplastic ammonium that derives from photorespiration
CC in shoots. Contributes with AMT1-3 to the overall ammonium uptake
CC capacity in roots under nitrogen-deficiency conditions.
CC {ECO:0000269|PubMed:12481062, ECO:0000269|PubMed:16806203,
CC ECO:0000269|PubMed:16917981, ECO:0000269|PubMed:17026539}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=22 uM for ammonium chloride (at external pH 6.1)
CC {ECO:0000269|PubMed:12481062, ECO:0000269|PubMed:16806203};
CC Note=Measured in yeast knockout mutant YCW012.;
CC -!- SUBUNIT: Self interacts. Interacts with the receptor protein kinases
CC CEPR2, At2g28990 and PAM74. {ECO:0000269|PubMed:21423366}.
CC -!- INTERACTION:
CC P54144; Q9SQH9: AMT1-3; NbExp=3; IntAct=EBI-16426081, EBI-16716530;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15308754,
CC ECO:0000269|PubMed:16917981, ECO:0000269|PubMed:17026539}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:15308754,
CC ECO:0000269|PubMed:16917981, ECO:0000269|PubMed:17026539}.
CC -!- TISSUE SPECIFICITY: Highly expressed in roots. Expressed in root tips,
CC root hairs, root epidermis, rhizodermis, cortex and pericycle.
CC Expressed in leaves epidermal and mesophyll cells.
CC {ECO:0000269|PubMed:10330477, ECO:0000269|PubMed:16917981,
CC ECO:0000269|PubMed:17026539, ECO:0000269|PubMed:17085512}.
CC -!- INDUCTION: By nitrogen deprivation in roots and nitrogen supply in
CC leaves. {ECO:0000269|PubMed:16917981, ECO:0000269|PubMed:17026539,
CC ECO:0000269|PubMed:17085512, ECO:0000269|PubMed:17172286}.
CC -!- DISRUPTION PHENOTYPE: No effect on ammonium uptake. Higher expression
CC of AMT1-2; AMT1-3 and AMT2-1. {ECO:0000269|PubMed:12427993}.
CC -!- SIMILARITY: Belongs to the ammonia transporter channel (TC 1.A.11.2)
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK59819.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAM47470.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X75879; CAA53473.1; -; mRNA.
DR EMBL; AL049656; CAB41109.1; -; Genomic_DNA.
DR EMBL; AL161536; CAB78393.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83287.1; -; Genomic_DNA.
DR EMBL; AY037219; AAK59819.1; ALT_FRAME; mRNA.
DR EMBL; AY113167; AAM47470.1; ALT_FRAME; mRNA.
DR PIR; T06653; T06653.
DR RefSeq; NP_193087.1; NM_117425.2.
DR AlphaFoldDB; P54144; -.
DR SMR; P54144; -.
DR BioGRID; 12280; 48.
DR ComplexPortal; CPX-1330; AMT1-1 homotrimer.
DR ComplexPortal; CPX-3582; AMT1-1 - AMT1-3 heterotrimer, variant 1.
DR ComplexPortal; CPX-3583; AMT1-1 - AMT1-3 heterotrimer, variant 2.
DR IntAct; P54144; 34.
DR STRING; 3702.AT4G13510.1; -.
DR TCDB; 1.A.11.2.1; the ammonium transporter channel (amt) family.
DR iPTMnet; P54144; -.
DR MetOSite; P54144; -.
DR PaxDb; P54144; -.
DR PRIDE; P54144; -.
DR ProteomicsDB; 244466; -.
DR EnsemblPlants; AT4G13510.1; AT4G13510.1; AT4G13510.
DR GeneID; 826983; -.
DR Gramene; AT4G13510.1; AT4G13510.1; AT4G13510.
DR KEGG; ath:AT4G13510; -.
DR Araport; AT4G13510; -.
DR TAIR; locus:2140877; AT4G13510.
DR eggNOG; KOG0682; Eukaryota.
DR HOGENOM; CLU_000445_33_1_1; -.
DR InParanoid; P54144; -.
DR OMA; IWLSIMS; -.
DR OrthoDB; 910733at2759; -.
DR PhylomeDB; P54144; -.
DR BioCyc; ARA:AT4G13510-MON; -.
DR BioCyc; MetaCyc:AT4G13510-MON; -.
DR SABIO-RK; P54144; -.
DR PRO; PR:P54144; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P54144; differential.
DR Genevisible; P54144; AT.
DR GO; GO:0110067; C:ammonium transmembrane transporter complex; IDA:ComplexPortal.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0008519; F:ammonium transmembrane transporter activity; IDA:TAIR.
DR GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
DR GO; GO:0097272; P:ammonium homeostasis; IBA:GO_Central.
DR GO; GO:0072488; P:ammonium transmembrane transport; IMP:ComplexPortal.
DR GO; GO:0080181; P:lateral root branching; IMP:TAIR.
DR GO; GO:0010311; P:lateral root formation; IMP:TAIR.
DR GO; GO:0051258; P:protein polymerization; IDA:TAIR.
DR Gene3D; 1.10.3430.10; -; 1.
DR InterPro; IPR029020; Ammonium/urea_transptr.
DR InterPro; IPR001905; Ammonium_transpt.
DR InterPro; IPR018047; Ammonium_transpt_CS.
DR InterPro; IPR024041; NH4_transpt_AmtB-like_dom.
DR Pfam; PF00909; Ammonium_transp; 1.
DR TIGRFAMs; TIGR00836; amt; 1.
DR PROSITE; PS01219; AMMONIUM_TRANSP; 1.
PE 1: Evidence at protein level;
KW Ammonia transport; Cell membrane; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..501
FT /note="Ammonium transporter 1 member 1"
FT /id="PRO_0000224180"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 333..353
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 366..386
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 419..439
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 460
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:14506206,
FT ECO:0007744|PubMed:15308754, ECO:0007744|PubMed:17869214,
FT ECO:0007744|PubMed:19245862"
FT MOD_RES 475
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157"
FT MOD_RES 488
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 490
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17869214"
FT MOD_RES 492
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17869214"
SQ SEQUENCE 501 AA; 53577 MW; 070BAF8228302BFF CRC64;
MSCSATDLAV LLGPNATAAA NYICGQLGDV NNKFIDTAFA IDNTYLLFSA YLVFSMQLGF
AMLCAGSVRA KNTMNIMLTN VLDAAAGGLF YYLFGYAFAF GSPSNGFIGK HYFGLKDIPT
ASADYSNFLY QWAFAIAAAG ITSGSIAERT QFVAYLIYSS FLTGFVYPVV SHWFWSVDGW
ASPFRTDGDL LFSTGAIDFA GSGVVHMVGG IAGLWGALIE GPRLGRFDNG GRAIALRGHS
ASLVVLGTFL LWFGWYGFNP GSFNKILVTY ETGTYNGQWS AVGRTAVTTT LAGCTAALTT
LFGKRLLSGH WNVTDVCNGL LGGFAAITGG CSVVEPWAAI ICGFVAALVL LGCNKLAEKL
KYDDPLEAAQ LHGGCGAWGL IFTALFAQEK YLNQIYGNKP GRPHGLFMGG GGKLLGAQLI
QIIVITGWVS ATMGTLFFIL KKMKLLRISS EDEMAGMDMT RHGGFAYMYF DDDESHKAIQ
LRRVEPRSPS PSGANTTPTP V
