HMA6_ARATH
ID HMA6_ARATH Reviewed; 949 AA.
AC Q9SZC9; O48600; O81870; Q0WPL5; Q93YP5;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Copper-transporting ATPase PAA1, chloroplastic;
DE EC=7.2.2.8;
DE AltName: Full=Protein HEAVY METAL ATPASE 6;
DE AltName: Full=Protein glucose insensitive root 1;
DE Flags: Precursor;
GN Name=PAA1; Synonyms=GIR1, HMA6; OrderedLocusNames=At4g33520;
GN ORFNames=F17M5.280, T16L1.10;
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] (ISOFORM 1).
RC STRAIN=cv. Landsberg erecta;
RX PubMed=9188794; DOI=10.1016/s0005-2736(97)00064-3;
RA Tabata K., Kashiwagi S., Mori H., Ueguchi C., Mizuno T.;
RT "Cloning of a cDNA encoding a putative metal-transporting P-type ATPase
RT from Arabidopsis thaliana.";
RL Biochim. Biophys. Acta 1326:1-6(1997).
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] (ISOFORM 2).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=12782727; DOI=10.1105/tpc.011817;
RA Shikanai T., Muller-Moule P., Munekage Y., Niyogi K.K., Pilon M.;
RT "PAA1, a P-type ATPase of Arabidopsis, functions in copper transport in
RT chloroplasts.";
RL Plant Cell 15:1333-1346(2003).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15772282; DOI=10.1105/tpc.104.030452;
RA Abdel-Ghany S.E., Muller-Moule P., Niyogi K.K., Pilon M., Shikanai T.;
RT "Two P-type ATPases are required for copper delivery in Arabidopsis
RT thaliana chloroplasts.";
RL Plant Cell 17:1233-1251(2005).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RA Lee S.A., Chang K.S., Hwang I., Cheong H., Lim J.;
RT "Analysis of gir1 (glucose insensitive root 1) reveals that a role of the
RT chloroplastic copper transporter paa1 in sugar signaling.";
RL (In) Proceedings of the 21st international conference on Arabidopsis
RL research, abstract#08115, Yokohama (2010).
RN [9]
RP FUNCTION.
RX PubMed=21878617; DOI=10.1074/jbc.m111.241034;
RA Catty P., Boutigny S., Miras R., Joyard J., Rolland N.,
RA Seigneurin-Berny D.;
RT "Biochemical characterization of AtHMA6/PAA1, a chloroplast envelope Cu(I)-
RT ATPase.";
RL J. Biol. Chem. 286:36188-36197(2011).
CC -!- FUNCTION: Mediates copper transfer across the plastid envelope.
CC Required for the delivery of copper into the plastid stroma, which is
CC essential for the function of copper proteins. Seems to be selective
CC for monovalent copper Cu(+) transport. Also plays a role in glucose
CC signaling-mediated cell proliferation of root meristem in non-green
CC tissues. {ECO:0000269|PubMed:12782727, ECO:0000269|PubMed:15772282,
CC ECO:0000269|PubMed:21878617, ECO:0000269|Ref.8}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + Cu(+)(in) + H2O = ADP + Cu(+)(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:25792, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:49552,
CC ChEBI:CHEBI:456216; EC=7.2.2.8;
CC -!- INTERACTION:
CC Q9SZC9; Q9LF53: RGL3; NbExp=3; IntAct=EBI-4441998, EBI-15681313;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane
CC {ECO:0000269|PubMed:12782727, ECO:0000269|PubMed:15772282}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:12782727,
CC ECO:0000269|PubMed:15772282}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9SZC9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SZC9-2; Sequence=VSP_040517, VSP_040518;
CC -!- TISSUE SPECIFICITY: Expressed in the shoots and roots.
CC {ECO:0000269|PubMed:15772282}.
CC -!- DISRUPTION PHENOTYPE: High-chlorophyll-fluorescence phenotype. Short
CC roots. {ECO:0000269|PubMed:12782727, ECO:0000269|Ref.8}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IB subfamily. {ECO:0000305}.
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DR EMBL; D89981; BAA23769.1; -; mRNA.
DR EMBL; AL031394; CAA20565.1; -; Genomic_DNA.
DR EMBL; AL035678; CAB38810.1; -; Genomic_DNA.
DR EMBL; AL161583; CAB80069.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86239.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86240.1; -; Genomic_DNA.
DR EMBL; AY059869; AAL24351.1; -; mRNA.
DR EMBL; AY093320; AAM13319.1; -; mRNA.
DR EMBL; AK229051; BAF00934.1; -; mRNA.
DR PIR; T06003; T06003.
DR RefSeq; NP_567924.1; NM_119506.4. [Q9SZC9-2]
DR RefSeq; NP_974675.1; NM_202946.3. [Q9SZC9-1]
DR PDB; 5LBD; X-ray; 1.50 A; A/B=607-734.
DR PDBsum; 5LBD; -.
DR AlphaFoldDB; Q9SZC9; -.
DR SMR; Q9SZC9; -.
DR BioGRID; 14774; 5.
DR IntAct; Q9SZC9; 3.
DR STRING; 3702.AT4G33520.2; -.
DR TCDB; 3.A.3.5.11; the p-type atpase (p-atpase) superfamily.
DR PaxDb; Q9SZC9; -.
DR ProteomicsDB; 230255; -. [Q9SZC9-1]
DR EnsemblPlants; AT4G33520.1; AT4G33520.1; AT4G33520. [Q9SZC9-2]
DR EnsemblPlants; AT4G33520.2; AT4G33520.2; AT4G33520. [Q9SZC9-1]
DR GeneID; 829490; -.
DR Gramene; AT4G33520.1; AT4G33520.1; AT4G33520. [Q9SZC9-2]
DR Gramene; AT4G33520.2; AT4G33520.2; AT4G33520. [Q9SZC9-1]
DR KEGG; ath:AT4G33520; -.
DR Araport; AT4G33520; -.
DR TAIR; locus:2119265; AT4G33520.
DR eggNOG; KOG0207; Eukaryota.
DR HOGENOM; CLU_001771_0_3_1; -.
DR InParanoid; Q9SZC9; -.
DR OMA; NAPLMHL; -.
DR PhylomeDB; Q9SZC9; -.
DR BioCyc; ARA:AT4G33520-MON; -.
DR BioCyc; MetaCyc:MON-14495; -.
DR BRENDA; 7.2.2.9; 399.
DR PRO; PR:Q9SZC9; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SZC9; baseline and differential.
DR Genevisible; Q9SZC9; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; IDA:TAIR.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0016531; F:copper chaperone activity; IDA:TAIR.
DR GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR GO; GO:0005375; F:copper ion transmembrane transporter activity; IMP:TAIR.
DR GO; GO:0043682; F:P-type divalent copper transporter activity; IBA:GO_Central.
DR GO; GO:0140581; F:P-type monovalent copper transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0055070; P:copper ion homeostasis; IDA:TAIR.
DR GO; GO:0035434; P:copper ion transmembrane transport; IMP:UniProtKB.
DR GO; GO:0009767; P:photosynthetic electron transport chain; IMP:UniProtKB.
DR CDD; cd00371; HMA; 1.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
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; IPR017969; Heavy-metal-associated_CS.
DR InterPro; IPR006121; HMA_dom.
DR InterPro; IPR036163; HMA_dom_sf.
DR InterPro; IPR027256; P-typ_ATPase_IB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR Pfam; PF00403; HMA; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF55008; SSF55008; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01525; ATPase-IB_hvy; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01047; HMA_1; 1.
DR PROSITE; PS50846; HMA_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Chloroplast; Copper;
KW Copper transport; Ion transport; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Plastid; Reference proteome; Transit peptide;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..103
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 104..949
FT /note="Copper-transporting ATPase PAA1, chloroplastic"
FT /id="PRO_0000046403"
FT TRANSMEM 253..274
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..306
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 314..334
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 349..369
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 502..524
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 543..560
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 863..882
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 895..913
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 148..222
FT /note="HMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT REGION 113..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 925..949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 925..941
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 598
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 159
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 162
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 807..814
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 808
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 812
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT VAR_SEQ 225..237
FT /note="DLVTENFFKVFET -> GEVPEDIAGEFAP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_040517"
FT VAR_SEQ 238..949
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_040518"
FT VARIANT 215
FT /note="T -> S (in strain: cv. Landsberg erecta)"
FT VARIANT 238..239
FT /note="KT -> QP (in strain: cv. Landsberg erecta)"
FT VARIANT 259
FT /note="L -> P (in strain: cv. Landsberg erecta)"
FT VARIANT 384
FT /note="P -> A (in strain: cv. Landsberg erecta)"
FT VARIANT 904
FT /note="S -> T (in strain: cv. Landsberg erecta)"
FT STRAND 609..614
FT /evidence="ECO:0007829|PDB:5LBD"
FT HELIX 629..640
FT /evidence="ECO:0007829|PDB:5LBD"
FT HELIX 646..655
FT /evidence="ECO:0007829|PDB:5LBD"
FT STRAND 671..673
FT /evidence="ECO:0007829|PDB:5LBD"
FT TURN 674..676
FT /evidence="ECO:0007829|PDB:5LBD"
FT STRAND 677..682
FT /evidence="ECO:0007829|PDB:5LBD"
FT STRAND 685..690
FT /evidence="ECO:0007829|PDB:5LBD"
FT HELIX 692..697
FT /evidence="ECO:0007829|PDB:5LBD"
FT HELIX 704..710
FT /evidence="ECO:0007829|PDB:5LBD"
FT STRAND 718..723
FT /evidence="ECO:0007829|PDB:5LBD"
FT STRAND 726..734
FT /evidence="ECO:0007829|PDB:5LBD"
SQ SEQUENCE 949 AA; 99997 MW; 716F5E6E63B7F9B8 CRC64;
MESTLSAFST VKATAMARSS GGPSLPLLTI SKALNRHFTG ARHLHPLLLA RCSPSVRRLG
GFHGSRFTSS NSALRSLGAA VLPVIRHRLE CLSSSSPSFR SISSGGGSGF GGYNGGSGGG
GGGGSESGDS KSKLGANASD GVSVPSSDII ILDVGGMTCG GCSASVKKIL ESQPQVASAS
VNLTTETAIV WPVPEAKSVP DWQKSLGETL ANHLTNCGFQ STPRDLVTEN FFKVFETKTK
DKQARLKESG RELAVSWALC AVCLVGHLTH FLGVNAPWIH AIHSTGFHVS LCLITLLGPG
RKLVLDGIKS LLKGSPNMNT LVGLGALSSF SVSSLAAMIP KLGWKTFFEE PVMLIAFVLL
GRNLEQRAKI KATSDMTGLL SVLPSKARLL LDGDLQNSTV EVPCNSLSVG DLVVILPGDR
VPADGVVKSG RSTIDESSFT GEPLPVTKES GSQVAAGSIN LNGTLTVEVH RSGGETAVGD
IIRLVEEAQS REAPVQQLVD KVAGRFTYGV MALSAATFTF WNLFGAHVLP SALHNGSPMS
LALQLSCSVL VVACPCALGL ATPTAMLVGT SLGARRGLLL RGGDILEKFS LVDTVVFDKT
GTLTKGHPVV TEVIIPENPR HNLNDTWSEV EVLMLAAAVE SNTTHPVGKA IVKAARARNC
QTMKAEDGTF TEEPGSGAVA IVNNKRVTVG TLEWVKRHGA TGNSLLALEE HEINNQSVVY
IGVDNTLAAV IRFEDKVRED AAQVVENLTR QGIDVYMLSG DKRNAANYVA SVVGINHERV
IAGVKPAEKK NFINELQKNK KIVAMVGDGI NDAAALASSN VGVAMGGGAG AASEVSPVVL
MGNRLTQLLD AMELSRQTMK TVKQNLWWAF GYNIVGIPIA AGVLLPLTGT MLTPSMAGAL
MGVSSLGVMT NSLLLRYRFF SNRNDKNVKP EPKEGTKQPH ENTRWKQSS
