ALA3_ARATH
ID ALA3_ARATH Reviewed; 1213 AA.
AC Q9XIE6; Q8RWQ3;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2003, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Phospholipid-transporting ATPase 3 {ECO:0000303|PubMed:11402198};
DE Short=AtALA3 {ECO:0000303|PubMed:11402198};
DE EC=7.6.2.1 {ECO:0000305|PubMed:11402198};
DE AltName: Full=Aminophospholipid ATPase 3 {ECO:0000303|PubMed:11402198};
DE AltName: Full=Aminophospholipid flippase 3 {ECO:0000303|PubMed:11402198};
DE AltName: Full=Protein ABERRANT LOCALIZATION OF PEN3 3 {ECO:0000303|PubMed:28434950};
DE AltName: Full=Protein IRREGULAR TRICHOME BRANCH 2 {ECO:0000303|PubMed:19566596};
GN Name=ALA3 {ECO:0000303|PubMed:11402198};
GN Synonyms=ALP3 {ECO:0000303|PubMed:28434950},
GN ITB2 {ECO:0000303|PubMed:19566596};
GN OrderedLocusNames=At1g59820 {ECO:0000312|Araport:AT1G59820};
GN ORFNames=F23H11.14 {ECO:0000312|EMBL:AAD39325.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
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 [3]
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 [4]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11402198; DOI=10.1104/pp.126.2.696;
RA Axelsen K.B., Palmgren M.G.;
RT "Inventory of the superfamily of P-type ion pumps in Arabidopsis.";
RL Plant Physiol. 126:696-706(2001).
RN [5]
RP FUNCTION, MUTAGENESIS OF ASP-413, DISRUPTION PHENOTYPE, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH ALIS1; ALIS3 AND ALIS5.
RX PubMed=18344284; DOI=10.1105/tpc.107.054767;
RA Poulsen L.R., Lopez-Marques R.L., McDowell S.C., Okkeri J., Licht D.,
RA Schulz A., Pomorski T., Harper J.F., Palmgren M.G.;
RT "The Arabidopsis P4-ATPase ALA3 localizes to the Golgi and requires a beta-
RT subunit to function in lipid translocation and secretory vesicle
RT formation.";
RL Plant Cell 20:658-676(2008).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=19566596; DOI=10.1111/j.1365-313x.2009.03954.x;
RA Zhang X., Oppenheimer D.G.;
RT "IRREGULAR TRICHOME BRANCH 2 (ITB2) encodes a putative aminophospholipid
RT translocase that regulates trichome branch elongation in Arabidopsis.";
RL Plant J. 60:195-206(2009).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ALIS1; ALIS3 AND
RP ALIS5.
RX PubMed=20053675; DOI=10.1091/mbc.e09-08-0656;
RA Lopez-Marques R.L., Poulsen L.R., Hanisch S., Meffert K.,
RA Buch-Pedersen M.J., Jakobsen M.K., Pomorski T.G., Palmgren M.G.;
RT "Intracellular targeting signals and lipid specificity determinants of the
RT ALA/ALIS P4-ATPase complex reside in the catalytic ALA alpha-subunit.";
RL Mol. Biol. Cell 21:791-801(2010).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23667493; DOI=10.1371/journal.pone.0062577;
RA McDowell S.C., Lopez-Marques R.L., Poulsen L.R., Palmgren M.G.,
RA Harper J.F.;
RT "Loss of the Arabidopsis thaliana P(4)-ATPase ALA3 reduces adaptability to
RT temperature stresses and impairs vegetative, pollen, and ovule
RT development.";
RL PLoS ONE 8:E62577-E62577(2013).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=28434950; DOI=10.1016/j.molp.2017.04.003;
RA Underwood W., Ryan A., Somerville S.C.;
RT "An Arabidopsis lipid flippase is required for timely recruitment of
RT defenses to the host-pathogen interface at the plant cell surface.";
RL Mol. Plant 10:805-820(2017).
CC -!- FUNCTION: Involved in transport of phospholipids. Contributes to
CC transmembrane flipping of lipids. Required for secretory processes
CC during plant development. Requires an interaction with an ALIS protein
CC for activity. Has activity with phosphatidylserine, phosphatidylcholine
CC and phosphatidylethanolamine, but not with lysolipid (PubMed:18344284,
CC PubMed:19566596, PubMed:20053675). Modifies endomembranes in multiple
CC cell types, enabling structural changes, or signaling functions that
CC are critical for normal development and adaptation to varied growth
CC environments (PubMed:23667493). Required for the trafficking and
CC endocytic recycling of ABCG36/PEN3 between the trans-Golgi network and
CC the plasma membrane; thus promoting ABCG36/PEN3 recruitment to the
CC host-pathogen interface upon infection by powdery mildews (e.g.
CC Blumeria graminis) and bacteria (e.g. Pseudomonas syringae), or upon
CC the detection of pathogen-associated molecular patterns (PAMPs) (e.g.
CC flg22 and chitin) (PubMed:28434950). {ECO:0000269|PubMed:18344284,
CC ECO:0000269|PubMed:19566596, ECO:0000269|PubMed:20053675,
CC ECO:0000269|PubMed:23667493, ECO:0000269|PubMed:28434950}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC Evidence={ECO:0000305|PubMed:11402198};
CC -!- SUBUNIT: Associates with ALIS1 to form a stable and active complex.
CC Interacts with ALIS3 and ALIS5 in a heterologous system.
CC {ECO:0000269|PubMed:18344284, ECO:0000269|PubMed:20053675}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:18344284, ECO:0000269|PubMed:20053675}; Multi-pass
CC membrane protein {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:20053675}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Requires the presence of an ALIS protein to exit
CC the endoplasmic reticulum to the Golgi. {ECO:0000269|PubMed:20053675}.
CC -!- TISSUE SPECIFICITY: Expressed in petals and sepals, but not in
CC reproductive tissues. In siliques, detected in the upper part of the
CC seed pod and in the area between the seed pod and the stem, but not in
CC developing seeds. Strong expression in vascular shoot tissues and in
CC stomatal guard cells of young rosettes leaves. In roots, expressed in
CC cells surrounding the xylem and in central and peripheral columella
CC cells. Detected in developing and mature trichomes, roots, pollen and
CC growing pollen tubes. {ECO:0000269|PubMed:18344284,
CC ECO:0000269|PubMed:19566596}.
CC -!- DISRUPTION PHENOTYPE: Impaired growth of roots and shoots
CC (PubMed:18344284, PubMed:23667493, PubMed:28434950). Roots devoided of
CC the characteristic trans-Golgi proliferation of slime vesicles
CC containing polysaccharides and enzymes for secretion (PubMed:18344284).
CC Aberrant trichome expansion, reduced primary root growth and longer
CC root hairs (PubMed:19566596, PubMed:28434950). Impaired pollen growth
CC (PubMed:19566596, PubMed:23667493, PubMed:28434950). Impaired ovule
CC development (PubMed:23667493, PubMed:28434950). Reduced adaptability to
CC temperature stresses (PubMed:23667493). Abnormal accumulation of
CC ABCG36/PEN3 in endomembrane compartments, likely in the trans-Golgi
CC network, instead of plasma membrane (PM), due to an impaired endocytic
CC trafficking of the ABCG36/PEN3 transporter, thus causing delays in
CC ABCG36/PEN3 recruitment to the host-pathogen interface upon infection
CC by powdery mildews (e.g. Blumeria graminis) within papillae and in
CC response to pathogenic bacteria (e.g. Pseudomonas syringae) or
CC pathogen-associated molecular patterns (PAMPs) (e.g. flg22 and chitin)
CC (PubMed:28434950). {ECO:0000269|PubMed:18344284,
CC ECO:0000269|PubMed:19566596, ECO:0000269|PubMed:23667493,
CC ECO:0000269|PubMed:28434950}.
CC -!- MISCELLANEOUS: The intracellular targeting signals and lipid
CC specificity determinants reside in the catalytic ALA subunit.
CC {ECO:0000269|PubMed:20053675}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IV subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD39325.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC007258; AAD39325.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE33621.1; -; Genomic_DNA.
DR EMBL; AY091777; AAM10325.1; -; mRNA.
DR PIR; C96622; C96622.
DR RefSeq; NP_176191.1; NM_104675.3.
DR AlphaFoldDB; Q9XIE6; -.
DR SMR; Q9XIE6; -.
DR BioGRID; 27500; 1.
DR STRING; 3702.AT1G59820.1; -.
DR TCDB; 3.A.3.8.6; the p-type atpase (p-atpase) superfamily.
DR iPTMnet; Q9XIE6; -.
DR PaxDb; Q9XIE6; -.
DR PRIDE; Q9XIE6; -.
DR ProteomicsDB; 244925; -.
DR EnsemblPlants; AT1G59820.1; AT1G59820.1; AT1G59820.
DR GeneID; 842275; -.
DR Gramene; AT1G59820.1; AT1G59820.1; AT1G59820.
DR KEGG; ath:AT1G59820; -.
DR Araport; AT1G59820; -.
DR TAIR; locus:2025961; AT1G59820.
DR eggNOG; KOG0206; Eukaryota.
DR HOGENOM; CLU_000846_5_2_1; -.
DR InParanoid; Q9XIE6; -.
DR OMA; MGNQRSY; -.
DR OrthoDB; 587717at2759; -.
DR PhylomeDB; Q9XIE6; -.
DR BioCyc; ARA:AT1G59820-MON; -.
DR BRENDA; 7.6.2.1; 399.
DR PRO; PR:Q9XIE6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9XIE6; baseline and differential.
DR Genevisible; Q9XIE6; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
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:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0090404; C:pollen tube tip; IDA:TAIR.
DR GO; GO:0055037; C:recycling endosome; IDA:TAIR.
DR GO; GO:0005802; C:trans-Golgi network; IDA:TAIR.
DR GO; GO:0031982; C:vesicle; IDA:TAIR.
DR GO; GO:0015247; F:aminophospholipid flippase activity; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140326; F:ATPase-coupled intramembrane lipid transporter activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; IMP:UniProtKB.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; IMP:UniProtKB.
DR GO; GO:0048194; P:Golgi vesicle budding; IMP:TAIR.
DR GO; GO:0045332; P:phospholipid translocation; IBA:GO_Central.
DR GO; GO:0008104; P:protein localization; IMP:UniProtKB.
DR GO; GO:1901703; P:protein localization involved in auxin polar transport; IDA:TAIR.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0002237; P:response to molecule of bacterial origin; IMP:UniProtKB.
DR GO; GO:0002238; P:response to molecule of fungal origin; IMP:UniProtKB.
DR GO; GO:0048364; P:root development; IMP:TAIR.
DR GO; GO:0048367; P:shoot system development; IMP:TAIR.
DR GO; GO:0016192; P:vesicle-mediated transport; IMP:TAIR.
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; IPR006539; P-type_ATPase_IV.
DR InterPro; IPR032631; P-type_ATPase_N.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR032630; P_typ_ATPase_c.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR Pfam; PF16212; PhoLip_ATPase_C; 1.
DR Pfam; PF16209; PhoLip_ATPase_N; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81660; SSF81660; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01652; ATPase-Plipid; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Endoplasmic reticulum; Golgi apparatus; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Plant defense; Protein transport;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..1213
FT /note="Phospholipid-transporting ATPase 3"
FT /id="PRO_0000046387"
FT TOPO_DOM 1..67
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 90..93
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 117..297
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..319
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 320..346
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 347..364
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 365..900
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 901..920
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 921..934
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 935..954
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 955..984
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 985..1006
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1007..1013
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1014..1036
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1037..1042
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1043..1063
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1064..1076
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1077..1087
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1088..1213
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 413
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 845
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 849
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MUTAGEN 413
FT /note="D->A: Loss of internalization of phospholipids."
FT /evidence="ECO:0000269|PubMed:18344284"
SQ SEQUENCE 1213 AA; 137753 MW; 938642DEFDA28B66 CRC64;
MVRSGSFSVD SSATHQRTPS RTVTLGHIQP QAPTYRTVYC NDRESNQPVR FKGNSISTTK
YNVFTFLPKG LFEQFRRIAN IYFLGISCLS MTPISPVSPI TNVAPLSMVL LVSLIKEAFE
DWKRFQNDMS INNSTVEILQ DQQWVSIPWR KLQVGDIVKI KKDGFFPADI LFMSSTNSDG
ICYVETANLD GETNLKIRKA LERTWDYLVP EKAYEFKGEI QCEQPNNSLY TFTGNLVVQK
QTLPLSPDQL LLRGCSLRNT EYIVGAVVFT GHETKVMMNA MNAPSKRSTL EKKLDKLIIT
IFCVLVTMCL IGAIGCSIVT DREDKYLGLH NSDWEYRNGL MIGFFTFFTL VTLFSSIIPI
SLYVSIEMIK FIQSTQFINR DLNMYHAETN TPASARTSNL NEELGQVEYI FSDKTGTLTR
NLMEFFKCSI GGVSYGCGVT EIEKGIAQRH GLKVQEEQRS TGAIREKGFN FDDPRLMRGA
WRNEPNPDLC KELFRCLAIC HTVLPEGDES PEKIVYQAAS PDEAALVTAA KNFGFFFYRR
TPTMVYVRES HVEKMGKIQD VAYEILNVLE FNSTRKRQSV VCRFPDGRLV LYCKGADNVI
FERLANGMDD VRKVTREHLE HFGSSGLRTL CLAYKDLNPE TYDSWNEKFI QAKSALRDRE
KKLDEVAELI EKDLILIGST AIEDKLQEGV PTCIETLSRA GIKIWVLTGD KMETAINIAY
ACNLINNEMK QFVISSETDA IREAEERGDQ VEIARVIKEE VKRELKKSLE EAQHSLHTVA
GPKLSLVIDG KCLMYALDPS LRVMLLSLSL NCTSVVCCRV SPLQKAQVTS LVRKGAQKIT
LSIGDGANDV SMIQAAHVGI GISGMEGMQA VMASDFAIAQ FRFLTDLLLV HGRWSYLRIC
KVVMYFFYKN LTFTLTQFWF TFRTGFSGQR FYDDWFQSLF NVVFTALPVI VLGLFEKDVS
ASLSKRYPEL YREGIRNSFF KWRVVAVWAT SAVYQSLVCY LFVTTSSFGA VNSSGKVFGL
WDVSTMVFTC LVIAVNVRIL LMSNSITRWH YITVGGSILA WLVFAFVYCG IMTPHDRNEN
VYFVIYVLMS TFYFYFTLLL VPIVSLLGDF IFQGVERWFF PYDYQIVQEI HRHESDASKA
DQLEVENELT PQEARSYAIS QLPRELSKHT GFAFDSPGYE SFFASQLGIY APQKAWDVAR
RASMRSRPKV PKK
