VPS4_ARATH
ID VPS4_ARATH Reviewed; 435 AA.
AC Q9ZNT0; Q8LAK9;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Protein SUPPRESSOR OF K(+) TRANSPORT GROWTH DEFECT 1 {ECO:0000303|PubMed:17468262};
DE Short=AtSKD1 {ECO:0000303|PubMed:17468262};
DE EC=3.6.4.6 {ECO:0000269|PubMed:17468262, ECO:0000269|PubMed:20663085, ECO:0000269|PubMed:24385429};
DE AltName: Full=Protein VACUOLAR PROTEIN SORTING 4 {ECO:0000303|PubMed:17468262};
GN Name=SKD1 {ECO:0000303|PubMed:17468262};
GN Synonyms=VPS4 {ECO:0000303|PubMed:17468262};
GN OrderedLocusNames=At2g27600 {ECO:0000312|Araport:AT2G27600};
GN ORFNames=F10A12.27 {ECO:0000312|EMBL:AAM15184.1},
GN F15K20 {ECO:0000312|EMBL:AAC73040.1};
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 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, MUTAGENESIS OF GLU-232, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP INTERACTION WITH LIP5, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RC STRAIN=cv. Columbia;
RX PubMed=17468262; DOI=10.1105/tpc.106.049346;
RA Haas T.J., Sliwinski M.K., Martinez D.E., Preuss M., Ebine K., Ueda T.,
RA Nielsen E., Odorizzi G., Otegui M.S.;
RT "The Arabidopsis AAA ATPase SKD1 is involved in multivesicular endosome
RT function and interacts with its positive regulator LYST-INTERACTING
RT PROTEIN5.";
RL Plant Cell 19:1295-1312(2007).
RN [6]
RP INTERACTION WITH CHMP1A.
RX PubMed=19304934; DOI=10.1105/tpc.108.064865;
RA Spitzer C., Reyes F.C., Buono R., Sliwinski M.K., Haas T.J., Otegui M.S.;
RT "The ESCRT-related CHMP1A and B proteins mediate multivesicular body
RT sorting of auxin carriers in Arabidopsis and are required for plant
RT development.";
RL Plant Cell 21:749-766(2009).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF LYS-178 AND GLU-232,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, SUBUNIT, AND INTERACTION WITH LIP5; VPS20.1; VPS20.2;
RP VPS24-1; VPS32.1; VPS32.2; CHMP1A AND VPS60-1.
RC STRAIN=cv. Columbia;
RX PubMed=20663085; DOI=10.1111/j.1365-313x.2010.04310.x;
RA Shahriari M., Keshavaiah C., Scheuring D., Sabovljevic A., Pimpl P.,
RA Haeusler R.E., Huelskamp M., Schellmann S.;
RT "The AAA-type ATPase AtSKD1 contributes to vacuolar maintenance of
RT Arabidopsis thaliana.";
RL Plant J. 64:71-85(2010).
RN [8]
RP FUNCTION, AND MUTAGENESIS OF LYS-178 AND GLU-232.
RC STRAIN=cv. Columbia;
RX PubMed=20930567; DOI=10.4161/psb.5.10.13134;
RA Shahriari M., Hulskamp M., Schellmann S.;
RT "Seeds of Arabidopsis plants expressing dominant-negative AtSKD1 under
RT control of the GL2 promoter show a transparent testa phenotype and a
RT mucilage defect.";
RL Plant Signal. Behav. 5:1308-1310(2010).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH VPS2.1.
RX PubMed=21810997; DOI=10.1105/tpc.111.087254;
RA Katsiarimpa A., Anzenberger F., Schlager N., Neubert S., Hauser M.T.,
RA Schwechheimer C., Isono E.;
RT "The Arabidopsis deubiquitinating enzyme AMSH3 interacts with ESCRT-III
RT subunits and regulates their localization.";
RL Plant Cell 23:3026-3040(2011).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=22258747; DOI=10.1007/s00425-012-1587-0;
RA Herberth S., Shahriari M., Bruderek M., Hessner F., Muller B., Hulskamp M.,
RA Schellmann S.;
RT "Artificial ubiquitylation is sufficient for sorting of a plasma membrane
RT ATPase to the vacuolar lumen of Arabidopsis cells.";
RL Planta 236:63-77(2012).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23580756; DOI=10.1093/jxb/ert097;
RA Chiang C.-P., Li C.-H., Jou Y., Chen Y.-C., Lin Y.-C., Yang F.-Y.,
RA Huang N.-C., Yen H.E.;
RT "Suppressor of K+ transport growth defect 1 (SKD1) interacts with RING-type
RT ubiquitin ligase and sucrose non-fermenting 1-related protein kinase
RT (SnRK1) in the halophyte ice plant.";
RL J. Exp. Bot. 64:2385-2400(2013).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF LEU-63, ACTIVITY REGULATION,
RP AND INTERACTION WITH PROS/AT4G24370.
RX PubMed=24385429; DOI=10.1074/jbc.m113.529685;
RA Reyes F.C., Buono R.A., Roschzttardtz H., Di Rubbo S., Yeun L.H.,
RA Russinova E., Otegui M.S.;
RT "A novel endosomal sorting complex required for transport (ESCRT) component
RT in Arabidopsis thaliana controls cell expansion and development.";
RL J. Biol. Chem. 289:4980-4988(2014).
RN [13]
RP FUNCTION, MUTAGENESIS OF GLU-232, INTERACTION WITH VPS20.1; VPS32.2 AND
RP VPS2.1, AND REVIEW ON ESCRT-III.
RX PubMed=24812106; DOI=10.1104/pp.114.238378;
RA Cai Y., Zhuang X., Gao C., Wang X., Jiang L.;
RT "The Arabidopsis endosomal sorting complex required for transport III
RT regulates internal vesicle formation of the prevacuolar compartment and is
RT required for plant development.";
RL Plant Physiol. 165:1328-1343(2014).
RN [14]
RP INTERACTION WITH LIP5, INDUCTION BY PSEUDOMONAS SYRINGAE, AND SUBCELLULAR
RP LOCATION.
RX PubMed=25010425; DOI=10.1371/journal.ppat.1004243;
RA Wang F., Shang Y., Fan B., Yu J.-Q., Chen Z.;
RT "Arabidopsis LIP5, a positive regulator of multivesicular body biogenesis,
RT is a critical target of pathogen-responsive MAPK cascade in plant basal
RT defense.";
RL PLoS Pathog. 10:E1004243-E1004243(2014).
CC -!- FUNCTION: Involved in the transport of biosynthetic membrane proteins
CC from the prevacuolar/endosomal compartment to the vacuole. Required for
CC multivesicular body (MVB) protein sorting. Catalyzes the ATP-dependent
CC dissociation of class E VPS proteins from endosomal membranes, such as
CC the disassembly of the ESCRT-III complex (PubMed:17468262,
CC PubMed:20663085, PubMed:21810997, PubMed:22258747, PubMed:24812106).
CC May also regulate cell cycle (PubMed:20663085). Required during seed
CC development for the formation of mucilage in seed coat and testa
CC (PubMed:20930567). Involved in the maintenance of Na(+)/K(+)
CC homeostasis under salt stress (PubMed:23580756). Required for cell
CC expansion (PubMed:24385429). {ECO:0000269|PubMed:17468262,
CC ECO:0000269|PubMed:20663085, ECO:0000269|PubMed:20930567,
CC ECO:0000269|PubMed:21810997, ECO:0000269|PubMed:22258747,
CC ECO:0000269|PubMed:24385429, ECO:0000269|PubMed:24812106,
CC ECO:0000303|PubMed:23580756}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.6;
CC Evidence={ECO:0000269|PubMed:17468262, ECO:0000269|PubMed:20663085,
CC ECO:0000269|PubMed:24385429};
CC -!- ACTIVITY REGULATION: Activated by LIP5 and PROS.
CC {ECO:0000269|PubMed:17468262, ECO:0000269|PubMed:24385429}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=266 uM for ATP (at pH 7.8 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:20663085};
CC Vmax=1.77 umol/min/mg enzyme with ATP as substrate (at pH 7.8 and 30
CC degrees Celsius) {ECO:0000269|PubMed:20663085};
CC -!- SUBUNIT: Monomer or homodimer (in nucleotide-free form). Decamer,
CC dodecamer or tetradecamer of two stacked respective homooligomeric
CC rings (when bound to ATP); the dodecameric form seems to be predominant
CC (By similarity). Interacts with members of the ESCRT-III subcomplex
CC such as LIP5, VPS60-1, VPS2.1, VPS20.1, VPS20.2, VPS24-1, VPS32.1,
CC VPS32.2, CHMP1A and VPS24 (PubMed:17468262, PubMed:19304934,
CC PubMed:20663085, PubMed:24812106, PubMed:25010425). Binds to
CC PROS/At4g24370 (PubMed:24385429). {ECO:0000250|UniProtKB:P52917,
CC ECO:0000269|PubMed:17468262, ECO:0000269|PubMed:19304934,
CC ECO:0000269|PubMed:20663085, ECO:0000269|PubMed:21810997,
CC ECO:0000269|PubMed:24385429, ECO:0000269|PubMed:24812106,
CC ECO:0000269|PubMed:25010425}.
CC -!- INTERACTION:
CC Q9ZNT0; Q9SZ15: LIP5; NbExp=2; IntAct=EBI-1606459, EBI-1606558;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17468262,
CC ECO:0000269|PubMed:20663085}. Nucleus {ECO:0000269|PubMed:20663085}.
CC Endosome, multivesicular body membrane {ECO:0000269|PubMed:17468262,
CC ECO:0000269|PubMed:20663085, ECO:0000269|PubMed:25010425}; Peripheral
CC membrane protein {ECO:0000269|PubMed:17468262,
CC ECO:0000269|PubMed:20663085}. Prevacuolar compartment membrane
CC {ECO:0000250|UniProtKB:P46467}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P46467}. Note=In young trichome vacuole-free
CC cells, present in the cytosol and in the nucleus. In vacuole-containing
CC cells, present in punctae and large speckles corresponding to
CC prevacuolar compartments (PubMed:20663085). Localized in multivesicular
CC body when associated with LIP5 (PubMed:25010425).
CC {ECO:0000269|PubMed:20663085, ECO:0000269|PubMed:25010425}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in leaves, to a lower extent in
CC seeds, and barely in roots and flowers (at protein level)
CC (PubMed:17468262). Particularly expressed in trichomes
CC (PubMed:20663085). {ECO:0000269|PubMed:17468262,
CC ECO:0000269|PubMed:20663085}.
CC -!- INDUCTION: By Pseudomonas syringae pv. tomato strain DC3000
CC (PstDC3000). {ECO:0000269|PubMed:25010425}.
CC -!- DOMAIN: The MIT domain serves as an adapter for ESCRT-III proteins. It
CC forms an asymmetric three-helix bundle that binds amphipathic MIM (MIT
CC interacting motif) helices along the groove between MIT helices 2 and 3
CC present in a subset of ESCRT-III proteins thus establishing the
CC canonical MIM-MIT interaction. In an extended conformation along the
CC groove between helices 1 and 3, also binds to a type-2 MIT interacting
CC motif (MIM2). {ECO:0000250|UniProtKB:O75351}.
CC -!- DISRUPTION PHENOTYPE: Normal vacuolar development in early stages of
CC trichome development shortly followed by fragmentation of the large
CC central vacuole which finally disappears completely, associated with
CC the formation of abnormally enlarged late endosomes. Abnormal sorting
CC of vacuolar proteins that are instead secreted. Trichomes contain
CC frequently multiple nuclei (PubMed:20663085). Reduced ESCRT-III
CC disassembly (PubMed:21810997). Blocked vacuolar trafficking
CC (PubMed:22258747). Imbalanced Na(+)/K(+) ratio under salt stress
CC (PubMed:23580756). {ECO:0000269|PubMed:20663085,
CC ECO:0000269|PubMed:21810997, ECO:0000269|PubMed:22258747,
CC ECO:0000303|PubMed:23580756}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR EMBL; AC005824; AAC73040.1; -; Genomic_DNA.
DR EMBL; AC006232; AAM15184.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08019.1; -; Genomic_DNA.
DR EMBL; AF367297; AAK32884.1; -; mRNA.
DR EMBL; AY091684; AAM10283.1; -; mRNA.
DR EMBL; AY087749; AAM65285.1; -; mRNA.
DR PIR; F84674; F84674.
DR RefSeq; NP_180328.1; NM_128319.4.
DR AlphaFoldDB; Q9ZNT0; -.
DR SMR; Q9ZNT0; -.
DR IntAct; Q9ZNT0; 4.
DR STRING; 3702.AT2G27600.1; -.
DR TCDB; 3.A.31.1.2; the endosomal sorting complexes required for transport iii (escrt-iii) family.
DR PaxDb; Q9ZNT0; -.
DR PRIDE; Q9ZNT0; -.
DR ProteomicsDB; 242683; -.
DR EnsemblPlants; AT2G27600.1; AT2G27600.1; AT2G27600.
DR GeneID; 817306; -.
DR Gramene; AT2G27600.1; AT2G27600.1; AT2G27600.
DR KEGG; ath:AT2G27600; -.
DR Araport; AT2G27600; -.
DR TAIR; locus:2038678; AT2G27600.
DR eggNOG; KOG0739; Eukaryota.
DR HOGENOM; CLU_000688_21_2_1; -.
DR InParanoid; Q9ZNT0; -.
DR OMA; AVQYFIH; -.
DR OrthoDB; 787710at2759; -.
DR PhylomeDB; Q9ZNT0; -.
DR BRENDA; 3.6.4.6; 399.
DR SABIO-RK; Q9ZNT0; -.
DR PRO; PR:Q9ZNT0; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZNT0; baseline and differential.
DR Genevisible; Q9ZNT0; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005771; C:multivesicular body; IDA:UniProtKB.
DR GO; GO:0032585; C:multivesicular body membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005777; C:peroxisome; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; 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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0016197; P:endosomal transport; IBA:GO_Central.
DR GO; GO:0007032; P:endosome organization; IMP:TAIR.
DR GO; GO:0055075; P:potassium ion homeostasis; TAS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0055078; P:sodium ion homeostasis; TAS:UniProtKB.
DR GO; GO:0010091; P:trichome branching; IMP:TAIR.
DR GO; GO:0007033; P:vacuole organization; IMP:TAIR.
DR GO; GO:0016192; P:vesicle-mediated transport; IMP:TAIR.
DR CDD; cd02678; MIT_VPS4; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR007330; MIT_dom.
DR InterPro; IPR036181; MIT_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015415; Vps4_C.
DR InterPro; IPR045253; VPS4_MIT.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF04212; MIT; 1.
DR Pfam; PF09336; Vps4_C; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00745; MIT; 1.
DR SUPFAM; SSF116846; SSF116846; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00674; AAA; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cytoplasm; Endosome; Hydrolase; Membrane;
KW Nucleotide-binding; Nucleus; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..435
FT /note="Protein SUPPRESSOR OF K(+) TRANSPORT GROWTH DEFECT
FT 1"
FT /id="PRO_0000431528"
FT DOMAIN 7..72
FT /note="MIT"
FT /evidence="ECO:0000255"
FT REGION 73..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 172..179
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT MUTAGEN 63
FT /note="L->A: Impaired PROS/At4g24370 interaction."
FT /evidence="ECO:0000269|PubMed:24385429"
FT MUTAGEN 178
FT /note="K->A: Loss of ATP binding and ATPase activity. Pale
FT seeds, transparent testa phenotype caused by a lack of
FT proanthocyanidin (PA) and mucilage defect in seed coat."
FT /evidence="ECO:0000269|PubMed:20663085,
FT ECO:0000269|PubMed:20930567"
FT MUTAGEN 232
FT /note="E->Q: Loss of ATPase activity. Enlarged endosomes
FT with a reduced number of internal vesicles, as well as
FT abnormal localization of ESCRT-III subunits. Pale seeds,
FT transparent testa phenotype caused by a lack of
FT proanthocyanidin (PA) and mucilage defect in seed coat."
FT /evidence="ECO:0000269|PubMed:17468262,
FT ECO:0000269|PubMed:20663085, ECO:0000269|PubMed:20930567,
FT ECO:0000269|PubMed:24812106"
FT CONFLICT 394
FT /note="Missing (in Ref. 4; AAM65285)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 435 AA; 48593 MW; B56F8B39419C20AA CRC64;
MYSNFKEQAI EYVKQAVHED NAGNYNKAFP LYMNALEYFK THLKYEKNPK IREAITQKFT
EYLRRAEEIR AVLDEGGSGP GSNGDAAVAT RPKTKPKDGE GGGKDGEDPE QSKLRAGLNS
AIVREKPNIK WSDVAGLESA KQALQEAVIL PVKFPQFFTG KRRPWRAFLL YGPPGTGKSY
LAKAVATEAD STFFSVSSSD LVSKWMGESE KLVSNLFEMA RESAPSIIFV DEIDSLCGTR
GEGNESEASR RIKTELLVQM QGVGHNDEKV LVLAATNTPY ALDQAIRRRF DKRIYIPLPE
AKARQHMFKV HLGDTPHNLT EPDFEYLGQK TEGFSGSDVS VCVKDVLFEP VRKTQDAMFF
FKSPDGTWMP CGPRHPGAIQ TTMQDLATKG LAEKIIPPPI TRTDFEKVLA RQRPTVSKSD
LDVHERFTQE FGEEG
