ID DEK1_ARATH Reviewed; 2151 AA.
AC Q8RVL2; Q8VXW6; Q949X8; Q9C8A6;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 24-JAN-2024, entry version 140.
DE RecName: Full=Calpain-type cysteine protease DEK1 {ECO:0000303|PubMed:11929961};
DE EC=3.4.22.-;
DE AltName: Full=Phytocalpain DEK1 {ECO:0000303|PubMed:11929961};
DE AltName: Full=Protein DEFECTIVE KERNEL 1 {ECO:0000303|PubMed:11929961};
DE Short=AtDEK1 {ECO:0000303|PubMed:11929961};
DE AltName: Full=Protein EMBRYO DEFECTIVE 1275 {ECO:0000303|PubMed:19812694};
DE AltName: Full=Protein EMBRYO DEFECTIVE 80 {ECO:0000303|PubMed:19812694};
DE Flags: Precursor;
GN Name=DEK1 {ECO:0000303|PubMed:11929961};
GN Synonyms=EMB1275 {ECO:0000303|PubMed:19812694},
GN EMB80 {ECO:0000303|PubMed:19812694};
GN OrderedLocusNames=At1g55350 {ECO:0000312|Araport:AT1G55350};
GN ORFNames=F7A10.23 {ECO:0000312|EMBL:AAG51565.1};
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 [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia; TISSUE=Seed;
RX PubMed=11929961; DOI=10.1073/pnas.042098799;
RA Lid S.E., Gruis D., Jung R., Lorentzen J.A., Ananiev E., Chamberlin M.,
RA Niu X., Meeley R., Nichols S., Olsen O.-A.;
RT "The defective kernel 1 (dek1) gene required for aleurone cell development
RT in the endosperm of maize grains encodes a membrane protein of the calpain
RT gene superfamily.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:5460-5465(2002).
RN [2]
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 [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] OF 1-543 AND 1603-2151.
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 SUBCELLULAR LOCATION.
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 [6]
RP SUBCELLULAR LOCATION.
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 [7]
RP IDENTIFICATION [LARGE SCALE ANALYSIS], AND DISRUPTION PHENOTYPE [LARGE
RP SCALE ANALYSIS].
RX PubMed=15266054; DOI=10.1104/pp.104.045179;
RA Tzafrir I., Pena-Muralla R., Dickerman A., Berg M., Rogers R., Hutchens S.,
RA Sweeney T.C., McElver J., Aux G., Patton D., Meinke D.;
RT "Identification of genes required for embryo development in Arabidopsis.";
RL Plant Physiol. 135:1206-1220(2004).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=15647902; DOI=10.1007/s00425-004-1448-6;
RA Lid S.E., Olsen L., Nestestog R., Aukerman M., Brown R.C., Lemmon B.,
RA Mucha M., Opsahl-Sorteberg H.-G., Olsen O.-A.;
RT "Mutation in the Arabidopisis thaliana DEK1 calpain gene perturbs endosperm
RT and embryo development while over-expression affects organ development
RT globally.";
RL Planta 221:339-351(2005).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=16167900; DOI=10.1111/j.1365-313x.2005.02514.x;
RA Johnson K.L., Degnan K.A., Ross Walker J., Ingram G.C.;
RT "AtDEK1 is essential for specification of embryonic epidermal cell fate.";
RL Plant J. 44:114-127(2005).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=17933905; DOI=10.1105/tpc.106.048868;
RA Tian Q., Olsen L., Sun B., Lid S.E., Brown R.C., Lemmon B.E., Fosnes K.,
RA Gruis D.F., Opsahl-Sorteberg H.-G., Otegui M.S., Olsen O.-A.;
RT "Subcellular localization and functional domain studies of DEFECTIVE
RT KERNEL1 in maize and Arabidopsis suggest a model for aleurone cell fate
RT specification involving CRINKLY4 and SUPERNUMERARY ALEURONE LAYER1.";
RL Plant Cell 19:3127-3145(2007).
RN [11]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, PROTEOLYSIS,
RP MUTAGENESIS OF CYS-1761, AND DOMAIN.
RX PubMed=18952779; DOI=10.1105/tpc.108.059964;
RA Johnson K.L., Faulkner C., Jeffree C.E., Ingram G.C.;
RT "The phytocalpain defective kernel 1 is a novel Arabidopsis growth
RT regulator whose activity is regulated by proteolytic processing.";
RL Plant Cell 20:2619-2630(2008).
RN [12]
RP IDENTIFICATION [LARGE SCALE ANALYSIS], AND DISRUPTION PHENOTYPE [LARGE
RP SCALE ANALYSIS].
RX PubMed=19812694; DOI=10.1371/journal.pone.0007386;
RA Meinke D., Sweeney C., Muralla R.;
RT "Integrating the genetic and physical maps of Arabidopsis thaliana:
RT identification of mapped alleles of cloned essential (EMB) genes.";
RL PLoS ONE 4:E7386-E7386(2009).
RN [13]
RP FUNCTION, AND MUTAGENESIS OF ARG-2106.
RX PubMed=23095885; DOI=10.1242/dev.082925;
RA Roeder A.H.K., Cunha A., Ohno C.K., Meyerowitz E.M.;
RT "Cell cycle regulates cell type in the Arabidopsis sepal.";
RL Development 139:4416-4427(2012).
RN [14]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=25315606; DOI=10.1104/pp.114.246033;
RA Qu X., Chatty P.R., Roeder A.H.K.;
RT "Endomembrane trafficking protein SEC24A regulates cell size patterning in
RT Arabidopsis.";
RL Plant Physiol. 166:1877-1890(2014).
CC -!- FUNCTION: Essential protease involved in epiderm development. Required
CC for aleurone cell development in the endosperm probably by maintaining
CC and restricting the aleurone and embryonic epidermal L1 cell-layer
CC fates as well as meristems organization. Involved in the maintenance of
CC adaxial/abaxial axis information in developing leaves, probably by
CC regulating cell proliferation and expansion. Does not need calcium ions
CC to be active. Required for the formation of giant cells in sepals by
CC determining cell fate and promoting endoreplication (PubMed:25315606).
CC {ECO:0000269|PubMed:15647902, ECO:0000269|PubMed:16167900,
CC ECO:0000269|PubMed:17933905, ECO:0000269|PubMed:18952779,
CC ECO:0000269|PubMed:23095885, ECO:0000269|PubMed:25315606}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC Endosome membrane; Multi-pass membrane protein. Endoplasmic reticulum
CC membrane; Multi-pass membrane protein. Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=Additional isoforms may exist.;
CC Name=1;
CC IsoId=Q8RVL2-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Mostly expressed in meristems and organ primordia.
CC Expressed at low levels in young and germinating seeds at 10 ppm and in
CC seedling roots at 67 ppm. Present in most tissues at a low level.
CC {ECO:0000269|PubMed:11929961, ECO:0000269|PubMed:16167900}.
CC -!- DEVELOPMENTAL STAGE: Mostly observed in vegetative, inflorescence and
CC floral meristems as well as in young leaf and floral organ primordia.
CC Strongly expressed in developing ovules and during early embryogenesis.
CC Expressed evenly throughout the endosperm and the embryo in developing
CC seed. Present in the embryo proper, but excluded from the suspensor,
CC until the late heart stage, and fades out later, especially in the
CC hypocotyl region, to be present at low levels throughout walking-stick
CC embryos. Accumulates at the margins and in the tips of cotyledons and
CC lateral organs, in the apical meristem, in a subset of cells at the
CC root pole and in a restricted number of cells within the presumptive
CC vasculature of the hypocotyls. Also detected during early endosperm
CC development, prior to cellularization. {ECO:0000269|PubMed:15647902,
CC ECO:0000269|PubMed:16167900}.
CC -!- DOMAIN: The transmembrane regions are not required for calpain activity
CC but may play regulatory roles. {ECO:0000269|PubMed:18952779}.
CC -!- PTM: Autocatalytic proteolytic cleavage leading to the production of
CC mainly cytoplasmic localized subproducts of about 85 and 120 kDa.
CC -!- DISRUPTION PHENOTYPE: Defective embryo arrested at preglobular/globular
CC stage. Disturbed endosperm lacking the aleurone-like peripheral cell
CC layer and unorganized embryo development displaying irregular mitotic
CC divisions in the embryo proper and suspensor. In a partially disrupted
CC phenotype, impaired meristems organization characterized by vacuolated
CC cells, abnormal cotyledon epiderm made of chloroplast-containing cells,
CC and radialized leaves. Decreased numbers of giant cells in sepal
CC epidermis of dek1-4 (PubMed:25315606). {ECO:0000269|PubMed:15266054,
CC ECO:0000269|PubMed:15647902, ECO:0000269|PubMed:16167900,
CC ECO:0000269|PubMed:17933905, ECO:0000269|PubMed:18952779,
CC ECO:0000269|PubMed:19812694, ECO:0000269|PubMed:25315606}.
CC -!- MISCELLANEOUS: Although homology to other calpains is high within the
CC protease domain, the lack of calcium-binding sites suggests that this
CC protein is a protease that may not be activated by calcium ions.
CC -!- SIMILARITY: Belongs to the peptidase C2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG51565.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Seed defective Arabidopsis mutants;
CC URL="http://seedgenes.org/MutantList";
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DR EMBL; AY061803; AAL38186.1; -; mRNA.
DR EMBL; AC027034; AAG51565.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE33232.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33233.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33234.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33235.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM58867.1; -; Genomic_DNA.
DR EMBL; AY050822; AAK92757.1; -; mRNA.
DR EMBL; AY074514; AAL67128.1; -; mRNA.
DR PIR; G96595; G96595.
DR RefSeq; NP_001319240.1; NM_001333706.1. [Q8RVL2-1]
DR RefSeq; NP_001321273.1; NM_001333707.1. [Q8RVL2-1]
DR RefSeq; NP_175932.2; NM_104411.4. [Q8RVL2-1]
DR RefSeq; NP_850966.1; NM_180635.1. [Q8RVL2-1]
DR RefSeq; NP_850967.1; NM_180636.1. [Q8RVL2-1]
DR AlphaFoldDB; Q8RVL2; -.
DR SMR; Q8RVL2; -.
DR BioGRID; 27206; 2.
DR IntAct; Q8RVL2; 1.
DR STRING; 3702.Q8RVL2; -.
DR MEROPS; C02.019; -.
DR iPTMnet; Q8RVL2; -.
DR PaxDb; 3702-AT1G55350-5; -.
DR ProteomicsDB; 224622; -. [Q8RVL2-1]
DR EnsemblPlants; AT1G55350.1; AT1G55350.1; AT1G55350. [Q8RVL2-1]
DR EnsemblPlants; AT1G55350.2; AT1G55350.2; AT1G55350. [Q8RVL2-1]
DR EnsemblPlants; AT1G55350.3; AT1G55350.3; AT1G55350. [Q8RVL2-1]
DR EnsemblPlants; AT1G55350.4; AT1G55350.4; AT1G55350. [Q8RVL2-1]
DR EnsemblPlants; AT1G55350.6; AT1G55350.6; AT1G55350. [Q8RVL2-1]
DR GeneID; 841981; -.
DR Gramene; AT1G55350.1; AT1G55350.1; AT1G55350. [Q8RVL2-1]
DR Gramene; AT1G55350.2; AT1G55350.2; AT1G55350. [Q8RVL2-1]
DR Gramene; AT1G55350.3; AT1G55350.3; AT1G55350. [Q8RVL2-1]
DR Gramene; AT1G55350.4; AT1G55350.4; AT1G55350. [Q8RVL2-1]
DR Gramene; AT1G55350.6; AT1G55350.6; AT1G55350. [Q8RVL2-1]
DR KEGG; ath:AT1G55350; -.
DR Araport; AT1G55350; -.
DR TAIR; AT1G55350; DEK1.
DR eggNOG; KOG0045; Eukaryota.
DR InParanoid; Q8RVL2; -.
DR OMA; IYVCRIY; -.
DR PhylomeDB; Q8RVL2; -.
DR PRO; PR:Q8RVL2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8RVL2; baseline and differential.
DR Genevisible; Q8RVL2; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IMP:UniProtKB.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:UniProtKB.
DR GO; GO:0090628; P:plant epidermal cell fate specification; IMP:UniProtKB.
DR GO; GO:0032877; P:positive regulation of DNA endoreduplication; IMP:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR GO; GO:2000011; P:regulation of adaxial/abaxial pattern formation; ISS:UniProtKB.
DR GO; GO:0001558; P:regulation of cell growth; IMP:UniProtKB.
DR GO; GO:0042127; P:regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:2000014; P:regulation of endosperm development; IMP:UniProtKB.
DR GO; GO:2000024; P:regulation of leaf development; IMP:UniProtKB.
DR GO; GO:0009934; P:regulation of meristem structural organization; IMP:UniProtKB.
DR GO; GO:0097264; P:self proteolysis; IDA:UniProtKB.
DR GO; GO:0090392; P:sepal giant cell differentiation; IMP:UniProtKB.
DR CDD; cd00214; Calpain_III; 1.
DR CDD; cd00044; CysPc; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.60.120.380; -; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR033883; C2_III.
DR InterPro; IPR022684; Calpain_cysteine_protease.
DR InterPro; IPR022682; Calpain_domain_III.
DR InterPro; IPR022683; Calpain_III.
DR InterPro; IPR036213; Calpain_III_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR001300; Peptidase_C2_calpain_cat.
DR PANTHER; PTHR10183; CALPAIN; 1.
DR PANTHER; PTHR10183:SF379; CALPAIN-A-RELATED; 1.
DR Pfam; PF01067; Calpain_III; 1.
DR Pfam; PF00648; Peptidase_C2; 1.
DR PRINTS; PR00704; CALPAIN.
DR SMART; SM00720; calpain_III; 1.
DR SMART; SM00230; CysPc; 1.
DR SUPFAM; SSF49758; Calpain large subunit, middle domain (domain III); 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS50203; CALPAIN_CAT; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cytoplasm; Developmental protein;
KW Endoplasmic reticulum; Endosome; Hydrolase; Membrane; Protease;
KW Reference proteome; Repeat; Signal; Thiol protease; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..2151
FT /note="Calpain-type cysteine protease DEK1"
FT /id="PRO_0000423437"
FT PROPEP 33..?
FT /id="PRO_0000423438"
FT TOPO_DOM 33..69
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 91..94
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..115
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 116..126
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..147
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 148..163
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 185..235
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..256
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 257..263
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 264..284
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 285..293
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..314
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 315..319
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 320..340
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 341..615
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 616..636
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 637..652
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 653..673
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 674..686
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 687..707
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 708..711
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 712..732
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 733..760
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 761..782
FT /note="Helical; Name=13"
FT /evidence="ECO:0000255"
FT TOPO_DOM 783..813
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 814..834
FT /note="Helical; Name=14"
FT /evidence="ECO:0000255"
FT TOPO_DOM 835..844
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 845..865
FT /note="Helical; Name=15"
FT /evidence="ECO:0000255"
FT TOPO_DOM 866..878
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 879..899
FT /note="Helical; Name=16"
FT /evidence="ECO:0000255"
FT TOPO_DOM 900..912
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 913..933
FT /note="Helical; Name=17"
FT /evidence="ECO:0000255"
FT TOPO_DOM 934..936
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 937..957
FT /note="Helical; Name=18"
FT /evidence="ECO:0000255"
FT TOPO_DOM 958..971
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 972..992
FT /note="Helical; Name=19"
FT /evidence="ECO:0000255"
FT TOPO_DOM 993..1006
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1007..1027
FT /note="Helical; Name=20"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1028..1050
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1051..1071
FT /note="Helical; Name=21"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1072..2151
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 1407..1600
FT /note="Calpain catalytic 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT DOMAIN 1695..1997
FT /note="Calpain catalytic 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT REGION 363..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1761
FT /evidence="ECO:0000250|UniProtKB:Q07009"
FT ACT_SITE 1919
FT /evidence="ECO:0000250|UniProtKB:Q07009"
FT ACT_SITE 1939
FT /evidence="ECO:0000250|UniProtKB:Q07009"
FT MUTAGEN 1761
FT /note="C->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:18952779"
FT MUTAGEN 2106
FT /note="R->C: In dek1-4; near absence of giant cells in
FT sepals due to a reduced endoreduplication."
FT /evidence="ECO:0000269|PubMed:23095885"
SQ SEQUENCE 2151 AA; 238264 MW; 50D571D7446A5609 CRC64;
MEGDERGVLL ACVISGTLFT VFGSGSFWIL WAVNWRPWRL YSWIFARKWP KVLQGPQLDI
LCGVLSLFAW IVVVSPIAIL IGWGSWLIVI LDRHIIGLAI IMAGTALLLA FYSIMLWWRT
QWQSSRAVAL LLLLGVALLC AYELCAVYVT AGAHASQQYS PSGFFFGVSA IALAINMLFI
CRMVFNGNGL DVDEYVRRAY KFAYSDCIEV GPVACLPEPP DPNELYPRQT SRASHLGLLY
LGSLVVLLAY SVLYGLTARE SRWLGGITSA AVIVLDWNIG ACLYGFKLLQ NRVLALFVAG
ISRLFLICFG IHYWYLGHCI SYIFVASVLS GAAVSRHLSI TDPSAARRDA LQSTVIRLRE
GFRRKEQNSS SSSSDGCGSS IKRSSSIDAG HTGCTNEANR TAESCTADNL TRTGSSQEGI
NSDKSEESGR PSLGLRSSSC RSVVQEPEAG TSYFMDKVSD QNNTLVVCSS SGLDSQGYES
STSNSANQQL LDMNLALAFQ DQLNNPRIAS ILKKKAKEGD LELTNLLQDK GLDPNFAVML
KEKNLDPTIL ALLQRSSLDA DRDHRDNTDI TIIDSNSVDN TLPNQISLSE ELRLRGLEKW
LKLSRLLLHH VAGTPERAWG LFSLVFILET IIVAIFRPKT ITIINSSHQQ FEFGFSVLLL
SPVVCSIMAF LRSLQVEEMA LTSKSRKYGF VAWLLSTSVG LSLSFLSKSS VLLGISLTVP
LMAACLSIAV PIWMHNGYQF WVPQLSCGDQ ARDLRSPRIK GFILWICVVL FAGSVISLGA
IISAKPLDDL KYKLFSAREN NVTSPYTSSV YLGWAMSSGI ALVVTAILPI VSWFATYRFS
HSSAVCLMIF SVVLVAFCGT SYLEVVKSRD DQLPTKGDFL AALLPLACIP ALLSLCCGMV
KWKDDCWILS RGVYVFFSIG LLLLFGAIAA VIAVKPWTIG VSFLLVLFLM VVTIGVIHLW
ASNNFYLTRK QTSFVCFLAL LLGLAAFLLG WHQDKAFAGA SVGYFTFLSL LAGRALAVLL
SPPIVVYSPR VLPVYVYDAH ADCGKNVSAA FLVLYGIALA TEGWGVVASL IIYPPFAGAA
VSAITLVVAF GFAVSRPCLT LEMMEVAVRF LSKDTIVQAI SRSATKTRNA LSGTYSAPQR
SASSAALLVG DPSAMRDKAG NFVLPRDDVM KLRDRLRNEE RVAGSIFYKM QCRKGFRHEP
PTNVDYRRDM CAHARVLALE EAIDTEWVYM WDKFGGYLLL LLGLTAKAER VQDEVRLRLF
LDSIGFSDLS ARKISKWKPE DRRQFEIIQE SYLREKEMEE ESLMQRREEE GRGKERRKAL
LEKEERKWKE IEASLIPSIP NAGSREAAAM AAAIRAVGGD SVLEDSFARE RVSGIARRIR
TAQLERRAQQ TGISGAVCVL DDEPMISGKH CGQMDSSVCQ SQKISFSVTA MIQSDSGPVC
LFGTEFQKKV CWEILVAGSE QGIEAGQVGL RLITKGERQT TVAREWYIGA TSITDGRWHT
VTITIDADAG EATCYIDGGF DGYQNGLPLS IGSAIWEQGA EVWLGVRPPI DVDAFGRSDS
DGVESKMHIM DVFLWGKCLS EEEAASLHAA IGMADLDMID LSDDNWQWTD SPPRVDGWDS
DPADVDLYDR DDVDWDGQYS SGRKRRSGRD FVMSVDSFAR RHRKPRMETQ EDINQRMRSV
ELAVKEALSA RGDKQFTDQE FPPNDRSLFV DTQNPPSKLQ VVSEWMRPDS IVKENGSDSR
PCLFSGDANP SDVCQGRLGD CWFLSAVAVL TEVSRISEVI ITPEYNEEGI YTVRFCIQGE
WVPVVIDDWI PCESPGKPAF ATSRKLNELW VSMVEKAYAK LHGSYEALEG GLVQDALVDL
TGGAGEEIDL RSAQAQIDLA SGRLWSQLLR FKQEGFLLGA GSPSGSDVHV SSSGIVQGHA
YSVLQVREVD GHRLVQIRNP WANEVEWNGP WSDSSPEWTD RMKHKLKHVP QSKEGIFWMS
WQDFQIHFRS IYVCRVYPRE MRYSVNGQWR GYSAGGCQDY SSWHQNPQFR LRATGSDASL
PIHVFITLTQ GVGFSRTTPG FRNYQSSHDS QLFYIGLRIL KTRGRRAAYN IFLHESVGGT
DYVNSREISC EMVLDPDPKG YTIVPTTIHP GEEAPFVLSV FTKASIVLEA L
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