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Protein

Calpain-type cysteine protease DEK1

Gene

DEK1

Organism
Zea mays (Maize)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Essential protein involved in epiderm development. Required for aleurone cell development in the endosperm probably by maintaining and restricting the aleurone and embryonic epidermal L1 cell-layer fates as well as meristems organization. Involved in the maintenance of adaxial/abaxial axis information in developing leaves, probably by regulating cell proliferation and expansion. Does not need calcium ions to be active.3 Publications

Catalytic activityi

Broad endopeptidase specificity.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei1769 – 17691By similarity
Active sitei1927 – 19271By similarity
Active sitei1947 – 19471By similarity

GO - Molecular functioni

  • calcium-dependent cysteine-type endopeptidase activity Source: InterPro
  • cysteine-type peptidase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Hydrolase, Protease, Thiol protease

Protein family/group databases

MEROPSiC02.019.

Names & Taxonomyi

Protein namesi
Recommended name:
Calpain-type cysteine protease DEK1 (EC:3.4.22.-)
Alternative name(s):
Phytocalpain DEK1
Protein DEFECTIVE KERNEL 1
Short name:
ZmDEK1
Gene namesi
Name:DEK1
OrganismiZea mays (Maize)
Taxonomic identifieri4577 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogonodaeAndropogoneaeTripsacinaeZea
Proteomesi
  • UP000007305 Componenti: Chromosome 1

Organism-specific databases

MaizeGDBi12148.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini34 – 7037ExtracellularSequence analysisAdd
BLAST
Transmembranei71 – 9121Helical; Name=1Sequence analysisAdd
BLAST
Topological domaini92 – 954CytoplasmicSequence analysis
Transmembranei96 – 11621Helical; Name=2Sequence analysisAdd
BLAST
Topological domaini117 – 12711ExtracellularSequence analysisAdd
BLAST
Transmembranei128 – 14821Helical; Name=3Sequence analysisAdd
BLAST
Topological domaini149 – 16416CytoplasmicSequence analysisAdd
BLAST
Transmembranei165 – 18521Helical; Name=4Sequence analysisAdd
BLAST
Topological domaini186 – 23651ExtracellularSequence analysisAdd
BLAST
Transmembranei237 – 25721Helical; Name=5Sequence analysisAdd
BLAST
Topological domaini258 – 2647CytoplasmicSequence analysis
Transmembranei265 – 28521Helical; Name=6Sequence analysisAdd
BLAST
Topological domaini286 – 2949ExtracellularSequence analysis
Transmembranei295 – 31521Helical; Name=7Sequence analysisAdd
BLAST
Topological domaini316 – 3205CytoplasmicSequence analysis
Transmembranei321 – 34121Helical; Name=8Sequence analysisAdd
BLAST
Topological domaini342 – 623282ExtracellularSequence analysisAdd
BLAST
Transmembranei624 – 64421Helical; Name=9Sequence analysisAdd
BLAST
Topological domaini645 – 66016CytoplasmicSequence analysisAdd
BLAST
Transmembranei661 – 68121Helical; Name=10Sequence analysisAdd
BLAST
Topological domaini682 – 69413ExtracellularSequence analysisAdd
BLAST
Transmembranei695 – 71521Helical; Name=11Sequence analysisAdd
BLAST
Topological domaini716 – 7194CytoplasmicSequence analysis
Transmembranei720 – 74021Helical; Name=12Sequence analysisAdd
BLAST
Topological domaini741 – 77030ExtracellularSequence analysisAdd
BLAST
Transmembranei771 – 79121Helical; Name=13Sequence analysisAdd
BLAST
Topological domaini792 – 82231CytoplasmicSequence analysisAdd
BLAST
Transmembranei823 – 84321Helical; Name=14Sequence analysisAdd
BLAST
Topological domaini844 – 85310ExtracellularSequence analysis
Transmembranei854 – 87421Helical; Name=15Sequence analysisAdd
BLAST
Topological domaini875 – 88713CytoplasmicSequence analysisAdd
BLAST
Transmembranei888 – 90821Helical; Name=16Sequence analysisAdd
BLAST
Topological domaini909 – 92113ExtracellularSequence analysisAdd
BLAST
Transmembranei922 – 94221Helical; Name=17Sequence analysisAdd
BLAST
Topological domaini943 – 9464CytoplasmicSequence analysis
Transmembranei947 – 96721Helical; Name=18Sequence analysisAdd
BLAST
Topological domaini968 – 98114ExtracellularSequence analysisAdd
BLAST
Transmembranei982 – 100221Helical; Name=19Sequence analysisAdd
BLAST
Topological domaini1003 – 101614CytoplasmicSequence analysisAdd
BLAST
Transmembranei1017 – 103721Helical; Name=20Sequence analysisAdd
BLAST
Topological domaini1038 – 106023ExtracellularSequence analysisAdd
BLAST
Transmembranei1061 – 108121Helical; Name=21Sequence analysisAdd
BLAST
Topological domaini1082 – 21591078CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • endoplasmic reticulum membrane Source: UniProtKB
  • endosome membrane Source: UniProtKB
  • integral component of plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Endoplasmic reticulum, Endosome, Membrane

Pathology & Biotechi

Disruption phenotypei

Loss of aleurone cells leading to white grains. Embryos arrest at the juvenile globoid stage and are devoid of shoot structures.2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1769 – 17691C → S: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3333Sequence analysisAdd
BLAST
Chaini34 – 21592126Calpain-type cysteine protease DEK1PRO_0000423439Add
BLAST
Propeptidei34 – ?By similarityPRO_0000423440

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1371 – 13711PhosphoserineBy similarity
Modified residuei1376 – 13761PhosphoserineBy similarity
Modified residuei1665 – 16651PhosphoserineBy similarity

Post-translational modificationi

Autocatalytic proteolytic cleavage leading to the production of mainly cytoplasmic localized subproducts of about 85 and 120 kDa.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ8RVL1.

Expressioni

Tissue specificityi

Expressed in most tissues at low levels ranging from 30 to 55 ppm. Present in all endosperm cells at transcript level, but confined to aleurones at protein level.2 Publications

Developmental stagei

In endosperm, accumulates during early developmental stages and declines near maturity. In embryos, levels peak at middevelopment with highest expression in the embryonic axis. Also present in young pericarp and immature ear tip and base.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi4577.GRMZM2G321753_P01.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1417 – 1609193Calpain catalytic 1PROSITE-ProRule annotationAdd
BLAST
Domaini1703 – 2005303Calpain catalytic 2PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi370 – 493124Ser-richAdd
BLAST
Compositional biasi1248 – 12547Poly-Leu

Domaini

The transmembrane regions are not required for calpain activity but may play regulatory roles.By similarity

Sequence similaritiesi

Belongs to the peptidase C2 family.Curated
Contains 2 calpain catalytic domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0045. Eukaryota.
ENOG410XP0B. LUCA.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR022682. Calpain_domain_III.
IPR022683. Calpain_III.
IPR013320. ConA-like_dom.
IPR000169. Pept_cys_AS.
IPR001300. Peptidase_C2_calpain_cat.
[Graphical view]
PfamiPF01067. Calpain_III. 1 hit.
PF00648. Peptidase_C2. 1 hit.
[Graphical view]
SMARTiSM00720. calpain_III. 1 hit.
SM00230. CysPc. 1 hit.
[Graphical view]
SUPFAMiSSF49758. SSF49758. 1 hit.
SSF49899. SSF49899. 1 hit.
PROSITEiPS50203. CALPAIN_CAT. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8RVL1-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MEGEGHHGVV LACSICGFLF AVLSPFSFWV LWAVNWRPWR LYSWIYARKW
60 70 80 90 100
PTYVQGPQLS TLCSLLTLCA WLVVISPIAV LLVWGSVLIA LMERNIIGLA
110 120 130 140 150
VIMAGVALLL SFYSIMLWWR TQWQSSEAVA YLLLLAVCLL CAYDFCAIYV
160 170 180 190 200
TAGASASELN SPSGFFFGVS VISLAINMLF ICKILFNVSG FDVDEYVRRS
210 220 230 240 250
YKFAYSDCVE VAPVSCSPEP PDPSELYMTK SSRVKHLGLL YISSLLVLVG
260 270 280 290 300
YSILYGLTSK EARWLGALTS VAVVILDWNL GLCSFRFELL KSRMIVLFVA
310 320 330 340 350
GTSRAFLVSF GVHYWYLGHC ISYAFVASVL LSAAVSSWLS ISNPSVARID
360 370 380 390 400
ALRSTVIKLR EGFRRKGQNS SSNSSEGCGS SVKRSSGSVE AGQNGNAMDS
410 420 430 440 450
MYRSNSQSDG VNWSSIPFDR SNSCQEGRSS DKNIDSARAS LAHRSNSCLS
460 470 480 490 500
AVQDSETAVV SVDRHGDPIT SLVCSSSGLE SHGCEPSGSA TTSGNQQLLD
510 520 530 540 550
LNLAAIFQDR LNDPRISSML KKNGGLGDVE LANLLQDKGL DPNFSYMLKD
560 570 580 590 600
KVMDPRILAL LQRSSLDADR EHQDDVDVTA TDSDRLDTTI ANQISLSEEL
610 620 630 640 650
RRSGLEKWLN ISRLIFHHLA GSPIRAFIVF TVMFIIETAT VAIYRPETIK
660 670 680 690 700
VINATHEQFE FGFSILLLSP VVCSIMAFIW SLRAEEMLMT SKPQKYGFIA
710 720 730 740 750
WLLSTCVGLF LSFLSKSSVI LGLSLTVPLM VACLSFAVPI WIRNGYSFWI
760 770 780 790 800
PGREFANREN VSQAPGEKER ALFVITIAVF TASIIGLGAI VSAKPLDALG
810 820 830 840 850
YKGWDADKNS SYSPYATSMY LGWALSSTIA VITTGLIPIV AWFATYRFSP
860 870 880 890 900
SSAICVGLFA TVLVSFCGAS YWGVVNSRED GVPLKADFLA ALLPLLCIPA
910 920 930 940 950
FFSLFTGLYK WKDDDWKISR GVYLFVGMGM LLLFGAVAAV IVTIRPWTVG
960 970 980 990 1000
VACLVAILFL VFVIGVIHYW TSNNFYLTRT QMLLVCSIAF LLALAAFLMG
1010 1020 1030 1040 1050
LFHGKPFVGA SIGYFSFIFL LTGRALTVLL SPPIVVYSPR VLPVYVYDAH
1060 1070 1080 1090 1100
ADSAKNVSYA FLILYGIALA TEVWGVIASL IMNPPFVGAG VSATTLVIAF
1110 1120 1130 1140 1150
SFAVSRPCLT LKMMEDAVHF LSKDTVVQAM SRSANKTRNA ISGTYSAPQR
1160 1170 1180 1190 1200
SASSAALLVG DPALTLDRAG NFVLPRADVM KLRDRLRNEE IAAGSFLCGV
1210 1220 1230 1240 1250
KDCLLICPQS LSNIDYRRNM CAHARILALE EAIDTEWVYM WDKFGGYLLL
1260 1270 1280 1290 1300
LLGLTAKAEQ IQDEVRLRLF LDSIGLSDLS AKEIKKWMPE DRRQFELIQE
1310 1320 1330 1340 1350
SYIREKEMEE EALMQRREEE GKGRERRRAL LEREERKWKE LEISLLSSIP
1360 1370 1380 1390 1400
NTGSRDAAAM AAAVRAVGGD SALEDSFARD RVSSIANHIR KAQLARRAEQ
1410 1420 1430 1440 1450
TGIPGTICIL DDEPRSTGRH CGELDLCLCQ SQKVTLSIAV MVQPVSGPVC
1460 1470 1480 1490 1500
LFGSEFQKVC WEILVAGSEQ GMEAGQVGLR LVTKGERMTT VAKEWNIGAS
1510 1520 1530 1540 1550
SIADGRWHLV TVTLDADLGE ATSFIDGVYD GYQNGLPLPT DNGIWEPGTD
1560 1570 1580 1590 1600
IWVGARPPMD LDAFGRSDSE GSDSKMQIMD AFLWGRCLSE DEVTVLHTAM
1610 1620 1630 1640 1650
SPAEYGFFDL APGDAWHGSY SARVDDWESE EAYELYDQGD VEWDGQYSSG
1660 1670 1680 1690 1700
RKRPVHDAVA IDLDSFARRP RKPRFETRDE VNQRMLSVER AVRDALIAKG
1710 1720 1730 1740 1750
ERNFTDQEFP PEDRSLFVDP MNPPLKLQVV SEWMRPSDIA KDISISCQPC
1760 1770 1780 1790 1800
LFSGSVNSSD VCQGRLGDCW FLSAVAVLTE MSRISEVIIT PEYNDEGIYT
1810 1820 1830 1840 1850
VRFCIQGEWV AVVVDDWIPC ESPGKPAFAT SRKQNELWVS ILEKAYAKLH
1860 1870 1880 1890 1900
GSYEALEGGL VQDALVDLTG GAGEEIDMRS PQAQLDLASG RLWSQLLHFK
1910 1920 1930 1940 1950
QEGFLLGAGS PSGSDAHISS SGIVQGHAYS ILQVREVDGH KLIQIRNPWA
1960 1970 1980 1990 2000
NEVEWNGPWS DSSPEWTERM KHKLMHVPQS KNGVFWMSWQ DFQIHFRSIY
2010 2020 2030 2040 2050
VCRVYPPEMR YSVHGQWRGY NAGGCQDYDS WHQNPQYRLR VTGRDALYPV
2060 2070 2080 2090 2100
HVFITLTQGV GFSRKTNGFR NYQSSHDSSM FYIGMRILKT QGCRAAYNIY
2110 2120 2130 2140 2150
MHESAGGTDY VNSREISCEL VLDPYPKGYT IVPTTIHPGE EAPFVLSVFS

KASIRLEAV
Length:2,159
Mass (Da):239,106
Last modified:September 18, 2013 - v2
Checksum:i041D8974E4BA0AA5
GO
Isoform 2 (identifier: Q8RVL1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1877: Missing.

Show »
Length:282
Mass (Da):32,209
Checksum:iAED88901ABBBFCB1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti92 – 921M → L in AAL38189 (PubMed:11929961).Curated
Sequence conflicti127 – 1271E → K in AAL38189 (PubMed:11929961).Curated
Sequence conflicti138 – 1381C → G in AAL38189 (PubMed:11929961).Curated
Sequence conflicti398 – 3981M → T in AAL38189 (PubMed:11929961).Curated
Sequence conflicti469 – 4691I → T in AAL38189 (PubMed:11929961).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 18771877Missing in isoform 2. 2 PublicationsVSP_047871Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY061806 mRNA. Translation: AAL38189.1.
GK000031 Genomic DNA. No translation available.
BT035904 mRNA. Translation: ACF80909.1.
RefSeqiNP_001105528.1. NM_001112058.1.
XP_008648830.1. XM_008650608.1. [Q8RVL1-1]
UniGeneiZm.95757.

Genome annotation databases

EnsemblPlantsiGRMZM2G321753_T02; GRMZM2G321753_P02; GRMZM2G321753. [Q8RVL1-2]
GeneIDi542509.
KEGGizma:542509.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY061806 mRNA. Translation: AAL38189.1.
GK000031 Genomic DNA. No translation available.
BT035904 mRNA. Translation: ACF80909.1.
RefSeqiNP_001105528.1. NM_001112058.1.
XP_008648830.1. XM_008650608.1. [Q8RVL1-1]
UniGeneiZm.95757.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi4577.GRMZM2G321753_P01.

Protein family/group databases

MEROPSiC02.019.

Proteomic databases

PaxDbiQ8RVL1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiGRMZM2G321753_T02; GRMZM2G321753_P02; GRMZM2G321753. [Q8RVL1-2]
GeneIDi542509.
KEGGizma:542509.

Organism-specific databases

MaizeGDBi12148.

Phylogenomic databases

eggNOGiKOG0045. Eukaryota.
ENOG410XP0B. LUCA.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR022682. Calpain_domain_III.
IPR022683. Calpain_III.
IPR013320. ConA-like_dom.
IPR000169. Pept_cys_AS.
IPR001300. Peptidase_C2_calpain_cat.
[Graphical view]
PfamiPF01067. Calpain_III. 1 hit.
PF00648. Peptidase_C2. 1 hit.
[Graphical view]
SMARTiSM00720. calpain_III. 1 hit.
SM00230. CysPc. 1 hit.
[Graphical view]
SUPFAMiSSF49758. SSF49758. 1 hit.
SSF49899. SSF49899. 1 hit.
PROSITEiPS50203. CALPAIN_CAT. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The defective kernel 1 (dek1) gene required for aleurone cell development in the endosperm of maize grains encodes a membrane protein of the calpain gene superfamily."
    Lid S.E., Gruis D., Jung R., Lorentzen J.A., Ananiev E., Chamberlin M., Niu X., Meeley R., Nichols S., Olsen O.-A.
    Proc. Natl. Acad. Sci. U.S.A. 99:5460-5465(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Strain: cv. B73.
    Tissue: Endosperm.
  2. "The B73 maize genome: complexity, diversity, and dynamics."
    Schnable P.S., Ware D., Fulton R.S., Stein J.C., Wei F., Pasternak S., Liang C., Zhang J., Fulton L., Graves T.A., Minx P., Reily A.D., Courtney L., Kruchowski S.S., Tomlinson C., Strong C., Delehaunty K., Fronick C.
    , Courtney B., Rock S.M., Belter E., Du F., Kim K., Abbott R.M., Cotton M., Levy A., Marchetto P., Ochoa K., Jackson S.M., Gillam B., Chen W., Yan L., Higginbotham J., Cardenas M., Waligorski J., Applebaum E., Phelps L., Falcone J., Kanchi K., Thane T., Scimone A., Thane N., Henke J., Wang T., Ruppert J., Shah N., Rotter K., Hodges J., Ingenthron E., Cordes M., Kohlberg S., Sgro J., Delgado B., Mead K., Chinwalla A., Leonard S., Crouse K., Collura K., Kudrna D., Currie J., He R., Angelova A., Rajasekar S., Mueller T., Lomeli R., Scara G., Ko A., Delaney K., Wissotski M., Lopez G., Campos D., Braidotti M., Ashley E., Golser W., Kim H., Lee S., Lin J., Dujmic Z., Kim W., Talag J., Zuccolo A., Fan C., Sebastian A., Kramer M., Spiegel L., Nascimento L., Zutavern T., Miller B., Ambroise C., Muller S., Spooner W., Narechania A., Ren L., Wei S., Kumari S., Faga B., Levy M.J., McMahan L., Van Buren P., Vaughn M.W., Ying K., Yeh C.-T., Emrich S.J., Jia Y., Kalyanaraman A., Hsia A.-P., Barbazuk W.B., Baucom R.S., Brutnell T.P., Carpita N.C., Chaparro C., Chia J.-M., Deragon J.-M., Estill J.C., Fu Y., Jeddeloh J.A., Han Y., Lee H., Li P., Lisch D.R., Liu S., Liu Z., Nagel D.H., McCann M.C., SanMiguel P., Myers A.M., Nettleton D., Nguyen J., Penning B.W., Ponnala L., Schneider K.L., Schwartz D.C., Sharma A., Soderlund C., Springer N.M., Sun Q., Wang H., Waterman M., Westerman R., Wolfgruber T.K., Yang L., Yu Y., Zhang L., Zhou S., Zhu Q., Bennetzen J.L., Dawe R.K., Jiang J., Jiang N., Presting G.G., Wessler S.R., Aluru S., Martienssen R.A., Clifton S.W., McCombie W.R., Wing R.A., Wilson R.K.
    Science 326:1112-1115(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. B73.
  3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Strain: cv. B73.
  4. "The calpain domain of the maize DEK1 protein contains the conserved catalytic triad and functions as a cysteine proteinase."
    Wang C., Barry J.K., Min Z., Tordsen G., Rao A.G., Olsen O.A.
    J. Biol. Chem. 278:34467-34474(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-1769, TISSUE SPECIFICITY.
  5. "Subcellular localization and functional domain studies of DEFECTIVE KERNEL1 in maize and Arabidopsis suggest a model for aleurone cell fate specification involving CRINKLY4 and SUPERNUMERARY ALEURONE LAYER1."
    Tian Q., Olsen L., Sun B., Lid S.E., Brown R.C., Lemmon B.E., Fosnes K., Gruis D.F., Opsahl-Sorteberg H.-G., Otegui M.S., Olsen O.-A.
    Plant Cell 19:3127-3145(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiDEK1_MAIZE
AccessioniPrimary (citable) accession number: Q8RVL1
Secondary accession number(s): B4FFL6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 18, 2013
Last sequence update: September 18, 2013
Last modified: February 17, 2016
This is version 78 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Although homology to other calpains is high within the protease domain, the lack of calcium-binding sites suggests that this protein is a protease that may not be activated by calcium ions.By similarity

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.