DEK1_ORYSJ
ID DEK1_ORYSJ Reviewed; 2162 AA.
AC Q6ZFZ4; Q8RYA5;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=Calpain-type cysteine protease ADL1;
DE EC=3.4.22.-;
DE AltName: Full=Phytocalpain ADL1;
DE AltName: Full=Protein ADAXIALIZED LEAF1;
DE AltName: Full=Protein DEFECTIVE KERNEL 1;
DE Short=OsDEK1;
DE AltName: Full=Protein SHOOTLESS 3;
DE Flags: Precursor;
GN Name=ADL1; Synonyms=DEK1, ODM63, SHL3;
GN OrderedLocusNames=Os02g0709400, LOC_Os02g47970; ORFNames=OJ1311_H06.4;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Taichung 65;
RX PubMed=19665012; DOI=10.1016/j.ydbio.2009.07.042;
RA Hibara K., Obara M., Hayashida E., Abe M., Ishimaru T., Satoh H., Itoh J.,
RA Nagato Y.;
RT "The ADAXIALIZED LEAF1 gene functions in leaf and embryonic pattern
RT formation in rice.";
RL Dev. Biol. 334:345-354(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF TRP-1841.
RX DOI=10.1002/dvg.1020160403;
RA Hong S.K., Aoki T., Kitano H., Satoh H., Nagato Y.;
RT "Phenotypic diversity of 188 rice embryo mutants.";
RL Dev. Genet. 16:298-310(1995).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF SER-1776.
RC STRAIN=cv. Taichung 65;
RX PubMed=10409508; DOI=10.1242/dev.126.16.3629;
RA Satoh N., Hong S.-K., Nishimura A., Matsuoka M., Kitano H., Nagato Y.;
RT "Initiation of shoot apical meristem in rice: characterization of four
RT SHOOTLESS genes.";
RL Development 126:3629-3636(1999).
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. {ECO:0000269|PubMed:10409508,
CC ECO:0000269|PubMed:19665012, ECO:0000269|Ref.6}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC Endosome membrane {ECO:0000250}; Multi-pass membrane protein
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with higher levels in
CC embryos, vasculatures, leaf primordia, leaf margins, and shoot apical
CC meristem (SAM). {ECO:0000269|PubMed:19665012}.
CC -!- DOMAIN: The transmembrane regions are not required for calpain activity
CC but may play regulatory roles. {ECO:0000250}.
CC -!- PTM: Autocatalytic proteolytic cleavage leading to the production of
CC mainly cytoplasmic localized subproducts of about 85 and 120 kDa.
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Abnormal embryos arrested at the globular stage
CC with an abnormal aleurone layer on the ventral side.
CC {ECO:0000269|PubMed:10409508, ECO:0000269|PubMed:19665012,
CC ECO:0000269|Ref.6}.
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 {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase C2 family. {ECO:0000305}.
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DR EMBL; AB477099; BAI44850.1; -; mRNA.
DR EMBL; AY062272; AAL38190.1; -; mRNA.
DR EMBL; AP004161; BAD07761.1; -; Genomic_DNA.
DR EMBL; AP008208; BAF09804.1; -; Genomic_DNA.
DR EMBL; AP014958; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015625425.1; XM_015769939.1.
DR RefSeq; XP_015625426.1; XM_015769940.1.
DR AlphaFoldDB; Q6ZFZ4; -.
DR SMR; Q6ZFZ4; -.
DR STRING; 4530.OS02T0709400-01; -.
DR MEROPS; C02.019; -.
DR iPTMnet; Q6ZFZ4; -.
DR PaxDb; Q6ZFZ4; -.
DR PRIDE; Q6ZFZ4; -.
DR GeneID; 4330484; -.
DR KEGG; osa:4330484; -.
DR eggNOG; KOG0045; Eukaryota.
DR InParanoid; Q6ZFZ4; -.
DR OrthoDB; 23957at2759; -.
DR PlantReactome; R-OSA-9627657; Regulation of leaf development.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR Genevisible; Q6ZFZ4; OS.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0008234; F:cysteine-type peptidase activity; ISS:UniProtKB.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; ISS:UniProtKB.
DR GO; GO:0090628; P:plant epidermal cell fate specification; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR GO; GO:2000011; P:regulation of adaxial/abaxial pattern formation; IMP:UniProtKB.
DR GO; GO:0001558; P:regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:2000014; P:regulation of endosperm development; ISS: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; ISS:UniProtKB.
DR CDD; cd00044; CysPc; 1.
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 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; SSF49758; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50203; CALPAIN_CAT; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Developmental protein; Endoplasmic reticulum;
KW Endosome; Hydrolase; Membrane; Phosphoprotein; Protease;
KW Reference proteome; Repeat; Signal; Thiol protease; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..2162
FT /note="Calpain-type cysteine protease ADL1"
FT /id="PRO_0000423441"
FT PROPEP 34..?
FT /evidence="ECO:0000250"
FT /id="PRO_0000423442"
FT TOPO_DOM 34..70
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..91
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 92..95
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 117..127
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..148
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 149..164
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 186..236
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 258..264
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..285
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 286..294
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 295..315
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 316..320
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 321..341
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 342..626
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 627..647
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 648..663
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 664..684
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 685..697
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 698..718
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 719..722
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 723..743
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 744..773
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 774..794
FT /note="Helical; Name=13"
FT /evidence="ECO:0000255"
FT TOPO_DOM 795..825
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 826..846
FT /note="Helical; Name=14"
FT /evidence="ECO:0000255"
FT TOPO_DOM 847..856
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 857..877
FT /note="Helical; Name=15"
FT /evidence="ECO:0000255"
FT TOPO_DOM 878..890
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 891..911
FT /note="Helical; Name=16"
FT /evidence="ECO:0000255"
FT TOPO_DOM 912..924
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 925..945
FT /note="Helical; Name=17"
FT /evidence="ECO:0000255"
FT TOPO_DOM 946..949
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 950..970
FT /note="Helical; Name=18"
FT /evidence="ECO:0000255"
FT TOPO_DOM 971..984
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 985..1005
FT /note="Helical; Name=19"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1006..1019
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1020..1040
FT /note="Helical; Name=20"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1041..1063
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1064..1084
FT /note="Helical; Name=21"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1085..2162
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 1418..1611
FT /note="Calpain catalytic 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT DOMAIN 1706..2008
FT /note="Calpain catalytic 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT REGION 366..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1772
FT /evidence="ECO:0000250"
FT ACT_SITE 1930
FT /evidence="ECO:0000250"
FT ACT_SITE 1950
FT /evidence="ECO:0000250"
FT MOD_RES 1372
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 1377
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 1668
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MUTAGEN 1776
FT /note="S->N: In adl1-s1 and shl3-1; deletion of the apical
FT region including the shoot apical meristem (SAM),
FT coleoptile, and scutellum in embryos, and no clear root
FT organization."
FT /evidence="ECO:0000269|PubMed:10409508"
FT MUTAGEN 1777
FT /note="A->V: In adl1-2; abaxially rolled leaves covered
FT with bulliform-like cells, which are normally distributed
FT only on the adaxial surface; this adaxialization concerns
FT both epidermal and mesophyll tissues. Larger L1 cells in
FT shoot apical meristems (SAM)."
FT MUTAGEN 1841
FT /note="W->R: In adl1-g1 and odm-63; abnormal embryos
FT arrested at the globular stage with an abnormal aleurone
FT layer on the ventral side."
FT /evidence="ECO:0000269|Ref.6"
FT MUTAGEN 2110
FT /note="G->R: In adl1-1; abaxially rolled leaves covered
FT with bulliform-like cells, which are normally distributed
FT only on the adaxial surface; this adaxialization concerns
FT both epidermal and mesophyll tissues. Larger L1 cells in
FT shoot apical meristems (SAM)."
FT CONFLICT 42
FT /note="Y -> F (in Ref. 2; AAL38190)"
FT /evidence="ECO:0000305"
FT CONFLICT 713
FT /note="L -> F (in Ref. 2; AAL38190)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2162 AA; 239859 MW; 9FF44A8AE2B23F0B CRC64;
MEEEEHRGVV LVCSICGFLF AVLGPLSFWI LWAVNWRPWR LYSWIYARKW PAYVQGPQLS
TLCSFFTLFA WLVVVSPITV LLVWGGILIA LLERNIIGLA VIMVGVALLL SFYSIMLWWR
TQWQSSKAVA YLLLLAVGLL CAYEFCAVYV TTGASASELN SPSGFFFGVS AISLAINMLF
ISKILFNGSG FDVDEYVRRL YKFAYSDCVE VAPVSCSPDP PDPSELYMTK SSRVLHLGLL
YLCSLMVLVV YSILYGLTSK EARWLGALTS VAVVILDWNL GLCSFRFELL KSRMIALFVA
GTSRVFLICF GVHYWYLGHC ISYAFVASVL LAAAVSCWLS ISNPSVARID ALRSTVIKLR
EGFRRKGQTS SSNSSDGCGS SVKRSSGSVE AGPHGNATDS MYRSNSQSDC VNWNNVPFDR
SNSCQEGQSS DKNIDSGRAS LAHRSNSCLS AVAVQDPETA VVSADRHGDP TASLVVCSSS
GLESQGCESS GSATASGNQQ LLDLNLAAIF QDRLNDPRIT SMLKRNGGLG DVELANLLQD
KGLDPNFSYM MKDKVMDPRI LALLQRSSLD ADREHQDDVD VTGTDSDRLD TTIANQISLS
EELRRSGLEN WLNLSRLMFH QVAGSPIRAF VVFTLIFIIE TVTVAVHRPK PIKVINATHE
QFEFGFSILL LSPVVCSIMA FIWSLCAEEM TMTSKPRKYG FIAWLLSTCV GLLLSFLSKS
SVILGLSLTV PLMVACLSFA IPIWMRNGYR FWIPGGELDS RENIRQAPGK KERALFAISI
TVFTASVIGL GAIVSAKPLD ALGYKGWDAD KKSFYSPYAT SMYLGWALSS TIAVLATGVI
PIVAWFATYR FSPSSAICVG LFATVLVSFC GVSYWGVVNS RQDGVPLKAD FLAALLPLLC
IPAVFSLFTG MYKWKDDDWK ISRGVYLFVG MGVLLLLGAI SAVIVTIRPW TVGVACLLVI
LFLVFAIGVI HYWTSNNFYL TRTQMLLVCS LAFLLALAAF LMGLFQEKPF VGASIGYFSF
LFLLTGRALT VLLSPPIVVY SPRVLPVYVY DAHADSAKNV SYAFLILYGI ALATEVWGVI
ASLILNPPFI GAAISAITLV IAFSFAVSRP CLTLKMLEDA VHFLSKDTVV QAMSRSANKT
RNAISGTYSA PQRSASSAAL LVGDPAITLD RAGNFVLPRA DVMKLRDRLR NEEITAGSFF
CGVKNCLMIG SPVDVDYRRN MCAHARILAL EEAIDTEWVY MWDKFGGYLL LLLGLTAKAE
QIQDEVRLRL FLDSIGLSDL SAKEIKKWMP EDRRHFELIQ ESYIREKEME EEVLMQRREE
EGKGRERRKA LLEREERKWK ELEISLLSSI PNAGSRDAAA MAAAVRAVGG DSALEDSFAR
DRVSSIARHI RKAQLARRAE QTGIPDTVCI LDDEPRSTGR HCGEIDLCLC ESKKVSFSIA
VMVQPVSGPV CLFGTEFQKK VCWEILVAGS EQGMEAGQVG LRLVTKGERM TTVAKEWNIG
ASSIADGRWH LVTVTIDADL GEATSFIDGV YDGYQNALPL PRNNGIWEPG TDIWVGARPP
TDLDAFGRSD SEGSDSKMQI MDAFLWGRCL TEDEVAMLHT AICSAEYGLF DLAAEDAWHG
SYSARVDDWE SEEANFELYD QEDVEWDGQY SSGRKRHARD SVAIDIDSFA RRPRKPRFET
REEVNQRMLS VERAVREALI AKGERNFTDQ EFPPDDRSLF VDPMNPSLKL QVVSEWMRPS
DIAKEVSISS QPCLFSGSVN SSDVCQGRLG DCWFLSAVAV LTEMARISEV IITPEYNEEG
IYTVRFCIQG EWVAVVVDDW IPCESPGKPA FATSRKQNEL WVSILEKAYA KLHGSYEALE
GGLVQDALVD LTGGAGEEID MRSPQAQIDL ASGRLWSQLL HFKQEGFLLG AGSPSGSDAH
ISSSGIVQGH AYSILQVREV DGHKLVQIRN PWANEVEWNG PWSDSSQEWT ERMKHKLKHV
PQSKNGVFWM SWQDFQIHFR SIYVCRVYPP EMRYSVHGQW RGYSAGGCQD YDSWHQNPQY
RLRVTGRDAL YPVHVFITLT QGVGFSRKTN GFRNYQSSHD SSMFYIGMRI LKTRGCRAAY
NIYMHESVGG TDYVNSREIS CELVLEPYPK GYTIVPTTIH PGEEAPFVLS VFTKAPIKLE
AV
