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CAL1_ORYSJ
ID   CAL1_ORYSJ              Reviewed;          80 AA.
AC   Q6K209;
DT   23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Defensin-like protein CAL1 {ECO:0000305};
DE   AltName: Full=OsCPT1 {ECO:0000303|PubMed:19279197};
DE   AltName: Full=Pathogen-related protein 12 {ECO:0000305};
DE            Short=OsPR12 {ECO:0000305};
DE   AltName: Full=Protein CADMIUM ACCUMULATION IN LEAF 1 {ECO:0000303|PubMed:29440679};
DE   Flags: Precursor;
GN   Name=CAL1 {ECO:0000303|PubMed:29440679};
GN   Synonyms=CPT1 {ECO:0000303|PubMed:19279197}, PR12 {ECO:0000305};
GN   OrderedLocusNames=Os02g0629800 {ECO:0000312|EMBL:BAF09407.1},
GN   LOC_Os02g41904 {ECO:0000305};
GN   ORFNames=B1469H02.30 {ECO:0000312|EMBL:BAD23741.1},
GN   OsJ_07607 {ECO:0000312|EMBL:EEE57415.1};
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 [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   [2]
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   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [5]
RP   INDUCTION.
RX   PubMed=19279197; DOI=10.1104/pp.108.133454;
RA   Ma Q., Dai X., Xu Y., Guo J., Liu Y., Chen N., Xiao J., Zhang D., Xu Z.,
RA   Zhang X., Chong K.;
RT   "Enhanced tolerance to chilling stress in OsMYB3R-2 transgenic rice is
RT   mediated by alteration in cell cycle and ectopic expression of stress
RT   genes.";
RL   Plant Physiol. 150:244-256(2009).
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION BY CADMIUM,
RP   BIOTECHNOLOGY, AND MUTAGENESIS OF CYS-34; CYS-45; CYS-51; CYS-55; CYS-65;
RP   LEU-70; CYS-74; CYS-76 AND CYS-80.
RX   PubMed=29440679; DOI=10.1038/s41467-018-03088-0;
RA   Luo J.S., Huang J., Zeng D.L., Peng J.S., Zhang G.B., Ma H.L., Guan Y.,
RA   Yi H.Y., Fu Y.L., Han B., Lin H.X., Qian Q., Gong J.M.;
RT   "A defensin-like protein drives cadmium efflux and allocation in rice.";
RL   Nat. Commun. 9:645-645(2018).
CC   -!- FUNCTION: Plant defensin-like protein involved in accumulation of
CC       cadmium (Cd) in rice leaves. Mediates Cd efflux from cytosol into
CC       extracellular spaces via chelation. This drives Cd secretion from xylem
CC       parenchyma cells into the xylem vessels, hence lowering Cd levels in
CC       cytosol meanwhile promoting Cd translocation from roots to shoots.
CC       {ECO:0000269|PubMed:29440679}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC       {ECO:0000269|PubMed:29440679}.
CC   -!- TISSUE SPECIFICITY: Expressed preferentially in root exodermis and
CC       xylem parenchyma cells in vasculature of root and flag leaf sheath.
CC       {ECO:0000269|PubMed:29440679}.
CC   -!- INDUCTION: Induced by cadmium in roots (PubMed:29440679). Down-
CC       regulated by cold stress (PubMed:19279197).
CC       {ECO:0000269|PubMed:19279197, ECO:0000269|PubMed:29440679}.
CC   -!- BIOTECHNOLOGY: Rice varieties with high CAL1 activity over-accumulate
CC       cadmium (Cd) in rice straws, but are not affected by Cd accumulation,
CC       or the accumulation of other essential metals in rice grains. These
CC       functional characteristics could be used to breed dual-function rice
CC       varieties that produce safe grains while remediating paddy soils.
CC       {ECO:0000269|PubMed:29440679}.
CC   -!- SIMILARITY: Belongs to the DEFL family. {ECO:0000305}.
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DR   EMBL; AP006168; BAD23741.1; -; Genomic_DNA.
DR   EMBL; AP008208; BAF09407.1; -; Genomic_DNA.
DR   EMBL; AP014958; BAS79891.1; -; Genomic_DNA.
DR   EMBL; CM000139; EEE57415.1; -; Genomic_DNA.
DR   RefSeq; XP_015624063.1; XM_015768577.1.
DR   PDB; 6LCQ; X-ray; 1.62 A; A/B=32-80.
DR   PDBsum; 6LCQ; -.
DR   AlphaFoldDB; Q6K209; -.
DR   SMR; Q6K209; -.
DR   STRING; 4530.OS02T0629800-01; -.
DR   PaxDb; Q6K209; -.
DR   PRIDE; Q6K209; -.
DR   EnsemblPlants; Os02t0629800-01; Os02t0629800-01; Os02g0629800.
DR   GeneID; 4330051; -.
DR   Gramene; Os02t0629800-01; Os02t0629800-01; Os02g0629800.
DR   KEGG; osa:4330051; -.
DR   eggNOG; ENOG502STQ5; Eukaryota.
DR   HOGENOM; CLU_161668_1_1_1; -.
DR   InParanoid; Q6K209; -.
DR   OMA; EGATRKC; -.
DR   OrthoDB; 1625543at2759; -.
DR   PlantReactome; R-OSA-6787011; Jasmonic acid signaling.
DR   Proteomes; UP000000763; Chromosome 2.
DR   Proteomes; UP000007752; Chromosome 2.
DR   Proteomes; UP000059680; Chromosome 2.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0046870; F:cadmium ion binding; IDA:UniProtKB.
DR   GO; GO:0055073; P:cadmium ion homeostasis; IMP:UniProtKB.
DR   GO; GO:0006952; P:defense response; IEA:InterPro.
DR   Gene3D; 3.30.30.10; -; 1.
DR   InterPro; IPR008176; Defensin_plant.
DR   InterPro; IPR003614; Scorpion_toxin-like.
DR   InterPro; IPR036574; Scorpion_toxin-like_sf.
DR   PRINTS; PR00288; PUROTHIONIN.
DR   SMART; SM00505; Knot1; 1.
DR   SUPFAM; SSF57095; SSF57095; 1.
DR   PROSITE; PS00940; GAMMA_THIONIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cadmium; Disulfide bond; Metal-binding; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..80
FT                   /note="Defensin-like protein CAL1"
FT                   /id="PRO_5013533355"
FT   DISULFID        34..80
FT                   /evidence="ECO:0000250|UniProtKB:P69241"
FT   DISULFID        45..65
FT                   /evidence="ECO:0000250|UniProtKB:P69241"
FT   DISULFID        51..74
FT                   /evidence="ECO:0000250|UniProtKB:P69241"
FT   DISULFID        55..76
FT                   /evidence="ECO:0000250|UniProtKB:P69241"
FT   MUTAGEN         34
FT                   /note="C->A: No effect on the ability to bind cadmium."
FT                   /evidence="ECO:0000269|PubMed:29440679"
FT   MUTAGEN         45
FT                   /note="C->A: No effect on the ability to bind cadmium."
FT                   /evidence="ECO:0000269|PubMed:29440679"
FT   MUTAGEN         51
FT                   /note="C->A: No effect on the ability to bind cadmium."
FT                   /evidence="ECO:0000269|PubMed:29440679"
FT   MUTAGEN         55
FT                   /note="C->A: Decreases the ability to bind cadmium."
FT                   /evidence="ECO:0000269|PubMed:29440679"
FT   MUTAGEN         65
FT                   /note="C->A: Decreases the ability to bind cadmium."
FT                   /evidence="ECO:0000269|PubMed:29440679"
FT   MUTAGEN         70
FT                   /note="L->V: Decreases the ability to bind cadmium; No
FT                   effect on the localization to the extracellular space."
FT                   /evidence="ECO:0000269|PubMed:29440679"
FT   MUTAGEN         74
FT                   /note="C->A: Decreases the ability to bind cadmium."
FT                   /evidence="ECO:0000269|PubMed:29440679"
FT   MUTAGEN         76
FT                   /note="C->A: No effect on the ability to bind cadmium."
FT                   /evidence="ECO:0000269|PubMed:29440679"
FT   MUTAGEN         80
FT                   /note="C->A: No effect on the ability to bind cadmium."
FT                   /evidence="ECO:0000269|PubMed:29440679"
FT   STRAND          33..37
FT                   /evidence="ECO:0007829|PDB:6LCQ"
FT   HELIX           48..57
FT                   /evidence="ECO:0007829|PDB:6LCQ"
FT   STRAND          61..68
FT                   /evidence="ECO:0007829|PDB:6LCQ"
FT   STRAND          71..79
FT                   /evidence="ECO:0007829|PDB:6LCQ"
SQ   SEQUENCE   80 AA;  8784 MW;  3326C0461F10A1CA CRC64;
     MAPSRRMVAS AFLLLAILVA TEMGTTKVAE ARHCLSQSHR FKGMCVSSNN CANVCRTESF
     PDGECKSHGL ERKCFCKKVC
 
 
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