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STRK1_ORYSI
ID   STRK1_ORYSI             Reviewed;         361 AA.
AC   A2XW02;
DT   07-NOV-2018, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Salt tolerance receptor-like cytoplasmic kinase 1 {ECO:0000305};
DE            EC=2.7.12.1 {ECO:0000250|UniProtKB:Q7XR88};
DE   AltName: Full=Receptor-like cytoplasmic kinase 154 {ECO:0000305};
DE            Short=OsRLCK154 {ECO:0000305};
GN   ORFNames=OsI_16820 {ECO:0000312|EMBL:EAY95012.1};
OS   Oryza sativa subsp. indica (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=39946;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. 93-11;
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   [2]
RP   TISSUE SPECIFICITY, INDUCTION BY ABIOTIC STRESSES, GENE FAMILY, AND
RP   NOMENCLATURE.
RX   PubMed=19825577; DOI=10.1093/mp/ssn047;
RA   Vij S., Giri J., Dansana P.K., Kapoor S., Tyagi A.K.;
RT   "The receptor-like cytoplasmic kinase (OsRLCK) gene family in rice:
RT   organization, phylogenetic relationship, and expression during development
RT   and stress.";
RL   Mol. Plant 1:732-750(2008).
CC   -!- FUNCTION: Acts probably as a dual specificity protein kinase
CC       (Probable). Regulates hydrogen peroxide (H(2)O(2)) homeostasis and
CC       improves salt tolerance by phosphorylating tyrosine residues of CATC
CC       thus activating its catalase activity. Promotes growth at the seedling
CC       stage and prevents grain yield loss under salt stress conditions (By
CC       similarity). {ECO:0000250|UniProtKB:Q7XR88, ECO:0000305}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.12.1;
CC         Evidence={ECO:0000250|UniProtKB:Q7XR88};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.12.1; Evidence={ECO:0000250|UniProtKB:Q7XR88};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC         [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.1;
CC         Evidence={ECO:0000250|UniProtKB:Q7XR88};
CC   -!- SUBUNIT: Self-interacts. Interacts with CATA, CATB and CATC at the
CC       plasma membrane. {ECO:0000250|UniProtKB:Q7XR88}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q7XR88};
CC       Lipid-anchor {ECO:0000250|UniProtKB:Q7XR88}.
CC   -!- TISSUE SPECIFICITY: Accumulates in seeds.
CC       {ECO:0000269|PubMed:19825577}.
CC   -!- INDUCTION: By cold, salt and dehydration.
CC       {ECO:0000269|PubMed:19825577}.
CC   -!- PTM: Palmitoylated. {ECO:0000250|UniProtKB:Q7XR88}.
CC   -!- PTM: Autophosphorylated. {ECO:0000250|UniProtKB:Q7XR88}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; CM000129; EAY95012.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2XW02; -.
DR   SMR; A2XW02; -.
DR   STRING; 39946.A2XW02; -.
DR   EnsemblPlants; BGIOSGA014633-TA; BGIOSGA014633-PA; BGIOSGA014633.
DR   Gramene; BGIOSGA014633-TA; BGIOSGA014633-PA; BGIOSGA014633.
DR   HOGENOM; CLU_000288_21_4_1; -.
DR   OMA; LGNCDNG; -.
DR   Proteomes; UP000007015; Chromosome 4.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0043621; F:protein self-association; ISS:UniProtKB.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004713; F:protein tyrosine kinase activity; ISS:UniProtKB.
DR   GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:InterPro.
DR   GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
DR   GO; GO:0010310; P:regulation of hydrogen peroxide metabolic process; ISS:UniProtKB.
DR   GO; GO:1902882; P:regulation of response to oxidative stress; ISS:UniProtKB.
DR   GO; GO:1901000; P:regulation of response to salt stress; ISS:UniProtKB.
DR   GO; GO:0009409; P:response to cold; IEP:UniProtKB.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:EnsemblPlants.
DR   GO; GO:1902074; P:response to salt; IEP:UniProtKB.
DR   GO; GO:0009651; P:response to salt stress; IEA:EnsemblPlants.
DR   GO; GO:0009414; P:response to water deprivation; IEP:UniProtKB.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR045271; SRF-like.
DR   PANTHER; PTHR27001; PTHR27001; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cell membrane; Kinase; Lipoprotein; Membrane;
KW   Nucleotide-binding; Palmitate; Phosphoprotein; Reference proteome;
KW   Serine/threonine-protein kinase; Stress response; Transferase;
KW   Tyrosine-protein kinase.
FT   CHAIN           1..361
FT                   /note="Salt tolerance receptor-like cytoplasmic kinase 1"
FT                   /id="PRO_0000445632"
FT   DOMAIN          67..347
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        195
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         73..81
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         95
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   361 AA;  38394 MW;  35E5A77F9F1B6750 CRC64;
     MFTGCGLFAC VRRCDGGDVR KRGEAGAMSS RVAADPAGVE EEGSCKNVAA ASARQLAWAD
     VESVTGGFSS RVIGHGGFST VYLASLSSSR LGAVKVHCSS ERLHRAFRQE LEVLLSLRHP
     HIVRLLGYCD ERDEGVLVFE YAPNGDLHER LHCSEVAGGV ASVLPWARRV AIAFQVAMAL
     EYLHESRHPA VIHGDIKASN VLLDANMNAK LCDFGFAHVG FSATVGCRPS ARAVMGSPGY
     VDPHLIRSGV ATKKSDVYSF GVLLLELVTG KEAVCRDTGR RLTAAVGPML SEGKVADVVD
     RRLGGEHDGA EAAVMAELAM QCIGDSPGLR PSMADVVRAL QEKTSALASA VGSRLDRKMM
     F
 
 
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