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Y5332_ARATH
ID   Y5332_ARATH             Reviewed;         601 AA.
AC   Q9FK10; Q0WUK3;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Probable inactive receptor kinase At5g53320;
DE   Flags: Precursor;
GN   OrderedLocusNames=At5g53320; ORFNames=K19E1.12;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA   Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT   features of the regions of 1,367,185 bp covered by 19 physically assigned
RT   P1 and TAC clones.";
RL   DNA Res. 5:203-216(1998).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- INTERACTION:
CC       Q9FK10; F4I065: At1g49100; NbExp=2; IntAct=EBI-20654730, EBI-20654598;
CC       Q9FK10; A0A178WLG7: At1g51790; NbExp=2; IntAct=EBI-20654730, EBI-20652336;
CC       Q9FK10; A0A1P8ASI5: At1g56120; NbExp=3; IntAct=EBI-20654730, EBI-20656718;
CC       Q9FK10; O64556: At2g19230; NbExp=4; IntAct=EBI-20654730, EBI-20662335;
CC       Q9FK10; Q9LIG2: At3g21340; NbExp=2; IntAct=EBI-20654730, EBI-941096;
CC       Q9FK10; Q9SNA2: F18L15.70; NbExp=3; IntAct=EBI-20654730, EBI-20658889;
CC       Q9FK10; C0LGU0: PRK1; NbExp=2; IntAct=EBI-20654730, EBI-20665360;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC       inactive.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. {ECO:0000305}.
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DR   EMBL; AB013388; BAB09794.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED96339.1; -; Genomic_DNA.
DR   EMBL; AK227151; BAE99195.1; -; mRNA.
DR   RefSeq; NP_200144.1; NM_124711.4.
DR   AlphaFoldDB; Q9FK10; -.
DR   SMR; Q9FK10; -.
DR   BioGRID; 20658; 40.
DR   IntAct; Q9FK10; 46.
DR   STRING; 3702.AT5G53320.1; -.
DR   iPTMnet; Q9FK10; -.
DR   PaxDb; Q9FK10; -.
DR   PRIDE; Q9FK10; -.
DR   ProteomicsDB; 243159; -.
DR   EnsemblPlants; AT5G53320.1; AT5G53320.1; AT5G53320.
DR   GeneID; 835413; -.
DR   Gramene; AT5G53320.1; AT5G53320.1; AT5G53320.
DR   KEGG; ath:AT5G53320; -.
DR   Araport; AT5G53320; -.
DR   TAIR; locus:2154227; AT5G53320.
DR   eggNOG; ENOG502QTFK; Eukaryota.
DR   HOGENOM; CLU_000288_92_6_1; -.
DR   InParanoid; Q9FK10; -.
DR   OMA; SICTKWT; -.
DR   OrthoDB; 826997at2759; -.
DR   PhylomeDB; Q9FK10; -.
DR   PRO; PR:Q9FK10; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FK10; baseline and differential.
DR   Genevisible; Q9FK10; AT.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   Gene3D; 3.80.10.10; -; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR013210; LRR_N_plant-typ.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   Pfam; PF00560; LRR_1; 2.
DR   Pfam; PF08263; LRRNT_2; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Leucine-rich repeat; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..601
FT                   /note="Probable inactive receptor kinase At5g53320"
FT                   /id="PRO_0000324842"
FT   TRANSMEM        239..259
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REPEAT          91..114
FT                   /note="LRR 1"
FT   REPEAT          115..136
FT                   /note="LRR 2"
FT   REPEAT          139..161
FT                   /note="LRR 3"
FT   REPEAT          163..184
FT                   /note="LRR 4"
FT   REPEAT          185..206
FT                   /note="LRR 5"
FT   DOMAIN          308..569
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         314..322
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         336
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         310
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q94F62"
FT   MOD_RES         387
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT   MOD_RES         408
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT   MOD_RES         478
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT   MOD_RES         549
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT   CONFLICT        88
FT                   /note="R -> S (in Ref. 3; BAE99195)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   601 AA;  66863 MW;  4709B340F97DC4DE CRC64;
     MKCQVVLILI VVIFNVCIEA ETIKEDKHTL LQFVNNINHS HSLNWSPSLS ICTKWTGVTC
     NSDHSSVDAL HLAATGLRGD IELSIIARLS NLRFLILSSN NISGTFPTTL QALKNLTELK
     LDFNEFSGPL PSDLSSWERL QVLDLSNNRF NGSIPSSIGK LTLLHSLNLA YNKFSGEIPD
     LHIPGLKLLN LAHNNLTGTV PQSLQRFPLS AFVGNKVLAP VHSSLRKHTK HHNHVVLGIA
     LSVCFAILAL LAILLVIIIH NREEQRRSSK DKPSKRRKDS DPNVGEGDNK IVFFEGKNLV
     FDLEDLLRAS AEVLGKGPFG TTYKVDLEDS ATIVVKRIKE VSVPQREFEQ QIENIGSIKH
     ENVATLRGYF YSKDEKLVVY DYYEHGSLST LLHGQKGLRD RKRLEWETRL NMVYGTARGV
     AHIHSQSGGK LVHGNIKSSN IFLNGKGYGC ISGTGMATLM HSLPRHAVGY RAPEITDTRK
     GTQPSDVYSF GILIFEVLTG KSEVANLVRW VNSVVREEWT GEVFDEELLR CTQVEEEMVE
     MLQVGMVCTA RLPEKRPNMI EVVRMVEEIR PEKLASGYRS EVSTGATTTP IGSLSGSPYI
     L
 
 
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