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Y5516_ARATH
ID   Y5516_ARATH             Reviewed;         640 AA.
AC   Q9FHK7; C0LGS6;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 141.
DE   RecName: Full=Probable leucine-rich repeat receptor-like protein kinase At5g05160;
DE            EC=2.7.11.-;
DE   Flags: Precursor;
GN   OrderedLocusNames=At5g05160; ORFNames=K2A11.3;
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 [MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=20064227; DOI=10.1186/1471-2164-11-19;
RA   Gou X., He K., Yang H., Yuan T., Lin H., Clouse S.D., Li J.;
RT   "Genome-wide cloning and sequence analysis of leucine-rich repeat receptor-
RT   like protein kinase genes in Arabidopsis thaliana.";
RL   BMC Genomics 11:19-19(2010).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10470850; DOI=10.1093/dnares/6.3.183;
RA   Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA   Miyajima N., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT   features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT   clones.";
RL   DNA Res. 6:183-195(1999).
RN   [3]
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).
CC   -!- FUNCTION: Probable leucine-rich repeat receptor-like protein kinase.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
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; FJ708769; ACN59361.1; -; mRNA.
DR   EMBL; AB018111; BAB09692.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED90835.1; -; Genomic_DNA.
DR   RefSeq; NP_196135.1; NM_120598.4.
DR   AlphaFoldDB; Q9FHK7; -.
DR   SMR; Q9FHK7; -.
DR   BioGRID; 15677; 2.
DR   IntAct; Q9FHK7; 2.
DR   STRING; 3702.AT5G05160.1; -.
DR   iPTMnet; Q9FHK7; -.
DR   PaxDb; Q9FHK7; -.
DR   PRIDE; Q9FHK7; -.
DR   ProteomicsDB; 243141; -.
DR   EnsemblPlants; AT5G05160.1; AT5G05160.1; AT5G05160.
DR   GeneID; 830398; -.
DR   Gramene; AT5G05160.1; AT5G05160.1; AT5G05160.
DR   KEGG; ath:AT5G05160; -.
DR   Araport; AT5G05160; -.
DR   TAIR; locus:2156784; AT5G05160.
DR   eggNOG; ENOG502QT13; Eukaryota.
DR   HOGENOM; CLU_000288_92_6_1; -.
DR   InParanoid; Q9FHK7; -.
DR   OMA; NWSESTP; -.
DR   OrthoDB; 389502at2759; -.
DR   PhylomeDB; Q9FHK7; -.
DR   PRO; PR:Q9FHK7; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FHK7; baseline and differential.
DR   Genevisible; Q9FHK7; AT.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:2000605; P:positive regulation of secondary growth; IMP:TAIR.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   Gene3D; 3.80.10.10; -; 2.
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; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF13855; LRR_8; 1.
DR   Pfam; PF08263; LRRNT_2; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Leucine-rich repeat; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Receptor; Reference proteome; Repeat;
KW   Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..640
FT                   /note="Probable leucine-rich repeat receptor-like protein
FT                   kinase At5g05160"
FT                   /id="PRO_0000324846"
FT   TRANSMEM        267..287
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REPEAT          99..120
FT                   /note="LRR 1"
FT   REPEAT          123..144
FT                   /note="LRR 2"
FT   REPEAT          149..172
FT                   /note="LRR 3"
FT   REPEAT          173..194
FT                   /note="LRR 4"
FT   REPEAT          195..215
FT                   /note="LRR 5"
FT   DOMAIN          347..619
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          299..321
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          619..640
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        469
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         353..361
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         375
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         349
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q94F62"
FT   MOD_RES         370
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q94F62"
FT   MOD_RES         427
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT   MOD_RES         445
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT   MOD_RES         498
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q94F62"
FT   MOD_RES         503
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q94F62"
FT   MOD_RES         514
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT   MOD_RES         518
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q94AG2"
SQ   SEQUENCE   640 AA;  70564 MW;  0FA783835E8AECCA CRC64;
     MNSSHTAFVA ASFFFLLLAA TAVLVSADLA SDEQALLNFA ASVPHPPKLN WNKNLSLCSS
     WIGITCDESN PTSRVVAVRL PGVGLYGSIP PATLGKLDAL KVLSLRSNSL FGTLPSDILS
     LPSLEYLYLQ HNNFSGELTT NSLPSISKQL VVLDLSYNSL SGNIPSGLRN LSQITVLYLQ
     NNSFDGPIDS LDLPSVKVVN LSYNNLSGPI PEHLKKSPEY SFIGNSLLCG PPLNACSGGA
     ISPSSNLPRP LTENLHPVRR RQSKAYIIAI VVGCSVAVLF LGIVFLVCLV KKTKKEEGGG
     EGVRTQMGGV NSKKPQDFGS GVQDPEKNKL FFFERCNHNF DLEDLLKASA EVLGKGSFGT
     AYKAVLEDTT AVVVKRLREV VASKKEFEQQ MEIVGKINQH SNFVPLLAYY YSKDEKLLVY
     KYMTKGSLFG IMHGNRGDRG VDWETRMKIA TGTSKAISYL HSLKFVHGDI KSSNILLTED
     LEPCLSDTSL VTLFNLPTHT PRTIGYNAPE VIETRRVSQR SDVYSFGVVI LEMLTGKTPL
     TQPGLEDERV VIDLPRWVRS VVREEWTAEV FDVELLKFQN IEEEMVQMLQ LALACVARNP
     ESRPKMEEVA RMIEDVRRLD QSQQLQQNRT SSEATSNVSE
 
 
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