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Y5410_ARATH
ID   Y5410_ARATH             Reviewed;         614 AA.
AC   Q9FL63;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=Inactive leucine-rich repeat receptor-like serine/threonine-protein kinase At5g24100;
DE   Flags: Precursor;
GN   OrderedLocusNames=At5g24100; ORFNames=MZF18.1;
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=9679202; DOI=10.1093/dnares/5.2.131;
RA   Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT   features of the regions of 1,381,565 bp covered by twenty one physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:131-145(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA   Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT   features of the regions of 1,456,315 bp covered by nineteen physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:41-54(1998).
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).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE 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   [6]
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       Q9FL63; C0LGJ1: At1g74360; NbExp=3; IntAct=EBI-20657062, EBI-20652666;
CC       Q9FL63; C0LGS3: At4g37250; NbExp=3; IntAct=EBI-20657062, EBI-16955335;
CC       Q9FL63; C0LGQ4: MDIS2; NbExp=2; IntAct=EBI-20657062, EBI-20665429;
CC       Q9FL63; Q93ZS4: NIK3; NbExp=3; IntAct=EBI-20657062, EBI-17121474;
CC       Q9FL63; Q9ZVR7: PSKR1; NbExp=3; IntAct=EBI-20657062, EBI-16172949;
CC       Q9FL63; Q9FN37: PSKR2; NbExp=2; IntAct=EBI-20657062, EBI-16902047;
CC       Q9FL63; Q9M2R4: T10K17.40; NbExp=3; IntAct=EBI-20657062, EBI-20657109;
CC       Q9FL63; P43298: TMK1; NbExp=3; IntAct=EBI-20657062, EBI-2023970;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}.
CC   -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC       inactive.
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; AB010696; BAB11570.1; -; Genomic_DNA.
DR   EMBL; AB009056; BAB11570.1; JOINED; Genomic_DNA.
DR   EMBL; CP002688; AED93256.1; -; Genomic_DNA.
DR   EMBL; BT005989; AAO64924.1; -; mRNA.
DR   EMBL; FJ708782; ACN59373.1; -; mRNA.
DR   EMBL; AK227407; BAE99411.1; -; mRNA.
DR   RefSeq; NP_197798.1; NM_122315.4.
DR   AlphaFoldDB; Q9FL63; -.
DR   SMR; Q9FL63; -.
DR   BioGRID; 17750; 51.
DR   IntAct; Q9FL63; 53.
DR   STRING; 3702.AT5G24100.1; -.
DR   PaxDb; Q9FL63; -.
DR   PRIDE; Q9FL63; -.
DR   ProteomicsDB; 243140; -.
DR   EnsemblPlants; AT5G24100.1; AT5G24100.1; AT5G24100.
DR   GeneID; 832475; -.
DR   Gramene; AT5G24100.1; AT5G24100.1; AT5G24100.
DR   KEGG; ath:AT5G24100; -.
DR   Araport; AT5G24100; -.
DR   TAIR; locus:2178712; AT5G24100.
DR   eggNOG; ENOG502QTFK; Eukaryota.
DR   HOGENOM; CLU_000288_92_6_1; -.
DR   InParanoid; Q9FL63; -.
DR   OMA; ARTEKRY; -.
DR   OrthoDB; 338975at2759; -.
DR   PhylomeDB; Q9FL63; -.
DR   PRO; PR:Q9FL63; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FL63; baseline and differential.
DR   Genevisible; Q9FL63; AT.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; -; 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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   Pfam; PF00560; LRR_1; 1.
DR   Pfam; PF13855; LRR_8; 1.
DR   Pfam; PF08263; LRRNT_2; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell membrane; Glycoprotein; Leucine-rich repeat; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome; Repeat;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..614
FT                   /note="Inactive leucine-rich repeat receptor-like
FT                   serine/threonine-protein kinase At5g24100"
FT                   /id="PRO_0000403347"
FT   TOPO_DOM        22..251
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        252..272
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        273..614
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REPEAT          71..95
FT                   /note="LRR 1"
FT   REPEAT          96..120
FT                   /note="LRR 2"
FT   REPEAT          121..146
FT                   /note="LRR 3"
FT   REPEAT          148..167
FT                   /note="LRR 4"
FT   REPEAT          168..190
FT                   /note="LRR 5"
FT   REPEAT          191..214
FT                   /note="LRR 6"
FT   DOMAIN          341..611
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REPEAT          578..601
FT                   /note="LRR 7"
FT   BINDING         347..355
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         369
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         343
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q94F62"
FT   MOD_RES         420
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT   MOD_RES         441
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT   MOD_RES         514
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT   MOD_RES         591
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT   CARBOHYD        53
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        146
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        158
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        167
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        197
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        202
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   614 AA;  67963 MW;  C61DAD9A8B3A6B74 CRC64;
     MSRGRSFIFY FVLFLFFGSS ALYSQVTGDL AGDRQALLDF LNNIIHPRSL AWNTSSPVCT
     TWPGVTCDID GTRVTALHLP GASLLGVIPP GTISRLSELQ ILSLRSNGLR GPFPIDFLQL
     KKLKAISLGN NRFSGPLPSD YATWTNLTVL DLYSNRFNGS IPAGFANLTG LVSLNLAKNS
     FSGEIPDLNL PGLRRLNFSN NNLTGSIPNS LKRFGNSAFS GNNLVFENAP PPAVVSFKEQ
     KKNGIYISEP AILGIAISVC FVIFFVIAVV IIVCYVKRQR KSETEPKPDK LKLAKKMPSE
     KEVSKLGKEK NIEDMEDKSE INKVMFFEGS NLAFNLEDLL IASAEFLGKG VFGMTYKAVL
     EDSKVIAVKR LKDIVVSRKD FKHQMEIVGN IKHENVAPLR AYVCSKEEKL MVYDYDSNGS
     LSLRLHGKNA DEGHVPLNWE TRLRFMIGVA KGLGHIHTQN LAHGNIKSSN VFMNSEGYGC
     ISEAGLPLLT NPVVRADSSA RSVLRYRAPE VTDTRRSTPE SDIYSFGILM LETLTGRSIM
     DDRKEGIDLV VWVNDVISKQ WTGEVFDLEL VKTPNVEAKL LQMLQLGTSC TAMVPAKRPD
     MVKVVETLEE IERD
 
 
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