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Y3804_ARATH
ID   Y3804_ARATH             Reviewed;        1016 AA.
AC   Q9LRT1;
DT   24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Probably inactive leucine-rich repeat receptor-like protein kinase At3g28040;
DE   Flags: Precursor;
GN   OrderedLocusNames=At3g28040; ORFNames=MMG15.21;
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=10907853; DOI=10.1093/dnares/7.3.217;
RA   Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT   features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT   clones.";
RL   DNA Res. 7:217-221(2000).
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;
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).
CC   -!- INTERACTION:
CC       Q9LRT1; C0LGI2: At1g67720; NbExp=2; IntAct=EBI-16956175, EBI-17070892;
CC       Q9LRT1; Q9M9C5: At1g68400; NbExp=3; IntAct=EBI-16956175, EBI-1238661;
CC       Q9LRT1; C0LGJ9: At2g02780; NbExp=2; IntAct=EBI-16956175, EBI-20651541;
CC       Q9LRT1; C0LGL4: At2g28960; NbExp=2; IntAct=EBI-16956175, EBI-16946048;
CC       Q9LRT1; C0LGM1: LRR-RLK; NbExp=2; IntAct=EBI-16956175, EBI-20653589;
CC       Q9LRT1; O64483: SIRK; NbExp=2; IntAct=EBI-16956175, EBI-16905038;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC       inactive. Lacks the conserved Asp active site at position 854, which is
CC       replaced by an Asn residue.
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; AB028616; BAB01126.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE77394.1; -; Genomic_DNA.
DR   EMBL; FJ708729; ACN59324.1; -; mRNA.
DR   RefSeq; NP_189443.2; NM_113722.3.
DR   AlphaFoldDB; Q9LRT1; -.
DR   SMR; Q9LRT1; -.
DR   BioGRID; 7758; 46.
DR   IntAct; Q9LRT1; 43.
DR   STRING; 3702.AT3G28040.1; -.
DR   iPTMnet; Q9LRT1; -.
DR   PaxDb; Q9LRT1; -.
DR   PRIDE; Q9LRT1; -.
DR   ProteomicsDB; 242993; -.
DR   EnsemblPlants; AT3G28040.1; AT3G28040.1; AT3G28040.
DR   GeneID; 822428; -.
DR   Gramene; AT3G28040.1; AT3G28040.1; AT3G28040.
DR   KEGG; ath:AT3G28040; -.
DR   Araport; AT3G28040; -.
DR   TAIR; locus:2091353; AT3G28040.
DR   eggNOG; ENOG502QU7G; Eukaryota.
DR   HOGENOM; CLU_000288_22_1_1; -.
DR   InParanoid; Q9LRT1; -.
DR   OMA; PNEYPHG; -.
DR   OrthoDB; 826997at2759; -.
DR   PhylomeDB; Q9LRT1; -.
DR   PRO; PR:Q9LRT1; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LRT1; baseline and differential.
DR   Genevisible; Q9LRT1; AT.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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; -; 4.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
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   Pfam; PF13516; LRR_6; 1.
DR   Pfam; PF13855; LRR_8; 3.
DR   Pfam; PF08263; LRRNT_2; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00369; LRR_TYP; 11.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS51450; LRR; 16.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Glycoprotein; Leucine-rich repeat; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome; Repeat;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..1016
FT                   /note="Probably inactive leucine-rich repeat receptor-like
FT                   protein kinase At3g28040"
FT                   /id="PRO_0000389466"
FT   TOPO_DOM        27..646
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        647..667
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        668..1016
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REPEAT          102..124
FT                   /note="LRR 1"
FT   REPEAT          125..147
FT                   /note="LRR 2"
FT   REPEAT          149..171
FT                   /note="LRR 3"
FT   REPEAT          174..196
FT                   /note="LRR 4"
FT   REPEAT          198..219
FT                   /note="LRR 5"
FT   REPEAT          224..245
FT                   /note="LRR 6"
FT   REPEAT          248..270
FT                   /note="LRR 7"
FT   REPEAT          272..295
FT                   /note="LRR 8"
FT   REPEAT          296..318
FT                   /note="LRR 9"
FT   REPEAT          320..342
FT                   /note="LRR 10"
FT   REPEAT          344..366
FT                   /note="LRR 11"
FT   REPEAT          368..390
FT                   /note="LRR 12"
FT   REPEAT          391..413
FT                   /note="LRR 13"
FT   REPEAT          416..438
FT                   /note="LRR 14"
FT   REPEAT          440..462
FT                   /note="LRR 15"
FT   REPEAT          464..486
FT                   /note="LRR 16"
FT   REPEAT          488..510
FT                   /note="LRR 17"
FT   REPEAT          512..535
FT                   /note="LRR 18"
FT   REPEAT          536..559
FT                   /note="LRR 19"
FT   REPEAT          560..582
FT                   /note="LRR 20"
FT   DOMAIN          726..1013
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         732..740
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         755
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         841
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT   MOD_RES         898
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT   CARBOHYD        112
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        135
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        171
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        203
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        349
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        445
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        464
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        509
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        522
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        565
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1016 AA;  111932 MW;  84577A7A2777F1C4 CRC64;
     MGKQRRTMIS FTLFLTLTMM SSLINGDTDS IQLNDDVLGL IVFKSDLNDP FSHLESWTED
     DNTPCSWSYV KCNPKTSRVI ELSLDGLALT GKINRGIQKL QRLKVLSLSN NNFTGNINAL
     SNNNHLQKLD LSHNNLSGQI PSSLGSITSL QHLDLTGNSF SGTLSDDLFN NCSSLRYLSL
     SHNHLEGQIP STLFRCSVLN SLNLSRNRFS GNPSFVSGIW RLERLRALDL SSNSLSGSIP
     LGILSLHNLK ELQLQRNQFS GALPSDIGLC PHLNRVDLSS NHFSGELPRT LQKLKSLNHF
     DVSNNLLSGD FPPWIGDMTG LVHLDFSSNE LTGKLPSSIS NLRSLKDLNL SENKLSGEVP
     ESLESCKELM IVQLKGNDFS GNIPDGFFDL GLQEMDFSGN GLTGSIPRGS SRLFESLIRL
     DLSHNSLTGS IPGEVGLFIH MRYLNLSWNH FNTRVPPEIE FLQNLTVLDL RNSALIGSVP
     ADICESQSLQ ILQLDGNSLT GSIPEGIGNC SSLKLLSLSH NNLTGPIPKS LSNLQELKIL
     KLEANKLSGE IPKELGDLQN LLLVNVSFNR LIGRLPLGDV FQSLDQSAIQ GNLGICSPLL
     RGPCTLNVPK PLVINPNSYG NGNNMPGNRA SGGSGTFHRR MFLSVSVIVA ISAAILIFSG
     VIIITLLNAS VRRRLAFVDN ALESIFSGSS KSGRSLMMGK LVLLNSRTSR SSSSSQEFER
     NPESLLNKAS RIGEGVFGTV YKAPLGEQGR NLAVKKLVPS PILQNLEDFD REVRILAKAK
     HPNLVSIKGY FWTPDLHLLV SEYIPNGNLQ SKLHEREPST PPLSWDVRYK IILGTAKGLA
     YLHHTFRPTT IHFNLKPTNI LLDEKNNPKI SDFGLSRLLT TQDGNTMNNN RFQNALGYVA
     PELECQNLRV NEKCDVYGFG VLILELVTGR RPVEYGEDSF VILSDHVRVM LEQGNVLECI
     DPVMEEQYSE DEVLPVLKLA LVCTSQIPSN RPTMAEIVQI LQVINSPVPH RIMDSF
 
 
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