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Y5573_ARATH
ID   Y5573_ARATH             Reviewed;         892 AA.
AC   Q9SI06; F4IV71;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 2.
DT   03-AUG-2022, entry version 152.
DE   RecName: Full=Putative leucine-rich repeat receptor-like serine/threonine-protein kinase At2g04300;
DE            EC=2.7.11.1;
DE   Flags: Precursor;
GN   OrderedLocusNames=At2g04300; ORFNames=T23O15.8;
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=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
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).
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=2.7.11.1;
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=2.7.11.1;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD27909.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AEC05819.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC007213; AAD27909.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002685; AEC05819.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002685; ANM62529.1; -; Genomic_DNA.
DR   PIR; H84455; H84455.
DR   RefSeq; NP_001324680.1; NM_001335227.1.
DR   RefSeq; NP_178510.1; NM_126462.1.
DR   AlphaFoldDB; Q9SI06; -.
DR   SMR; Q9SI06; -.
DR   PaxDb; Q9SI06; -.
DR   PRIDE; Q9SI06; -.
DR   EnsemblPlants; AT2G04300.2; AT2G04300.2; AT2G04300.
DR   GeneID; 814968; -.
DR   Gramene; AT2G04300.2; AT2G04300.2; AT2G04300.
DR   KEGG; ath:AT2G04300; -.
DR   Araport; AT2G04300; -.
DR   TAIR; locus:2059804; AT2G04300.
DR   eggNOG; ENOG502QQCZ; Eukaryota.
DR   InParanoid; Q9SI06; -.
DR   OMA; AYENSRE; -.
DR   OrthoDB; 730902at2759; -.
DR   PhylomeDB; Q9SI06; -.
DR   PRO; PR:Q9SI06; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9SI06; differential.
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:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
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; IPR024788; Malectin-like_Carb-bd_dom.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF13855; LRR_8; 1.
DR   Pfam; PF12819; Malectin_like; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 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   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Glycoprotein; Kinase; Leucine-rich repeat;
KW   Membrane; Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome;
KW   Repeat; Serine/threonine-protein kinase; Signal; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..892
FT                   /note="Putative leucine-rich repeat receptor-like
FT                   serine/threonine-protein kinase At2g04300"
FT                   /id="PRO_0000403328"
FT   TOPO_DOM        27..523
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        524..544
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        545..892
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REPEAT          375..396
FT                   /note="LRR 1"
FT   REPEAT          399..422
FT                   /note="LRR 2"
FT   REPEAT          423..444
FT                   /note="LRR 3"
FT   REPEAT          447..467
FT                   /note="LRR 4"
FT   DOMAIN          582..855
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        707
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         588..596
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         610
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         573
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O48814"
FT   MOD_RES         655
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:O48814"
FT   MOD_RES         742
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O48814"
FT   MOD_RES         747
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O48814"
FT   MOD_RES         755
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:O48814"
FT   CARBOHYD        99
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        186
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        241
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        267
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        294
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        407
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        421
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        437
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        450
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        469
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   892 AA;  99519 MW;  C0AE27B3DFE2D507 CRC64;
     MKTHPQAILL CVLFFITFGL LHVVEAGNQE GFISLDCGLS PNEPPYVDAA TDLTYTTDND
     FVQSGKTGTI DKELESTYNK PILQLRYFPE GVRNCYTLNV TLGTNYLIRA SFVYGNYDGL
     NKELEFDLYL GPNLWANVNT AVYLMNGVTT EEIIHSTKSK VLQVCLIKTG ESIPIINSLE
     LRPLINDTYN TQSGSLKYLF RNYFSTSRRI IRYPNDVNDR HWYPFFDEDA WTELTTNLNV
     NSSNGYDPPK FVMASASTPI SKNAPFNFTW SLIPSTAKFY SYMHFADIQT LQANETREFD
     MMLNGNLALE RYRPKTFATG TIYFIKPQIC EGGQCIIELL KTSKSTLPPL CSALEVFTVI
     DFPELETNQD DVIAIKNIQN TYGVSKTSWQ GDPCVPKRFM WDGLNCNNSY ISTPPTITFL
     NLSSSHLTGI IASAIQNLTH LQNLDLSNNN LTGGVPEFLA GLKSLLVINL SGNNLSGSVP
     QTLLQKKGLK LNLEGNIYLN CPDGSCVSKD GNGGAKKKNV VVLVVVSIAL VVVLGSALAL
     FLVFRKRKTP RNEVSRTSRS LDPTITTKNR RFTYSEVVKM TNNFEKILGK GGFGMVYHGT
     VNDAEQVAVK MLSPSSSQGY KEFKAEVELL LRVHHKNLVG LVGYCDEGEN LSLIYEYMAK
     GDLKEHMLGN QGVSILDWKT RLKIVAESAQ GLEYLHNGCK PPMVHRDVKT TNILLDEHFQ
     AKLADFGLSR SFPLEGETRV DTVVAGTPGY LDPEYYRTNW LNEKSDVYSF GIVLLEIITN
     QHVINQSREK PHIAEWVGVM LTKGDIKSII DPKFSGDYDA GSVWRAVELA MSCVNPSSTG
     RPTMSQVVIE LNECLASENS RRGMSQNMES KGSIQYTEVS TNFGTEYTPE AR
 
 
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