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Y1561_ARATH
ID   Y1561_ARATH             Reviewed;        1032 AA.
AC   C0LGH2; Q9C7J1; Q9SGT9;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-NOV-2009, sequence version 2.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Probable LRR receptor-like serine/threonine-protein kinase At1g56130;
DE            EC=2.7.11.1;
DE   Flags: Precursor;
GN   OrderedLocusNames=At1g56130; ORFNames=F14G9.25, T6H22.8;
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=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(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] (ISOFORM 2).
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   -!- 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:0000255}; Single-pass type I
CC       membrane protein {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=C0LGH2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=C0LGH2-2; Sequence=VSP_038283, VSP_038284;
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF02838.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAG50912.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC009894; AAF02838.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC069159; AAG50912.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; ANM59201.1; -; Genomic_DNA.
DR   EMBL; FJ708662; ACN59257.1; -; mRNA.
DR   PIR; F96602; F96602.
DR   RefSeq; NP_176009.1; NM_104491.2. [C0LGH2-1]
DR   AlphaFoldDB; C0LGH2; -.
DR   SMR; C0LGH2; -.
DR   BioGRID; 27290; 20.
DR   IntAct; C0LGH2; 20.
DR   STRING; 3702.AT1G56130.1; -.
DR   PaxDb; C0LGH2; -.
DR   PRIDE; C0LGH2; -.
DR   ProteomicsDB; 242390; -. [C0LGH2-1]
DR   EnsemblPlants; AT1G56130.2; AT1G56130.2; AT1G56130. [C0LGH2-1]
DR   GeneID; 842065; -.
DR   Gramene; AT1G56130.2; AT1G56130.2; AT1G56130. [C0LGH2-1]
DR   KEGG; ath:AT1G56130; -.
DR   Araport; AT1G56130; -.
DR   TAIR; locus:2205250; AT1G56130.
DR   eggNOG; ENOG502QUW9; Eukaryota.
DR   HOGENOM; CLU_000288_114_1_1; -.
DR   InParanoid; C0LGH2; -.
DR   OMA; LEWAWYL; -.
DR   OrthoDB; 146580at2759; -.
DR   PhylomeDB; C0LGH2; -.
DR   PRO; PR:C0LGH2; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; C0LGH2; baseline and differential.
DR   Genevisible; C0LGH2; 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:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
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; IPR021720; Malectin_dom.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF13855; LRR_8; 1.
DR   Pfam; PF11721; Malectin; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; ATP-binding; Cell membrane; Glycoprotein; Kinase;
KW   Leucine-rich repeat; Membrane; Nucleotide-binding; Phosphoprotein;
KW   Receptor; Reference proteome; Repeat; Serine/threonine-protein kinase;
KW   Signal; Transferase; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..1032
FT                   /note="Probable LRR receptor-like serine/threonine-protein
FT                   kinase At1g56130"
FT                   /id="PRO_0000387535"
FT   TOPO_DOM        30..636
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        637..657
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        658..1032
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REPEAT          101..122
FT                   /note="LRR 1"
FT   REPEAT          123..146
FT                   /note="LRR 2"
FT   REPEAT          148..170
FT                   /note="LRR 3"
FT   REPEAT          171..194
FT                   /note="LRR 4"
FT   REPEAT          196..217
FT                   /note="LRR 5"
FT   REPEAT          242..265
FT                   /note="LRR 6"
FT   REPEAT          290..314
FT                   /note="LRR 7"
FT   REPEAT          315..338
FT                   /note="LRR 8"
FT   REPEAT          340..360
FT                   /note="LRR 9"
FT   REPEAT          361..385
FT                   /note="LRR 10"
FT   DOMAIN          694..968
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1008..1032
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        818
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         700..708
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         722
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         683
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O48814"
FT   MOD_RES         767
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:O48814"
FT   MOD_RES         822
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O48814"
FT   MOD_RES         851
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O48814"
FT   MOD_RES         852
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O48814"
FT   MOD_RES         857
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O48814"
FT   MOD_RES         865
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:O48814"
FT   CARBOHYD        31
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        61
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        95
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        145
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        182
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        265
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        302
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        337
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        348
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        352
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        394
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        580
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        633
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         509..522
FT                   /note="YYGLGLENGGYTVT -> FYFYHLERFGTTTF (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:20064227"
FT                   /id="VSP_038283"
FT   VAR_SEQ         523..1032
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:20064227"
FT                   /id="VSP_038284"
FT   CONFLICT        151
FT                   /note="W -> WI (in Ref. 1; AAG50912)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1032 AA;  113042 MW;  8E0AC1A89E52142E CRC64;
     MTRIRRSPCL LLLIIWFMCI AGSVQVVQSQ NQTGATTHPD EARALNSIFA AWKIQAPREW
     NISGELCSGA AIDASVLDSN PAYNPLIKCD CSFQNSTICR ITNIKVYAID VVGPIPPELW
     TLTYLTNLNL GQNVLTGSLP PAIGNLTRMQ WMTFGINALS GPVPKEIGLL TDLRLLGISS
     NNFSGSIPDE IGRCTKLQQM YIDSSGLSGR IPLSFANLVQ LEQAWIADLE VTDQIPDFIG
     DWTKLTTLRI IGTGLSGPIP SSFSNLTSLT ELRLGDISSG SSSLDFIKDM KSLSVLVLRN
     NNLTGTIPST IGEHSSLRQV DLSFNKLHGP IPASLFNLSQ LTHLFLGNNT LNGSFPTQKT
     QSLRNVDVSY NDLSGSLPSW VSLPSLKLNL VANNFTLEGL DNRVLPGLNC LQKNFPCNRG
     KGIYSDFSIN CGGPEKRSVT GALFEREDED FGPASFFVSA GQRWAASSVG LFAGSSNNIY
     IATSQSQFVN TLDSELFQSA RLSASSVRYY GLGLENGGYT VTLQFAEIQI LGSTSTTWKG
     LGRRRFDIYV QGRLVEKDFD VRRTAGDSTV RAVQRVYKAN VSENHLEVHL FWAGKGTCCI
     PIQGAYGPLI SAVSATPDFT PTVANKPPSK GKNRTGTIVG VIVGVGLLSI LAGVVMFTIR
     KRRKRYTDDE ELLGMDVKPY IFTYSELKSA TQDFDPSNKL GEGGFGPVYK GNLNDGRVVA
     VKLLSVGSRQ GKGQFVAEIV AISSVLHRNL VKLYGCCFEG EHRMLVYEYL PNGSLDQALF
     GDKTLHLDWS TRYEICLGVA RGLVYLHEEA SVRIVHRDVK ASNILLDSRL VPQISDFGLA
     KLYDDKKTHI STRVAGTIGY LAPEYAMRGH LTEKTDVYAF GVVALELVSG RPNSDENLEE
     EKKYLLEWAW NLHEKSRDIE LIDDKLTDFN MEEAKRMIGI ALLCTQTSHA LRPPMSRVVA
     MLSGDVEIGD VTSKPGYVSD WRFDDTTGSS LSGFQIKDTT GYSMSLVAPG SEISPRDSDF
     KPMLGSKINE GR
 
 
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