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Y2394_ARATH
ID   Y2394_ARATH             Reviewed;         453 AA.
AC   Q3EBR4; O80859;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 2.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Putative receptor-like protein kinase At2g30940;
DE            EC=2.7.11.1;
GN   OrderedLocusNames=At2g30940; ORFNames=F7F1.15;
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 membrane
CC       protein {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3EBR4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3EBR4-2; Sequence=VSP_040169;
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC20728.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC004669; AAC20728.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002685; AEC08463.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC08464.1; -; Genomic_DNA.
DR   PIR; E84714; E84714.
DR   RefSeq; NP_180651.2; NM_128647.2. [Q3EBR4-2]
DR   RefSeq; NP_973571.2; NM_201842.2. [Q3EBR4-1]
DR   AlphaFoldDB; Q3EBR4; -.
DR   SMR; Q3EBR4; -.
DR   STRING; 3702.AT2G30940.2; -.
DR   iPTMnet; Q3EBR4; -.
DR   PaxDb; Q3EBR4; -.
DR   PRIDE; Q3EBR4; -.
DR   ProteomicsDB; 243121; -. [Q3EBR4-1]
DR   EnsemblPlants; AT2G30940.1; AT2G30940.1; AT2G30940. [Q3EBR4-2]
DR   EnsemblPlants; AT2G30940.2; AT2G30940.2; AT2G30940. [Q3EBR4-1]
DR   GeneID; 817645; -.
DR   Gramene; AT2G30940.1; AT2G30940.1; AT2G30940. [Q3EBR4-2]
DR   Gramene; AT2G30940.2; AT2G30940.2; AT2G30940. [Q3EBR4-1]
DR   KEGG; ath:AT2G30940; -.
DR   Araport; AT2G30940; -.
DR   TAIR; locus:2052791; AT2G30940.
DR   eggNOG; KOG1187; Eukaryota.
DR   InParanoid; Q3EBR4; -.
DR   OMA; YFHEDIE; -.
DR   OrthoDB; 684563at2759; -.
DR   PhylomeDB; Q3EBR4; -.
DR   PRO; PR:Q3EBR4; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q3EBR4; baseline and differential.
DR   Genevisible; Q3EBR4; 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: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   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   3: Inferred from homology;
KW   Alternative splicing; ATP-binding; Cell membrane; Kinase; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..453
FT                   /note="Putative receptor-like protein kinase At2g30940"
FT                   /id="PRO_0000401354"
FT   TRANSMEM        60..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          166..428
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        293
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         172..180
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         194
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         155
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O48814"
FT   MOD_RES         240
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:O48814"
FT   MOD_RES         297
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O48814"
FT   MOD_RES         322
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O48814"
FT   VAR_SEQ         360..361
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_040169"
SQ   SEQUENCE   453 AA;  51829 MW;  140B2857B02D219E CRC64;
     MQEWLEILLI HTLIDSSSLS PQRLRVMNRI ISSQGSDLIK QKLSQHTSFF GIKLWILITA
     SASIAFLLVL IISVLLCFIF HRRRCSQEPF RLRSKLCLPL SHIPLTNKQQ IPYNRCGDDI
     ESQRISQVGW SSARLSYYTR SFSSTGSFGS FNVFTFMEIK NVTDSFADDN VITKGDSSTV
     YRGILMGTVT VAVKRFLPSN SRYEDKDFIT KAEMIANVRH KNVVRLLGYC IEGDERVLVY
     EYAEKGDLHE WLHGSAGRNR PLTWRKRMKI IQGVAKGLAY IHEDIEPKIT HQDIRPSKIL
     LDYQWNPKIL DVGFIGHSDI PTLIPSPGNM DEKIDVYSFG NMIMELVSGR VSVDQSSPHV
     RVYLVDWIKE MVANHMIVDV LDPSLPEFPT IKELKRIVLI SLRCVDPELK ERPKMGDVIH
     MLQPHDLLLN NNAIQKAQKI TRSHEVSAIS IRQ
 
 
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