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Y4539_ARATH
ID   Y4539_ARATH             Reviewed;         651 AA.
AC   Q9STJ8; Q3E7L1;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 148.
DE   RecName: Full=Receptor-like serine/threonine-protein kinase At4g25390;
DE            EC=2.7.11.1;
DE   Flags: Precursor;
GN   OrderedLocusNames=At4g25390; ORFNames=T30C3.60;
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=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(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).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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   -!- 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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9STJ8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9STJ8-2; Sequence=VSP_040370;
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AK229164; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AL079350; CAB45516.1; -; Genomic_DNA.
DR   EMBL; AL161563; CAB81350.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE85051.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE85052.1; -; Genomic_DNA.
DR   EMBL; AK229164; -; NOT_ANNOTATED_CDS; mRNA.
DR   PIR; T10219; T10219.
DR   RefSeq; NP_194269.1; NM_118671.3. [Q9STJ8-1]
DR   RefSeq; NP_849442.1; NM_179111.1. [Q9STJ8-2]
DR   AlphaFoldDB; Q9STJ8; -.
DR   SMR; Q9STJ8; -.
DR   BioGRID; 13929; 1.
DR   STRING; 3702.AT4G25390.1; -.
DR   iPTMnet; Q9STJ8; -.
DR   PaxDb; Q9STJ8; -.
DR   PRIDE; Q9STJ8; -.
DR   ProteomicsDB; 243000; -. [Q9STJ8-1]
DR   EnsemblPlants; AT4G25390.1; AT4G25390.1; AT4G25390. [Q9STJ8-1]
DR   EnsemblPlants; AT4G25390.2; AT4G25390.2; AT4G25390. [Q9STJ8-2]
DR   GeneID; 828642; -.
DR   Gramene; AT4G25390.1; AT4G25390.1; AT4G25390. [Q9STJ8-1]
DR   Gramene; AT4G25390.2; AT4G25390.2; AT4G25390. [Q9STJ8-2]
DR   KEGG; ath:AT4G25390; -.
DR   Araport; AT4G25390; -.
DR   TAIR; locus:2138014; AT4G25390.
DR   eggNOG; KOG1187; Eukaryota.
DR   HOGENOM; CLU_011728_0_0_1; -.
DR   InParanoid; Q9STJ8; -.
DR   OMA; WISMDEE; -.
DR   OrthoDB; 337129at2759; -.
DR   PhylomeDB; Q9STJ8; -.
DR   PRO; PR:Q9STJ8; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9STJ8; baseline and differential.
DR   Genevisible; Q9STJ8; 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; IPR044576; At4g25390-like.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
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   PANTHER; PTHR46821; PTHR46821; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF00069; Pkinase; 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   2: Evidence at transcript level;
KW   Alternative splicing; ATP-binding; Cell membrane; Glycoprotein; Kinase;
KW   Membrane; Nucleotide-binding; Receptor; Reference proteome;
KW   Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..651
FT                   /note="Receptor-like serine/threonine-protein kinase
FT                   At4g25390"
FT                   /id="PRO_0000403342"
FT   TOPO_DOM        26..40
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        41..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        62..651
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          99..633
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          66..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        69..87
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        225
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         105..113
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         127
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   CARBOHYD        32
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         465..619
FT                   /note="RGSGSGSSIDWWLDGLSGERWLRARGNSHDSVSGEIAKSCGISSTPSMRGTV
FT                   CYAAPEYCNLDNNVSEKCDVYSYGVLLLVLISGRRPLEMTGSASEIQRANLMSWARKLA
FT                   RRGKLVDLVDQKLQNLDQEQAVLCIKVALLCLQRLPISRPSMKE -> Q (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_040370"
FT   CONFLICT        405
FT                   /note="W -> G (in Ref. 3; AK229164)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   651 AA;  72240 MW;  EDC517150EA55878 CRC64;
     MPSRSISAPV PVLAPAPIVS SLVPAAPSGH QNKTTRIFPP FVVAGAGAGF SLFITLSVCF
     CKFSRKRSSP PAENASSSPR RPSPREFSYS SLRRATGSFS QANRLGQGGF GVVFRGTISG
     GENVAVKVMD SGSLQGEGEF QNELFFAAKL DSPHVVPVIG FSHDRKRRRL LLVYKLMDNG
     NLQDALLHRR CPELMDWNRR FLVAVNIADG IKHLHSLEPP VIHGDIKPSN VLLDSLFSAK
     IADFGLARLK AEQVEISVAP ERDGDGSMVE EVESVVTTVT GYEDFNFGLV DQSPESVAKV
     PGSVSASPEA TTVVSVSPEM GEKTDEDGGS VVVMKKGKES ESKDWWWKQE SNVERGRVKE
     YVMQWIGSEV KKERPSRSDW IEAAALSSSS SKKLEKKTSK RLDWWLSLEE EDENKKKKKR
     RMVREWWKDE YRRELAKKRK KKKKMTLEAE FCSDDGSSSV SQWRRGSGSG SSIDWWLDGL
     SGERWLRARG NSHDSVSGEI AKSCGISSTP SMRGTVCYAA PEYCNLDNNV SEKCDVYSYG
     VLLLVLISGR RPLEMTGSAS EIQRANLMSW ARKLARRGKL VDLVDQKLQN LDQEQAVLCI
     KVALLCLQRL PISRPSMKEV LGMLKGEVNL PELPSEFSPS PPLKTTRKQR R
 
 
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