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Y3868_ARATH
ID   Y3868_ARATH             Reviewed;         640 AA.
AC   Q9C9Y8; Q93ZK0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Probable inactive receptor kinase At3g08680;
DE   Flags: Precursor;
GN   OrderedLocusNames=At3g08680; ORFNames=F17O14.15;
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=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(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=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-564, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=15308754; DOI=10.1105/tpc.104.023150;
RA   Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT   "Phosphoproteomics of the Arabidopsis plasma membrane and a new
RT   phosphorylation site database.";
RL   Plant Cell 16:2394-2405(2004).
RN   [5]
RP   SUBCELLULAR LOCATION.
RX   PubMed=17397506; DOI=10.1111/j.1365-313x.2007.03028.x;
RA   Shahollari B., Vadassery J., Varma A., Oelmueller R.;
RT   "A leucine-rich repeat protein is required for growth promotion and
RT   enhanced seed production mediated by the endophytic fungus Piriformospora
RT   indica in Arabidopsis thaliana.";
RL   Plant J. 50:1-13(2007).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19376835; DOI=10.1104/pp.109.138677;
RA   Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA   Grossmann J., Gruissem W., Baginsky S.;
RT   "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT   chloroplast kinase substrates and phosphorylation networks.";
RL   Plant Physiol. 150:889-903(2009).
CC   -!- INTERACTION:
CC       Q9C9Y8; C0LGG6-2: At1g51890; NbExp=2; IntAct=EBI-16955024, EBI-20655952;
CC       Q9C9Y8; Q9M0D8: LRR-RLK; NbExp=3; IntAct=EBI-16955024, EBI-16955231;
CC       Q9C9Y8; C0LGP2: MEE39; NbExp=2; IntAct=EBI-16955024, EBI-20663701;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:17397506}; Single-
CC       pass membrane protein {ECO:0000269|PubMed:17397506}.
CC   -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC       inactive.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL09719.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AC012562; AAG51359.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE74662.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE74663.1; -; Genomic_DNA.
DR   EMBL; AY057485; AAL09719.1; ALT_FRAME; mRNA.
DR   EMBL; BT000497; AAN18066.1; -; mRNA.
DR   RefSeq; NP_187480.1; NM_111702.2.
DR   RefSeq; NP_974257.1; NM_202528.3.
DR   AlphaFoldDB; Q9C9Y8; -.
DR   SMR; Q9C9Y8; -.
DR   BioGRID; 5350; 43.
DR   IntAct; Q9C9Y8; 44.
DR   STRING; 3702.AT3G08680.2; -.
DR   iPTMnet; Q9C9Y8; -.
DR   SwissPalm; Q9C9Y8; -.
DR   PaxDb; Q9C9Y8; -.
DR   PRIDE; Q9C9Y8; -.
DR   ProteomicsDB; 242868; -.
DR   EnsemblPlants; AT3G08680.1; AT3G08680.1; AT3G08680.
DR   EnsemblPlants; AT3G08680.2; AT3G08680.2; AT3G08680.
DR   GeneID; 820015; -.
DR   Gramene; AT3G08680.1; AT3G08680.1; AT3G08680.
DR   Gramene; AT3G08680.2; AT3G08680.2; AT3G08680.
DR   KEGG; ath:AT3G08680; -.
DR   Araport; AT3G08680; -.
DR   TAIR; locus:2077898; AT3G08680.
DR   eggNOG; ENOG502QT13; Eukaryota.
DR   HOGENOM; CLU_000288_92_6_1; -.
DR   InParanoid; Q9C9Y8; -.
DR   OMA; CVGKSPE; -.
DR   OrthoDB; 389502at2759; -.
DR   PhylomeDB; Q9C9Y8; -.
DR   PRO; PR:Q9C9Y8; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9C9Y8; baseline and differential.
DR   Genevisible; Q9C9Y8; AT.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR   GO; GO:0009506; C:plasmodesma; HDA:TAIR.
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; -; 2.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
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   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   Pfam; PF08263; LRRNT_2; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Leucine-rich repeat; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..640
FT                   /note="Probable inactive receptor kinase At3g08680"
FT                   /id="PRO_0000317074"
FT   TRANSMEM        260..280
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REPEAT          93..115
FT                   /note="LRR 1"
FT   REPEAT          117..138
FT                   /note="LRR 2"
FT   REPEAT          139..162
FT                   /note="LRR 3"
FT   REPEAT          163..185
FT                   /note="LRR 4"
FT   REPEAT          186..206
FT                   /note="LRR 5"
FT   DOMAIN          341..614
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          222..249
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          289..315
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          612..640
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        621..640
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         347..355
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         369
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         343
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q94F62"
FT   MOD_RES         364
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q94F62"
FT   MOD_RES         441
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT   MOD_RES         514
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT   MOD_RES         564
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:15308754"
SQ   SEQUENCE   640 AA;  69406 MW;  C974C668F07657CF CRC64;
     MMKIIAAFLF LLVTTFVSRC LSADIESDKQ ALLEFASLVP HSRKLNWNST IPICASWTGI
     TCSKNNARVT ALRLPGSGLY GPLPEKTFEK LDALRIISLR SNHLQGNIPS VILSLPFIRS
     LYFHENNFSG TIPPVLSHRL VNLDLSANSL SGNIPTSLQN LTQLTDLSLQ NNSLSGPIPN
     LPPRLKYLNL SFNNLNGSVP SSVKSFPASS FQGNSLLCGA PLTPCPENTT APSPSPTTPT
     EGPGTTNIGR GTAKKVLSTG AIVGIAVGGS VLLFIILAII TLCCAKKRDG GQDSTAVPKA
     KPGRSDNKAE EFGSGVQEAE KNKLVFFEGS SYNFDLEDLL RASAEVLGKG SYGTTYKAIL
     EEGTTVVVKR LKEVAAGKRE FEQQMEAVGR ISPHVNVAPL RAYYFSKDEK LLVYDYYQGG
     NFSMLLHGNN EGGRAALDWE TRLRICLEAA RGISHIHSAS GAKLLHGNIK SPNVLLTQEL
     HVCVSDFGIA PLMSHHTLIP SRSLGYRAPE AIETRKHTQK SDVYSFGVLL LEMLTGKAAG
     KTTGHEEVVD LPKWVQSVVR EEWTGEVFDV ELIKQQHNVE EEMVQMLQIA MACVSKHPDS
     RPSMEEVVNM MEEIRPSGSG PGSGNRASSP EMIRSSDSPV
 
 
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