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IRE1L_ARATH
ID   IRE1L_ARATH             Reviewed;         554 AA.
AC   Q9SF12;
DT   01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Inactive serine/threonine-protein kinase/endoribonuclease IRE1-like;
DE   AltName: Full=Endoplasmic reticulum-to-nucleus signaling 1-like;
DE   AltName: Full=Inositol-requiring protein 1-like;
DE   Flags: Precursor;
GN   OrderedLocusNames=At3g11870; ORFNames=F26K24.16;
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   GENE FAMILY.
RX   PubMed=12805585; DOI=10.1104/pp.103.021964;
RA   Shiu S.H., Bleecker A.B.;
RT   "Expansion of the receptor-like kinase/Pelle gene family and receptor-like
RT   proteins in Arabidopsis.";
RL   Plant Physiol. 132:530-543(2003).
CC   -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC       inactive. As the kinase activity is required for activation of the
CC       endoribonuclease domain, the protein could be inactive.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; AC016795; AAF23203.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE75111.1; -; Genomic_DNA.
DR   RefSeq; NP_187793.1; NM_112020.1.
DR   AlphaFoldDB; Q9SF12; -.
DR   SMR; Q9SF12; -.
DR   STRING; 3702.AT3G11870.1; -.
DR   PaxDb; Q9SF12; -.
DR   PRIDE; Q9SF12; -.
DR   EnsemblPlants; AT3G11870.1; AT3G11870.1; AT3G11870.
DR   GeneID; 820360; -.
DR   Gramene; AT3G11870.1; AT3G11870.1; AT3G11870.
DR   KEGG; ath:AT3G11870; -.
DR   Araport; AT3G11870; -.
DR   TAIR; locus:2081551; AT3G11870.
DR   eggNOG; KOG1027; Eukaryota.
DR   HOGENOM; CLU_004875_3_2_1; -.
DR   InParanoid; Q9SF12; -.
DR   OMA; HWQDLPD; -.
DR   OrthoDB; 1019877at2759; -.
DR   PhylomeDB; Q9SF12; -.
DR   PRO; PR:Q9SF12; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9SF12; baseline and differential.
DR   Genevisible; Q9SF12; AT.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR   GO; GO:1990604; C:IRE1-TRAF2-ASK1 complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004521; F:endoribonuclease activity; IBA:GO_Central.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0036498; P:IRE1-mediated unfolded protein response; IBA:GO_Central.
DR   GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   Gene3D; 1.20.1440.180; -; 1.
DR   InterPro; IPR045133; IRE1/2-like.
DR   InterPro; IPR010513; KEN_dom.
DR   InterPro; IPR038357; KEN_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   PANTHER; PTHR13954; PTHR13954; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF06479; Ribonuc_2-5A; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS51392; KEN; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Nucleotide-binding; Reference proteome; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..554
FT                   /note="Inactive serine/threonine-protein
FT                   kinase/endoribonuclease IRE1-like"
FT                   /id="PRO_0000422139"
FT   DOMAIN          121..408
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          411..554
FT                   /note="KEN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00725"
FT   REGION          36..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..77
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         150
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   554 AA;  63260 MW;  3543FFF1A6651683 CRC64;
     MWLLAISLVG LLVVVVCVFL RFSKDKGLDG IVNEKKRDKN SAPRVSASGE DGTKNEQVEK
     KSDPSGGLGE ENEKTNSESK VLSVPSDQNI NKTLPVMLPS LELRKYDENE TPGKVVNRRL
     LVSTNEMKYG RNGYEVFQGV YGRRSSVAVK CLDLAHTTEA FIQNEIDNHC LCDDHSNIIR
     FHGLEQDQSF AYICLEPWKC SLDDLIKLSV RRTKRDTQAV APVDDLEKVM KRIKFWKEKG
     KPLPLTPMLK LMRDVVCGLA HLHKLKTIHR NLNPQNVLII VKDMTLTAKI SDMSLSKHLG
     GKKSSYKHLA TCSGSSGWQA PEQLNKDKKK KEDFPADMFN FGCLLHYAVM GTHPFGSPSE
     RDTNIKTNNK TNLSLVTNLE AINLIEQLLN YKPDLRPSAT QVLLHPLFWD SEKRLFFLRE
     ASDRIELDIT MWGDLNKTIA PRVLGESKDW ASKLGKTFIT HIENLAQAQP GQESRQYNRS
     YKYWSLRHLL RLIRNILSHH REILDDPKIK EMVGKVPEGL DIFFTARFPN LMMEIYAFIS
     MHCKGEEAFE KYFN
 
 
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