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EAP3_ARATH
ID   EAP3_ARATH              Reviewed;         460 AA.
AC   Q9S7R7; Q8GYS9;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Protein ENDOPLASMIC RETICULUM-ARRESTED PEN3 {ECO:0000303|PubMed:29085068};
DE            Short=Protein ER-ARRESTED PEN3 {ECO:0000303|PubMed:29085068};
GN   Name=EAP3 {ECO:0000303|PubMed:29085068};
GN   OrderedLocusNames=At3g09030 {ECO:0000312|Araport:AT3G09030};
GN   ORFNames=MZB10.6 {ECO:0000312|EMBL:AAD56319.1},
GN   T16O11.1 {ECO:0000312|EMBL:AAF07825.1};
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=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Kim C.J., Chen H., Quinitio C., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   DOMAIN BTB.
RX   PubMed=15749712; DOI=10.1074/jbc.m413247200;
RA   Gingerich D.J., Gagne J.M., Salter D.W., Hellmann H., Estelle M., Ma L.,
RA   Vierstra R.D.;
RT   "Cullins 3a and 3b assemble with members of the broad
RT   complex/tramtrack/bric-a-brac (BTB) protein family to form essential
RT   ubiquitin-protein ligases (E3s) in Arabidopsis.";
RL   J. Biol. Chem. 280:18810-18821(2005).
RN   [6]
RP   FUNCTION, MUTAGENESIS OF GLY-192, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY,
RP   AND SUBCELLULAR LOCATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=29085068; DOI=10.1038/s41477-017-0039-z;
RA   Mao H., Aryal B., Langenecker T., Hagmann J., Geisler M., Grebe M.;
RT   "Arabidopsis BTB/POZ protein-dependent PENETRATION3 trafficking and disease
RT   susceptibility.";
RL   Nat. Plants 3:854-858(2017).
CC   -!- FUNCTION: May act as a substrate-specific adapter of an E3 ubiquitin-
CC       protein ligase complex (CUL3-RBX1-BTB) which mediates the
CC       ubiquitination and subsequent proteasomal degradation of target
CC       proteins (By similarity). Confers resistance to soil-born pathogens
CC       (e.g. the root-penetrating fungus Fusarium oxysporum) by regulating
CC       membrane trafficking, specifically mediating ABCG36/PEN3 exit from the
CC       endoplasmic reticulum and subsequent relocalization at the host-
CC       pathogen interface of the plasma membrane (PubMed:29085068).
CC       {ECO:0000250, ECO:0000269|PubMed:29085068}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:29085068}.
CC   -!- TISSUE SPECIFICITY: Expressed at very low levels.
CC       {ECO:0000269|PubMed:29085068}.
CC   -!- DOMAIN: The BTB/POZ domain mediates the interaction with some component
CC       of ubiquitin ligase complexes. {ECO:0000269|PubMed:15749712}.
CC   -!- DISRUPTION PHENOTYPE: ABCG36/PEN3 retention and accumulation in the
CC       endoplasmic reticulum associated with an increased sensitivity to the
CC       root-penetrating pathogenic fungus Fusarium oxysporum.
CC       {ECO:0000269|PubMed:29085068}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC42077.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AC009326; AAD56319.1; -; Genomic_DNA.
DR   EMBL; AC010871; AAF07825.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE74710.1; -; Genomic_DNA.
DR   EMBL; AK117411; BAC42077.1; ALT_SEQ; mRNA.
DR   EMBL; BT026142; ABG48498.1; -; mRNA.
DR   RefSeq; NP_187515.1; NM_111737.5.
DR   AlphaFoldDB; Q9S7R7; -.
DR   BioGRID; 5389; 2.
DR   STRING; 3702.AT3G09030.1; -.
DR   PaxDb; Q9S7R7; -.
DR   PRIDE; Q9S7R7; -.
DR   ProteomicsDB; 242867; -.
DR   EnsemblPlants; AT3G09030.1; AT3G09030.1; AT3G09030.
DR   GeneID; 820055; -.
DR   Gramene; AT3G09030.1; AT3G09030.1; AT3G09030.
DR   KEGG; ath:AT3G09030; -.
DR   Araport; AT3G09030; -.
DR   TAIR; locus:2095279; AT3G09030.
DR   eggNOG; KOG2714; Eukaryota.
DR   HOGENOM; CLU_045194_1_0_1; -.
DR   InParanoid; Q9S7R7; -.
DR   OMA; ASFDCPH; -.
DR   OrthoDB; 918615at2759; -.
DR   PhylomeDB; Q9S7R7; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q9S7R7; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9S7R7; baseline and differential.
DR   Genevisible; Q9S7R7; AT.
DR   GO; GO:0005829; C:cytosol; IDA:TAIR.
DR   GO; GO:0050832; P:defense response to fungus; IMP:UniProtKB.
DR   GO; GO:0006886; P:intracellular protein transport; IMP:TAIR.
DR   GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.710.10; -; 1.
DR   InterPro; IPR045068; BACURD1-3.
DR   InterPro; IPR000210; BTB/POZ_dom.
DR   InterPro; IPR011044; Quino_amine_DH_bsu.
DR   InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR   InterPro; IPR003131; T1-type_BTB.
DR   PANTHER; PTHR11145; PTHR11145; 1.
DR   Pfam; PF02214; BTB_2; 1.
DR   SMART; SM00225; BTB; 1.
DR   SUPFAM; SSF50969; SSF50969; 1.
DR   SUPFAM; SSF54695; SSF54695; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Protein transport; Reference proteome; Transport;
KW   Ubl conjugation pathway.
FT   CHAIN           1..460
FT                   /note="Protein ENDOPLASMIC RETICULUM-ARRESTED PEN3"
FT                   /id="PRO_0000405330"
FT   DOMAIN          8..74
FT                   /note="BTB"
FT   MUTAGEN         192
FT                   /note="G->E: In eap3-1; ABCG36/PEN3 retention and
FT                   accumulation in the endoplasmic reticulum."
FT                   /evidence="ECO:0000269|PubMed:29085068"
SQ   SEQUENCE   460 AA;  49278 MW;  59CCB10EE974649E CRC64;
     MVVSDGGKRV KLNVGGEIFE TNASTIQSSC PDSLLAALST STSHGSNPVF IDRDPEIFAV
     ILNLLRTGRL PANSSGVFSK QELLDEAMYY GVESLLRLAM LPPPLLGFDA SLVSTIVPAA
     DGVPSALTAT AGDASLWIAH GGQISVYDWS LSHAGTVRTH LNDITSICRV WGEAAAIGSG
     SASGLHFYDL SGGRYIGSTH WTDPEDPRIH KARVAAVADS EGGVFASFDC LHRENSVLQI
     DKSTLQVAAV IGQQSGNSAK TTVPEKLRWL PAKGLLVGSA VQRGVFGCSG YIRIWDPRSR
     NIVWETNEPG SGRSTRFGDA LADMDVDVED SILFKVCSKS GDLGMADIRK LGEDPWVYMS
     DENPGAWKAG DGGGYSVVHC YRKQVLAARG GALEVWSSVK EKTSGDPIRR RNFVDKEDDS
     KRGMISKIEA GGDRLFVSRE CMEGVEVWET SSFSGVVSVE
 
 
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