NBR1_ARATH
ID NBR1_ARATH Reviewed; 704 AA.
AC Q9SB64;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Protein NBR1 homolog {ECO:0000305};
DE Short=AtNBR1 {ECO:0000303|PubMed:21606687};
DE AltName: Full=At4g24690 {ECO:0000312|EMBL:AAP37784.1};
GN Name=NBR1 {ECO:0000303|PubMed:21606687};
GN OrderedLocusNames=At4g24690 {ECO:0000312|Araport:AT4G24690};
GN ORFNames=F22K18.110 {ECO:0000312|EMBL:CAA22994.1};
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=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].
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 FUNCTION, SUBUNIT, INTERACTION WITH ATG8A; ATG8B; ATG8C; ATG8D; ATG8F AND
RP ATG8I, UBIQUITIN-BINDING, SUBCELLULAR LOCATION, DOMAIN, LIR MOTIF, AND
RP MUTAGENESIS OF LYS-11; ARG-19; ASP-60; ASP-73; TRP-661 AND ILE-664.
RX PubMed=21606687; DOI=10.4161/auto.7.9.16389;
RA Svenning S., Lamark T., Krause K., Johansen T.;
RT "Plant NBR1 is a selective autophagy substrate and a functional hybrid of
RT the mammalian autophagic adapters NBR1 and p62/SQSTM1.";
RL Autophagy 7:993-1010(2011).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [6]
RP FUNCTION, INDUCTION BY HEAT SHOCK, LIR MOTIF, MUTAGENESIS OF TRP-661 AND
RP ILE-664, AND DISRUPTION PHENOTYPE.
RX PubMed=23341779; DOI=10.1371/journal.pgen.1003196;
RA Zhou J., Wang J., Cheng Y., Chi Y.J., Fan B., Yu J.Q., Chen Z.;
RT "NBR1-mediated selective autophagy targets insoluble ubiquitinated protein
RT aggregates in plant stress responses.";
RL PLoS Genet. 9:E1003196-E1003196(2013).
RN [7]
RP FUNCTION.
RX PubMed=24497840; DOI=10.1371/journal.pgen.1004116;
RA Zhou J., Zhang Y., Qi J., Chi Y., Fan B., Yu J.Q., Chen Z.;
RT "E3 ubiquitin ligase CHIP and NBR1-mediated selective autophagy protect
RT additively against proteotoxicity in plant stress responses.";
RL PLoS Genet. 10:E1004116-E1004116(2014).
CC -!- FUNCTION: Autophagic substrate degraded in the vacuole by non-selective
CC autophagy. Requires ATG8 protein expression to be recognized as an
CC autophagic substrate (PubMed:21606687). Acts probably as a receptor for
CC autophagosomal degradation of ubiquitinated proteins. Targets
CC ubiquitinated protein aggregates derived from denatured or damaged non-
CC native proteins generated under stress conditions (PubMed:23341779).
CC Functions additively with the E3 ubiquitin-protein ligase CHIP for
CC autophagosomal degradation of proteotoxic aggregates formed under
CC stress conditions (PubMed:24497840). {ECO:0000269|PubMed:21606687,
CC ECO:0000269|PubMed:23341779, ECO:0000269|PubMed:24497840}.
CC -!- SUBUNIT: Homodimer. Interacts with ATG8A, ATG8B, ATG8C, ATG8D, ATG8F
CC and ATG8I. Binds to ubiquitin. {ECO:0000269|PubMed:21606687}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21606687}. Vacuole
CC {ECO:0000269|PubMed:21606687}. Note=Forms large punctated cytoplasmic
CC structures. Recruited to the central vacuole by non-selective
CC autophagy. {ECO:0000269|PubMed:21606687}.
CC -!- INDUCTION: By heat shock. {ECO:0000269|PubMed:23341779}.
CC -!- DOMAIN: The PB1 domain mediates homodimerization.
CC {ECO:0000269|PubMed:21606687}.
CC -!- DOMAIN: The UBA domain is required for ubiquitin binding.
CC {ECO:0000269|PubMed:21606687}.
CC -!- DOMAIN: The LIR motif is required for the interaction with ATG8
CC proteins and for vacuolar import (PubMed:21606687). The LIR motif is
CC required for NBR1 function as receptor for autophagosomal degradation
CC of ubiquitinated proteins under stress conditions (PubMed:23341779).
CC {ECO:0000269|PubMed:21606687, ECO:0000269|PubMed:23341779}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants show enhanced sensitivity to heat,
CC oxidative, salt, and drought stresses. {ECO:0000269|PubMed:23341779}.
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DR EMBL; AL035356; CAA22994.1; -; Genomic_DNA.
DR EMBL; AL161562; CAB79379.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84943.1; -; Genomic_DNA.
DR EMBL; AY062827; AAL32905.1; -; mRNA.
DR EMBL; AY128759; AAM91159.1; -; mRNA.
DR EMBL; AY140081; AAM98222.1; -; mRNA.
DR EMBL; BT008425; AAP37784.1; -; mRNA.
DR PIR; T05565; T05565.
DR RefSeq; NP_194200.1; NM_118602.4.
DR PDB; 6TGN; EM; 4.00 A; A=1-94.
DR PDB; 6TGP; EM; 4.50 A; A/B=1-94.
DR PDB; 6TGS; X-ray; 1.53 A; A=1-94.
DR PDBsum; 6TGN; -.
DR PDBsum; 6TGP; -.
DR PDBsum; 6TGS; -.
DR AlphaFoldDB; Q9SB64; -.
DR SMR; Q9SB64; -.
DR IntAct; Q9SB64; 7.
DR STRING; 3702.AT4G24690.1; -.
DR iPTMnet; Q9SB64; -.
DR PaxDb; Q9SB64; -.
DR PRIDE; Q9SB64; -.
DR ProteomicsDB; 251084; -.
DR EnsemblPlants; AT4G24690.1; AT4G24690.1; AT4G24690.
DR GeneID; 828571; -.
DR Gramene; AT4G24690.1; AT4G24690.1; AT4G24690.
DR KEGG; ath:AT4G24690; -.
DR Araport; AT4G24690; -.
DR TAIR; locus:2121899; AT4G24690.
DR eggNOG; KOG4351; Eukaryota.
DR eggNOG; KOG4582; Eukaryota.
DR HOGENOM; CLU_017180_0_0_1; -.
DR InParanoid; Q9SB64; -.
DR OMA; PIDQEID; -.
DR OrthoDB; 991378at2759; -.
DR PhylomeDB; Q9SB64; -.
DR PRO; PR:Q9SB64; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SB64; baseline and differential.
DR Genevisible; Q9SB64; AT.
DR GO; GO:0005776; C:autophagosome; IDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR GO; GO:0005773; C:vacuole; IDA:TAIR.
DR GO; GO:0043130; F:ubiquitin binding; IDA:TAIR.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0051258; P:protein polymerization; IDA:TAIR.
DR GO; GO:0071211; P:protein targeting to vacuole involved in autophagy; IMP:TAIR.
DR CDD; cd14947; NBR1_like; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR032350; N_BRCA1_central.
DR InterPro; IPR000270; PB1_dom.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR Pfam; PF16158; N_BRCA1_IG; 1.
DR Pfam; PF00564; PB1; 1.
DR Pfam; PF00569; ZZ; 1.
DR SMART; SM00666; PB1; 1.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Autophagy; Cytoplasm; Metal-binding;
KW Protein transport; Reference proteome; Stress response; Transport; Vacuole;
KW Zinc; Zinc-finger.
FT CHAIN 1..704
FT /note="Protein NBR1 homolog"
FT /id="PRO_0000434632"
FT DOMAIN 7..92
FT /note="PB1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01081"
FT DOMAIN 657..701
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT ZN_FING 286..336
FT /note="ZZ-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT REGION 95..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 661..664
FT /note="LIR"
FT /evidence="ECO:0000269|PubMed:21606687,
FT ECO:0000269|PubMed:23341779"
FT COMPBIAS 95..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 291
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 294
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 315
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 318
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MUTAGEN 11
FT /note="K->A: Loss of homodimerization; loss of capacity to
FT form large aggregated cytoplasmic structures."
FT /evidence="ECO:0000269|PubMed:21606687"
FT MUTAGEN 19
FT /note="R->A: Loss of homodimerization."
FT /evidence="ECO:0000269|PubMed:21606687"
FT MUTAGEN 60
FT /note="D->A: Loss of homodimerization."
FT /evidence="ECO:0000269|PubMed:21606687"
FT MUTAGEN 73
FT /note="D->A: Loss of homodimerization."
FT /evidence="ECO:0000269|PubMed:21606687"
FT MUTAGEN 661
FT /note="W->A: Loss of binding to ATG8 proteins; when
FT associated with A-664; Increased sensitivity to heat
FT stress; when associated with A-664."
FT /evidence="ECO:0000269|PubMed:21606687,
FT ECO:0000269|PubMed:23341779"
FT MUTAGEN 664
FT /note="I->A: Loss of binding to ATG8 proteins; when
FT associated with A-661; Increased sensitivity to heat
FT stress; when associated with A-661."
FT /evidence="ECO:0000269|PubMed:21606687,
FT ECO:0000269|PubMed:23341779"
FT STRAND 8..14
FT /evidence="ECO:0007829|PDB:6TGS"
FT STRAND 17..23
FT /evidence="ECO:0007829|PDB:6TGS"
FT HELIX 35..46
FT /evidence="ECO:0007829|PDB:6TGS"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:6TGS"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:6TGS"
FT HELIX 71..79
FT /evidence="ECO:0007829|PDB:6TGS"
FT STRAND 83..90
FT /evidence="ECO:0007829|PDB:6TGS"
SQ SEQUENCE 704 AA; 76186 MW; AFE631C573C4DB81 CRC64;
MESTANALVV KVSYGGVLRR FRVPVKANGQ LDLEMAGLKE KIAALFNLSA DAELSLTYSD
EDGDVVALVD DNDLFDVTNQ RLKFLKINVN AGVSTNSAAP ESSGSSTPAG MPNPVSKIQK
GINDVLMAVP NPMRDTISKV YMDLASKAST SSPVVGEMLD CISKLGQLSI PQESSPCSPV
TKPGSSGASL SRDVPSAGGK KDISERTQTG RKPVNLNEPT GAHSKTSGHV PNSSGLGANF
NECPFSGSTM NYSCPNPVNL NKHPRRVCHS KKSTNGDYWT SLGVFHKGIR CDGCGVLPIT
GPRFKSKVKE DYDLCTICYS VMGNEGDYTR MDKPVSVQHL HPFRGPFTQF PNPWLSHPVP
RATNGGAPLR CTRPKLDSRF VLDVNVIDGT VVAPSAPFTK IWKMRNSGSL VWPQGTQIVW
IGGDRFCNSL SVDLQIPKEG VPIYSELDVK VDFVAPELPG RYISYWRMAT SDGAKFGQRV
WVLIHVDASL KNSVVNEFHG LNLNASPSLD ENFPSEFLGI MNYESAQPGS SSVNPGTVKG
TDLEGEVGET QAVEKENLLV GEAHPAIPHG HSPSSSSSSF NMVDFPSMPA VEVLSGGSSS
TTKDVPVPLQ EDIEKNDVEI TMLKELEEMG FKEIDLNKEI LRDNEYNLEQ SVDALCGVSE
WDPILEELQE MGFCDDVTNK RLLKKNNGSI KGVVMDLLTG EKEA
