BOB1_ARATH
ID BOB1_ARATH Reviewed; 304 AA.
AC Q9LV09; Q8LAL5;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=Protein BOBBER 1;
GN Name=BOB1; OrderedLocusNames=At5g53400; ORFNames=MYN8.1;
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 [GENOMIC DNA], FUNCTION, DEVELOPMENTAL STAGE,
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=19648297; DOI=10.1105/tpc.108.065284;
RA Jurkuta R.J., Kaplinsky N.J., Spindel J.E., Barton M.K.;
RT "Partitioning the apical domain of the Arabidopsis embryo requires the
RT BOBBER1 NudC domain protein.";
RL Plant Cell 21:1957-1971(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF GLY-141,
RP INDUCTION BY HIGH TEMPERATURE, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=19571304; DOI=10.1104/pp.109.142125;
RA Perez D.E., Hoyer J.S., Johnson A.I., Moody Z.R., Lopez J., Kaplinsky N.J.;
RT "BOBBER1 is a noncanonical Arabidopsis small heat shock protein required
RT for both development and thermotolerance.";
RL Plant Physiol. 151:241-252(2009).
RN [8]
RP FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=20514234; DOI=10.4161/psb.4.12.9949;
RA Kaplinsky N.J.;
RT "Temperature compensation of auxin dependent developmental patterning.";
RL Plant Signal. Behav. 4:1157-1158(2009).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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).
CC -!- FUNCTION: Small heat shock protein required for the establishment of
CC auxin gradients and for patterning of the apical domain of the embryo.
CC Involved in the specification of the cotyledon primordia. Also required
CC for normal inflorescence and floral meristem function, normal
CC developmental patterning and thermotolerance. Acts as a molecular
CC chaperone. {ECO:0000269|PubMed:19571304, ECO:0000269|PubMed:19648297,
CC ECO:0000269|PubMed:20514234}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasmic granule. Note=cytoplasmic
CC at basal temperatures, but forms heat shock granules containing
CC canonical small heat shock proteins at high temperatures.
CC -!- TISSUE SPECIFICITY: Expressed in all seedling tissues with highest
CC expression levels at the root tip. {ECO:0000269|PubMed:19571304}.
CC -!- DEVELOPMENTAL STAGE: Expressed during early embryo development, from
CC the eight-cell stage until the end of the heart stage.
CC {ECO:0000269|PubMed:19648297}.
CC -!- INDUCTION: Up-regulated by heat shock. {ECO:0000269|PubMed:19571304}.
CC -!- DISRUPTION PHENOTYPE: Embryo lethal. {ECO:0000269|PubMed:19571304,
CC ECO:0000269|PubMed:19648297}.
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DR EMBL; AB020754; BAA97317.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96348.1; -; Genomic_DNA.
DR EMBL; BT003074; AAO23639.1; -; mRNA.
DR EMBL; AK227305; BAE99321.1; -; mRNA.
DR EMBL; AY087741; AAM65278.1; -; mRNA.
DR RefSeq; NP_200152.1; NM_124719.4.
DR AlphaFoldDB; Q9LV09; -.
DR SMR; Q9LV09; -.
DR BioGRID; 20666; 6.
DR IntAct; Q9LV09; 1.
DR STRING; 3702.AT5G53400.1; -.
DR iPTMnet; Q9LV09; -.
DR PaxDb; Q9LV09; -.
DR PRIDE; Q9LV09; -.
DR ProteomicsDB; 240435; -.
DR EnsemblPlants; AT5G53400.1; AT5G53400.1; AT5G53400.
DR GeneID; 835421; -.
DR Gramene; AT5G53400.1; AT5G53400.1; AT5G53400.
DR KEGG; ath:AT5G53400; -.
DR Araport; AT5G53400; -.
DR TAIR; locus:2178431; AT5G53400.
DR eggNOG; KOG2265; Eukaryota.
DR HOGENOM; CLU_047332_1_1_1; -.
DR InParanoid; Q9LV09; -.
DR OMA; PMKAEEM; -.
DR OrthoDB; 1474731at2759; -.
DR PhylomeDB; Q9LV09; -.
DR PRO; PR:Q9LV09; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LV09; baseline and differential.
DR Genevisible; Q9LV09; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0032502; P:developmental process; IMP:TAIR.
DR GO; GO:0009880; P:embryonic pattern specification; IMP:TAIR.
DR GO; GO:0048461; P:flower structural organization; IMP:CACAO.
DR GO; GO:0010286; P:heat acclimation; IMP:CACAO.
DR GO; GO:0010450; P:inflorescence meristem growth; IMP:TAIR.
DR GO; GO:0009965; P:leaf morphogenesis; IMP:TAIR.
DR GO; GO:0009555; P:pollen development; IMP:TAIR.
DR GO; GO:0006457; P:protein folding; IDA:TAIR.
DR GO; GO:0009408; P:response to heat; IMP:TAIR.
DR GO; GO:0048833; P:specification of floral organ number; IMP:TAIR.
DR GO; GO:0048448; P:stamen morphogenesis; IMP:TAIR.
DR Gene3D; 2.60.40.790; -; 1.
DR InterPro; IPR007052; CS_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR InterPro; IPR037898; NudC_fam.
DR PANTHER; PTHR12356; PTHR12356; 1.
DR Pfam; PF04969; CS; 1.
DR SUPFAM; SSF49764; SSF49764; 1.
DR PROSITE; PS51203; CS; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chaperone; Coiled coil; Cytoplasm; Developmental protein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..304
FT /note="Protein BOBBER 1"
FT /id="PRO_0000420923"
FT DOMAIN 142..231
FT /note="CS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00547"
FT REGION 111..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 54..106
FT /evidence="ECO:0000255"
FT COMPBIAS 117..133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MUTAGEN 141
FT /note="G->E: In bob1-3; general growth defects and reduced
FT fertility, but no effect on the in vitro chaperone
FT activity."
FT /evidence="ECO:0000269|PubMed:19571304"
FT CONFLICT 109
FT /note="I -> M (in Ref. 6; AAM65278)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="E -> D (in Ref. 6; AAM65278)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 304 AA; 34507 MW; C7521C733B2D5762 CRC64;
MAIISEVEEE SSSSRPMIFP FRATLSSANP LGFLEKVFDF LGEQSDFLKK PSAEDEIVVA
VRAAKEKLKK AEKKKAEKES VKPVEKKAEK EIVKLVEKKV EKESVKPTIA ASSAEPIEVE
KPKEEEEKKE SGPIVPNKGN GTDLENYSWI QNLQEVTVNI PVPTGTKART VVCEIKKNRL
KVGLKGQDPI VDGELYRSVK PDDCYWNIED QKVISILLTK SDQMEWWKCC VKGEPEIDTQ
KVEPETSKLG DLDPETRSTV EKMMFDQRQK QMGLPTSEEL QKQEILKKFM SEHPEMDFSN
AKFN
