BOB2_ARATH
ID BOB2_ARATH Reviewed; 293 AA.
AC Q9STN7;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Protein BOBBER 2;
GN Name=BOB2; OrderedLocusNames=At4g27890; ORFNames=T27E11.130;
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 IDENTIFICATION.
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 [5]
RP INDUCTION BY HIGH TEMPERATURE.
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).
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasmic granule
CC {ECO:0000250}.
CC -!- INDUCTION: Up-regulated by heat shock. {ECO:0000269|PubMed:19571304}.
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DR EMBL; AL078579; CAB43977.1; -; Genomic_DNA.
DR EMBL; AL161571; CAB81438.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85405.1; -; Genomic_DNA.
DR EMBL; AY142524; AAN13067.1; -; mRNA.
DR PIR; T09028; T09028.
DR RefSeq; NP_194518.1; NM_118927.5.
DR AlphaFoldDB; Q9STN7; -.
DR SMR; Q9STN7; -.
DR STRING; 3702.AT4G27890.1; -.
DR PaxDb; Q9STN7; -.
DR PRIDE; Q9STN7; -.
DR ProteomicsDB; 240357; -.
DR EnsemblPlants; AT4G27890.1; AT4G27890.1; AT4G27890.
DR GeneID; 828902; -.
DR Gramene; AT4G27890.1; AT4G27890.1; AT4G27890.
DR KEGG; ath:AT4G27890; -.
DR Araport; AT4G27890; -.
DR TAIR; locus:2137345; AT4G27890.
DR eggNOG; KOG2265; Eukaryota.
DR HOGENOM; CLU_047332_1_1_1; -.
DR InParanoid; Q9STN7; -.
DR OMA; QNPGMDF; -.
DR OrthoDB; 1474731at2759; -.
DR PhylomeDB; Q9STN7; -.
DR PRO; PR:Q9STN7; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9STN7; baseline and differential.
DR Genevisible; Q9STN7; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Acetylation; Chaperone; Coiled coil; Cytoplasm; Developmental protein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9LV09"
FT CHAIN 2..293
FT /note="Protein BOBBER 2"
FT /id="PRO_0000420924"
FT DOMAIN 131..220
FT /note="CS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00547"
FT REGION 67..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 50..80
FT /evidence="ECO:0000255"
FT COMPBIAS 67..122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9LV09"
SQ SEQUENCE 293 AA; 33521 MW; B44F0B0D95665CAC CRC64;
MAIISEMEEA RPSMVPFTAS FDPSNPIAFL EKVLDVIGKE SNFLKKDTAE KEIVAAVMAA
KQRLREAEKK KLEKESVKSM EVEKPKKDSL KPTELEKPKE ESLMATDPME IEKPKEEKES
GPIVPNKGNG LDFEKYSWGQ NLQEVTINIP MPEGTKSRSV TCEIKKNRLK VGLKGQDLIV
DGEFFNSVKP DDCFWNIEDQ KMISVLLTKQ DQMEWWKYCV KGEPEIDTQK VEPETSKLGD
LDPETRASVE KMMFDQRQKQ MGLPRSDEIE KKDMLKKFMA QNPGMDFSNA KFN
