BIP2_ORYSJ
ID BIP2_ORYSJ Reviewed; 669 AA.
AC Q53RJ5;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Heat shock 70 kDa protein BIP2 {ECO:0000305};
DE AltName: Full=Luminal-binding protein 2 {ECO:0000305};
DE Short=OsBiP2 {ECO:0000303|PubMed:22050533};
DE Flags: Precursor;
GN Name=BIP2 {ECO:0000303|PubMed:22050533};
GN OrderedLocusNames=Os03g0710500 {ECO:0000312|EMBL:BAF12962.1},
GN LOC_Os03g50250 {ECO:0000312|EMBL:ABF98501.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16109971; DOI=10.1101/gr.3869505;
RG The rice chromosome 3 sequencing consortium;
RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA Jin W., Lee H.R., Jiang J., Jackson S.;
RT "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT and diverged grass species.";
RL Genome Res. 15:1284-1291(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP INDUCTION BY DITHIOTHREITOL, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=22050533; DOI=10.1111/j.1365-313x.2011.04844.x;
RA Hayashi S., Wakasa Y., Takahashi H., Kawakatsu T., Takaiwa F.;
RT "Signal transduction by IRE1-mediated splicing of bZIP50 and other stress
RT sensors in the endoplasmic reticulum stress response of rice.";
RL Plant J. 69:946-956(2012).
RN [6]
RP INDUCTION.
RX PubMed=24153418; DOI=10.1093/jxb/ert312;
RA Ohta M., Wakasa Y., Takahashi H., Hayashi S., Kudo K., Takaiwa F.;
RT "Analysis of rice ER-resident J-proteins reveals diversity and functional
RT differentiation of the ER-resident Hsp70 system in plants.";
RL J. Exp. Bot. 64:5429-5441(2013).
CC -!- FUNCTION: Functions as chaperone during endoplasmic reticulum (ER)
CC stress response. {ECO:0000250|UniProtKB:Q6Z7B0}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000255|PROSITE-
CC ProRule:PRU10138}.
CC -!- INDUCTION: By dithiothreitol-induced endoplasmic reticulum (ER) stress
CC response (PubMed:22050533, PubMed:24153418). Induced by tunicamycin-
CC induced ER stress response (PubMed:24153418).
CC {ECO:0000269|PubMed:22050533, ECO:0000269|PubMed:24153418}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; AC087181; AAX95660.1; -; Genomic_DNA.
DR EMBL; DP000009; ABF98501.1; -; Genomic_DNA.
DR EMBL; AP008209; BAF12962.1; -; Genomic_DNA.
DR EMBL; AP014959; BAS86012.1; -; Genomic_DNA.
DR AlphaFoldDB; Q53RJ5; -.
DR SMR; Q53RJ5; -.
DR STRING; 4530.OS03T0710500-00; -.
DR PaxDb; Q53RJ5; -.
DR PRIDE; Q53RJ5; -.
DR EnsemblPlants; Os03t0710500-00; Os03t0710500-00; Os03g0710500.
DR Gramene; Os03t0710500-00; Os03t0710500-00; Os03g0710500.
DR eggNOG; KOG0100; Eukaryota.
DR HOGENOM; CLU_005965_7_2_1; -.
DR InParanoid; Q53RJ5; -.
DR OMA; PMKGGER; -.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0034663; C:endoplasmic reticulum chaperone complex; IBA:GO_Central.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0031072; F:heat shock protein binding; IBA:GO_Central.
DR GO; GO:0051787; F:misfolded protein binding; IBA:GO_Central.
DR GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0034620; P:cellular response to unfolded protein; IBA:GO_Central.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR CDD; cd10241; HSPA5-like_NBD; 1.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 2.60.34.10; -; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR042050; BIP_NBD.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029048; HSP70_C_sf.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR PANTHER; PTHR19375; PTHR19375; 1.
DR Pfam; PF00012; HSP70; 1.
DR SUPFAM; SSF100920; SSF100920; 1.
DR SUPFAM; SSF100934; SSF100934; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Chaperone; Endoplasmic reticulum; Nucleotide-binding;
KW Reference proteome; Signal; Stress response.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..669
FT /note="Heat shock 70 kDa protein BIP2"
FT /id="PRO_5008174748"
FT MOTIF 666..669
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
SQ SEQUENCE 669 AA; 73374 MW; A5ABDB618EC7185F CRC64;
MARDKQSALI VAAFVLLCSG CLCGVADGAK GGRKTKGPVI GIDLGTTYSC VGVYRNGHVD
IVANDQGNRI TPSWVAFTDD ERLVGEAAKN QAALNPDRTI FDIKRLIGRR FDDEEVQRDV
KYLPYKVVDK GGKPYVEVRV KAGEVKVFSP EEISAMILAK MKETAESYLG QRVTDAVVTV
PAYFNDAQRQ ATKDAGTIAG LNVPRIINEP TAAAIAYGLD RKGAGEMTNV LVYDLGGGTF
DVSVLSLDHG VFEVLATSGD THLGGEDFDR RVMDHFIRLV KRQHGRDIGG DGRALGKLRR
ECERAKRALS RQHQVRVEIE ALFVGVDFSE TLTRAKFEEL NMDLFKKTLG PVRKAIADAK
LKKSDIDEIV LVGGSTRIPK VQELLKEMFD GKEPTKGINP DEAVAYGAAV QGSIISGEGG
AETKDILLLD VTPLTLGIET AGGVMTKLIP RNTRIPVKKS QVFTTYEDHQ TTVSIKVFEG
ERSLTKDCRE LGRFDLSGIA PAPRGVPQIE VTFEVDENGI LHVTASDKAA GRSKSITITN
DKGRLSQEEI DRMVREAEEF AEEDRRVRER VDARNRLENY VYRMRSAVRD GGMAGKIGDD
DRERMESALT EALEWLEDND GGARTAEKED YEEKLKEVEQ VCGPIIKQVY KKSGDASAGA
GDDDDVNEL
