BIP1_ORYSJ
ID BIP1_ORYSJ Reviewed; 665 AA.
AC Q6Z7B0; O24182;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Heat shock 70 kDa protein BIP1 {ECO:0000305};
DE AltName: Full=Luminal-binding protein 1 {ECO:0000305};
DE Short=OsBiP1 {ECO:0000303|PubMed:22050533};
DE Flags: Precursor;
GN Name=BIP1 {ECO:0000303|PubMed:21223397};
GN Synonyms=BIP {ECO:0000303|PubMed:9177027};
GN OrderedLocusNames=Os02g0115900 {ECO:0000312|EMBL:BAF07589.1},
GN LOC_Os02g02410 {ECO:0000305};
GN ORFNames=OJ1442_E05.10 {ECO:0000312|EMBL:BAD07713.1},
GN OsJ_05115 {ECO:0000312|EMBL:EAZ21491.1},
GN P0036E06.29 {ECO:0000312|EMBL:BAD07938.1};
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 [MRNA], SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=9177027; DOI=10.1093/oxfordjournals.pcp.a029183;
RA Muench D.G., Wu Y., Zhang Y., Li X., Boston R.S., Okita T.W.;
RT "Molecular cloning, expression and subcellular localization of a BiP
RT homolog from rice endosperm tissue.";
RL Plant Cell Physiol. 38:404-412(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Ilpoombyeo;
RA Yoon U.H., Kim Y.H.;
RT "Molecular cloning of the dnak-type molecular chaperone Bip gene in rice.";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19567376; DOI=10.1093/pcp/pcp098;
RA Yasuda H., Hirose S., Kawakatsu T., Wakasa Y., Takaiwa F.;
RT "Overexpression of BiP has inhibitory effects on the accumulation of seed
RT storage proteins in endosperm cells of rice.";
RL Plant Cell Physiol. 50:1532-1543(2009).
RN [8]
RP FUNCTION, AND INDUCTION BY DITHIOTHREITOL.
RX PubMed=21223397; DOI=10.1111/j.1365-313x.2010.04453.x;
RA Wakasa Y., Yasuda H., Oono Y., Kawakatsu T., Hirose S., Takahashi H.,
RA Hayashi S., Yang L., Takaiwa F.;
RT "Expression of ER quality control-related genes in response to changes in
RT BiP1 levels in developing rice endosperm.";
RL Plant J. 65:675-689(2011).
RN [9]
RP 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 [10]
RP INTERACTION WITH P58A; P58B AND ERDJ3B, AND 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: Key chaperone involved in folding of secretory proteins in
CC the endoplasmic reticulum (ER) lumen (Probable). Involved in ER quality
CC control for seed storage proteins during seed maturation
CC (PubMed:19567376, PubMed:21223397). Functions as a sensor of the ER
CC stress response, and provides suitable conditions for the production of
CC secretory proteins by alleviating ER stress (PubMed:19567376,
CC PubMed:21223397). {ECO:0000269|PubMed:19567376,
CC ECO:0000269|PubMed:21223397, ECO:0000305|PubMed:21223397}.
CC -!- SUBUNIT: Interacts with P58A, P58B and ERDJ3B.
CC {ECO:0000269|PubMed:24153418}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000269|PubMed:19567376, ECO:0000269|PubMed:9177027}.
CC Note=Localizes close to the endoplasmic reticulum (ER) membrane complex
CC of developing endosperm cells. Localizes to the periphery of the
CC prolamine protein bodies which originate directly from the ER.
CC {ECO:0000269|PubMed:9177027}.
CC -!- DEVELOPMENTAL STAGE: During seed development, expressed from 5 to 20
CC days after flowering (DAF), with a peak at 10 DAF. Not expressed in
CC mature seeds. {ECO:0000269|PubMed:9177027}.
CC -!- INDUCTION: By dithiothreitol-induced endoplasmic reticulum (ER) stress
CC response (PubMed:21223397, PubMed:24153418). Induced by tunicamycin-
CC induced ER stress response (PubMed:24153418).
CC {ECO:0000269|PubMed:21223397, ECO:0000269|PubMed:24153418}.
CC -!- MISCELLANEOUS: The kernels of the over-expressing transformant exhibit
CC floury and shrunken features due to defects in seed storage proteins
CC and starch synthesis. {ECO:0000269|PubMed:19567376}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; AF006825; AAB63469.1; -; mRNA.
DR EMBL; EU267978; ACA50500.1; -; mRNA.
DR EMBL; AP004121; BAD07713.1; -; Genomic_DNA.
DR EMBL; AP004867; BAD07938.1; -; Genomic_DNA.
DR EMBL; AP008208; BAF07589.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS76651.1; -; Genomic_DNA.
DR EMBL; CM000139; EAZ21491.1; -; Genomic_DNA.
DR PIR; T03581; T03581.
DR RefSeq; XP_015625618.1; XM_015770132.1.
DR AlphaFoldDB; Q6Z7B0; -.
DR SMR; Q6Z7B0; -.
DR STRING; 4530.OS02T0115900-02; -.
DR CarbonylDB; Q6Z7B0; -.
DR PaxDb; Q6Z7B0; -.
DR PRIDE; Q6Z7B0; -.
DR EnsemblPlants; Os02t0115900-01; Os02t0115900-01; Os02g0115900.
DR EnsemblPlants; Os02t0115900-02; Os02t0115900-02; Os02g0115900.
DR GeneID; 4328075; -.
DR Gramene; Os02t0115900-01; Os02t0115900-01; Os02g0115900.
DR Gramene; Os02t0115900-02; Os02t0115900-02; Os02g0115900.
DR KEGG; osa:4328075; -.
DR eggNOG; KOG0100; Eukaryota.
DR HOGENOM; CLU_005965_7_2_1; -.
DR InParanoid; Q6Z7B0; -.
DR OMA; DSKPCIE; -.
DR OrthoDB; 288077at2759; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000007752; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR ExpressionAtlas; Q6Z7B0; baseline and differential.
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; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0009705; C:plant-type vacuole membrane; IDA:UniProtKB.
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:0034975; P:protein folding in endoplasmic reticulum; IMP:UniProtKB.
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; PS00014; ER_TARGET; 1.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chaperone; Endoplasmic reticulum; Glycoprotein;
KW Nucleotide-binding; Reference proteome; Signal; Stress response.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..665
FT /note="Heat shock 70 kDa protein BIP1"
FT /id="PRO_5008176825"
FT REGION 641..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 662..665
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT CARBOHYD 614
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 7
FT /note="C -> S (in Ref. 1; AAB63469)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="L -> D (in Ref. 1; AAB63469)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="D -> E (in Ref. 1; AAB63469)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="D -> I (in Ref. 1; AAB63469)"
FT /evidence="ECO:0000305"
FT CONFLICT 651..658
FT /note="GADGEGGV -> RRRGRL (in Ref. 1; AAB63469)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 665 AA; 73390 MW; C6E587D999AB42F5 CRC64;
MDRVRGCAFL LGVLLAGSLF AFSVAKEETK KLGTVIGIDL GTTYSCVGVY KNGHVEIIAN
DQGNRITPSW VAFTDSERLI GEAAKNQAAV NPERTIFDVK RLIGRKFEDK EVQRDMKLVP
YKIVNKDGKP YIQVKIKDGE NKVFSPEEVS AMILGKMKET AEAYLGKKIN DAVVTVPAYF
NDAQRQATKD AGVIAGLNVA RIINEPTAAA IAYGLDKKGG EKNILVFDLG GGTFDVSILT
IDNGVFEVLA TNGDTHLGGE DFDQRIMEYF IKLIKKKYSK DISKDNRALG KLRREAERAK
RALSNQHQVR VEIESLFDGT DFSEPLTRAR FEELNNDLFR KTMGPVKKAM DDAGLEKSQI
HEIVLVGGST RIPKVQQLLR DYFEGKEPNK GVNPDEAVAY GAAVQGSILS GEGGDETKDI
LLLDVAPLTL GIETVGGVMT KLIPRNTVIP TKKSQVFTTY QDQQTTVSIQ VFEGERSMTK
DCRLLGKFDL SGIPAAPRGT PQIEVTFEVD ANGILNVKAE DKGTGKSEKI TITNEKGRLS
QEEIDRMVRE AEEFAEEDKK VKERIDARNQ LETYVYNMKN TVGDKDKLAD KLESEEKEKV
EEALKEALEW LDENQTAEKE EYEEKLKEVE AVCNPIISAV YQRTGGAPGG GADGEGGVDD
EHDEL
