ID   BIP3_ORYSJ              Reviewed;         669 AA.
AC   Q6L590;
DT   30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Heat shock 70 kDa protein BIP3 {ECO:0000305};
DE   AltName: Full=Luminal-binding protein 3 {ECO:0000305};
DE            Short=OsBiP3 {ECO:0000303|PubMed:22050533};
DE   Flags: Precursor;
GN   Name=BIP3 {ECO:0000303|PubMed:22050533};
GN   OrderedLocusNames=Os05g0367800 {ECO:0000312|EMBL:BAF17253.1},
GN   LOC_Os05g30480 {ECO:0000305};
GN   ORFNames=OJ1393_A07.8 {ECO:0000312|EMBL:AAT38017.1};
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=16261349; DOI=10.1007/s00438-005-0039-y;
RA   Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J.,
RA   Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F.,
RA   Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.;
RT   "A fine physical map of the rice chromosome 5.";
RL   Mol. Genet. Genomics 274:337-345(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; AC104279; AAT38017.1; -; Genomic_DNA.
DR   EMBL; AP008211; BAF17253.1; -; Genomic_DNA.
DR   EMBL; AP014961; BAS93656.1; -; Genomic_DNA.
DR   RefSeq; XP_015638605.1; XM_015783119.1.
DR   AlphaFoldDB; Q6L590; -.
DR   SMR; Q6L590; -.
DR   STRING; 4530.OS05T0367800-00; -.
DR   PaxDb; Q6L590; -.
DR   PRIDE; Q6L590; -.
DR   EnsemblPlants; Os05t0367800-00; Os05t0367800-00; Os05g0367800.
DR   GeneID; 4338568; -.
DR   Gramene; Os05t0367800-00; Os05t0367800-00; Os05g0367800.
DR   KEGG; osa:4338568; -.
DR   eggNOG; KOG0100; Eukaryota.
DR   HOGENOM; CLU_005965_2_3_1; -.
DR   InParanoid; Q6L590; -.
DR   OMA; DKGGKPH; -.
DR   OrthoDB; 288077at2759; -.
DR   Proteomes; UP000000763; Chromosome 5.
DR   Proteomes; UP000059680; Chromosome 5.
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; PS00014; ER_TARGET; 1.
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; Glycoprotein;
KW   Nucleotide-binding; Reference proteome; Signal; Stress response.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000255"
FT   CHAIN           33..669
FT                   /note="Heat shock 70 kDa protein BIP3"
FT                   /id="PRO_5008176461"
FT   REGION          646..669
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           666..669
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT   CARBOHYD        423
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   669 AA;  72218 MW;  0F220341EAED1632 CRC64;
     MARGATWTRR LHLHGLFLAV LLLLTLPAGS TAAAGGGGGT VIGIDLGTTY SCVGVYRNGH
     VEIIANDQGN RITPSWVAFT GGGERLIGEA AKNQAAANPG RTVYDAKRLI GRRFADAEVQ
     RDMRLLPFAV VDKGGKPHVR VEVRGGDVRL LSPEEVSAMV LARMKETAEA YLGEEVTRAV
     VTVPAYFNDA QRQATKDAAT IAGLAVERIL NEPTAAALAY GVGKEGAGGK NVLVFDLGGG
     TFDVSVLAID GGVYEVLATN GDTHLGGEDF DQRVMEHFVE LVRRKHGRDI AGDARALGKL
     RRECERAKRA LSIQHQVRVE VESLFDGVDL SEPLSRARFE ELNNDLFRKT MAPVRKAMAD
     ARLSNADIDE IVLVGGSTRI PKVRQLLRDY FGGKQPNQGV NPDEAVAYGA AIQANIVGGD
     TDNKTRDMVV LDVTPLTLGL ETAGGVMATL IPRNTPVPTK RAQLFSTYKD KQTTVTVKVF
     EGERSMTRDN RLLGRFDLAG IAPAPRGAPQ IEVAFEVDAD GILSVSAADR ATGRSERITI
     SGDDRKTSRE EIDRMLGEAE EFADEDRRHR ERAGARNSLE AYVYGVKNAV VGGEMAGAMD
     GGEKEKVEAA VMEAYEWLDG NQDVGKEEYE EKLRELEDVC NPVMSAVYQR SGGSRRDGDG
     GGDDDHDEL