ID   BIP5_ORYSJ              Reviewed;         676 AA.
AC   Q6Z058; A0A0P0XCZ2;
DT   30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Heat shock 70 kDa protein BIP5 {ECO:0000305};
DE   AltName: Full=Luminal-binding protein 5 {ECO:0000305};
DE            Short=OsBiP5 {ECO:0000303|PubMed:22050533};
DE   Flags: Precursor;
GN   Name=BIP5 {ECO:0000303|PubMed:22050533};
GN   OrderedLocusNames=Os08g0197700 {ECO:0000312|EMBL:BAF23108.1},
GN   LOC_Os08g09770 {ECO:0000305};
GN   ORFNames=P0412D08.27 {ECO:0000312|EMBL:BAD03698.1};
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=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   [2]
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   [3]
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   [4]
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   [5]
RP   INTERACTION WITH ERDJ3A, 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: Functions as chaperone during endoplasmic reticulum (ER)
CC       stress response. {ECO:0000250|UniProtKB:Q6Z7B0}.
CC   -!- SUBUNIT: Interacts with ERDJ3A. {ECO:0000269|PubMed:24153418}.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAT04227.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AP005499; BAD03698.1; -; Genomic_DNA.
DR   EMBL; AP008214; BAF23108.1; -; Genomic_DNA.
DR   EMBL; AP014964; BAT04227.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q6Z058; -.
DR   SMR; Q6Z058; -.
DR   STRING; 4530.OS08T0197700-00; -.
DR   PRIDE; Q6Z058; -.
DR   eggNOG; KOG0100; Eukaryota.
DR   HOGENOM; CLU_005965_7_2_1; -.
DR   InParanoid; Q6Z058; -.
DR   Proteomes; UP000000763; Chromosome 8.
DR   Proteomes; UP000059680; Chromosome 8.
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   1: Evidence at protein level;
KW   ATP-binding; Chaperone; Endoplasmic reticulum; Nucleotide-binding;
KW   Reference proteome; Signal; Stress response.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..676
FT                   /note="Heat shock 70 kDa protein BIP5"
FT                   /id="PRO_5007709809"
FT   REGION          650..676
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           673..676
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
SQ   SEQUENCE   676 AA;  73504 MW;  6345F0EC0D9C3A15 CRC64;
     MARPRRASTM QLGLFLAALL LLTPSPAGSV AAAKGGGAKS GGGGTVIGID LGTTYSCVGV
     YRNGHVEIIA NDQGNRITPS WVAFTDGGER LIGEAAKNQA AANPERTIYD AKRLIGRQFS
     DAEVQRDMKL LPFAVVDRNG KPHVRVEVKD GDVRVFSPEE VSAMVLTRMK ETAEAYLGEK
     VTRAVVTVPA YFNDAQRQAT KDAGVIAGLT VDRIINEPTA AAIAYGIDKK GAEKNVLVFD
     LGGGTFDVSI LAIDNGVFEV LATNGDTHLG GEDFDQRLMD HFVKVIRRKH GRDITGDARA
     LGKLRRECER AKRALSNQHQ VRVEVESLFD GVDLSEPLSR ARFEELNSDL FKKTMVPVRK
     AMADARLSKG DIDEIVLVGG STRIPKVQQL LKDYFGGKEP NRGVNPDEAV AYGAAVQASI
     ISGHVDENTE SMILLDVAPL TLGLETAGGV MAKLIPRNTV VPTKKTQVFT TYKDKQTTVT
     IQVFEGERSM TRDNRLLGRF DLAGIAPAPR GAPQIEVTFE VDANGILSVL AADKATGRSE
     KITISGDDRK ISQEEIDRMV REAEEFAEED RRHREQVDAR NSLEAYVYNI KNTLGGKMAD
     AMEGEEKDKV EEAVREAYEW LDGNPDAGKE EYEEKLRELE DVCNPVMSAV YQRSGGGGGG
     APEDGNVDDE DDHDEL