ID   BIP4_ORYSJ              Reviewed;         687 AA.
AC   Q75HQ0;
DT   30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Heat shock 70 kDa protein BIP4 {ECO:0000305};
DE   AltName: Full=Luminal-binding protein 4 {ECO:0000305};
DE            Short=OsBiP4 {ECO:0000303|PubMed:22050533};
DE   Flags: Precursor;
GN   Name=BIP4 {ECO:0000303|PubMed:22050533};
GN   OrderedLocusNames=Os05g0428600 {ECO:0000312|EMBL:BAF17527.1},
GN   LOC_Os05g35400 {ECO:0000305};
GN   ORFNames=OSJNBb0048I21.2 {ECO:0000312|EMBL:AAV59416.1},
GN   P0636F09.18 {ECO:0000312|EMBL:AAS90667.1};
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; AC130600; AAV59416.1; -; Genomic_DNA.
DR   EMBL; AC135429; AAS90667.1; -; Genomic_DNA.
DR   EMBL; AP008211; BAF17527.1; -; Genomic_DNA.
DR   EMBL; AP014961; BAS94137.1; -; Genomic_DNA.
DR   RefSeq; XP_015638801.1; XM_015783315.1.
DR   AlphaFoldDB; Q75HQ0; -.
DR   SMR; Q75HQ0; -.
DR   STRING; 4530.OS05T0428600-01; -.
DR   PaxDb; Q75HQ0; -.
DR   PRIDE; Q75HQ0; -.
DR   EnsemblPlants; Os05t0428600-01; Os05t0428600-01; Os05g0428600.
DR   GeneID; 4338866; -.
DR   Gramene; Os05t0428600-01; Os05t0428600-01; Os05g0428600.
DR   KEGG; osa:4338866; -.
DR   eggNOG; KOG0100; Eukaryota.
DR   HOGENOM; CLU_005965_2_1_1; -.
DR   InParanoid; Q75HQ0; -.
DR   OMA; GHVDDNT; -.
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; Nucleotide-binding;
KW   Reference proteome; Signal; Stress response.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..687
FT                   /note="Heat shock 70 kDa protein BIP4"
FT                   /id="PRO_5008176954"
FT   REGION          662..687
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           684..687
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
SQ   SEQUENCE   687 AA;  74313 MW;  5569437875DBC014 CRC64;
     MARPRRASTA TTMQLGLLLA ALLLFTSSLA GSVAAAAPPP PAGAKGGGAK SGGGGGTVIG
     IDLGTTYSCV GVYRNDRVEI IANDQGNRIT PSWVAFTDGG ERLIGEAAKN QAAANPERTI
     YDAKRLIGRQ FSDAEVQRDM KLLPFAVVDR NGKPHVRVEV KDGDVRVFSP EEVSAMVLTR
     MKETAEAYLG EKVTRAVVTV PAYFNDAQRQ ATKDAGVIAG LTVDRIINEP TAAAIAYGID
     KKGAEKNVLV FDLGGGTFDV SILAIDNGVF EVLATNGDTH LGGEDFDQRL MDHFVKVIRR
     KHGRDIAGDA RALGKLRREC ERAKRALSNQ HQVRVEIESL FDGVDFSEPL SRARFEELNG
     DLFKKTMVPV RKAMADAGLG KGDIDEIVLV GGSTRIPKVQ QLLKDYFGGK EPNRGVNPDE
     AVAYGAAVQA SIISGHVDEN TESMILLDVA PLTLGLETAG GVMTKLIPRN TVVPTKKTQV
     FTTYKDRQTT VTIQVFEGER SMTRDNRLLG KFDLTGIAPA PRGAPQIAVT FEVDANGILS
     VLAADKATGR SEKITISGDD RKISQEEIDR MVREAEEFAD EDRRHREQVD ARNSLEAYVY
     NVKSTLGGKM ADAMEGEEKE KVEEAVREAH EWLDGNPDAG KEEYEEKLRE LEDVCNPVMS
     AVYQRSGGGG GAPEDGNVDD EDDHDEL