ID   BIP3_ARATH              Reviewed;         675 AA.
AC   Q8H1B3; F4HZD5; O04022;
DT   22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 147.
DE   RecName: Full=Heat shock 70 kDa protein BIP3;
DE   AltName: Full=BiP chaperone BIP-L {ECO:0000303|PubMed:12853141};
DE   AltName: Full=Heat shock 70 kDa protein 13 {ECO:0000303|PubMed:11599561};
DE   AltName: Full=Heat shock protein 70-13 {ECO:0000303|PubMed:11599561};
DE            Short=AtHsp70-13 {ECO:0000303|PubMed:11599561};
DE   AltName: Full=Hsp70 protein BiP chaperone BIP-L {ECO:0000305};
DE   AltName: Full=Luminal-binding protein 3;
DE            Short=AtBP3;
DE            Short=BiP3 {ECO:0000303|PubMed:21482766};
DE   Flags: Precursor;
GN   Name=BIP3 {ECO:0000303|PubMed:21482766};
GN   Synonyms=BIP-L {ECO:0000303|PubMed:12853141}, HSP70-13
GN   {ECO:0000303|PubMed:11599561}, MED37_1 {ECO:0000303|PubMed:22021418},
GN   MED37B; OrderedLocusNames=At1g09080 {ECO:0000312|Araport:AT1G09080};
GN   ORFNames=F7G19.5 {ECO:0000312|EMBL:AAB70400.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INDUCTION.
RC   STRAIN=cv. Columbia;
RX   PubMed=12853141; DOI=10.1016/s0378-1119(03)00559-6;
RA   Noh S.J., Kwon C.S., Oh D.H., Moon J.S., Chung W.I.;
RT   "Expression of an evolutionarily distinct novel BiP gene during the
RT   unfolded protein response in Arabidopsis thaliana.";
RL   Gene 311:81-91(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=11599561; DOI=10.1379/1466-1268(2001)006<0201:gaoths>2.0.co;2;
RA   Lin B.L., Wang J.S., Liu H.C., Chen R.W., Meyer Y., Barakat A., Delseny M.;
RT   "Genomic analysis of the Hsp70 superfamily in Arabidopsis thaliana.";
RL   Cell Stress Chaperones 6:201-208(2001).
RN   [5]
RP   DNAK GENE SUBFAMILY.
RX   PubMed=11402207; DOI=10.1104/pp.126.2.789;
RA   Sung D.Y., Vierling E., Guy C.L.;
RT   "Comprehensive expression profile analysis of the Arabidopsis Hsp70 gene
RT   family.";
RL   Plant Physiol. 126:789-800(2001).
RN   [6]
RP   INDUCTION BY DTT.
RX   PubMed=21482766; DOI=10.1073/pnas.1102117108;
RA   Deng Y., Humbert S., Liu J.X., Srivastava R., Rothstein S.J., Howell S.H.;
RT   "Heat induces the splicing by IRE1 of a mRNA encoding a transcription
RT   factor involved in the unfolded protein response in Arabidopsis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:7247-7252(2011).
RN   [7]
RP   NOMENCLATURE.
RX   PubMed=22021418; DOI=10.1104/pp.111.188300;
RA   Mathur S., Vyas S., Kapoor S., Tyagi A.K.;
RT   "The Mediator complex in plants: structure, phylogeny, and expression
RT   profiling of representative genes in a dicot (Arabidopsis) and a monocot
RT   (rice) during reproduction and abiotic stress.";
RL   Plant Physiol. 157:1609-1627(2011).
RN   [8]
RP   INTERACTION WITH BZIP28, AND SUBCELLULAR LOCATION.
RX   PubMed=23624714; DOI=10.1105/tpc.113.110684;
RA   Srivastava R., Deng Y., Shah S., Rao A.G., Howell S.H.;
RT   "BINDING PROTEIN is a master regulator of the endoplasmic reticulum stress
RT   sensor/transducer bZIP28 in Arabidopsis.";
RL   Plant Cell 25:1416-1429(2013).
RN   [9]
RP   FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=24486762; DOI=10.1093/pcp/pcu018;
RA   Maruyama D., Sugiyama T., Endo T., Nishikawa S.;
RT   "Multiple BiP genes of Arabidopsis thaliana are required for male
RT   gametogenesis and pollen competitiveness.";
RL   Plant Cell Physiol. 55:801-810(2014).
RN   [10]
RP   FUNCTION, ACTIVITY REGULATION, AND INTERACTION WITH ERDJ3A.
RX   PubMed=26186593; DOI=10.1371/journal.pone.0132500;
RA   Ma Z.X., Leng Y.J., Chen G.X., Zhou P.M., Ye D., Chen L.Q.;
RT   "The THERMOSENSITIVE MALE STERILE 1 interacts with the BiPs via DnaJ domain
RT   and stimulates their ATPase enzyme activities in Arabidopsis.";
RL   PLoS ONE 10:E0132500-E0132500(2015).
RN   [11]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=26251880; DOI=10.1080/15592324.2015.1035853;
RA   Maruyama D., Endo T., Nishikawa S.;
RT   "BiP3 supports the early stages of female gametogenesis in the absence of
RT   BiP1 and BiP2 in Arabidopsis thaliana.";
RL   Plant Signal. Behav. 10:E1035853-E1035853(2015).
CC   -!- FUNCTION: In cooperation with other chaperones, Hsp70s are key
CC       components that facilitate folding of de novo synthesized proteins,
CC       assist translocation of precursor proteins into organelles, and are
CC       responsible for degradation of damaged protein under stress conditions
CC       (Probable). Required for pollen development and pollen tube growth
CC       (PubMed:24486762). May be required for the early stages of female
CC       gametophyte development, but not for polar nuclei fusion during female
CC       gametophyte (PubMed:26251880). Possesses ATPase activity in vitro
CC       (PubMed:26186593). {ECO:0000269|PubMed:24486762,
CC       ECO:0000269|PubMed:26186593, ECO:0000269|PubMed:26251880,
CC       ECO:0000305|PubMed:11402207}.
CC   -!- ACTIVITY REGULATION: Binding to ERDJ3A activates the ATPase activity of
CC       BIP3. {ECO:0000269|PubMed:26186593}.
CC   -!- SUBUNIT: Interacts with BZIP28 (via C-terminus) (PubMed:23624714).
CC       Interacts with ERDJ3A (PubMed:26186593). {ECO:0000269|PubMed:23624714,
CC       ECO:0000269|PubMed:26186593}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC       ProRule:PRU10138, ECO:0000269|PubMed:23624714}. Nucleus {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8H1B3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8H1B3-2; Sequence=VSP_042244;
CC   -!- TISSUE SPECIFICITY: Expressed in mature pollen grains, and pollen
CC       tubes. {ECO:0000269|PubMed:24486762}.
CC   -!- INDUCTION: Induced by tunicamycin and DTT.
CC       {ECO:0000269|PubMed:12853141, ECO:0000269|PubMed:21482766}.
CC   -!- DISRUPTION PHENOTYPE: Bip1, bip2 and bip3 triple mutation is pollen
CC       lethal (PubMed:24486762). Bip1, bip2 and bip3 triple mutation affects
CC       female gametophyte development during the early stages
CC       (PubMed:26186593). {ECO:0000269|PubMed:24486762,
CC       ECO:0000269|PubMed:26186593}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 (TC 1.A.33) family.
CC       DnaK subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB70400.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AY156728; AAN60163.1; -; mRNA.
DR   EMBL; AC000106; AAB70400.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE28392.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE28393.1; -; Genomic_DNA.
DR   PIR; H86222; H86222.
DR   RefSeq; NP_001184944.1; NM_001198015.2. [Q8H1B3-2]
DR   RefSeq; NP_172382.4; NM_100779.5. [Q8H1B3-1]
DR   AlphaFoldDB; Q8H1B3; -.
DR   SMR; Q8H1B3; -.
DR   BioGRID; 22670; 2.
DR   IntAct; Q8H1B3; 2.
DR   MINT; Q8H1B3; -.
DR   STRING; 3702.Q8H1B3; -.
DR   PaxDb; 3702-AT1G09080-1; -.
DR   ProMEX; Q8H1B3; -.
DR   ProteomicsDB; 238248; -. [Q8H1B3-1]
DR   EnsemblPlants; AT1G09080.1; AT1G09080.1; AT1G09080. [Q8H1B3-1]
DR   EnsemblPlants; AT1G09080.2; AT1G09080.2; AT1G09080. [Q8H1B3-2]
DR   GeneID; 837429; -.
DR   Gramene; AT1G09080.1; AT1G09080.1; AT1G09080. [Q8H1B3-1]
DR   Gramene; AT1G09080.2; AT1G09080.2; AT1G09080. [Q8H1B3-2]
DR   KEGG; ath:AT1G09080; -.
DR   Araport; AT1G09080; -.
DR   TAIR; AT1G09080; BIP3.
DR   eggNOG; KOG0100; Eukaryota.
DR   InParanoid; Q8H1B3; -.
DR   OMA; DEYMCLW; -.
DR   OrthoDB; 143at2759; -.
DR   PhylomeDB; Q8H1B3; -.
DR   PRO; PR:Q8H1B3; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q8H1B3; baseline and differential.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0016592; C:mediator complex; IDA:UniProtKB.
DR   GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0009860; P:pollen tube growth; IEP:TAIR.
DR   GO; GO:0000304; P:response to singlet oxygen; IMP:TAIR.
DR   CDD; cd10241; HSPA5-like_NBD; 1.
DR   Gene3D; 1.20.1270.10; -; 1.
DR   Gene3D; 3.30.420.40; -; 2.
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:SF542; HEAT SHOCK 70 KDA PROTEIN BIP3; 1.
DR   PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
DR   SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
DR   PROSITE; PS00014; ER_TARGET; 1.
DR   PROSITE; PS00297; HSP70_1; 1.
DR   PROSITE; PS00329; HSP70_2; 1.
DR   PROSITE; PS01036; HSP70_3; 1.
DR   Genevisible; Q8H1B3; AT.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Chaperone; Endoplasmic reticulum;
KW   Nucleotide-binding; Nucleus; Reference proteome; Signal; Transcription;
KW   Transcription regulation.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000255"
FT   CHAIN           36..675
FT                   /note="Heat shock 70 kDa protein BIP3"
FT                   /id="PRO_0000415430"
FT   REGION          656..675
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           673..675
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT   VAR_SEQ         25..34
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_042244"
SQ   SEQUENCE   675 AA;  75149 MW;  6FF9FAE4B2A4702D CRC64;
     MIFIKENTAK MTRNKAIACL VFLTVLDFLM NIGAALMSSL AIEGEEQKLG TVIGIDLGTT
     YSCVGVYHNK HVEIIANDQG NRITPSWVAF TDTERLIGEA AKNQAAKNPE RTIFDPKRLI
     GRKFDDPDVQ RDIKFLPYKV VNKDGKPYIQ VKVKGEEKLF SPEEISAMIL TKMKETAEAF
     LGKKIKDAVI TVPAYFNDAQ RQATKDAGAI AGLNVVRIIN EPTGAAIAYG LDKKGGESNI
     LVYDLGGGTF DVSILTIDNG VFEVLSTSGD THLGGEDFDH RVMDYFIKLV KKKYNKDISK
     DHKALGKLRR ECELAKRSLS NQHQVRVEIE SLFDGVDFSE PLTRARFEEL NMDLFKKTME
     PVKKALKDAG LKKSDIDEIV LVGGSTRIPK VQQMLKDFFD GKEPSKGTNP DEAVAYGAAV
     QGGVLSGEGG EETQNILLLD VAPLSLGIET VGGVMTNIIP RNTVIPTKKS QVFTTYQDQQ
     TTVTINVYEG ERSMTKDNRE LGKFDLTGIL PAPRGVPQIE VTFEVDANGI LQVKAEDKVA
     KTSQSITITN DKGRLTEEEI EEMIREAEEF AEEDKIMKEK IDARNKLETY VYNMKSTVAD
     KEKLAKKISD EDKEKMEGVL KEALEWLEEN VNAEKEDYDE KLKEVELVCD PVIKSVYEKT
     EGENEDDDGD DHDEL
//