BIP2_ARATH
ID BIP2_ARATH Reviewed; 668 AA.
AC Q39043; Q39042;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Heat shock 70 kDa protein BIP2;
DE AltName: Full=Heat shock 70 kDa protein 12 {ECO:0000303|PubMed:11599561};
DE AltName: Full=Heat shock protein 70-12 {ECO:0000303|PubMed:11599561};
DE Short=AtHsp70-12 {ECO:0000303|PubMed:11599561};
DE AltName: Full=Luminal-binding protein 2;
DE Short=AtBP2 {ECO:0000303|Ref.2};
DE Short=BiP2 {ECO:0000303|PubMed:20231441};
DE Flags: Precursor;
GN Name=BIP2 {ECO:0000303|PubMed:20231441};
GN Synonyms=BIP {ECO:0000303|PubMed:8888624},
GN HSP70-12 {ECO:0000303|PubMed:11599561},
GN MED37_6 {ECO:0000303|PubMed:22021418}, MED37F;
GN OrderedLocusNames=At5g42020 {ECO:0000312|Araport:AT5G42020};
GN ORFNames=MJC20.12 {ECO:0000312|EMBL:BAB08435.1};
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], AND INDUCTION.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=8888624; DOI=10.1093/oxfordjournals.pcp.a029023;
RA Koizumi N.;
RT "Isolation and responses to stress of a gene that encodes a luminal binding
RT protein in Arabidopsis thaliana.";
RL Plant Cell Physiol. 37:862-865(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Koizumi N., Sano H.;
RT "Isolation of two genes encoding luminal binding protein from Arabidopsis
RT thaliana.";
RL (er) Plant Gene Register PGR97-028(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10470850; DOI=10.1093/dnares/6.3.183;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT clones.";
RL DNA Res. 6:183-195(1999).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
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 [7]
RP DNAK GENE SUBFAMILY, INDUCTION, AND DEVELOPMENTAL STAGE.
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 [8]
RP INDUCTION BY SUGAR.
RX PubMed=16781668; DOI=10.1016/j.bbrc.2006.05.189;
RA Tajima H., Koizumi N.;
RT "Induction of BiP by sugar independent of a cis-element for the unfolded
RT protein response in Arabidopsis thaliana.";
RL Biochem. Biophys. Res. Commun. 346:926-930(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17560376; DOI=10.1016/j.molcel.2007.05.007;
RA Baeckstroem S., Elfving N., Nilsson R., Wingsle G., Bjoerklund S.;
RT "Purification of a plant mediator from Arabidopsis thaliana identifies PFT1
RT as the Med25 subunit.";
RL Mol. Cell 26:717-729(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [11]
RP INDUCTION BY LIGHT; DTT AND TUNICAMYCIN.
RX PubMed=18494858; DOI=10.1111/j.1399-3054.2008.01133.x;
RA Lu D.P., Christopher D.A.;
RT "Light enhances the unfolded protein response as measured by BiP2 gene
RT expression and the secretory GFP-2SC marker in Arabidopsis.";
RL Physiol. Plantarum 134:360-368(2008).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20080634; DOI=10.1073/pnas.0905795107;
RA Maruyama D., Endo T., Nishikawa S.;
RT "BiP-mediated polar nuclei fusion is essential for the regulation of
RT endosperm nuclei proliferation in Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:1684-1689(2010).
RN [13]
RP INTERACTION WITH BAG7.
RX PubMed=20231441; DOI=10.1073/pnas.0912670107;
RA Williams B., Kabbage M., Britt R., Dickman M.B.;
RT "AtBAG7, an Arabidopsis Bcl-2-associated athanogene, resides in the
RT endoplasmic reticulum and is involved in the unfolded protein response.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:6088-6093(2010).
RN [14]
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 [15]
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 [16]
RP 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).
RN [17]
RP FUNCTION.
RX PubMed=31410484; DOI=10.1093/pcp/pcz158;
RA Maruyama D., Higashiyama T., Endo T., Nishikawa S.I.;
RT "Fertilization-coupled sperm nuclear fusion is required for normal
RT endosperm nuclear proliferation.";
RL Plant Cell Physiol. 61:29-40(2020).
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). Involved in polar nuclei fusion during female gametophyte
CC development and is essential for the regulation of endosperm nuclei
CC proliferation (PubMed:20080634). Involved in sperm nuclear fusion with
CC central cell polar nuclei at fertilization, which is critical for
CC normal endosperm nuclear proliferation (PubMed:31410484). Required for
CC pollen development and pollen tube growth (PubMed:24486762).
CC {ECO:0000269|PubMed:20080634, ECO:0000269|PubMed:24486762,
CC ECO:0000269|PubMed:31410484, ECO:0000305|PubMed:11402207}.
CC -!- SUBUNIT: Interacts with BAG7. {ECO:0000269|PubMed:20231441}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC ProRule:PRU10138}. Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q39043-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in mature pollen grains, and pollen
CC tubes. {ECO:0000269|PubMed:24486762}.
CC -!- DEVELOPMENTAL STAGE: Down-regulated during seed maturation. Up-
CC regulated during germination. {ECO:0000269|PubMed:11402207}.
CC -!- INDUCTION: Induced by heat shock and sugar. Up-regulated by light, DTT
CC and tunicamycin treatment. {ECO:0000269|PubMed:11402207,
CC ECO:0000269|PubMed:16781668, ECO:0000269|PubMed:18494858,
CC ECO:0000269|PubMed:8888624}.
CC -!- DISRUPTION PHENOTYPE: Bip1 and bip2 double mutation affects the fusion
CC of polar nuclei during female gametophyte development
CC (PubMed:20080634). Bip1 and bip2 double mutation affects pollen tube
CC growth and length (PubMed:24486762). Bip1, bip2 and bip3 triple
CC mutation is pollen lethal (PubMed:24486762). Bip1, bip2 and bip3 triple
CC mutation affects female gametophyte development during the early stages
CC (PubMed:26251880). {ECO:0000269|PubMed:20080634,
CC ECO:0000269|PubMed:24486762, ECO:0000269|PubMed:26251880}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 (TC 1.A.33) family.
CC DnaK subfamily. {ECO:0000305}.
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DR EMBL; D84414; BAA12348.1; -; mRNA.
DR EMBL; D89342; BAA13948.1; -; Genomic_DNA.
DR EMBL; AB017067; BAB08435.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94755.1; -; Genomic_DNA.
DR EMBL; BT002392; AAO00752.1; -; mRNA.
DR EMBL; BT008406; AAP37765.1; -; mRNA.
DR PIR; S71171; S71171.
DR RefSeq; NP_851119.1; NM_180788.3. [Q39043-1]
DR AlphaFoldDB; Q39043; -.
DR SMR; Q39043; -.
DR BioGRID; 19457; 26.
DR IntAct; Q39043; 3.
DR MINT; Q39043; -.
DR STRING; 3702.AT5G42020.1; -.
DR iPTMnet; Q39043; -.
DR MetOSite; Q39043; -.
DR SwissPalm; Q39043; -.
DR SWISS-2DPAGE; Q39043; -.
DR PaxDb; Q39043; -.
DR PRIDE; Q39043; -.
DR EnsemblPlants; AT5G42020.1; AT5G42020.1; AT5G42020. [Q39043-1]
DR GeneID; 834207; -.
DR Gramene; AT5G42020.1; AT5G42020.1; AT5G42020. [Q39043-1]
DR KEGG; ath:AT5G42020; -.
DR Araport; AT5G42020; -.
DR TAIR; locus:2165715; AT5G42020.
DR eggNOG; KOG0100; Eukaryota.
DR HOGENOM; CLU_005965_7_2_1; -.
DR InParanoid; Q39043; -.
DR OMA; DSKPCIE; -.
DR PhylomeDB; Q39043; -.
DR PRO; PR:Q39043; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q39043; baseline and differential.
DR Genevisible; Q39043; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
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:0016592; C:mediator complex; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
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:0034976; P:response to endoplasmic reticulum stress; IEP:TAIR.
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 Alternative splicing; ATP-binding; Chaperone; Endoplasmic reticulum;
KW Nucleotide-binding; Nucleus; Reference proteome; Signal; Transcription;
KW Transcription regulation.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..668
FT /note="Heat shock 70 kDa protein BIP2"
FT /id="PRO_0000013589"
FT REGION 643..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 665..668
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT CONFLICT 163
FT /note="A -> T (in Ref. 2; BAA13948)"
FT /evidence="ECO:0000305"
FT CONFLICT 485
FT /note="R -> S (in Ref. 1; BAA12348)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 668 AA; 73561 MW; 584DB253E91E68CA CRC64;
MARSFGANST VVLAIIFFGC LFAFSTAKEE ATKLGSVIGI DLGTTYSCVG VYKNGHVEII
ANDQGNRITP SWVGFTDSER LIGEAAKNQA AVNPERTVFD VKRLIGRKFE DKEVQKDRKL
VPYQIVNKDG KPYIQVKIKD GETKVFSPEE ISAMILTKMK ETAEAYLGKK IKDAVVTVPA
YFNDAQRQAT KDAGVIAGLN VARIINEPTA AAIAYGLDKK GGEKNILVFD LGGGTFDVSV
LTIDNGVFEV LSTNGDTHLG GEDFDHRIME YFIKLIKKKH QKDISKDNKA LGKLRRECER
AKRALSSQHQ VRVEIESLFD GVDLSEPLTR ARFEELNNDL FRKTMGPVKK AMDDAGLQKS
QIDEIVLVGG STRIPKVQQL LKDFFEGKEP NKGVNPDEAV AYGAAVQGGI LSGEGGDETK
DILLLDVAPL TLGIETVGGV MTKLIPRNTV IPTKKSQVFT TYQDQQTTVS IQVFEGERSL
TKDCRLLGKF DLTGVPPAPR GTPQIEVTFE VDANGILNVK AEDKASGKSE KITITNEKGR
LSQEEIDRMV KEAEEFAEED KKVKEKIDAR NALETYVYNM KNQVSDKDKL ADKLEGDEKE
KIEAATKEAL EWLDENQNSE KEEYDEKLKE VEAVCNPIIT AVYQRSGGAP GAGGESSTEE
EDESHDEL
