BIP3_ARATH
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 03-AUG-2022, entry version 139.
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},
GN HSP70-13 {ECO:0000303|PubMed:11599561},
GN MED37_1 {ECO:0000303|PubMed:22021418}, MED37B;
GN 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.AT1G09080.1; -.
DR PaxDb; Q8H1B3; -.
DR PRIDE; Q8H1B3; -.
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; locus:2035994; AT1G09080.
DR eggNOG; KOG0100; Eukaryota.
DR InParanoid; Q8H1B3; -.
DR OMA; ERNTMIP; -.
DR OrthoDB; 288077at2759; -.
DR PhylomeDB; Q8H1B3; -.
DR PRO; PR:Q8H1B3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8H1B3; baseline and differential.
DR Genevisible; Q8H1B3; AT.
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:0016592; C:mediator complex; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0009860; P:pollen tube growth; IEP:TAIR.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0000304; P:response to singlet oxygen; IMP: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..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
