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Heat shock 70 kDa protein 1A (Heat shock 70 kDa protein 3) (HSP70.3) (Hsp68)

 HS71A_MOUSE             Reviewed;         641 AA.
Q61696; Q61697; Q7TQD8; Q9QWJ5;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
21-DEC-2004, sequence version 2.
22-NOV-2017, entry version 148.
RecName: Full=Heat shock 70 kDa protein 1A;
AltName: Full=Heat shock 70 kDa protein 3;
Short=HSP70.3;
AltName: Full=Hsp68;
Name=Hspa1a; Synonyms=Hsp70-3, Hsp70A1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
TISSUE=Liver;
PubMed=8076831; DOI=10.1016/0378-1119(94)90305-0;
Perry M.D., Aujame L., Shtang S., Moran L.A.;
"Structure and expression of an inducible HSP70-encoding gene from Mus
musculus.";
Gene 146:273-278(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=129;
PubMed=14656967; DOI=10.1101/gr.1736803;
Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S.,
Campbell R.D., Hood L.;
"Analysis of the gene-dense major histocompatibility complex class III
region and its comparison to mouse.";
Genome Res. 13:2621-2636(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PROTEIN SEQUENCE OF 26-49 AND 103-112, AND IDENTIFICATION BY MASS
SPECTROMETRY.
STRAIN=C57BL/6J; TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 221-641.
PubMed=2868009;
Lowe D.G., Moran L.A.;
"Molecular cloning and analysis of DNA complementary to three mouse Mr
= 68,000 heat shock protein mRNAs.";
J. Biol. Chem. 261:2102-2112(1986).
[6]
INTERACTION WITH DNAAF2.
PubMed=19052621; DOI=10.1038/nature07471;
Omran H., Kobayashi D., Olbrich H., Tsukahara T., Loges N.T.,
Hagiwara H., Zhang Q., Leblond G., O'Toole E., Hara C., Mizuno H.,
Kawano H., Fliegauf M., Yagi T., Koshida S., Miyawaki A., Zentgraf H.,
Seithe H., Reinhardt R., Watanabe Y., Kamiya R., Mitchell D.R.,
Takeda H.;
"Ktu/PF13 is required for cytoplasmic pre-assembly of axonemal
dyneins.";
Nature 456:611-616(2008).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-604, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Kidney, Lung, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[8]
INTERACTION WITH FOXP3.
PubMed=23973223; DOI=10.1016/j.immuni.2013.08.006;
Chen Z., Barbi J., Bu S., Yang H.Y., Li Z., Gao Y., Jinasena D.,
Fu J., Lin F., Chen C., Zhang J., Yu N., Li X., Shan Z., Nie J.,
Gao Z., Tian H., Li Y., Yao Z., Zheng Y., Park B.V., Pan Z., Zhang J.,
Dang E., Li Z., Wang H., Luo W., Li L., Semenza G.L., Zheng S.G.,
Loser K., Tsun A., Greene M.I., Pardoll D.M., Pan F., Li B.;
"The ubiquitin ligase Stub1 negatively modulates regulatory T cell
suppressive activity by promoting degradation of the transcription
factor Foxp3.";
Immunity 39:272-285(2013).
-!- FUNCTION: Molecular chaperone implicated in a wide variety of
cellular processes, including protection of the proteome from
stress, folding and transport of newly synthesized polypeptides,
activation of proteolysis of misfolded proteins and the formation
and dissociation of protein complexes. Plays a pivotal role in the
protein quality control system, ensuring the correct folding of
proteins, the re-folding of misfolded proteins and controlling the
targeting of proteins for subsequent degradation. This is achieved
through cycles of ATP binding, ATP hydrolysis and ADP release,
mediated by co-chaperones. The co-chaperones have been shown to
not only regulate different steps of the ATPase cycle, but they
also have an individual specificity such that one co-chaperone may
promote folding of a substrate while another may promote
degradation. The affinity for polypeptides is regulated by its
nucleotide bound state. In the ATP-bound form, it has a low
affinity for substrate proteins. However, upon hydrolysis of the
ATP to ADP, it undergoes a conformational change that increases
its affinity for substrate proteins. It goes through repeated
cycles of ATP hydrolysis and nucleotide exchange, which permits
cycles of substrate binding and release. The co-chaperones are of
three types: J-domain co-chaperones such as HSP40s (stimulate
ATPase hydrolysis by HSP70), the nucleotide exchange factors (NEF)
such as BAG1/2/3 (facilitate conversion of HSP70 from the ADP-
bound to the ATP-bound state thereby promoting substrate release),
and the TPR domain chaperones such as HOPX and STUB1. Maintains
protein homeostasis during cellular stress through two opposing
mechanisms: protein refolding and degradation. Its
acetylation/deacetylation state determines whether it functions in
protein refolding or protein degradation by controlling the
competitive binding of co-chaperones HOPX and STUB1. During the
early stress response, the acetylated form binds to HOPX which
assists in chaperone-mediated protein refolding, thereafter, it is
deacetylated and binds to ubiquitin ligase STUB1 that promotes
ubiquitin-mediated protein degradation. Regulates centrosome
integrity during mitosis, and is required for the maintenance of a
functional mitotic centrosome that supports the assembly of a
bipolar mitotic spindle. Enhances STUB1-mediated SMAD3
ubiquitination and degradation and facilitates STUB1-mediated
inhibition of TGF-beta signaling. Essential for STUB1-mediated
ubiquitination and degradation of FOXP3 in regulatory T-cells
(Treg) during inflammation. Negatively regulates heat shock-
induced HSF1 transcriptional activity during the attenuation and
recovery phase period of the heat shock response.
{ECO:0000250|UniProtKB:P0DMV8}.
-!- SUBUNIT: Component of the CatSper complex (By similarity).
Identified in a IGF2BP1-dependent mRNP granule complex containing
untranslated mRNAs (By similarity). Interacts with CHCHD3, DNAJC7,
IRAK1BP1, PPP5C and TSC2 (By similarity). Interacts with TERT; the
interaction occurs in the absence of the RNA component, TERC, and
dissociates once the TERT complex has formed (By similarity).
Interacts with METTL21A (By similarity). Interacts with DNAAF2
(PubMed:19052621). Interacts with TRIM5 (via B30.2/SPRY domain)
(By similarity). Interacts with PRKN (By similarity). Interacts
with FOXP3 (PubMed:23973223). Interacts with NOD2; the interaction
enhances NOD2 stability (By similarity). Interacts with DNAJC9
(via J domain) (By similarity). Interacts with ATF5; the
interaction protects ATF5 from degradation via proteasome-
dependent and caspase-dependent processes (By similarity).
Interacts with RNF207 (via the C-terminus); this interaction
additively increases KCNH2 expression (By similarity). Interacts
with HSF1 (via transactivation domain); this interaction results
in the inhibition of heat shock- and HSF1-induced transcriptional
activity during the attenuation and recovery phase period of the
heat shock response. Interacts with NAA10, HSP40, HSP90 and HDAC4.
The acetylated form and the non-acetylated form interact with HOPX
and STUB1 respectively. Interacts with NEDD1 and SMAD3. Interacts
(via NBD) with BAG1, BAG2, BAG3 and HSPH1/HSP105. Interacts with
DNAJC8 (By similarity). {ECO:0000250|UniProtKB:P0DMV8,
ECO:0000269|PubMed:19052621, ECO:0000269|PubMed:23973223}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0DMV8}.
Nucleus {ECO:0000250|UniProtKB:P0DMV8}. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome
{ECO:0000250|UniProtKB:P0DMV8}. Note=Localized in cytoplasmic mRNP
granules containing untranslated mRNAs.
{ECO:0000250|UniProtKB:P0DMV8}.
-!- DOMAIN: The N-terminal nucleotide binding domain (NBD) (also known
as the ATPase domain) is responsible for binding and hydrolyzing
ATP. The C-terminal substrate-binding domain (SBD) (also known as
peptide-binding domain) binds to the client/substrate proteins.
The two domains are allosterically coupled so that, when ATP is
bound to the NBD, the SBD binds relatively weakly to clients. When
ADP is bound in the NBD, a conformational change enhances the
affinity of the SBD for client proteins.
{ECO:0000250|UniProtKB:P0DMV8}.
-!- PTM: In response to cellular stress, acetylated at Lys-77 by NA110
and then gradually deacetylated by HDAC4 at later stages.
Acetylation enhances its chaperone activity and also determines
whether it will function as a chaperone for protein refolding or
degradation by controlling its binding to co-chaperones HOPX and
STUB1. The acetylated form and the non-acetylated form bind to
HOPX and STUB1 respectively. Acetylation also protects cells
against various types of cellular stress.
{ECO:0000250|UniProtKB:P0DMV8}.
-!- SIMILARITY: Belongs to the heat shock protein 70 family.
{ECO:0000305}.
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EMBL; M76613; AAA57233.1; -; Genomic_DNA.
EMBL; AF109906; AAC84169.1; -; Genomic_DNA.
EMBL; BC054782; AAH54782.1; -; mRNA.
EMBL; M12571; AAA57234.1; -; mRNA.
EMBL; M12572; AAA57235.1; -; mRNA.
CCDS; CCDS50080.1; -.
PIR; A26283; A26283.
RefSeq; NP_034609.2; NM_010479.2.
UniGene; Mm.6388; -.
ProteinModelPortal; Q61696; -.
SMR; Q61696; -.
BioGrid; 228756; 1.
CORUM; Q61696; -.
IntAct; Q61696; 5.
MINT; MINT-1866478; -.
STRING; 10090.ENSMUSP00000084586; -.
iPTMnet; Q61696; -.
PhosphoSitePlus; Q61696; -.
REPRODUCTION-2DPAGE; Q61696; -.
EPD; Q61696; -.
MaxQB; Q61696; -.
PaxDb; Q61696; -.
PRIDE; Q61696; -.
Ensembl; ENSMUST00000087328; ENSMUSP00000084586; ENSMUSG00000091971.
GeneID; 193740; -.
KEGG; mmu:193740; -.
UCSC; uc008cep.1; mouse.
CTD; 3303; -.
MGI; MGI:96244; Hspa1a.
eggNOG; KOG0101; Eukaryota.
eggNOG; COG0443; LUCA.
GeneTree; ENSGT00900000140908; -.
HOGENOM; HOG000228135; -.
HOVERGEN; HBG051845; -.
InParanoid; Q61696; -.
KO; K03283; -.
OMA; QLESYCF; -.
OrthoDB; EOG091G03SF; -.
PhylomeDB; Q61696; -.
TreeFam; TF105042; -.
PRO; PR:Q61696; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000091971; -.
CleanEx; MM_HSPA1A; -.
ExpressionAtlas; Q61696; baseline and differential.
Genevisible; Q61696; MM.
GO; GO:0016235; C:aggresome; ISO:MGI.
GO; GO:0072562; C:blood microparticle; ISO:MGI.
GO; GO:0005814; C:centriole; ISO:MGI.
GO; GO:0005813; C:centrosome; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005925; C:focal adhesion; ISO:MGI.
GO; GO:0016234; C:inclusion body; ISO:MGI.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; ISO:MGI.
GO; GO:0005739; C:mitochondrion; ISS:MGI.
GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
GO; GO:0043234; C:protein complex; ISO:MGI.
GO; GO:0031982; C:vesicle; ISO:MGI.
GO; GO:0005524; F:ATP binding; ISO:MGI.
GO; GO:0016887; F:ATPase activity; ISO:MGI.
GO; GO:0042623; F:ATPase activity, coupled; ISO:MGI.
GO; GO:0055131; F:C3HC4-type RING finger domain binding; ISO:MGI.
GO; GO:0045296; F:cadherin binding; ISO:MGI.
GO; GO:0031249; F:denatured protein binding; ISO:MGI.
GO; GO:0097718; F:disordered domain specific binding; ISO:MGI.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0001664; F:G-protein coupled receptor binding; ISO:MGI.
GO; GO:0031072; F:heat shock protein binding; ISO:MGI.
GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
GO; GO:0044183; F:protein binding involved in protein folding; ISO:MGI.
GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
GO; GO:0005102; F:receptor binding; ISO:MGI.
GO; GO:0003723; F:RNA binding; ISO:MGI.
GO; GO:0001106; F:RNA polymerase II transcription corepressor activity; ISS:UniProtKB.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:0051082; F:unfolded protein binding; ISO:MGI.
GO; GO:0006281; P:DNA repair; IMP:MGI.
GO; GO:0006402; P:mRNA catabolic process; ISS:UniProtKB.
GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; ISS:UniProtKB.
GO; GO:0097201; P:negative regulation of transcription from RNA polymerase II promoter in response to stress; ISS:UniProtKB.
GO; GO:0090063; P:positive regulation of microtubule nucleation; ISS:UniProtKB.
GO; GO:0042026; P:protein refolding; ISS:UniProtKB.
GO; GO:1901673; P:regulation of mitotic spindle assembly; ISS:UniProtKB.
GO; GO:0009408; P:response to heat; IDA:MGI.
GO; GO:0006986; P:response to unfolded protein; ISS:UniProtKB.
GO; GO:0000723; P:telomere maintenance; IMP:MGI.
Gene3D; 1.20.1270.10; -; 1.
Gene3D; 2.60.34.10; -; 1.
InterPro; IPR018181; Heat_shock_70_CS.
InterPro; IPR029048; HSP70_C_sf.
InterPro; IPR029047; HSP70_peptide-bd_sf.
InterPro; IPR013126; Hsp_70_fam.
Pfam; PF00012; HSP70; 1.
PRINTS; PR00301; HEATSHOCK70.
SUPFAM; SSF100920; SSF100920; 1.
SUPFAM; SSF100934; SSF100934; 1.
PROSITE; PS00297; HSP70_1; 1.
PROSITE; PS00329; HSP70_2; 1.
PROSITE; PS01036; HSP70_3; 1.
1: Evidence at protein level;
Acetylation; ATP-binding; Chaperone; Complete proteome; Cytoplasm;
Cytoskeleton; Direct protein sequencing; Methylation;
Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
Stress response.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P0DMV8}.
CHAIN 2 641 Heat shock 70 kDa protein 1A.
/FTId=PRO_0000078250.
NP_BIND 12 15 ATP. {ECO:0000250}.
NP_BIND 202 204 ATP. {ECO:0000250}.
NP_BIND 268 275 ATP. {ECO:0000250}.
NP_BIND 339 342 ATP. {ECO:0000250}.
REGION 2 386 Nucleotide-binding domain (NBD).
{ECO:0000250|UniProtKB:P11142}.
REGION 394 509 Substrate-binding domain (SBD).
{ECO:0000250|UniProtKB:P11142}.
BINDING 71 71 ATP. {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:P0DMV8}.
MOD_RES 77 77 N6-acetyllysine.
{ECO:0000250|UniProtKB:P0DMV8}.
MOD_RES 108 108 N6-acetyllysine.
{ECO:0000250|UniProtKB:P0DMV8}.
MOD_RES 246 246 N6-acetyllysine.
{ECO:0000250|UniProtKB:P0DMV8}.
MOD_RES 348 348 N6-acetyllysine.
{ECO:0000250|UniProtKB:P0DMV8}.
MOD_RES 469 469 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P0DMV8}.
MOD_RES 561 561 N6,N6,N6-trimethyllysine; by METTL21A;
alternate.
{ECO:0000250|UniProtKB:P0DMV8}.
MOD_RES 561 561 N6,N6-dimethyllysine; alternate.
{ECO:0000250|UniProtKB:P0DMV8}.
MOD_RES 604 604 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 631 631 Phosphoserine.
{ECO:0000250|UniProtKB:P0DMV8}.
MOD_RES 633 633 Phosphoserine.
{ECO:0000250|UniProtKB:P0DMV8}.
MOD_RES 636 636 Phosphothreonine.
{ECO:0000250|UniProtKB:P0DMV8}.
CONFLICT 221 225 ATAGD -> TDGRT (in Ref. 5; AAA57234).
{ECO:0000305}.
CONFLICT 229 229 G -> E (in Ref. 5; AAA57234).
{ECO:0000305}.
CONFLICT 233 233 F -> V (in Ref. 5; AAA57234).
{ECO:0000305}.
CONFLICT 238 244 VSHFVEE -> EDLREQ (in Ref. 5; AAA57234).
{ECO:0000305}.
CONFLICT 295 295 T -> R (in Ref. 5; AAA57234).
{ECO:0000305}.
CONFLICT 332 332 H -> Q (in Ref. 5; AAA57234).
{ECO:0000305}.
CONFLICT 342 342 R -> A (in Ref. 1; AAA57233).
{ECO:0000305}.
CONFLICT 409 409 V -> G (in Ref. 5; AAA57235).
{ECO:0000305}.
CONFLICT 413 416 LIKR -> RHQA (in Ref. 5; AAA57234/
AAA57235). {ECO:0000305}.
CONFLICT 494 494 S -> T (in Ref. 3; AAH54782).
{ECO:0000305}.
SEQUENCE 641 AA; 70079 MW; F49C33E602EAE334 CRC64;
MAKNTAIGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL IGDAAKNQVA
LNPQNTVFDA KRLIGRKFGD AVVQSDMKHW PFQVVNDGDK PKVQVNYKGE SRSFFPEEIS
SMVLTKMKEI AEAYLGHPVT NAVITVPAYF NDSQRQATKD AGVIAGLNVL RIINEPTAAA
IAYGLDRTGK GERNVLIFDL GGGTFDVSIL TIDDGIFEVK ATAGDTHLGG EDFDNRLVSH
FVEEFKRKHK KDISQNKRAV RRLRTACERA KRTLSSSTQA SLEIDSLFEG IDFYTSITRA
RFEELCSDLF RGTLEPVEKA LRDAKMDKAQ IHDLVLVGGS TRIPKVQKLL QDFFNGRDLN
KSINPDEAVA YGAAVQAAIL MGDKSENVQD LLLLDVAPLS LGLETAGGVM TALIKRNSTI
PTKQTQTFTT YSDNQPGVLI QVYEGERAMT RDNNLLGRFE LSGIPPAPRG VPQIEVTFDI
DANGILNVTA TDKSTGKANK ITITNDKGRL SKEEIERMVQ EAERYKAEDE VQRDRVAAKN
ALESYAFNMK SAVEDEGLKG KLSEADKKKV LDKCQEVISW LDSNTLADKE EFVHKREELE
RVCSPIISGL YQGAGAPGAG GFGAQAPKGA SGSGPTIEEV D


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