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Heat shock 70 kDa protein 1A (Heat shock 70 kDa protein 2) (HSP70-2) (HSP70.2)

 HS71A_RAT               Reviewed;         641 AA.
P0DMW0; P42853; Q07439; Q63256;
27-MAY-2015, integrated into UniProtKB/Swiss-Prot.
27-MAY-2015, sequence version 1.
22-NOV-2017, entry version 25.
RecName: Full=Heat shock 70 kDa protein 1A;
AltName: Full=Heat shock 70 kDa protein 2;
Short=HSP70-2;
Short=HSP70.2;
Name=Hspa1a; Synonyms=Hsp70-1, Hspa1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=LEW.1W/GUN;
PubMed=7927536; DOI=10.1007/BF01246673;
Walter L., Rauh F., Guenther E.;
"Comparative analysis of the three major histocompatibility complex-
linked heat shock protein 70 (Hsp70) genes of the rat.";
Immunogenetics 40:325-330(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
PubMed=15060004; DOI=10.1101/gr.1987704;
Hurt P., Walter L., Sudbrak R., Klages S., Mueller I., Shiina T.,
Inoko H., Lehrach H., Guenther E., Reinhardt R., Himmelbauer H.;
"The genomic sequence and comparative analysis of the rat major
histocompatibility complex.";
Genome Res. 14:631-639(2004).
-!- 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. Identified in a
IGF2BP1-dependent mRNP granule complex containing untranslated
mRNAs. Interacts with CHCHD3, DNAJC7, IRAK1BP1, PPP5C and TSC2.
Interacts with TERT; the interaction occurs in the absence of the
RNA component, TERC, and dissociates once the TERT complex has
formed. Interacts with METTL21A. Interacts with DNAAF2. Interacts
with TRIM5 (via B30.2/SPRY domain). Interacts with PRKN. Interacts
with FOXP3. Interacts with NOD2; the interaction enhances NOD2
stability. Interacts with DNAJC9 (via J domain). Interacts with
ATF5; the interaction protects ATF5 from degradation via
proteasome-dependent and caspase-dependent processes. Interacts
with RNF207 (via the C-terminus); this interaction additively
increases KCNH2 expression. 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. {ECO:0000250|UniProtKB:P0DMV8,
ECO:0000250|UniProtKB:Q61696}.
-!- 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}.
-!- INDUCTION: By heat shock.
-!- 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; X77208; CAA54423.1; -; Genomic_DNA.
EMBL; BX883045; CAE83978.1; -; Genomic_DNA.
PIR; I54542; I54542.
RefSeq; NP_114177.2; NM_031971.2.
RefSeq; NP_997669.1; NM_212504.1.
RefSeq; XP_017457331.1; XM_017601842.1.
UniGene; Rn.1950; -.
UniGene; Rn.228581; -.
ProteinModelPortal; P0DMW0; -.
SMR; P0DMW0; -.
CORUM; P0DMW0; -.
MINT; MINT-240978; -.
STRING; 10116.ENSRNOP00000067749; -.
Ensembl; ENSRNOT00000049667; ENSRNOP00000050605; ENSRNOG00000045654.
Ensembl; ENSRNOT00000061950; ENSRNOP00000067749; ENSRNOG00000045654.
Ensembl; ENSRNOT00000081924; ENSRNOP00000075599; ENSRNOG00000050647.
GeneID; 108348108; -.
GeneID; 24472; -.
GeneID; 294254; -.
KEGG; rno:24472; -.
KEGG; rno:294254; -.
CTD; 3303; -.
CTD; 3304; -.
RGD; 1593284; Hspa1a.
HOGENOM; HOG000228135; -.
HOVERGEN; HBG051845; -.
KO; K03283; -.
OMA; VDWLDHN; -.
PhylomeDB; P0DMW0; -.
Reactome; R-RNO-3371453; Regulation of HSF1-mediated heat shock response.
Reactome; R-RNO-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR).
Reactome; R-RNO-3371568; Attenuation phase.
Reactome; R-RNO-3371571; HSF1-dependent transactivation.
Reactome; R-RNO-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
Reactome; R-RNO-6798695; Neutrophil degranulation.
PRO; PR:P0DMW0; -.
Proteomes; UP000002494; Chromosome 20.
Bgee; ENSRNOG00000045654; -.
ExpressionAtlas; P0DMW0; baseline and differential.
GO; GO:0016235; C:aggresome; ISO:RGD.
GO; GO:0072562; C:blood microparticle; ISO:RGD.
GO; GO:0005814; C:centriole; ISO:RGD.
GO; GO:0005813; C:centrosome; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; ISO:RGD.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0005925; C:focal adhesion; ISO:RGD.
GO; GO:0016234; C:inclusion body; ISO:RGD.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; ISO:RGD.
GO; GO:0045121; C:membrane raft; IDA:CAFA.
GO; GO:0005739; C:mitochondrion; IEA:GOC.
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:RGD.
GO; GO:0031982; C:vesicle; ISO:RGD.
GO; GO:0005524; F:ATP binding; ISO:RGD.
GO; GO:0016887; F:ATPase activity; ISO:RGD.
GO; GO:0042623; F:ATPase activity, coupled; ISO:RGD.
GO; GO:0055131; F:C3HC4-type RING finger domain binding; ISO:RGD.
GO; GO:0045296; F:cadherin binding; ISO:RGD.
GO; GO:0031249; F:denatured protein binding; ISO:RGD.
GO; GO:0097718; F:disordered domain specific binding; ISO:RGD.
GO; GO:0019899; F:enzyme binding; ISO:RGD.
GO; GO:0001664; F:G-protein coupled receptor binding; ISO:RGD.
GO; GO:0031072; F:heat shock protein binding; ISO:RGD.
GO; GO:0042826; F:histone deacetylase binding; ISO:RGD.
GO; GO:0044183; F:protein binding involved in protein folding; ISO:RGD.
GO; GO:0047485; F:protein N-terminus binding; ISO:RGD.
GO; GO:0005102; F:receptor binding; ISO:RGD.
GO; GO:0003723; F:RNA binding; ISO:RGD.
GO; GO:0001106; F:RNA polymerase II transcription corepressor activity; ISS:UniProtKB.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
GO; GO:0051082; F:unfolded protein binding; ISO:RGD.
GO; GO:0046034; P:ATP metabolic process; ISO:RGD.
GO; GO:0070370; P:cellular heat acclimation; ISO:RGD.
GO; GO:0034605; P:cellular response to heat; ISO:RGD.
GO; GO:0051131; P:chaperone-mediated protein complex assembly; ISO:RGD.
GO; GO:0006281; P:DNA repair; ISO:RGD.
GO; GO:0006402; P:mRNA catabolic process; ISS:UniProtKB.
GO; GO:0060548; P:negative regulation of cell death; IDA:RGD.
GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; ISS:UniProtKB.
GO; GO:1902236; P:negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; ISO:RGD.
GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; ISO:RGD.
GO; GO:0090084; P:negative regulation of inclusion body assembly; ISO:RGD.
GO; GO:1901029; P:negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; ISO:RGD.
GO; GO:0031397; P:negative regulation of protein ubiquitination; ISO:RGD.
GO; GO:0097201; P:negative regulation of transcription from RNA polymerase II promoter in response to stress; ISS:UniProtKB.
GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; ISO:RGD.
GO; GO:0030182; P:neuron differentiation; IEP:RGD.
GO; GO:1902380; P:positive regulation of endoribonuclease activity; ISO:RGD.
GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
GO; GO:0032757; P:positive regulation of interleukin-8 production; ISO:RGD.
GO; GO:0090063; P:positive regulation of microtubule nucleation; ISS:UniProtKB.
GO; GO:1904722; P:positive regulation of mRNA endonucleolytic cleavage involved in unfolded protein response; ISO:RGD.
GO; GO:0045666; P:positive regulation of neuron differentiation; IMP:RGD.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:RGD.
GO; GO:0070434; P:positive regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway; ISO:RGD.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISO:RGD.
GO; GO:1903265; P:positive regulation of tumor necrosis factor-mediated signaling pathway; ISO:RGD.
GO; GO:0042026; P:protein refolding; ISS:UniProtKB.
GO; GO:0050821; P:protein stabilization; ISO:RGD.
GO; GO:1901673; P:regulation of mitotic spindle assembly; ISS:UniProtKB.
GO; GO:0031396; P:regulation of protein ubiquitination; ISO:RGD.
GO; GO:0045471; P:response to ethanol; IEP:RGD.
GO; GO:0009408; P:response to heat; ISO:RGD.
GO; GO:0002931; P:response to ischemia; IEP:RGD.
GO; GO:0009612; P:response to mechanical stimulus; IEP:RGD.
GO; GO:0009314; P:response to radiation; IEP:RGD.
GO; GO:0006986; P:response to unfolded protein; IMP:RGD.
GO; GO:0000723; P:telomere maintenance; ISO:RGD.
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.
2: Evidence at transcript level;
Acetylation; ATP-binding; Chaperone; Complete proteome; Cytoplasm;
Cytoskeleton; 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_0000078254.
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 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}.
SEQUENCE 641 AA; 70185 MW; 2D745B1013F64E7B CRC64;
MAKKTAIGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL IGDAAKNQVA
LNPQNTVFDA KRLIGRKFGD PVVQSDMKHW PFQVVNDGDK PKVQVNYKGE NRSFYPEEIS
SMVLTKMKEI AEAYLGHPVT NAVITVPAYF NDSQRQATKD AGVIAGLNVL RIINEPTAAA
IAYGLDRTGK GERNVLIFDL GGGTFDVSIL TIDDGIFEVK ATAGDTHLGG EDFDNRLVSH
FVEEFKRKHK KDISQNKRAV RRLRTACERA KRTLSSSTQA SLEIDSLFEG IDFYTSITRA
RFEELCSDLF RGTLEPVEKA LRDAKLDKAQ IHDLVLVGGS TRIPKVQKLL QDFFNGRDLN
KSINPDEAVA YGAAVQAAIL MGDKSENVQD LLLLDVAPLS LGLETAGGVM TALIKRNSTI
PTKQTQTFTT YSDNQPGVLI QVYEGERAMT RDNNLLGRFE LSGIPPAPRG VPQIEVTFDI
DANGILNVTA TDKSTGKANK ITITNDKGRL SKEEIERMVQ EAERYKAEDE VQRERVAAKN
ALESYAFNMK SAVEDEGLKG KISEADKKKV LDKCQEVISW LDSNTLAEKE EFVHKREELE
RVCNPIISGL YQGAGAPGAG GFGAQAPKGG SGSGPTIEEV D


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