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Heat shock 70 kDa protein 1-like (Heat shock 70 kDa protein 1L) (Heat shock 70 kDa protein 3) (HSP70.3)

 HS71L_RAT               Reviewed;         641 AA.
P55063; Q32P36; Q6MG67;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
21-DEC-2004, sequence version 2.
23-MAY-2018, entry version 116.
RecName: Full=Heat shock 70 kDa protein 1-like;
Short=Heat shock 70 kDa protein 1L;
AltName: Full=Heat shock 70 kDa protein 3;
Short=HSP70.3;
Name=Hspa1l; Synonyms=Hsp70-3;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
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).
-!- 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 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. Positive
regulator of PRKN translocation to damaged mitochondria.
{ECO:0000250|UniProtKB:P34931}.
-!- SUBUNIT: Interacts with PRKN. {ECO:0000250|UniProtKB:P34931}.
-!- 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:P34931}.
-!- SIMILARITY: Belongs to the heat shock protein 70 family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X77209; CAA54424.1; -; Genomic_DNA.
EMBL; BX883045; CAE83979.1; -; Genomic_DNA.
EMBL; BC108294; AAI08295.1; -; mRNA.
EMBL; BC108297; AAI08298.1; -; mRNA.
PIR; S41415; S41415.
RefSeq; NP_997711.1; NM_212546.4.
RefSeq; XP_017457033.1; XM_017601544.1.
UniGene; Rn.187184; -.
ProteinModelPortal; P55063; -.
SMR; P55063; -.
IntAct; P55063; 2.
MINT; P55063; -.
STRING; 10116.ENSRNOP00000063974; -.
iPTMnet; P55063; -.
PhosphoSitePlus; P55063; -.
PaxDb; P55063; -.
PRIDE; P55063; -.
Ensembl; ENSRNOT00000074223; ENSRNOP00000063974; ENSRNOG00000047966.
GeneID; 24963; -.
KEGG; rno:24963; -.
CTD; 3305; -.
RGD; 1595925; Hspa1l.
eggNOG; KOG0101; Eukaryota.
eggNOG; COG0443; LUCA.
GeneTree; ENSGT00910000144045; -.
HOVERGEN; HBG051845; -.
InParanoid; P55063; -.
KO; K03283; -.
OMA; GEKKAFY; -.
OrthoDB; EOG091G03SF; -.
PhylomeDB; P55063; -.
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.
PRO; PR:P55063; -.
Proteomes; UP000002494; Chromosome 20.
Bgee; ENSRNOG00000047966; -.
Genevisible; P55063; RN.
GO; GO:0044297; C:cell body; IEA:Ensembl.
GO; GO:0005759; C:mitochondrial matrix; IDA:MGI.
GO; GO:0005739; C:mitochondrion; IDA:MGI.
GO; GO:0002199; C:zona pellucida receptor complex; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0007339; P:binding of sperm to zona pellucida; IEA:Ensembl.
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.
PANTHER; PTHR19375; PTHR19375; 1.
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;
ATP-binding; Chaperone; Complete proteome; Nucleotide-binding;
Reference proteome; Stress response.
CHAIN 1 641 Heat shock 70 kDa protein 1-like.
/FTId=PRO_0000078257.
NP_BIND 14 17 ATP. {ECO:0000250}.
NP_BIND 204 206 ATP. {ECO:0000250}.
NP_BIND 270 277 ATP. {ECO:0000250}.
NP_BIND 341 344 ATP. {ECO:0000250}.
REGION 3 388 Nucleotide-binding domain (NBD).
{ECO:0000250|UniProtKB:P11142}.
REGION 396 511 Substrate-binding domain (SBD).
{ECO:0000250|UniProtKB:P11142}.
BINDING 73 73 ATP. {ECO:0000250}.
CONFLICT 266 266 R -> A (in Ref. 1; CAA54424).
{ECO:0000305}.
CONFLICT 632 632 A -> R (in Ref. 1; CAA54424).
{ECO:0000305}.
SEQUENCE 641 AA; 70549 MW; C9FAE59B4685DD51 CRC64;
MAANKGMAIG IDLGTTYSCV GVFQHGKVEI IANDQGNRTT PSYVAFTDTE RLIGDAAKNQ
VAMNPQNTVF DAKRLIGRKF NDPVVQSDMK LWPFQVINEA GKPKVLVSYK GEKKAFYPEE
ISSMVLTKMK ETAEAFLGHS VTNAVITVPA YFNDSQRQAT KDAGVIAGLN VLRIINEPTA
AAIAYGLDKG SHGERHVLIF DLGGGTFDVS ILTIDDGIFE VKATAGDTHL GGEDFDNRLV
SHFVEEFKRK HKKDISQNKR AVRRLRTACE RAKRTLSSST QANLEIDSLY EGIDFYTSIT
RARFEELCAD LFRGTLEPVE KSLRDAKMDK AKIHDIVLVG GSTRIPKVQK LLQDYFNGRD
LNKSINPDEA VAYGAAVQAA ILMGDKSEKV QDLLLLDVAP LSLGLETAGG VMTVLIKRNS
TIPTKQTQIF TTYSDNQPGV LIQVYEGERA MTRDNNLLGR FDLTGIPPAP RGVPQIEVTF
DIDANGILNV TAMDKSTGKA NKITITNDKG RLSKEEIERM VQEAERYKAE DEGQREKIAA
KNALESYAFN MKSAVGDEGL KDKISESDKK KILDKCSEVL SWLEANQLAE KEEFDHKRKE
LENMCNPIIT KLYQSGCTGP TCAPGYTPGR AATGPTIEEV D


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