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Protein

Heat shock 70 kDa protein 1-like

Gene

Hspa1l

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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 PARK2 translocation to damaged mitochondria.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei73ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi14 – 17ATPBy similarity4
Nucleotide bindingi204 – 206ATPBy similarity3
Nucleotide bindingi270 – 277ATPBy similarity8
Nucleotide bindingi341 – 344ATPBy similarity4

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionChaperone
Biological processStress response
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-RNO-3371571. HSF1-dependent transactivation.

Names & Taxonomyi

Protein namesi
Recommended name:
Heat shock 70 kDa protein 1-like
Short name:
Heat shock 70 kDa protein 1L
Alternative name(s):
Heat shock 70 kDa protein 3
Short name:
HSP70.3
Gene namesi
Name:Hspa1l
Synonyms:Hsp70-3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 20

Organism-specific databases

RGDi1595925. Hspa1l.

Subcellular locationi

GO - Cellular componenti

  • blood microparticle Source: Ensembl
  • cell body Source: Ensembl
  • COP9 signalosome Source: Ensembl
  • cytosol Source: Ensembl
  • mitochondrial matrix Source: MGI
  • mitochondrion Source: MGI
  • zona pellucida receptor complex Source: Ensembl

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000782571 – 641Heat shock 70 kDa protein 1-likeAdd BLAST641

Proteomic databases

PaxDbiP55063.
PRIDEiP55063.

PTM databases

iPTMnetiP55063.
PhosphoSitePlusiP55063.

Expressioni

Inductioni

By heat shock.

Gene expression databases

BgeeiENSRNOG00000047966.
GenevisibleiP55063. RN.

Interactioni

Subunit structurei

Interacts with PARK2.By similarity

Protein-protein interaction databases

IntActiP55063. 2 interactors.
MINTiMINT-7138508.
STRINGi10116.ENSRNOP00000063974.

Structurei

3D structure databases

ProteinModelPortaliP55063.
SMRiP55063.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni3 – 388Nucleotide-binding domain (NBD)By similarityAdd BLAST386
Regioni396 – 511Substrate-binding domain (SBD)By similarityAdd BLAST116

Domaini

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.By similarity

Sequence similaritiesi

Belongs to the heat shock protein 70 family.Curated

Phylogenomic databases

eggNOGiKOG0101. Eukaryota.
COG0443. LUCA.
GeneTreeiENSGT00870000136409.
HOVERGENiHBG051845.
InParanoidiP55063.
KOiK03283.
OMAiKELENMC.
OrthoDBiEOG091G03SF.
PhylomeDBiP55063.

Family and domain databases

Gene3Di1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
InterProiView protein in InterPro
IPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
PfamiView protein in Pfam
PF00012. HSP70. 1 hit.
PRINTSiPR00301. HEATSHOCK70.
SUPFAMiSSF100920. SSF100920. 1 hit.
SSF100934. SSF100934. 1 hit.
PROSITEiView protein in PROSITE
PS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.

Sequencei

Sequence statusi: Complete.

P55063-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAANKGMAIG IDLGTTYSCV GVFQHGKVEI IANDQGNRTT PSYVAFTDTE
60 70 80 90 100
RLIGDAAKNQ VAMNPQNTVF DAKRLIGRKF NDPVVQSDMK LWPFQVINEA
110 120 130 140 150
GKPKVLVSYK GEKKAFYPEE ISSMVLTKMK ETAEAFLGHS VTNAVITVPA
160 170 180 190 200
YFNDSQRQAT KDAGVIAGLN VLRIINEPTA AAIAYGLDKG SHGERHVLIF
210 220 230 240 250
DLGGGTFDVS ILTIDDGIFE VKATAGDTHL GGEDFDNRLV SHFVEEFKRK
260 270 280 290 300
HKKDISQNKR AVRRLRTACE RAKRTLSSST QANLEIDSLY EGIDFYTSIT
310 320 330 340 350
RARFEELCAD LFRGTLEPVE KSLRDAKMDK AKIHDIVLVG GSTRIPKVQK
360 370 380 390 400
LLQDYFNGRD LNKSINPDEA VAYGAAVQAA ILMGDKSEKV QDLLLLDVAP
410 420 430 440 450
LSLGLETAGG VMTVLIKRNS TIPTKQTQIF TTYSDNQPGV LIQVYEGERA
460 470 480 490 500
MTRDNNLLGR FDLTGIPPAP RGVPQIEVTF DIDANGILNV TAMDKSTGKA
510 520 530 540 550
NKITITNDKG RLSKEEIERM VQEAERYKAE DEGQREKIAA KNALESYAFN
560 570 580 590 600
MKSAVGDEGL KDKISESDKK KILDKCSEVL SWLEANQLAE KEEFDHKRKE
610 620 630 640
LENMCNPIIT KLYQSGCTGP TCAPGYTPGR AATGPTIEEV D
Length:641
Mass (Da):70,549
Last modified:December 21, 2004 - v2
Checksum:iC9FAE59B4685DD51
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti266R → A in CAA54424 (PubMed:7927536).Curated1
Sequence conflicti632A → R in CAA54424 (PubMed:7927536).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X77209 Genomic DNA. Translation: CAA54424.1.
BX883045 Genomic DNA. Translation: CAE83979.1.
BC108294 mRNA. Translation: AAI08295.1.
BC108297 mRNA. Translation: AAI08298.1.
PIRiS41415.
RefSeqiNP_997711.1. NM_212546.4.
XP_017457033.1. XM_017601544.1.
UniGeneiRn.187184.

Genome annotation databases

EnsembliENSRNOT00000074223; ENSRNOP00000063974; ENSRNOG00000047966.
GeneIDi24963.
KEGGirno:24963.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X77209 Genomic DNA. Translation: CAA54424.1.
BX883045 Genomic DNA. Translation: CAE83979.1.
BC108294 mRNA. Translation: AAI08295.1.
BC108297 mRNA. Translation: AAI08298.1.
PIRiS41415.
RefSeqiNP_997711.1. NM_212546.4.
XP_017457033.1. XM_017601544.1.
UniGeneiRn.187184.

3D structure databases

ProteinModelPortaliP55063.
SMRiP55063.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP55063. 2 interactors.
MINTiMINT-7138508.
STRINGi10116.ENSRNOP00000063974.

PTM databases

iPTMnetiP55063.
PhosphoSitePlusiP55063.

Proteomic databases

PaxDbiP55063.
PRIDEiP55063.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000074223; ENSRNOP00000063974; ENSRNOG00000047966.
GeneIDi24963.
KEGGirno:24963.

Organism-specific databases

CTDi3305.
RGDi1595925. Hspa1l.

Phylogenomic databases

eggNOGiKOG0101. Eukaryota.
COG0443. LUCA.
GeneTreeiENSGT00870000136409.
HOVERGENiHBG051845.
InParanoidiP55063.
KOiK03283.
OMAiKELENMC.
OrthoDBiEOG091G03SF.
PhylomeDBiP55063.

Enzyme and pathway databases

ReactomeiR-RNO-3371571. HSF1-dependent transactivation.

Miscellaneous databases

PROiP55063.

Gene expression databases

BgeeiENSRNOG00000047966.
GenevisibleiP55063. RN.

Family and domain databases

Gene3Di1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
InterProiView protein in InterPro
IPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
PfamiView protein in Pfam
PF00012. HSP70. 1 hit.
PRINTSiPR00301. HEATSHOCK70.
SUPFAMiSSF100920. SSF100920. 1 hit.
SSF100934. SSF100934. 1 hit.
PROSITEiView protein in PROSITE
PS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiHS71L_RAT
AccessioniPrimary (citable) accession number: P55063
Secondary accession number(s): Q32P36, Q6MG67
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: December 21, 2004
Last modified: March 15, 2017
This is version 108 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.