Skip Header

Contribute Send feedback
Read comments (?) or add your own

P83581 (HS74L_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Heat shock 70 kDa protein 4L
Alternative name(s):
Heat shock 70-related protein APG-1
Osmotic stress protein 94
Gene names
Name:Hspa4l
Synonyms:Apg1, Hsp4l, Osp94
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length24 AA.
Sequence statusFragments.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Possesses chaperone activity in vitro where it inhibits aggregation of citrate synthase. Ref.1

Subunit structure

Homodimer. In the testis, forms a complex with p53 at 32.5 degrees Celsius which is scrotal temperature but not at 37 or 42 degrees Celsius. Ref.2 Ref.4

Subcellular location

Cytoplasm. Nucleus. Note: May translocate to the nucleus of germ cells after heat shock. Ref.1 Ref.4

Tissue specificity

Expressed at high levels in testis and at much lower levels in brain. In testis, expressed mainly in germ cells. Widespread in brain with highest expression in cerebellum and medulla oblongata. Also expressed in renal medulla of water-restricted animals. Ref.1 Ref.2 Ref.4

Developmental stage

Expression is first detected in the testis 5 weeks after birth and coincides with the appearance of spermatozoa. In the brain, expression is first detected 3.5 days after birth. Ref.1 Ref.3

Induction

By heat shock. Ref.4

Sequence similarities

Belongs to the heat shock protein 70 family.

Ontologies

Keywords
   Biological processStress response
   Cellular componentCytoplasm
Nucleus
   LigandATP-binding
Nucleotide-binding
   Molecular functionChaperone
   PTMPhosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processprotein folding

Inferred from direct assay Ref.1. Source: UniProtKB

response to unfolded protein

Inferred from direct assay Ref.1. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay Ref.1. Source: UniProtKB

nucleus

Inferred from direct assay Ref.4. Source: UniProtKB

   Molecular_functionATP binding

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›24›24Heat shock 70 kDa protein 4L
PRO_0000078282

Amino acid modifications

Modified residue191Phosphothreonine By similarity

Experimental info

Non-adjacent residues15 – 162
Non-terminal residue241

Sequences

Sequence LengthMass (Da)Tools
P83581 [UniParc].

Last modified May 23, 2003. Version 1.
Checksum: 62B092E031786E9F

FASTA242,796
        10         20 
LSAMLEDTEN WLYEELSLTQ DPVV 

« Hide

References

[1]"Characterization of the 105-kDa molecular chaperone. Identification, biochemical properties, and localization."
Matsumori M., Itoh H., Toyoshima I., Komatsuda A., Sawada K., Fukuda J., Tanaka T., Okubo A., Kinouchi H., Mizoi K., Hama T., Suzuki A., Hamada F., Otaka M., Shoji Y., Takada G.
Eur. J. Biochem. 269:5632-5641(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Tissue: Testis.
[2]"A novel testis-specific 105-kDa protein related to the 90-kDa heat-shock protein."
Itoh H., Tashima Y.
Eur. J. Biochem. 193:429-435(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, TISSUE SPECIFICITY.
[3]"Different expression time of the 105-kDa protein and 90-kDa heat-shock protein in rat testis."
Itoh H., Tashima Y.
FEBS Lett. 289:110-112(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE.
[4]"Germ cell-specific heat shock protein 105 binds to p53 in a temperature-sensitive manner in rat testis."
Kumagai J., Fukuda J., Kodama H., Murata M., Kawamura K., Itoh H., Tanaka T.
Eur. J. Biochem. 267:3073-3078(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, FORMATION OF COMPLEX WITH P53.
Strain: Wistar.
Tissue: Testis.

Cross-references

Sequence databases

IPIIPI00337270.
UniGeneRn.144829.

3D structure databases

ModBaseSearch...

PTM databases

PhosphoSiteP83581.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCRGD:1306528. rat.

Organism-specific databases

RGD1306528. Hspa4l.

Gene expression databases

GenevestigatorP83581.

Family and domain databases

PROSITEPS00297. HSP70_1. Partial match.
PS00329. HSP70_2. Partial match.
PS01036. HSP70_3. Partial match.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHS74L_RAT
AccessionPrimary (citable) accession number: P83581
Entry history
Integrated into UniProtKB/Swiss-Prot: May 23, 2003
Last sequence update: May 23, 2003
Last modified: April 3, 2013
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families