Search Results

Overview

Uniprot IDA0A8W4FMW6
Protein Name60 kDa heat shock protein, mitochondrial
Gene NameHSPD1
OrganismSus scrofa

Kla Sites from experimental identification

Position Flanking peptide
125 VLARSIAKEGFEKIS
130 IAKEGFEKISKGANP
133 EGFEKISKGANPVEI
159 YVLLSEKKISSVQSI
201 TLVLNRLKVGLQVVA
210 GLQVVAVKAPGFGDN
268 KDDAMLLKGKGDKAQ
273 LLKGKGDKAQIEKRI
305 KLNERLAKLSDGVAV
31 RAYAKDVKFGADARA
326 SDVEVNEKKDRVTDA
378 KIGLEIIKKALKIPA
382 EIIKKALKIPAMTIA
432 KGIIDPTKVVRTALL
72 EQSWGSPKVTKDGVT
75 WGSPKVTKDGVTVAK
91 IDLKDKYKNIGAKLV

Function

Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein

Protein Sequence

10 MLRLPAVLRQ 20 IRPVSRALAP 30 HLTRAYAKDV 40 KFGADARALM 50 LQGVDLLADA 60 VAVTMGPKGR 70 TVIIEQSWGS 80 PKVTKDGVTV 90 AKSIDLKDKY 100 KNIGAKLVQD 110 VANNTNEEAG 120 DGTTTATVLA 130 RSIAKEGFEK 140 ISKGANPVEI 150 RRGQKCEFQD 160 AYVLLSEKKI 170 SSVQSIVPAL 180 EIANAHRKPL 190 VIIAEDVDGE 200 ALSTLVLNRL 210 KVGLQVVAVK 220 APGFGDNRKN 230 QLKDMAIATG 240 GAVFGEEGLT 250 LNLEDVQPHD 260 LGKVGEVIVT 270 KDDAMLLKGK 280 GDKAQIEKRI 290 QEIIEQLDVT 300 TSEYEKEKLN 310 ERLAKLSDGV 320 AVLKVGGTSD 330 VEVNEKKDRV 340 TDALNATRAA 350 VEEGIVLGGG 360 CALLRCIPAL 370 ESITPANEDQ 380 KIGLEIIKKA 390 LKIPAMTIAK 400 NAGVEGSLIV 410 EKILQSSPEV 420 GYDAMLGDFV 430 NMVEKGIIDP 440 TKVVRTALLD 450 AAGVASLLTT 460 AEVVVTEIPK 470 EEKDPGMGGM 480 GGMGGGMGGG MF

Gene Ontology

Classification GO ID Description
Cellular Component GO:0009986 cell surface
Cellular Component GO:0005832 chaperonin-containing T-complex
Cellular Component GO:0005905 clathrin-coated pit
Cellular Component GO:0030135 coated vesicle
Cellular Component GO:0005769 early endosome
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0046696 lipopolysaccharide receptor complex
Cellular Component GO:0140494 migrasome
Cellular Component GO:0005743 mitochondrial inner membrane
Cellular Component GO:0005759 mitochondrial matrix
Cellular Component GO:0005886 plasma membrane
Cellular Component GO:0030141 secretory granule
Cellular Component GO:0097225 sperm midpiece
Molecular Function GO:0034186 apolipoprotein A-I binding
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0140662 ATP-dependent protein folding chaperone
Molecular Function GO:0140608 cysteine-type endopeptidase activator activity
Molecular Function GO:0003725 double-stranded RNA binding
Molecular Function GO:0008035 high-density lipoprotein particle binding
Molecular Function GO:0001530 lipopolysaccharide binding
Molecular Function GO:0002039 p53 binding
Molecular Function GO:0051087 protein-folding chaperone binding
Molecular Function GO:0031625 ubiquitin protein ligase binding
Biological Process GO:0008637 apoptotic mitochondrial changes
Biological Process GO:0042100 B cell proliferation
Biological Process GO:0051702 biological process involved in interaction with symbiont
Biological Process GO:0048291 isotype switching to IgG isotypes
Biological Process GO:0034514 mitochondrial unfolded protein response
Biological Process GO:0002755 MyD88-dependent toll-like receptor signaling pathway
Biological Process GO:1900118 negative regulation of execution phase of apoptosis
Biological Process GO:1900119 positive regulation of execution phase of apoptosis
Biological Process GO:0032727 positive regulation of interferon-alpha production
Biological Process GO:0032733 positive regulation of interleukin-10 production
Biological Process GO:0032735 positive regulation of interleukin-12 production
Biological Process GO:0032755 positive regulation of interleukin-6 production
Biological Process GO:0043032 positive regulation of macrophage activation
Biological Process GO:0050870 positive regulation of T cell activation
Biological Process GO:0002842 positive regulation of T cell mediated immune response to tumor cell
Biological Process GO:0032729 positive regulation of type II interferon production
Biological Process GO:0006457 protein folding
Biological Process GO:0045041 protein import into mitochondrial intermembrane space
Biological Process GO:0042026 protein refolding
Biological Process GO:0050821 protein stabilization
Biological Process GO:0042110 T cell activation

Reference

[1] Fan S, Zhou R, Wen H, Ye H, Ma S et al.. Global profiling of protein lactylome in porcine granulosa cells.. J Ovarian Res 18(1):177. 2025 Aug 8. PMID: 40781717.