P48721 · GRP75_RAT
- ProteinStress-70 protein, mitochondrial
- GeneHspa9
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids679 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Chaperone protein which plays an important role in mitochondrial iron-sulfur cluster (ISC) biogenesis. Interacts with and stabilizes ISC cluster assembly proteins FXN, NFU1, NFS1 and ISCU. Regulates erythropoiesis via stabilization of ISC assembly. May play a role in cell cycle regulation via its interaction with and promotion of degradation of TP53 (By similarity).
May play a role in the control of cell proliferation and cellular aging (By similarity).
Molecular adapter that regulates mitochondrial calcium-dependent apoptosis by coupling two calcium channels, ITPR1 and VDAC1, at the mitochondria-associated endoplasmic reticulum (ER) membrane to facilitate calcium transport from the ER lumen to the mitochondria intermembrane space, thus providing calcium for the downstream calcium channel MCU that directly releases it into mitochondria matrix (By similarity).
May play a role in the control of cell proliferation and cellular aging (By similarity).
Molecular adapter that regulates mitochondrial calcium-dependent apoptosis by coupling two calcium channels, ITPR1 and VDAC1, at the mitochondria-associated endoplasmic reticulum (ER) membrane to facilitate calcium transport from the ER lumen to the mitochondria intermembrane space, thus providing calcium for the downstream calcium channel MCU that directly releases it into mitochondria matrix (By similarity).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameStress-70 protein, mitochondrial
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionP48721
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Found in a complex with HSPA9 and VDAC1 at the endoplasmic reticulum-mitochondria contact sites.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for transit peptide, chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-46 | Mitochondrion | ||||
Sequence: MISASRAAAARLVGTTASRSPAAARHQDGWNGLSHEVFRFVSRRDY | ||||||
Chain | PRO_0000013565 | 47-679 | Stress-70 protein, mitochondrial | |||
Sequence: ASEAIKGAVVGIDLGTTNSCVAVMEGKQAKVLENAEGARTTPSVVAFTPDGERLVGMPAKRQAVTNPNNTFYATKRLIGRRYDDPEVQKDTKNVPFKIVRASNGDAWVEAHGKLYSPSQIGAFVLMKMKETAENYLGHTAKNAVITVPAYFNDSQRQATKDAGQISGLNVLRVINEPTAAALAYGLDKSEDKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLRHIVKEFKRETGVDLTKDNMALQRVREAAEKAKCELSSSVQTDINLPYLTMDASGPKHLNMKLTRAQFEGIVTDLIKRTIAPCQKAMQDREVSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAIQGGVLAGDVTDVLLLDVTPLSLGIETLGGVFTKLINRNTTIPTKKSQVFSTAADGQTQVEIKVCQGEREMAGDNKLLGQFTLIGIPPAPRGVPQIEVTFDIDANGIVHVSAKDKGTGREQQIVIQSSGGLSKDDIENMVKNAEKYAEEDRRKKERVEAVNMAEGIIHDTETKMEEFKDQLPADECNKLKEEISKMRELLARKDSETGENIRQAASSLQQASLKLFEMAYKKMASEREGSGSSSTGEQKEDQKEEKQ | ||||||
Modified residue | 76 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 87 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 135 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 135 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 138 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 138 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 143 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 206 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 206 | N6-malonyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 206 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 234 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 288 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 300 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 300 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 360 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 360 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 368 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 394 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 408 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 513 | Omega-N-methylarginine | ||||
Sequence: R | ||||||
Modified residue | 567 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 567 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 600 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 600 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 610 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 612 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 646 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 646 | N6-succinyllysine; alternate | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Interacts strongly with the intermediate form of FXN and weakly with its mature form. Interacts with HSCB. Associates with the mitochondrial contact site and cristae organizing system (MICOS) complex, composed of at least MICOS10/MIC10, CHCHD3/MIC19, CHCHD6/MIC25, APOOL/MIC27, IMMT/MIC60, APOO/MIC23/MIC26 and QIL1/MIC13. This complex was also known under the names MINOS or MitOS complex. The MICOS complex associates with mitochondrial outer membrane proteins SAMM50, MTX1, MTX2 and DNAJC11, mitochondrial inner membrane protein TMEM11 and with HSPA9. Interacts with DNLZ, the interaction is required to prevent self-aggregation. Interacts with TESPA1. Interacts with PDPN. Interacts with NFU1, NFS1 and ISCU. Interacts with TP53; the interaction promotes TP53 degradation (By similarity).
Interacts (via SBD domain) with UBXN2A; the interaction with UBXN2A inhibits HSPA9/MOT-2 interaction with and degradation of TP53, thereby promotes TP53 translocation to the nucleus (By similarity).
Interacts with ITPR1 AND VDAC1; this interaction couples ITPR1 to VDAC1 (PubMed:17178908).
Interacts (via SBD domain) with UBXN2A; the interaction with UBXN2A inhibits HSPA9/MOT-2 interaction with and degradation of TP53, thereby promotes TP53 translocation to the nucleus (By similarity).
Interacts with ITPR1 AND VDAC1; this interaction couples ITPR1 to VDAC1 (PubMed:17178908).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-432 | Interaction with NFS1 | ||||
Sequence: MISASRAAAARLVGTTASRSPAAARHQDGWNGLSHEVFRFVSRRDYASEAIKGAVVGIDLGTTNSCVAVMEGKQAKVLENAEGARTTPSVVAFTPDGERLVGMPAKRQAVTNPNNTFYATKRLIGRRYDDPEVQKDTKNVPFKIVRASNGDAWVEAHGKLYSPSQIGAFVLMKMKETAENYLGHTAKNAVITVPAYFNDSQRQATKDAGQISGLNVLRVINEPTAAALAYGLDKSEDKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDQALLRHIVKEFKRETGVDLTKDNMALQRVREAAEKAKCELSSSVQTDINLPYLTMDASGPKHLNMKLTRAQFEGIVTDLIKRTIAPCQKAMQDREVSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEAVAIGAAIQGGVLAGDV | ||||||
Region | 432-679 | Interaction with FXN and ISCU | ||||
Sequence: VTDVLLLDVTPLSLGIETLGGVFTKLINRNTTIPTKKSQVFSTAADGQTQVEIKVCQGEREMAGDNKLLGQFTLIGIPPAPRGVPQIEVTFDIDANGIVHVSAKDKGTGREQQIVIQSSGGLSKDDIENMVKNAEKYAEEDRRKKERVEAVNMAEGIIHDTETKMEEFKDQLPADECNKLKEEISKMRELLARKDSETGENIRQAASSLQQASLKLFEMAYKKMASEREGSGSSSTGEQKEDQKEEKQ | ||||||
Region | 655-679 | Disordered | ||||
Sequence: MASEREGSGSSSTGEQKEDQKEEKQ | ||||||
Compositional bias | 665-679 | Basic and acidic residues | ||||
Sequence: SSTGEQKEDQKEEKQ |
Sequence similarities
Belongs to the heat shock protein 70 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length679
- Mass (Da)73,858
- Last updated2006-10-17 v3
- Checksum4616EDE5307691A4
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F1M953 | F1M953_RAT | Hspa9 | 679 | ||
A0A8I5ZR52 | A0A8I5ZR52_RAT | Hspa9 | 670 |
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 37 | in Ref. 2; AAB34982 | ||||
Sequence: V → A | ||||||
Sequence conflict | 81 | in Ref. 1; AAB33049 | ||||
Sequence: A → S | ||||||
Sequence conflict | 373 | in Ref. 2; AAB34982 | ||||
Sequence: R → A | ||||||
Sequence conflict | 487 | in Ref. 3; AA sequence | ||||
Sequence: C → T | ||||||
Sequence conflict | 493 | in Ref. 3; AA sequence | ||||
Sequence: M → Q | ||||||
Sequence conflict | 589 | in Ref. 1; AAB33049 | ||||
Sequence: I → V | ||||||
Compositional bias | 665-679 | Basic and acidic residues | ||||
Sequence: SSTGEQKEDQKEEKQ |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
S75280 EMBL· GenBank· DDBJ | AAB33049.1 EMBL· GenBank· DDBJ | mRNA | ||
S78556 EMBL· GenBank· DDBJ | AAB34982.1 EMBL· GenBank· DDBJ | mRNA |