Q80SU3 · ZAR1_MOUSE
- ProteinZygote arrest protein 1
- GeneZar1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids361 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
mRNA-binding protein that mediates formation of MARDO (mitochondria-associated ribonucleoprotein domain), a membraneless compartment that stores maternal mRNAs in oocytes (PubMed:36264786).
MARDO assembly around mitochondria is directed by an increase in mitochondrial membrane potential during oocyte growth (PubMed:36264786).
Promotes formation of MARDO phase-separated membraneless compartment by undergoing liquid-liquid phase separation upon binding to maternal mRNAs (PubMed:36264786).
Binds to the 3'-UTR of maternal mRNAs (PubMed:31598710).
Maternal mRNAs stored in the MARDO are translationally repressed (PubMed:36264786).
Essential for female fertility and oocyte-to-embryo transition by coordinating maternal mRNA storage, translation and degradation (PubMed:12539046, PubMed:31598710, PubMed:36264786).
MARDO assembly around mitochondria is directed by an increase in mitochondrial membrane potential during oocyte growth (PubMed:36264786).
Promotes formation of MARDO phase-separated membraneless compartment by undergoing liquid-liquid phase separation upon binding to maternal mRNAs (PubMed:36264786).
Binds to the 3'-UTR of maternal mRNAs (PubMed:31598710).
Maternal mRNAs stored in the MARDO are translationally repressed (PubMed:36264786).
Essential for female fertility and oocyte-to-embryo transition by coordinating maternal mRNA storage, translation and degradation (PubMed:12539046, PubMed:31598710, PubMed:36264786).
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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Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytoplasmic ribonucleoprotein granule | |
Cellular Component | intracellular non-membrane-bounded organelle | |
Molecular Function | metal ion binding | |
Molecular Function | molecular condensate scaffold activity | |
Molecular Function | mRNA 3'-UTR binding | |
Molecular Function | RNA sequestering activity | |
Biological Process | mRNA stabilization | |
Biological Process | negative regulation of translation | |
Biological Process | non-membrane-bounded organelle assembly | |
Biological Process | oocyte maturation | |
Biological Process | translation |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameZygote arrest protein 1
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ80SU3
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Specifically localizes to MARDO (mitochondria-associated ribonucleoprotein domain), a mitochondria-associated membraneless compartment that stores mRNAs in oocytes.
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Mice are viable but females are infertile (PubMed:12539046).
Ovarian development and oogenesis through the early stages of fertilization are normal, but most embryos from mutant females arrest at the one-cell stage (PubMed:12539046, PubMed:36264786).
Abolished formation of MARDO phase-separated membraneless compartment and mitochondrial clustering in oocytes (PubMed:36264786).
Mice lacking Zar1 and Zar1l oocytes display delayed meiotic resumption and polar body-1 emission and a higher incidence of abnormal meiotic spindle formation and chromosome aneuploidy (PubMed:31598710).
The grown oocytes of Zar1 and Zar1l mutant mice contain decreased levels of many maternal mRNAs and display a reduced level of protein synthesis (PubMed:31598710).
Ovarian development and oogenesis through the early stages of fertilization are normal, but most embryos from mutant females arrest at the one-cell stage (PubMed:12539046, PubMed:36264786).
Abolished formation of MARDO phase-separated membraneless compartment and mitochondrial clustering in oocytes (PubMed:36264786).
Mice lacking Zar1 and Zar1l oocytes display delayed meiotic resumption and polar body-1 emission and a higher incidence of abnormal meiotic spindle formation and chromosome aneuploidy (PubMed:31598710).
The grown oocytes of Zar1 and Zar1l mutant mice contain decreased levels of many maternal mRNAs and display a reduced level of protein synthesis (PubMed:31598710).
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 154 | Does not regulate formation of MARDO membraneless compartment; when associated with A-161. | ||||
Sequence: T → A | ||||||
Mutagenesis | 154 | Mimics phosphorylation state; does not regulate formation of MARDO membraneless compartment; when associated with D-161. | ||||
Sequence: T → D | ||||||
Mutagenesis | 161 | Does not regulate formation of MARDO membraneless compartment; when associated with A-154. | ||||
Sequence: S → A | ||||||
Mutagenesis | 161 | Mimics phosphorylation state; does not regulate formation of MARDO membraneless compartment; when associated with D-154. | ||||
Sequence: S → D | ||||||
Mutagenesis | 269 | In 4CS mutant; abolished binding to the 3'-UTR of maternal mRNAs; when associated with S-296, S-313 and S-341. | ||||
Sequence: C → S | ||||||
Mutagenesis | 296 | In 4CS mutant; abolished binding to the 3'-UTR of maternal mRNAs; when associated with S-269, S-313 and S-341. | ||||
Sequence: C → S | ||||||
Mutagenesis | 313 | In 4CS mutant; abolished binding to the 3'-UTR of maternal mRNAs; when associated with S-269, S-296 and S-341. | ||||
Sequence: C → S | ||||||
Mutagenesis | 341 | In 4CS mutant; abolished binding to the 3'-UTR of maternal mRNAs; when associated with S-269, S-296 and S-313. | ||||
Sequence: C → S |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 29 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000187012 | 1-361 | Zygote arrest protein 1 | |||
Sequence: MFPASTFHPCPHPYPQATKAGDGWRFGARGCRPAPPSFLPGYRQLMAAEYVDSHQRAQLMALLSRMGPRSVSSRDAAVQVNPRRDASVQCSLGRRTLQPAGCRASPDARSGSCQPRGHAGAGRSPRSWQTVAPFSSVTFCGLSSSLEVAGGRQTPTKGEGSPASSGTREPEPREVAARKAVPQPRSEEGDVQAAGQAGWEQQPPPEDRNSVAAMQSEPGSEEPCPAAEMAQDPGDSDAPRDQASPQSTEQDKERLRFQFLEQKYGYYHCKDCKIRWESAYVWCVQGTSKVYFKQFCRVCEKSYNPYRVEDITCQSCKRTRCACPVRLRHVDPKRPHRQDLCGRCKDKRLSCDSTFSFKYII | ||||||
Modified residue | 154 | Phosphothreonine; by CDK1 | ||||
Sequence: T | ||||||
Modified residue | 161 | Phosphoserine; by CDK1 | ||||
Sequence: S |
Post-translational modification
Phosphorylation by CDK1 does not regulate formation of MARDO (mitochondria-associated ribonucleoprotein domain) membraneless compartment.
Ubiquitinated and degradaded by the proteasome during oocyte meiotic maturation, leading to MARDO (mitochondria-associated ribonucleoprotein domain) membraneless compartment dissolution.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Ovary (PubMed:12539046, PubMed:12773403).
Expressed in primary oocytes (from primary through antral follicle stages) and during the progression from Meiosis I to Meiosis II (PubMed:12539046, PubMed:12773403, PubMed:31598710).
The mRNA is detected in growing oocytes (early primary follicle, type 3a) through fully grown oocytes (antral follicle, type 8) (PubMed:12539046, PubMed:12773403).
Expressed in primary oocytes (from primary through antral follicle stages) and during the progression from Meiosis I to Meiosis II (PubMed:12539046, PubMed:12773403, PubMed:31598710).
The mRNA is detected in growing oocytes (early primary follicle, type 3a) through fully grown oocytes (antral follicle, type 8) (PubMed:12539046, PubMed:12773403).
Developmental stage
Expressed in zygote at the one-cell embryo, markedly less abundant at the two-cell embryo.
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, zinc finger.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-23 | Disordered | ||||
Sequence: MFPASTFHPCPHPYPQATKAGDG | ||||||
Region | 98-128 | Disordered | ||||
Sequence: QPAGCRASPDARSGSCQPRGHAGAGRSPRSW | ||||||
Compositional bias | 148-163 | Polar residues | ||||
Sequence: VAGGRQTPTKGEGSPA | ||||||
Region | 148-252 | Disordered | ||||
Sequence: VAGGRQTPTKGEGSPASSGTREPEPREVAARKAVPQPRSEEGDVQAAGQAGWEQQPPPEDRNSVAAMQSEPGSEEPCPAAEMAQDPGDSDAPRDQASPQSTEQDK | ||||||
Compositional bias | 171-185 | Basic and acidic residues | ||||
Sequence: EPREVAARKAVPQPR | ||||||
Zinc finger | 263-346 | 3CxxC-type | ||||
Sequence: KYGYYHCKDCKIRWESAYVWCVQGTSKVYFKQFCRVCEKSYNPYRVEDITCQSCKRTRCACPVRLRHVDPKRPHRQDLCGRCKD |
Domain
Disordered region at the N-terminus undergoes liquid-liquid phase separation (LLPS) for the formation of MARDO (mitochondria-associated ribonucleoprotein domain), a membraneless compartment that stores maternal mRNAs in oocytes.
The 3CxxC-type mediates binding to the 3'-UTR of mRNAs.
Sequence similarities
Belongs to the ZAR1 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length361
- Mass (Da)39,986
- Last updated2003-06-01 v1
- ChecksumC34AE85F76839242
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0J9YU98 | A0A0J9YU98_MOUSE | Zar1 | 204 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 148-163 | Polar residues | ||||
Sequence: VAGGRQTPTKGEGSPA | ||||||
Compositional bias | 171-185 | Basic and acidic residues | ||||
Sequence: EPREVAARKAVPQPR |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY191415 EMBL· GenBank· DDBJ | AAO24706.1 EMBL· GenBank· DDBJ | mRNA | ||
AY193889 EMBL· GenBank· DDBJ | AAO24708.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC099399 EMBL· GenBank· DDBJ | AAH99399.1 EMBL· GenBank· DDBJ | mRNA |