P34808 · KTNA1_CAEEL
- ProteinMeiotic spindle formation protein mei-1
- Genemei-1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids472 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalytic subunit of a complex which severs microtubules in an ATP-dependent manner (PubMed:28783150).
Microtubule severing may promote rapid reorganization of cellular microtubule arrays. Required specifically for meiotic spindle formation in the female germline; the presence of this protein is inimical to the formation of mitotic spindles (PubMed:10809666, PubMed:12885567, PubMed:19087961, PubMed:23918937, PubMed:8027178).
In body wall muscles, regulates organization of myosin thick filaments (PubMed:22621901).
Microtubule severing may promote rapid reorganization of cellular microtubule arrays. Required specifically for meiotic spindle formation in the female germline; the presence of this protein is inimical to the formation of mitotic spindles (PubMed:10809666, PubMed:12885567, PubMed:19087961, PubMed:23918937, PubMed:8027178).
In body wall muscles, regulates organization of myosin thick filaments (PubMed:22621901).
Catalytic activity
Activity regulation
ATPase activity is stimulated by microtubules, which promote homooligomerization. ATP-dependent microtubule severing is stimulated by interaction with mei-2.
Features
Showing features for binding site.
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMeiotic spindle formation protein mei-1
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Rhabditina > Rhabditomorpha > Rhabditoidea > Rhabditidae > Peloderinae > Caenorhabditis
Accessions
- Primary accessionP34808
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Localizes to the spindle poles and condensed chromatin during female meiosis (PubMed:10809666, PubMed:12781129, PubMed:16338136, PubMed:8027178).
This localization requires mei-2 (PubMed:10809666).
Also localizes to the polar body (PubMed:12781129).
Ser-92 phosphorylated mei-1 is first detected on the maternal chromatin in anaphase of meiosis I, then localizes to the cytoplasm during meiosis II and quickly disappears between pronuclear formation and the first cell division, except in the polar bodies (PubMed:16338136).
This localization requires mei-2 (PubMed:10809666).
Also localizes to the polar body (PubMed:12781129).
Ser-92 phosphorylated mei-1 is first detected on the maternal chromatin in anaphase of meiosis I, then localizes to the cytoplasm during meiosis II and quickly disappears between pronuclear formation and the first cell division, except in the polar bodies (PubMed:16338136).
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
RNAi-mediated knockdown at the L1 larval stage results in the disorganization of myosin thick filaments in adult body wall muscles characterized by the formation of abnormal myosin heavy chain myo-3 aggregates and V-shaped crossing of A-bands. In addition, body wall muscle cells appear shorter and broader.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 36 | In ct46ct99; loss of function. Does not affect mei-1 degradation. Prevents mei-1 degradation during the transition from meiosis to mitosis; when associated with A-92. | ||||
Sequence: R → C | ||||||
Mutagenesis | 66 | In ct46sb18; gain of function. | ||||
Sequence: E → K | ||||||
Mutagenesis | 92 | Abolishes phosphorylation by mbk-2. Abolishes interaction with mel-26. Prevents mei-1 degradation during the transition from meiosis to mitosis; when associated with C-36. | ||||
Sequence: S → A | ||||||
Mutagenesis | 92 | Phosphomimetic mutant. No effect on the interaction with mel-26. | ||||
Sequence: S → D | ||||||
Mutagenesis | 99 | In ct46; gain of function. Embryonic lethal. Abolishes interaction with mel-26 and probably mel-26-mediated degradation. Simultaneous RNAi-mediated knockdown of ppfr-1, pph-4.1 or ppfr-4, partially rescues embryonic lethality. Myosin thick filaments are disorganized in body wall muscles in an unc-29 (e1072) mutant background. | ||||
Sequence: P → L | ||||||
Mutagenesis | 126 | In ct46sb9 and ct46sb17; gain of function. | ||||
Sequence: G → S | ||||||
Mutagenesis | 128 | In ct46sb22; gain of function. | ||||
Sequence: R → C | ||||||
Mutagenesis | 195 | In ct46sb3; dominant negative. | ||||
Sequence: I → K | ||||||
Mutagenesis | 225 | In b284; dominant negative. | ||||
Sequence: P → L | ||||||
Mutagenesis | 231 | In ct81; dominant negative. | ||||
Sequence: L → P | ||||||
Mutagenesis | 235 | In ct93; dominant negative. | ||||
Sequence: P → L | ||||||
Mutagenesis | 235 | In ct46ct103; dominant negative. Formation of an abnormally large polar body during oocyte meiosis II. Increased in metaphase and anaphase meiotic spindle length, failure of chromosomes to align on the metaphase plate persistence of spindle poles during anaphase resulting in their mis-positioning and delay in anaphase meiotic spindle disassembly. | ||||
Sequence: P → S | ||||||
Mutagenesis | 308 | In ct46ct101; null. Formation of an abnormally large polar body during oocyte meiosis II. Myosin thick filaments are disorganized in body wall muscles in an unc-29 (e1072) mutant background. | ||||
Sequence: E → D | ||||||
Mutagenesis | 322 | Severe loss of ATPase activity and complete loss of microtubule severing activity. | ||||
Sequence: D → R | ||||||
Mutagenesis | 351 | Severe loss of ATPase activity and complete loss of microtubule severing activity. | ||||
Sequence: R → A | ||||||
Mutagenesis | 352 | Severe loss of ATPase activity and complete loss of microtubule severing activity. | ||||
Sequence: R → A | ||||||
Mutagenesis | 360 | In ct46sb23; gain of function. | ||||
Sequence: P → S | ||||||
Mutagenesis | 414 | In ct46ct89; dominant negative. | ||||
Sequence: R → K | ||||||
Mutagenesis | 469 | Severe loss of ATPase activity and complete loss of microtubule severing activity. | ||||
Sequence: F → A | ||||||
Mutagenesis | 470 | In ct46ct82; dominant negative. | ||||
Sequence: G → D |
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000084599 | 1-472 | Meiotic spindle formation protein mei-1 | |||
Sequence: MNGDVQSVIRGYLERAQVAKTMSDAGRWNEAGDLLRQLMTDVKSCKISASNRDEHDARNTFLRALEANLKLVQQNVRDEDDLHEAMTRQSGSPEPPADPDVWSKPSPPLPSSSKFGATKKGVGAAGPRPREISKSTSSMSTNPADVKPANPTQGILPQNSAGDSFDASAYDAYIVQAVRGTMATNTENTMSLDDIIGMHDVKQVLHEAVTLPLLVPEFFQGLRSPWKAMVLAGPPGTGKTLIARAIASESSSTFFTVSSTDLSSKWRGDSEKIVRLLFELARFYAPSIIFIDEIDTLGGQRGNSGEHEASRRVKSEFLVQMDGSQNKFDSRRVFVLAATNIPWELDEALRRRFEKRIFIPLPDIDARKKLIEKSMEGTPKSDEINYDDLAARTEGFSGADVVSLCRTAAINVLRRYDTKSLRGGELTAAMESLKAELVRNIDFEAALQAVSPSAGPDTMLKCKEWCDSFGAM | ||||||
Modified residue | 92 | Phosphoserine; by mbk-2 | ||||
Sequence: S |
Post-translational modification
Phosphorylated (PubMed:16338136, PubMed:23918937).
Phosphorylation by mbk-2 is required for its rapid degradation following meiosis II (PubMed:16338136).
Likely dephosphorylated by the PP4 complex composed of catalytic subunit pph-4.1 and regulatory subunit ppfr-1 (PubMed:23918937).
Phosphorylation by mbk-2 is required for its rapid degradation following meiosis II (PubMed:16338136).
Likely dephosphorylated by the PP4 complex composed of catalytic subunit pph-4.1 and regulatory subunit ppfr-1 (PubMed:23918937).
Polyubiquitination targets the protein for rapid degradation via the ubiquitin system at the end of meiosis. The BTB domain protein mel-26 may serve to specifically target mei-1 for ubiquitination by cul-3 containing complexes. The cul-3 protein is in turn regulated by neddylation by ned-8.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Developmental stage
Highly expressed in the female germline. Degradation at the meiosis-mitosis transition reduces cytoplasmic microtubule severing activity, thereby allowing the formation of larger mitotic spindles.
Gene expression databases
Interaction
Subunit
Homohexamer; ATP hydrolysis initiates a cycle between an open spiral and a closed ring conformation which is probably involved in pulling tubulin dimers out from microtubules (PubMed:28783150).
Interacts with mei-2, which may serve as a targeting subunit (PubMed:10809666).
Interacts with mel-26, which targets mei-1 for ubiquitin mediated proteolysis (PubMed:13679921, PubMed:14528312, PubMed:23918937).
Interacts with phosphatase pph-4.1 (PubMed:19087961).
Interacts with mei-2, which may serve as a targeting subunit (PubMed:10809666).
Interacts with mel-26, which targets mei-1 for ubiquitin mediated proteolysis (PubMed:13679921, PubMed:14528312, PubMed:23918937).
Interacts with phosphatase pph-4.1 (PubMed:19087961).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P34808 | CELE_F47G4.4 Q9XTS1 | 3 | EBI-323248, EBI-312192 | |
BINARY | P34808 | CELE_F47G4.5 Q9XTS3 | 4 | EBI-323248, EBI-2417913 | |
BINARY | P34808 | mbk-2 Q9XTF3-2 | 2 | EBI-323248, EBI-2565597 | |
BINARY | P34808 | mei-1 P34808 | 6 | EBI-323248, EBI-323248 | |
BINARY | P34808 | mei-2 O44740 | 3 | EBI-323248, EBI-323243 | |
BINARY | P34808 | mel-26 Q94420 | 6 | EBI-323248, EBI-320790 | |
BINARY | P34808-2 | mel-26 Q94420 | 3 | EBI-521381, EBI-320790 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 83-161 | Disordered | ||||
Sequence: HEAMTRQSGSPEPPADPDVWSKPSPPLPSSSKFGATKKGVGAAGPRPREISKSTSSMSTNPADVKPANPTQGILPQNSA | ||||||
Compositional bias | 131-161 | Polar residues | ||||
Sequence: EISKSTSSMSTNPADVKPANPTQGILPQNSA |
Sequence similarities
Belongs to the AAA ATPase family. Katanin p60 subunit A1 subfamily.
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
P34808-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Namea
- Length472
- Mass (Da)51,739
- Last updated1994-02-01 v1
- Checksum167A3929E573CD59
P34808-2
- Nameb
- Differences from canonical
- 416-416: Y → YFRY
Features
Showing features for compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 131-161 | Polar residues | ||||
Sequence: EISKSTSSMSTNPADVKPANPTQGILPQNSA | ||||||
Alternative sequence | VSP_012951 | 416 | in isoform b | |||
Sequence: Y → YFRY |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L25423 EMBL· GenBank· DDBJ | AAA28109.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z75713 EMBL· GenBank· DDBJ | CAB00052.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z75713 EMBL· GenBank· DDBJ | CAD56596.1 EMBL· GenBank· DDBJ | Genomic DNA |