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TACC1_CAEEL
ID   TACC1_CAEEL             Reviewed;         260 AA.
AC   G5ECG0;
DT   11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Transforming acid coiled-coil-containing protein 1 {ECO:0000312|WormBase:Y54E2A.3};
GN   Name=tac-1 {ECO:0000312|WormBase:Y54E2A.3};
GN   Synonyms=2P40 {ECO:0000312|WormBase:Y54E2A.3};
GN   ORFNames=Y54E2A.3 {ECO:0000312|WormBase:Y54E2A.3};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN   [1] {ECO:0000312|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2] {ECO:0000312|EMBL:AAG49387.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Bristol N2;
RA   Kohara Y., Shin'i T., Suzuki Y., Sugano S., Potdevin M., Thierry-Mieg Y.,
RA   Thierry-Mieg D., Thierry-Mieg J.;
RT   "The Caenorhabditis elegans transcriptome project, a complementary view of
RT   the genome.";
RL   Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000305}
RP   FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=12956950; DOI=10.1016/s0960-9822(03)00582-7;
RA   Bellanger J.M., Goenczy P.;
RT   "TAC-1 and ZYG-9 form a complex that promotes microtubule assembly in C.
RT   elegans embryos.";
RL   Curr. Biol. 13:1488-1498(2003).
RN   [4] {ECO:0000305}
RP   FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=12956951; DOI=10.1016/s0960-9822(03)00577-3;
RA   Le Bot N., Tsai M.C., Andrews R.K., Ahringer J.;
RT   "TAC-1, a regulator of microtubule length in the C. elegans embryo.";
RL   Curr. Biol. 13:1499-1505(2003).
RN   [5] {ECO:0000305}
RP   FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=12956952; DOI=10.1016/s0960-9822(03)00597-9;
RA   Srayko M., Quintin S., Schwager A., Hyman A.A.;
RT   "Caenorhabditis elegans TAC-1 and ZYG-9 form a complex that is essential
RT   for long astral and spindle microtubules.";
RL   Curr. Biol. 13:1506-1511(2003).
RN   [6] {ECO:0000305}
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=16054029; DOI=10.1016/j.devcel.2005.07.003;
RA   Srayko M., Kaya A., Stamford J., Hyman A.A.;
RT   "Identification and characterization of factors required for microtubule
RT   growth and nucleation in the early C. elegans embryo.";
RL   Dev. Cell 9:223-236(2005).
RN   [7] {ECO:0000305}
RP   FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND
RP   MUTAGENESIS OF MET-58 AND LEU-229.
RX   PubMed=17666432; DOI=10.1242/jcs.004812;
RA   Bellanger J.M., Carter J.C., Phillips J.B., Canard C., Bowerman B.,
RA   Gonczy P.;
RT   "ZYG-9, TAC-1 and ZYG-8 together ensure correct microtubule function
RT   throughout the cell cycle of C. elegans embryos.";
RL   J. Cell Sci. 120:2963-2973(2007).
RN   [8] {ECO:0000305}
RP   DISRUPTION PHENOTYPE, AND MUTAGENESIS OF CYS-94.
RX   PubMed=23155404; DOI=10.1371/journal.pone.0048762;
RA   Tarailo-Graovac M., Chen N.;
RT   "Mos1-mediated transgenesis to probe consequences of single gene mutations
RT   in variation-rich isolates of Caenorhabditis elegans.";
RL   PLoS ONE 7:E48762-E48762(2012).
RN   [9] {ECO:0000305}
RP   FUNCTION, INTERACTION WITH EFA-6, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=26339988; DOI=10.7554/elife.08695;
RA   Chen L., Chuang M., Koorman T., Boxem M., Jin Y., Chisholm A.D.;
RT   "Axon injury triggers EFA-6 mediated destabilization of axonal microtubules
RT   via TACC and doublecortin like kinase.";
RL   Elife 4:0-0(2015).
CC   -!- FUNCTION: Involved in microtubule formation, polymerization and
CC       assembly, regulating microtubule nucleation and length
CC       (PubMed:12956950, PubMed:12956951, PubMed:16054029). Plays a role in
CC       pronuclear migration and mitotic and meiotic spindle elongation during
CC       early embryogenesis (PubMed:12956950, PubMed:12956951). In complex with
CC       zyg-9, functions during the early stages of embryonic development to
CC       regulate microtubule assembly throughout the cell cycle
CC       (PubMed:12956950, PubMed:12956952). Specifically, the complex is
CC       required for the formation and growth of astral microtubules and
CC       spindle microtubules during mitotic spindle assembly (PubMed:12956952).
CC       At anaphase, the complex is required for mitotic spindle positioning in
CC       one-cell stage embryos (PubMed:17666432). The complex acts in a
CC       partially redundant manner with the tac-1/zyg-8 complex to regulate
CC       microtubule assembly and processes during interphase, mitosis and
CC       meiosis in embryos (PubMed:17666432). Plays a role in injury-induced
CC       axonal regrowth, regeneration and microtubule stability in PLM neurons
CC       and this may be downstream of efa-6 (PubMed:26339988).
CC       {ECO:0000269|PubMed:12956950, ECO:0000269|PubMed:12956951,
CC       ECO:0000269|PubMed:12956952, ECO:0000269|PubMed:17666432,
CC       ECO:0000269|PubMed:23155404, ECO:0000269|PubMed:26339988}.
CC   -!- SUBUNIT: Interacts with zyg-9 to form a heterodimer (PubMed:12956950,
CC       PubMed:12956951, PubMed:12956952). Interacts with zyg-8 to form a
CC       heterodimer (PubMed:17666432). Interacts with efa-6 (via N-terminus)
CC       (PubMed:26339988). {ECO:0000269|PubMed:12956950,
CC       ECO:0000269|PubMed:12956951, ECO:0000269|PubMed:12956952,
CC       ECO:0000269|PubMed:17666432, ECO:0000269|PubMed:26339988}.
CC   -!- INTERACTION:
CC       G5ECG0; O01901: ddl-1; NbExp=3; IntAct=EBI-320612, EBI-323542;
CC       G5ECG0; G5ECY0: dlg-1; NbExp=3; IntAct=EBI-320612, EBI-312458;
CC       G5ECG0; Q22227: mig-5; NbExp=3; IntAct=EBI-320612, EBI-316403;
CC       G5ECG0; Q95QA6: pat-12; NbExp=3; IntAct=EBI-320612, EBI-327642;
CC       G5ECG0; Q95QC4: zyg-8; NbExp=3; IntAct=EBI-320612, EBI-331795;
CC       G5ECG0; G5EEM5: zyg-9; NbExp=13; IntAct=EBI-320612, EBI-320102;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle pole
CC       {ECO:0000269|PubMed:12956950, ECO:0000269|PubMed:12956951}. Cytoplasm,
CC       cytoskeleton, microtubule organizing center, centrosome
CC       {ECO:0000269|PubMed:12956950, ECO:0000269|PubMed:12956951,
CC       ECO:0000269|PubMed:12956952, ECO:0000269|PubMed:17666432}. Cytoplasm
CC       {ECO:0000269|PubMed:12956950, ECO:0000269|PubMed:17666432}. Chromosome,
CC       centromere, kinetochore {ECO:0000269|PubMed:12956952}. Cell projection,
CC       axon {ECO:0000269|PubMed:26339988}. Perikaryon
CC       {ECO:0000269|PubMed:26339988}. Note=Initially enriched at meiotic
CC       spindle poles, but then recruited to the sperm centrosome
CC       (PubMed:12956950, PubMed:12956951). Localized to centrosomes early in
CC       pronuclear migration (PubMed:12956952). Centrosomal localization is
CC       dependent on air-1, tbg-1 and zyg-9 and is also controlled during the
CC       cell cycle, with high expression during prophase and metaphase, but
CC       with expression reducing from anaphase to telophase (PubMed:12956950,
CC       PubMed:12956951, PubMed:12956952). Accumulates at the centrosome during
CC       interphase, ready for the next mitotic cycle (PubMed:12956951). Cycles
CC       between cytoplasm and centrosome during mitosis in a cell cycle-
CC       dependent manner (PubMed:12956950, PubMed:17666432). Diffuse
CC       localization along the axon and localizes to perinuclear spots in the
CC       perikaryon (PubMed:26339988). Following injury co-localizes with efa-6
CC       and ptrn-1 in puncta of the perikaryon (PubMed:26339988). The zyg-
CC       9/tac-1 complex localizes to centrosomes throughout the cell cycle and
CC       the kinetochore of metaphase and early anaphase chromosomes
CC       (PubMed:12956952). {ECO:0000269|PubMed:12956950,
CC       ECO:0000269|PubMed:12956951, ECO:0000269|PubMed:12956952,
CC       ECO:0000269|PubMed:17666432, ECO:0000269|PubMed:26339988}.
CC   -!- TISSUE SPECIFICITY: Expressed in touch neurons.
CC       {ECO:0000269|PubMed:26339988}.
CC   -!- DISRUPTION PHENOTYPE: Maternal-effect embryonic lethal
CC       (PubMed:23155404). RNAi-mediated knockdown results in a meiotic defect
CC       in 30% of early embryos and defective microtubule related processes
CC       during the first cell cycle in early embryogenesis (PubMed:12956950,
CC       PubMed:12956951, PubMed:12956952). In one-cell embryos, the maternal
CC       pronuclei fail to migrate and the breakdown of the pronuclear envelope
CC       is delayed (PubMed:12956950, PubMed:12956951, PubMed:12956952). The
CC       sperm pronuclear complex also exhibits a migratory defect whereby it
CC       does not move to the center of the embryo or rotate on the anterior-
CC       posterior axis leading to the assembly of a misaligned spindle at the
CC       posterior of the embryo and ingression of the cleavage furrow from the
CC       posterior cortex (PubMed:12956950, PubMed:12956951, PubMed:12956952,
CC       PubMed:17666432). Reduced microtubule growth rate in embryos
CC       (PubMed:16054029). Defective microtubule elongation in one-cell embryos
CC       resulting in short microtubules that extend from the centrosome, but do
CC       not extend to the cortex, and mitotic spindles that are 20% shorter
CC       than in wild-type one-cell embryos (PubMed:12956950, PubMed:12956951).
CC       Specifically, one-cell embryos have shorter astral and mitotic spindle
CC       microtubules (PubMed:12956952). Reduced stability of the zyg-9/tac-1
CC       complex with reduced accumulation of zyg-9 at the centrosomes
CC       (PubMed:12956950). {ECO:0000269|PubMed:12956950,
CC       ECO:0000269|PubMed:12956951, ECO:0000269|PubMed:12956952,
CC       ECO:0000269|PubMed:16054029, ECO:0000269|PubMed:17666432}.
CC   -!- SIMILARITY: Belongs to the TACC family. {ECO:0000305}.
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DR   EMBL; BX284602; CAA21677.1; -; Genomic_DNA.
DR   EMBL; AF326937; AAG49387.1; -; mRNA.
DR   PIR; T27144; T27144.
DR   RefSeq; NP_497059.1; NM_064658.6.
DR   AlphaFoldDB; G5ECG0; -.
DR   SMR; G5ECG0; -.
DR   ComplexPortal; CPX-372; Zyg-9/Tac-1 complex.
DR   ComplexPortal; CPX-374; Zyg-8/Tac-1 complex.
DR   IntAct; G5ECG0; 47.
DR   MINT; G5ECG0; -.
DR   STRING; 6239.Y54E2A.3; -.
DR   EPD; G5ECG0; -.
DR   PaxDb; G5ECG0; -.
DR   PeptideAtlas; G5ECG0; -.
DR   EnsemblMetazoa; Y54E2A.3.1; Y54E2A.3.1; WBGene00006381.
DR   GeneID; 175133; -.
DR   KEGG; cel:CELE_Y54E2A.3; -.
DR   CTD; 175133; -.
DR   WormBase; Y54E2A.3; CE20302; WBGene00006381; tac-1.
DR   eggNOG; ENOG502TKNX; Eukaryota.
DR   HOGENOM; CLU_071396_0_0_1; -.
DR   InParanoid; G5ECG0; -.
DR   OMA; EFEVRRC; -.
DR   OrthoDB; 1459025at2759; -.
DR   SignaLink; G5ECG0; -.
DR   PRO; PR:G5ECG0; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00006381; Expressed in germ line (C elegans) and 4 other tissues.
DR   GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR   GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0000776; C:kinetochore; IDA:WormBase.
DR   GO; GO:0072687; C:meiotic spindle; EXP:ComplexPortal.
DR   GO; GO:0061673; C:mitotic spindle astral microtubule; IDA:ComplexPortal.
DR   GO; GO:1990498; C:mitotic spindle microtubule; IDA:ComplexPortal.
DR   GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR   GO; GO:0005819; C:spindle; IDA:WormBase.
DR   GO; GO:0000922; C:spindle pole; IDA:WormBase.
DR   GO; GO:0019904; F:protein domain specific binding; IPI:WormBase.
DR   GO; GO:0030953; P:astral microtubule organization; IMP:WormBase.
DR   GO; GO:0051301; P:cell division; IMP:WormBase.
DR   GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR   GO; GO:0051321; P:meiotic cell cycle; IMP:WormBase.
DR   GO; GO:0007017; P:microtubule-based process; IDA:ComplexPortal.
DR   GO; GO:0000022; P:mitotic spindle elongation; IMP:WormBase.
DR   GO; GO:0007052; P:mitotic spindle organization; IMP:WormBase.
DR   GO; GO:0007026; P:negative regulation of microtubule depolymerization; IMP:WormBase.
DR   GO; GO:0035046; P:pronuclear migration; IMP:WormBase.
DR   GO; GO:0031113; P:regulation of microtubule polymerization; IMP:WormBase.
DR   InterPro; IPR007707; TACC_C.
DR   Pfam; PF05010; TACC_C; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Cell projection; Centromere; Chromosome;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Kinetochore; Meiosis; Microtubule;
KW   Mitosis; Reference proteome.
FT   CHAIN           1..260
FT                   /note="Transforming acid coiled-coil-containing protein 1"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000436234"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          108..249
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..27
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         58
FT                   /note="M->I: In or455; temperature sensitive mutant which
FT                   is embryonic lethal at 26 degrees Celsius, with defective
FT                   pronuclear migration."
FT                   /evidence="ECO:0000269|PubMed:17666432"
FT   MUTAGEN         94
FT                   /note="C->W: No obvious phenotype."
FT                   /evidence="ECO:0000269|PubMed:23155404"
FT   MUTAGEN         229
FT                   /note="L->F: In or369 and or402; temperature sensitive
FT                   mutant which is embryonic lethal at 26 degrees Celsius,
FT                   with defective pronuclear migration and reduced zyg-9
FT                   binding."
FT                   /evidence="ECO:0000269|PubMed:17666432"
SQ   SEQUENCE   260 AA;  28543 MW;  31D20FF3E5AF562B CRC64;
     MSLNTTFTKE DGTEVVIPFN GSQNGHPENE EPEVEEAAEP SSSVETLCGA TRGDIIVMKH
     TTKALTELIE RLLHSDEFEV RRCSNGQIIS QGRCNGTTPG NGIGGGGASS EELEKALKDR
     DAARAEADKL HANYATLFAS FNTVREAAND IRGEYEDARD KLKLAAAEVD EWQAKFLAVK
     DNANSELERA SVEYDDLLRS HDENTKGLRL RVKRQEIELS SKNDEIKVLT NRVSELSQIC
     DQLLNDVDVS DGMSVISTDA
 
 
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