ATX2_CAEEL
ID ATX2_CAEEL Reviewed; 959 AA.
AC G5ED29; B2D6K7; Q5FC83;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Ataxin-2 homolog {ECO:0000305};
GN Name=atx-2 {ECO:0000303|PubMed:11303786, ECO:0000312|WormBase:D2045.1a};
GN ORFNames=D2045.1 {ECO:0000312|WormBase:D2045.1a};
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|EMBL:AAS78587.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15514056; DOI=10.1534/genetics.104.029355;
RA Maine E.M., Hansen D., Springer D., Vought V.E.;
RT "Caenorhabditis elegans atx-2 promotes germline proliferation and the
RT oocyte fate.";
RL Genetics 168:817-830(2004).
RN [2] {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 [3] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=11303786; DOI=10.1385/jmn:15:3:231;
RA Kiehl T.R., Shibata H., Pulst S.M.;
RT "The ortholog of human ataxin-2 is essential for early embryonic patterning
RT in C. elegans.";
RL J. Mol. Neurosci. 15:231-241(2000).
RN [4] {ECO:0000305}
RP FUNCTION, INTERACTION WITH PAB-1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=15342467; DOI=10.1242/dev.01352;
RA Ciosk R., DePalma M., Priess J.R.;
RT "ATX-2, the C. elegans ortholog of ataxin 2, functions in translational
RT regulation in the germline.";
RL Development 131:4831-4841(2004).
RN [5] {ECO:0000305}
RP FUNCTION, INTERACTION WITH GDI-1, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=27457958; DOI=10.1073/pnas.1512156113;
RA Bar D.Z., Charar C., Dorfman J., Yadid T., Tafforeau L., Lafontaine D.L.,
RA Gruenbaum Y.;
RT "Cell size and fat content of dietary-restricted Caenorhabditis elegans are
RT regulated by ATX-2, an mTOR repressor.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:E4620-E4629(2016).
RN [6] {ECO:0000305}
RP FUNCTION, INTERACTION WITH SZY-20, SUBCELLULAR LOCATION, DOMAIN, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=27689799; DOI=10.1371/journal.pgen.1006370;
RA Stubenvoll M.D., Medley J.C., Irwin M., Song M.H.;
RT "ATX-2, the C. elegans ortholog of human Ataxin-2, regulates centrosome
RT size and microtubule dynamics.";
RL PLoS Genet. 12:E1006370-E1006370(2016).
CC -!- FUNCTION: Probable RNA-binding protein that negatively regulates the
CC translation of targets (PubMed:15342467, PubMed:27689799). Functions
CC with RNA-binding protein szy-20 to ensure embryonic cell division, and
CC to this end, plays a role in the regulation of centrosome assembly,
CC position and size, and in astral microtubule outgrowth and nucleation
CC (PubMed:27689799). Required for gonad development, germ cell
CC proliferation and for the production of oocytes (PubMed:15514056,
CC PubMed:11303786, PubMed:15342467). Regulates whole body growth and fat
CC accumulation in response to food availability, and this may be through
CC the mTOR pathway, upstream of daf-15 and rheb-1 (PubMed:27457958).
CC {ECO:0000269|PubMed:11303786, ECO:0000269|PubMed:15342467,
CC ECO:0000269|PubMed:15514056, ECO:0000269|PubMed:27457958,
CC ECO:0000269|PubMed:27689799}.
CC -!- SUBUNIT: Interacts (via C-terminus) with szy-20 (via C-terminus); the
CC interaction is RNA independent (PubMed:27689799). Interacts with pab-1
CC (PubMed:15342467). Interacts with gdi-1 (PubMed:27457958).
CC {ECO:0000269|PubMed:15342467, ECO:0000269|PubMed:27457958,
CC ECO:0000269|PubMed:27689799}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15342467,
CC ECO:0000269|PubMed:27457958, ECO:0000269|PubMed:27689799}. Nucleus
CC {ECO:0000269|PubMed:27457958}. Note=Co-localizes with szy-20 and pab-1
CC in the cytoplasm. {ECO:0000269|PubMed:27689799}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=a {ECO:0000312|WormBase:D2045.1a};
CC IsoId=G5ED29-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:D2045.1b};
CC IsoId=G5ED29-2; Sequence=VSP_058818;
CC Name=c {ECO:0000312|WormBase:D2045.1c};
CC IsoId=G5ED29-3; Sequence=VSP_058819, VSP_058820;
CC -!- TISSUE SPECIFICITY: Expressed in the central nervous system, dorsal and
CC ventral nerve chord, intestinal lining and body-wall muscle
CC (PubMed:11303786). Expressed in the gonad (PubMed:15342467).
CC {ECO:0000269|PubMed:11303786, ECO:0000269|PubMed:15342467}.
CC -!- DEVELOPMENTAL STAGE: Expressed in 4-cell stage embryos and during
CC larval stages L3 and L4. {ECO:0000269|PubMed:11303786}.
CC -!- DOMAIN: The C-terminal part is necessary for interaction with szy-20.
CC {ECO:0000269|PubMed:27689799}.
CC -!- DISRUPTION PHENOTYPE: Sterile, however growth rate, size and fat
CC accumulation are not altered in response to a restricted diet in
CC contrast to wild-type animals under the same conditions
CC (PubMed:27457958). RNAi-mediated knockdown results in embryonic
CC lethality as a result of cell division defects at the one-cell stage
CC (PubMed:27689799). Cell division defects include polar body extrusion
CC failure, abnormal spindle positioning, chromosome missegregation and
CC cytokinesis failure (PubMed:27689799). One-cell embryos also have
CC enlarged centrosomes and microtubule growth defects characterized by
CC increased microtubule nucleation, short astral microtubules and
CC elevated expression levels of zyg-1, which is involved in centriole
CC duplication, and tbg-1, a pericentriolar materials factor involved in
CC microtubule nucleation (PubMed:27689799). In other contrasting studies,
CC RNAi-mediated knockdown at the L4 stage of larval development, results
CC in the initial production of viable progeny, that with continued RNAi
CC exposure, grow into sterile adults in which germ cells have a
CC proliferation defect that leads to a reduced sized gonad containing
CC large quantities of sperm and no oocytes (PubMed:15514056,
CC PubMed:15342467). The masculinization of the germline phenotype (also
CC called the Mog phenotype) is likely due to altered activity of the
CC translational repressor gld-1 in these mutants and the translational
CC repression of 'feminizing' genes including tra-2 and rme-2
CC (PubMed:15342467). RNAi-mediated knockdown in both arms of the
CC syncytial gonad of adult hermaphrodites results in the production of
CC 95% fewer eggs than wild-type and of the eggs produced, all arrest
CC during embryogenesis possibly due to cell division defcts
CC (PubMed:11303786). {ECO:0000269|PubMed:11303786,
CC ECO:0000269|PubMed:15342467, ECO:0000269|PubMed:15514056,
CC ECO:0000269|PubMed:27457958, ECO:0000269|PubMed:27689799}.
CC -!- SIMILARITY: Belongs to the ataxin-2 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY571963; AAS78587.1; -; mRNA.
DR EMBL; BX284603; CAA84697.3; -; Genomic_DNA.
DR EMBL; BX284603; CAI46560.1; -; Genomic_DNA.
DR EMBL; BX284603; CAQ35032.1; -; Genomic_DNA.
DR PIR; T20369; T20369.
DR RefSeq; NP_001021230.1; NM_001026059.2.
DR RefSeq; NP_001021231.1; NM_001026060.2.
DR RefSeq; NP_001122690.1; NM_001129218.2.
DR AlphaFoldDB; G5ED29; -.
DR IntAct; G5ED29; 1.
DR STRING; 6239.D2045.1d; -.
DR EPD; G5ED29; -.
DR PeptideAtlas; G5ED29; -.
DR EnsemblMetazoa; D2045.1a.1; D2045.1a.1; WBGene00000231.
DR EnsemblMetazoa; D2045.1b.1; D2045.1b.1; WBGene00000231.
DR EnsemblMetazoa; D2045.1c.1; D2045.1c.1; WBGene00000231.
DR UCSC; D2045.1b.2; c. elegans.
DR WormBase; D2045.1a; CE37889; WBGene00000231; atx-2. [G5ED29-1]
DR WormBase; D2045.1b; CE37967; WBGene00000231; atx-2. [G5ED29-2]
DR WormBase; D2045.1c; CE42488; WBGene00000231; atx-2. [G5ED29-3]
DR eggNOG; KOG2375; Eukaryota.
DR GeneTree; ENSGT00940000174882; -.
DR PRO; PR:G5ED29; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00000231; Expressed in pharyngeal muscle cell (C elegans) and 6 other tissues.
DR ExpressionAtlas; G5ED29; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0010494; C:cytoplasmic stress granule; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0030953; P:astral microtubule organization; IMP:UniProtKB.
DR GO; GO:0007059; P:chromosome segregation; IMP:UniProtKB.
DR GO; GO:0016048; P:detection of temperature stimulus; IMP:UniProtKB.
DR GO; GO:0040001; P:establishment of mitotic spindle localization; IMP:UniProtKB.
DR GO; GO:0008585; P:female gonad development; IGI:UniProtKB.
DR GO; GO:0051661; P:maintenance of centrosome location; IMP:UniProtKB.
DR GO; GO:0010826; P:negative regulation of centrosome duplication; IMP:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
DR GO; GO:1905833; P:negative regulation of microtubule nucleation; IMP:UniProtKB.
DR GO; GO:1904780; P:negative regulation of protein localization to centrosome; IMP:UniProtKB.
DR GO; GO:0048599; P:oocyte development; IGI:UniProtKB.
DR GO; GO:0030716; P:oocyte fate determination; IMP:UniProtKB.
DR GO; GO:0040038; P:polar body extrusion after meiotic divisions; IMP:UniProtKB.
DR GO; GO:2000196; P:positive regulation of female gonad development; IMP:UniProtKB.
DR GO; GO:1905516; P:positive regulation of fertilization; IGI:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:1905938; P:positive regulation of germ cell proliferation; IMP:UniProtKB.
DR GO; GO:0060903; P:positive regulation of meiosis I; IGI:UniProtKB.
DR GO; GO:0045977; P:positive regulation of mitotic cell cycle, embryonic; IMP:UniProtKB.
DR GO; GO:1903438; P:positive regulation of mitotic cytokinetic process; IMP:UniProtKB.
DR GO; GO:1902846; P:positive regulation of mitotic spindle elongation; IMP:UniProtKB.
DR GO; GO:0060282; P:positive regulation of oocyte development; IMP:UniProtKB.
DR GO; GO:0071539; P:protein localization to centrosome; IGI:UniProtKB.
DR GO; GO:0010824; P:regulation of centrosome duplication; IGI:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IGI:UniProtKB.
DR GO; GO:1905936; P:regulation of germ cell proliferation; IGI:UniProtKB.
DR GO; GO:0009794; P:regulation of mitotic cell cycle, embryonic; IGI:UniProtKB.
DR GO; GO:1903436; P:regulation of mitotic cytokinetic process; IGI:UniProtKB.
DR GO; GO:1904779; P:regulation of protein localization to centrosome; IGI:UniProtKB.
DR GO; GO:0090169; P:regulation of spindle assembly; IGI:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IGI:UniProtKB.
DR GO; GO:0034063; P:stress granule assembly; IBA:GO_Central.
DR InterPro; IPR045117; ATXN2-like.
DR InterPro; IPR009604; LsmAD_domain.
DR InterPro; IPR025852; SM_dom_ATX.
DR PANTHER; PTHR12854; PTHR12854; 1.
DR Pfam; PF14438; SM-ATX; 1.
DR SMART; SM01272; LsmAD; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Cytoplasm; Nucleus;
KW Reference proteome; RNA-binding.
FT CHAIN 1..959
FT /note="Ataxin-2 homolog"
FT /evidence="ECO:0000305"
FT /id="PRO_0000439258"
FT REGION 203..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 501..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..831
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 867..959
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..241
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..528
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..745
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 756..786
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..802
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 867..884
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 895..932
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 933..947
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..325
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_058818"
FT VAR_SEQ 927..930
FT /note="GVNP -> ALKV (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_058819"
FT VAR_SEQ 931..959
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_058820"
SQ SEQUENCE 959 AA; 106041 MW; 4B1C79F10A91F97D CRC64;
MSTPTGLPAL NGDVLSAIND MIGRVIIINT TDKKRYSGVL GAVSQDFDFG MQCVVEITKE
NENNLLRTES ECRDKMVFHY SDIVDFAYVT QEIKKQHAVS KFVTDRQYHG DTPIEGEELQ
EWNGGEEDGL GGSIEDDVVV AGGQTAARRS NNHNNGTGWS VNDMFAANEK MNVVSTFKED
LTQYTTVEVV GTDEDRARAE RLAREIESNS SSKFMANLEN DDDERDLDKI TRQEDFENGN
GRKRNNNSFN QQQQQRRNPN IAPNGQPVNR RAEGLRGDRR NSGSSSANNS RYGAPAAAQQ
NYSQNQQQQQ GQKGYRRQNE ENDWQMAKGK GQNQGHDHSF RQQQKQMLDP RPNNNVKPAD
DKAQSATTAT AAAGGSRVTD LKNWGNEFSI ATAPKDQAPA VPAGNSGSAW NRGPPSSLVA
KGSSNESTPP PTTNGEEAET KKEEAPSTSV DVAAAPVQNV QNDAEKHQED DNVSVTSEND
SVITSKSSSF KFNINAPEFK PRVAPATPTA TTPVQNEYHP QQQPHPAMMA PQQGPPAPGM
GMVPPHMGGP QNQGQPPMMM WQQTGQQQQG GGGYPQNHQF PIQHVPMQGV PGQMYGPGAA
TPVTVAQQPN QQHQVPTSAA GGQNHQLRDG EYREKQPLYM PYGPPQMVPV TSQQFYHSQY
QGQMQQAAPY QMKMMPQQAP QGAYQQRYQQ PQVYMMPPQG QQQQPRYQGP PPPQQQQQQQ
PQQQQFSGEQ SRPQSHPNSQ PTTPGPRGEL PKMSGAPQNG NMQAESSSNA SHSGSTSSQS
GQRSGSPPGA VPPPPPPQQQ HQQQQHPPHH APPHVGAPPP QMMQQQQQHI QQYMVMQGPH
QMHPQIPNYY QQPQQVFYPM IMPQQMPMQQ NQHPQQSLMG ERSDQGFPTS GYFDYRTMPN
YQQQQQQQQQ QMHRQNSLPQ QFQGNQGVNP SGQQSGPPPP PPPSQQGTPR DQQHSQSPP
