ATX2_DROPS
ID ATX2_DROPS Reviewed; 1121 AA.
AC Q29A33;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 2.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Ataxin-2 homolog;
GN Name=Atx2 {ECO:0000250|UniProtKB:Q8SWR8}; ORFNames=GA18704;
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MV2-25 / Tucson 14011-0121.94;
RX PubMed=15632085; DOI=10.1101/gr.3059305;
RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA Weinstock G.M., Gibbs R.A.;
RT "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT gene, and cis-element evolution.";
RL Genome Res. 15:1-18(2005).
CC -!- FUNCTION: Regulator of actin filament formation, though it does not
CC directly assemble with actin filaments. Required for oocyte
CC specification and oocyte positioning in the female germline. Also
CC required for normal eye development and bristle morphology (By
CC similarity). {ECO:0000250|UniProtKB:Q8SWR8}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8SWR8}.
CC -!- SIMILARITY: Belongs to the ataxin-2 family. {ECO:0000305}.
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DR EMBL; CM000070; EAL27518.2; -; Genomic_DNA.
DR RefSeq; XP_001358379.2; XM_001358342.4.
DR AlphaFoldDB; Q29A33; -.
DR SMR; Q29A33; -.
DR STRING; 7237.FBpp0282317; -.
DR EnsemblMetazoa; FBtr0283879; FBpp0282317; FBgn0078704.
DR GeneID; 4801256; -.
DR KEGG; dpo:Dpse_GA18704; -.
DR eggNOG; KOG2375; Eukaryota.
DR HOGENOM; CLU_282884_0_0_1; -.
DR InParanoid; Q29A33; -.
DR OMA; MRVYQDQ; -.
DR ChiTaRS; Atx2; fly.
DR Proteomes; UP000001819; Chromosome 2.
DR Bgee; FBgn0078704; Expressed in insect adult head and 2 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0022416; P:chaeta development; ISS:UniProtKB.
DR GO; GO:0048749; P:compound eye development; ISS:UniProtKB.
DR GO; GO:0009994; P:oocyte differentiation; ISS:UniProtKB.
DR GO; GO:0030833; P:regulation of actin filament polymerization; ISS:UniProtKB.
DR InterPro; IPR045117; ATXN2-like.
DR InterPro; IPR009604; LsmAD_domain.
DR InterPro; IPR025852; SM_dom_ATX.
DR PANTHER; PTHR12854; PTHR12854; 1.
DR Pfam; PF06741; LsmAD; 1.
DR Pfam; PF14438; SM-ATX; 1.
DR SMART; SM01272; LsmAD; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Developmental protein; Phosphoprotein; Reference proteome.
FT CHAIN 1..1121
FT /note="Ataxin-2 homolog"
FT /id="PRO_0000311704"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1039..1076
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..458
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..528
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..682
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..722
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..771
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 772..792
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..872
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 878..892
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1047..1070
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1121 AA; 120519 MW; FEBC3AECEE28BB96 CRC64;
MNNNSKRKTR PSGGGGGGGA SGGISRYNAN DNSLRPANNK SGAAGNSAGA GAGTGGTAIR
PVAQGVYNNT FFMHSATALV GSVVEVVLRS GNIYEGVFRT FSGNFDIALE LPACIKSKNL
PEEGKVPKHI IFPADTVVKI VAKDFDSQYA TAGAFKTDEA ISDKCNGARL DEKELEPWDS
GANGDIDIEL DGAANGWDAN EMFRKNENTF GVTSTFDDSL ATYTIPLDKG DSLEFKEAEA
KAEKLAAEIE NNPTCRDRLD LENGDEEALF AAVERPEQDH RRDGDRERER NDRDREREER
DRDRDRDRGN KPPRGAGDFQ LRETMSSDRY ITKQTRGPQM SHVSMSSQGG GGGGRDRDNG
LMMPGVISGG GAGQGGATQS AAVLLLAGGL KASGPASSAN AAGMDASGKY SMVKRKTVTQ
GGKVMRGNVP PNSSGGGNIS AVQGGNGNPV GQSKGGYQPT MVMQNQYAYQ GNSQIMHGSS
QYRNPSHMSG GPSKLNGDAN ANTNKPLPQR QIRQYQGSQS NSLNYGGEPQ PQMGKPMHSS
HGGHPGQNSN SPPLQTGGQP QQQQQQQQQQ QQQQAPQQQQ HQNMAPQGQQ PQPQRQMRSR
DNQLQDLRQF GQDFQLAPTN NSPPQQQPQQ PQQQQQQQQV QVQVQAQVQQ QQQRALLQSA
SPPQQQSQQQ QQQQQQQHVP MQHQGPPPHL HQAALSQPHY VPQPQQQQPQ PQQQPPPPQQ
QQQQQHVPLH LQQKAQQPPQ QQQQLVETQH QLVPKQHQQP PAQQQQPQLA PEPSQQPLPL
YHPMPPPQTS PVVITSPVLL EAPPPQILTA QQPPQQQQLA ATPKPDASPA PGSNTTTPTG
IVSTPTTAAA SSAGSEKSTP AAASSGATSG TAAAAVGATG ATGSTGSTPV VKKHVLNPSA
KPFTPRAGAG TPNPSRPHTP QTPVPMPGIY TTTGTHVPAA ATNQPIYVVQ QQHPFPPPTH
PQAGQPPRLR RNNYAPMGAS QMHVSATTAT GQPLMAAGPM TQFIQYPHAP QQHFQSQGYA
PMPMRLYPDQ QPQLQFLTQT PQSTTPSPGQ PHQPFHPPPQ PSPAGGGPQP AYTPPTQQTY
QLMCLHSQHV LPNPYFQPQP TPHHAPQNPQ YQIVMQQHHA Q
