ATX2_DICDI
ID ATX2_DICDI Reviewed; 1103 AA.
AC Q55DE7;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Ataxin-2 homolog;
GN Name=atxn2; ORFNames=DDB_G0269682;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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; AAFI02000005; EAL72191.1; -; Genomic_DNA.
DR RefSeq; XP_646184.1; XM_641092.1.
DR AlphaFoldDB; Q55DE7; -.
DR STRING; 44689.DDB0237977; -.
DR PaxDb; Q55DE7; -.
DR PRIDE; Q55DE7; -.
DR EnsemblProtists; EAL72191; EAL72191; DDB_G0269682.
DR GeneID; 8617136; -.
DR KEGG; ddi:DDB_G0269682; -.
DR dictyBase; DDB_G0269682; atxn2.
DR eggNOG; KOG2375; Eukaryota.
DR HOGENOM; CLU_282930_0_0_1; -.
DR InParanoid; Q55DE7; -.
DR OMA; MMMHQNS; -.
DR PRO; PR:Q55DE7; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0010494; C:cytoplasmic stress granule; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0034063; P:stress granule assembly; IBA:GO_Central.
DR InterPro; IPR009818; Ataxin-2_C.
DR InterPro; IPR045117; ATXN2-like.
DR InterPro; IPR009604; LsmAD_domain.
DR InterPro; IPR025852; SM_dom_ATX.
DR PANTHER; PTHR12854; PTHR12854; 2.
DR Pfam; PF06741; LsmAD; 1.
DR Pfam; PF07145; PAM2; 1.
DR Pfam; PF14438; SM-ATX; 1.
DR SMART; SM01272; LsmAD; 1.
PE 3: Inferred from homology;
KW Coiled coil; Reference proteome.
FT CHAIN 1..1103
FT /note="Ataxin-2 homolog"
FT /id="PRO_0000363972"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 615..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 901..920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 930..1103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 258..287
FT /evidence="ECO:0000255"
FT COILED 366..403
FT /evidence="ECO:0000255"
FT COILED 691..730
FT /evidence="ECO:0000255"
FT COMPBIAS 26..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..693
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..736
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..763
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 943..963
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 973..988
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1053..1086
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1103 AA; 121136 MW; ACB31CD0BBDB8056 CRC64;
MSQSKDKKKF VGGGGGGGGN NSGGGGYGSP KHNNNNNNRN SSNNKSPHQS HHNQQHHQQQ
QQQQQQQQQQ QQQPFDSLTA MKERTVFMSM SLVGQNVSVT LKNGDVYEGI LHTTSTSTGS
SGGGWGVALK MARKKDTNNR VITTLPLPLV IIEAKDFLQI TATGVVLDHY RDSFMNRDQQ
SFITDTELSG FDGNLKEREL TPWTPDPSVG ESLDDFAANS EAKKPANWDQ FETNEKLFGV
RTTYEEEIYT TRLDRDSEFY KINQSVAEKK AQEIENEKSG NIHLLEERGF VEGADYDEEE
RYSSVVRKGL LPTSTTSTTT SPPTQNPTPS SSVYIPPSKR NNNNNTPSTP SVTSPPIVDK
KHQQTHQDKK QTQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ QTQPTTTATA TASTSTSTTT
TTNESPSSSS TSSTPSTPST PKNITTTTAT TSTNNTPTAT NTNVNSPLGD RESPTISKLR
LHQSTIDQDV MGSPRENLSP RSVAYTRYRQ ILSEPTNKSM NKSGSNISTT PVNGSGNVGP
NGTPLLSSVH SDQAPKSPVP TIVSNHGLVK ALSLELATPT VPEKFVNDFN NFKLKINNVD
RGSETQGLKS FSSNLVIKSK SRPGSPLIGS GSPRPTPTQL SLSGSSTSTN TSTTSPPTTN
TTTTTTTATN STTPSTTEDD KSTTTPITTT ILTENKSDDK EKEKEKEKEK VDEKEKEKEK
EKSDEKDKDQ SSTLVEKKDE SSSSSNTTTT TTNTTNNNNN NTTTVTKLSK LKLNPNAKEF
VPVVVNKPQP SFKSTTESNT DSVTPINEIY YDSMRKRQLQ PESPDQVSLY WVDPFYPRYE
EDPYAAAYQM RAHHHMVGHQ PPPQLQFNPQ FYSQQGHPQL QPHHHMVPPQ LQQVPPGVNV
HTMKPPGSLQ PGGGGVVQPQ GIVQPQGIVQ PQGGVVQPSA GGAPKTMYQQ QQQQQQQTGQ
PGGPMGVQRG GHLPPQQQPQ QQQQQPPPQF IQGIPPGANL VISNGPPNQP FVFQGAHPPY
AVPHPQYPMP PQGIQGGNKR FYQPPPQGYP QVQPMIIPQQ GQVVSQNSPQ QDSPSNRLNQ
QVPPYSYMTH PPRGYHPNEN QYH