ATH1_SCHPO
ID ATH1_SCHPO Reviewed; 791 AA.
AC Q9USW1;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Ataxin-2 homolog {ECO:0000312|PomBase:SPBC21B10.03c};
DE AltName: Full=Pab1-binding protein 1 {ECO:0000305};
DE AltName: Full=Poly(A)-binding protein-binding protein {ECO:0000305};
GN Name=ath1 {ECO:0000312|PomBase:SPBC21B10.03c};
GN ORFNames=SPBC21B10.03c {ECO:0000312|PomBase:SPBC21B10.03c};
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP FUNCTION, INTERACTION WITH MKT1, AND DISRUPTION PHENOTYPE.
RX PubMed=31822915; DOI=10.1093/nar/gkz1157;
RA Taglini F., Chapman E., van Nues R., Theron E., Bayne E.H.;
RT "Mkt1 is required for RNAi-mediated silencing and establishment of
RT heterochromatin in fission yeast.";
RL Nucleic Acids Res. 48:1239-1253(2020).
CC -!- FUNCTION: Involved in post-transcriptional regulation of gene
CC expression, probably by association with mkt1.
CC {ECO:0000269|PubMed:31822915}.
CC -!- SUBUNIT: Interacts with mkt1. {ECO:0000305|PubMed:31822915}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC Note=Localizes at the barrier septum.
CC -!- DISRUPTION PHENOTYPE: Impaired RNAi-mediated heterochromatin silencing.
CC {ECO:0000269|PubMed:31822915}.
CC -!- SIMILARITY: Belongs to the ataxin-2 family. {ECO:0000305}.
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DR EMBL; CU329671; CAB57927.1; -; Genomic_DNA.
DR PIR; T39924; T39924.
DR RefSeq; NP_595684.1; NM_001021579.2.
DR AlphaFoldDB; Q9USW1; -.
DR BioGRID; 277202; 60.
DR IntAct; Q9USW1; 2.
DR STRING; 4896.SPBC21B10.03c.1; -.
DR iPTMnet; Q9USW1; -.
DR MaxQB; Q9USW1; -.
DR PaxDb; Q9USW1; -.
DR PRIDE; Q9USW1; -.
DR EnsemblFungi; SPBC21B10.03c.1; SPBC21B10.03c.1:pep; SPBC21B10.03c.
DR GeneID; 2540677; -.
DR KEGG; spo:SPBC21B10.03c; -.
DR PomBase; SPBC21B10.03c; -.
DR VEuPathDB; FungiDB:SPBC21B10.03c; -.
DR eggNOG; KOG2375; Eukaryota.
DR HOGENOM; CLU_354943_0_0_1; -.
DR InParanoid; Q9USW1; -.
DR OMA; NNGMMNM; -.
DR PRO; PR:Q9USW1; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0032153; C:cell division site; HDA:PomBase.
DR GO; GO:0010494; C:cytoplasmic stress granule; EXP:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0016071; P:mRNA metabolic process; ISO:PomBase.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR GO; GO:0034063; P:stress granule assembly; IBA:GO_Central.
DR InterPro; IPR045117; ATXN2-like.
DR InterPro; IPR009604; LsmAD_domain.
DR PANTHER; PTHR12854; PTHR12854; 1.
DR Pfam; PF06741; LsmAD; 1.
DR SMART; SM01272; LsmAD; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Reference proteome; Translation regulation.
FT CHAIN 1..791
FT /note="Ataxin-2 homolog"
FT /id="PRO_0000450800"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 60..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 112..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 326..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 613..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 707..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..311
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..411
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 710..772
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..791
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 791 AA; 85524 MW; 02579D93CF5D68B8 CRC64;
MATRSVSMKQ TSQRAASPNK TQGAKKWSAV AARGSKIAQS ATNDHRNVES IKVVPENRVR
GGVAAKATDS SSNVTSLASS EENVSSVSGS AKSNNSQQRV WKTDVAISAE KRTETRQREL
RRWMPDPEDA GVPLAGLEES TDNVEWDQFA TNEKLFGVKS HFDEDLYTSR IDRSHPKYKE
KEQEADRIAK EIEGTVTNNI HIAEERGLKV DDSGLDEEDL YSGVHRSIDV VRNYTRSNAY
NKNNKDQKPK NHEAPHQHPQ QKVVPPDDPA IVSHRHLALP RAPGPDSRAA ERFFNARRKA
GPLSRREKEG QIKEFMQFSQ SLKIGSLDSK QPSSTKSVAE VKVADEKQLP DASSQATPAD
SKEPRKEEAE KPVTSATEVS SEKVEKVDGN TSSPSKEEEK PSTEPEKPSV VTQRKETTGT
KLGTKLNAKA ISFKPNVAAP VFTPGKFTIP SKPAPVNASR PMMPQQSNNS EASIPSTTPQ
SPSVVSNGEN KPSSSPVFFN GPVSSEKEPI LDNFNVFKNV GEEHQGAEQI DKPFSCPPTW
NTGPNSLQQT IANSRPEGNS GSAKKAAAAN PMIPSIVLPN SAMPSAMPMY PTPTMPYIPV
GYPVPGYTPY MRNPSQHTSV APSPNGTPTS GNSSTVGSPM IGYMAPQFIP PYAMPQFPPS
GNGRGASAPA TYFVPQMGGM MAYTMNGVPP MYGQYAPNNG MMNMHYPMYG DSRRSNSQRS
FNSSNGKRSN VHKNNNASNT FSHSNASTSS SLNAAPNTTA KSSSQTAPPV SKGDATEKTE
KDASANQEAK P
