STU1_ASHGO
ID STU1_ASHGO Reviewed; 1475 AA.
AC Q75B70;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Protein STU1;
GN Name=STU1; OrderedLocusNames=ADL298C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 364; 406; 410; 853-856; 882;
RP 962; 967; 974-987; 990; 998-999 AND 1002.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
CC -!- FUNCTION: Microtubule binding protein that promotes the stabilization
CC of dynamic microtubules. Required for mitotic spindle formation (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with microtubules. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Nucleus
CC {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CLASP family. {ECO:0000305}.
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DR EMBL; AE016817; AAS51622.2; -; Genomic_DNA.
DR RefSeq; NP_983798.2; NM_209151.2.
DR AlphaFoldDB; Q75B70; -.
DR SMR; Q75B70; -.
DR STRING; 33169.AAS51622; -.
DR PRIDE; Q75B70; -.
DR EnsemblFungi; AAS51622; AAS51622; AGOS_ADL298C.
DR GeneID; 4619933; -.
DR KEGG; ago:AGOS_ADL298C; -.
DR eggNOG; ENOG502QT5T; Eukaryota.
DR HOGENOM; CLU_256206_0_0_1; -.
DR InParanoid; Q75B70; -.
DR OMA; TFWYYYK; -.
DR Proteomes; UP000000591; Chromosome IV.
DR GO; GO:0005881; C:cytoplasmic microtubule; IBA:GO_Central.
DR GO; GO:0005815; C:microtubule organizing center; IBA:GO_Central.
DR GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
DR GO; GO:1990023; C:mitotic spindle midzone; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005876; C:spindle microtubule; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0060172; P:astral microtubule depolymerization; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0090307; P:mitotic spindle assembly; IBA:GO_Central.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR024395; CLASP_N_dom.
DR Pfam; PF12348; CLASP_N; 1.
DR SUPFAM; SSF48371; SSF48371; 2.
PE 3: Inferred from homology;
KW Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Microtubule; Mitosis;
KW Nucleus; Reference proteome.
FT CHAIN 1..1475
FT /note="Protein STU1"
FT /id="PRO_0000272281"
FT REGION 870..913
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1113..1134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 871..893
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1118..1134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1475 AA; 166314 MW; 49AD5F45BDB71BF8 CRC64;
MEEPRVHNLE KLMDEGVAGI EQLQILTAFK THVKKELVRD DSIERYFDAL VRFLGQPVED
RKVQQLGHSS LCYLIKRVAM QQPGRFQGAR IRDLVRVVLL QEQLQERKVW GSAVKSLEAI
YLCKPQAFEA ELASICAATR GSDRTKCLLF MDELIQLQQM NNRNPMEVVN RFVDLWVDVL
NESDPGCSKR DIELIHDILK KYFNEAMLQQ FAERVVNTRS LKHFMHTEHA APSSAQTTSS
MPSGPFDVDE ELTRVMEELP PNVVNSNIGE ARDYLSFEHV VKDLEHITVA FQAIKETEHN
WKQRQEGIIT LRKIVNGNVS RQFPDEFIQA CRDLNIADCI SKAALSLRTT LSSHSCHLIK
EMAFKLGPLL EPLLDVLFVP LRSLLSATKK ISSQTAFATA AILLCTAPYH NRLFQQCIAL
SRDKNVSPRT FAAVFLRIYI IRFHRRLEHS SVLVEEWLHK GLTDPQTQVR EAMRVTLWYW
YVPNAQSAKK VLDSMPHQMK RIIEGSIPTY LNIEYHVTAS VSSNESSRRS SFGVRRYPSY
AAPTQSSNLQ KLAANSLGGS ANVRSLSENT NRHLTTYTSL AKKSLATRHE SLSPRVASSG
LISSAGAANL SSENLELTEE LTSNHSNTLL KKYLNTNEPA VIRKSEGEPT GDLESMYSHL
SSTTLQEKQQ GLLFLKNLLL LKAPLDIAKL NPLLVQLSIQ SPKSFKDLLT LASFHPLIPL
ANLIELFAIN DLPTNVLLDE FSSTDLLETV IHSFQTFFPD HHDQLFLYYV KYRSVIFNYC
FGIMIDLLSG DFAFSEGSTL FREVCTRIIE ACGNDFNMEK YYTLISILYR ADKSQFVELL
RDAPVSSKFK IANELQRCDS TFNLHSIMSR ESTAESHHSD PNQQYKDGAH GGDARDANGT
SNSSSDSDNE PDLESTKHLL EMTMVNPIGL GCVENVLQSH IHAYKQDQQH QDPIAEKSLS
TVAEVNDEDG DGSTTTQMKL MGANTTEPSN ESDKDKTSDI VAESMRGTDD PNYAKLCAID
SALIDSEDEP ELNNFGGLKG LTEMTKVVSI YEKLDGDEDV EMVDDEKFKD PVEQENQETG
LDEIFRDEKH DQSVKFNDIP RIIDVNKSWD RYDGESIEDT SGNTSHGTDE NRPASFGTVS
ELVRKEMEKS PTLPLNEEDS KLLSDGINEI ELKHKDDPFV RDSEDCENGT PQDRSNFLSC
KQHIDILGAL PDNSLTAFEL GLLEILDVSD MDANRILETV NTIQNSRLRS ADVSRIVGAI
VSHCTDPLLH WLTDSNGLQR LWSMLTALST ADGFSDSYKC VVLYTALLIA NSQLSSSHLS
TDELSDAWAF ALRELSKLSS YNNETYIACC ELRETLIEHY SSSYLPQLLE SAIKELNVAE
DRVRITFLLQ TLSDALDHMN TLLSLEVLGS MSSLLQQFVT NDFTEWRYHS IKLLAQIYGI
LVARNSPASY IRSMFSILRQ PEFDLVKSYY TMDHN
