STU1_SCHPO
ID STU1_SCHPO Reviewed; 1462 AA.
AC O42874;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Protein peg1;
GN Name=peg1; ORFNames=SPAC3G9.12;
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 FUNCTION, INTERACTION WITH DHC1; MAL3 AND TEA1, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF LEU-747.
RX PubMed=16951255; DOI=10.1101/gad.381306;
RA Grallert A., Beuter C., Craven R.A., Bagley S., Wilks D., Fleig U.,
RA Hagan I.M.;
RT "S. pombe CLASP needs dynein, not EB1 or CLIP170, to induce microtubule
RT instability and slows polymerization rates at cell tips in a dynein-
RT dependent manner.";
RL Genes Dev. 20:2421-2436(2006).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-599 AND SER-1221, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Microtubule binding protein that regulates the stability of
CC dynamic microtubules. Required for mitotic spindle formation.
CC {ECO:0000269|PubMed:16951255}.
CC -!- SUBUNIT: Interacts with microtubules (By similarity). Interacts with
CC dhc1, mal3 and tea1. {ECO:0000250, ECO:0000269|PubMed:16951255}.
CC -!- INTERACTION:
CC O42874; Q10113: mal3; NbExp=4; IntAct=EBI-1112382, EBI-1002268;
CC O42874; P79065: tip1; NbExp=4; IntAct=EBI-1112382, EBI-1102463;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:16951255}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:16951255}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, spindle pole body {ECO:0000269|PubMed:16951255}.
CC Note=Colocalizes with cytoplasmic microtubules and associates with the
CC mitotic spindle throughout mitosis.
CC -!- SIMILARITY: Belongs to the CLASP family. {ECO:0000305}.
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DR EMBL; CU329670; CAA15921.1; -; Genomic_DNA.
DR PIR; T11648; T11648.
DR RefSeq; NP_594084.1; NM_001019501.2.
DR AlphaFoldDB; O42874; -.
DR BioGRID; 279821; 20.
DR IntAct; O42874; 3.
DR STRING; 4896.SPAC3G9.12.1; -.
DR iPTMnet; O42874; -.
DR MaxQB; O42874; -.
DR PaxDb; O42874; -.
DR PRIDE; O42874; -.
DR EnsemblFungi; SPAC3G9.12.1; SPAC3G9.12.1:pep; SPAC3G9.12.
DR GeneID; 2543399; -.
DR KEGG; spo:SPAC3G9.12; -.
DR PomBase; SPAC3G9.12; peg1.
DR VEuPathDB; FungiDB:SPAC3G9.12; -.
DR eggNOG; ENOG502QT5T; Eukaryota.
DR HOGENOM; CLU_259521_0_0_1; -.
DR InParanoid; O42874; -.
DR OMA; IHGCLLW; -.
DR PRO; PR:O42874; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005881; C:cytoplasmic microtubule; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0000776; C:kinetochore; IDA:PomBase.
DR GO; GO:0005875; C:microtubule associated complex; IDA:PomBase.
DR GO; GO:0015630; C:microtubule cytoskeleton; HDA:PomBase.
DR GO; GO:0005815; C:microtubule organizing center; IBA:GO_Central.
DR GO; GO:0072686; C:mitotic spindle; IDA:PomBase.
DR GO; GO:1990023; C:mitotic spindle midzone; IDA:PomBase.
DR GO; GO:0044732; C:mitotic spindle pole body; HDA:PomBase.
DR GO; GO:0005635; C:nuclear envelope; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005876; C:spindle microtubule; IDA:PomBase.
DR GO; GO:0099070; C:static microtubule bundle; IDA:PomBase.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0060172; P:astral microtubule depolymerization; IMP:PomBase.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0001578; P:microtubule bundle formation; IMP:PomBase.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0090307; P:mitotic spindle assembly; IMP:PomBase.
DR Gene3D; 1.25.10.10; -; 3.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR024395; CLASP_N_dom.
DR InterPro; IPR034085; TOG.
DR Pfam; PF12348; CLASP_N; 2.
DR SMART; SM01349; TOG; 2.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Coiled coil; Cytoplasm; Cytoskeleton;
KW Microtubule; Mitosis; Phosphoprotein; Reference proteome.
FT CHAIN 1..1462
FT /note="Protein peg1"
FT /id="PRO_0000272294"
FT REGION 528..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 838..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1342..1367
FT /evidence="ECO:0000255"
FT COMPBIAS 528..551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 842..867
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 869..928
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 599
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 1221
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MUTAGEN 747
FT /note="L->F: In allele peg1.1; abrogates bipolar spindle
FT formation at 36 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:16951255"
SQ SEQUENCE 1462 AA; 164095 MW; A91BE37CE4595706 CRC64;
MADKDAQDFL KFLKSNASTD EKTRCLDTLR SFFNKNNIPN ADLGLFVECF RLALTTVNPL
LLRSSVACFE TFLRRLRAQY PTWLKFRVPM LKNLVIDHIA SRDLQKRVLN ILIDLWHFNP
SEIEKSLIHL STTSKSAETR IQCFKWFVLA HNAHLSFDVK SLRPALYINL ENANPSVREE
AKEVLLLIYK NLSTSAKMQF ITDVETTSGL RREILQSLVE ELSLISSSSE VIIVQNSASS
FQPAPFMTAV ATLYPGVELE NVKPLLANFS KQLEQDSASM LPAFEGRETE QNWSVRQDSV
LRLRQYLRGN ACIDYLPELL SVLKTLLPGI LLALLSLRTT LSSSAIQLIK EMAIILKSNI
DPFLELILPN LLKVCSVTKK LASQAANVTF AAILVNCGVL SRNLSFISLA AHDTNAQLRV
FSSNWIFMLI SLSPELKNLA SLQTNLKAFE KLICRGLADS NSQVREVYRK SFWKLSEYFP
SVQEELTNTL EPSVLKQLHL ANPNRQAASF NFSGPKRAPI RPLSNLRSFS KSQKEETSSN
SSNSSGTRRL GLPQRATPAS RERVLPYTRS QAFHSTSLPP SLPSGHSPSI AIPSKRSVSA
TIKDESKTFE LLKNIQRKYE LILSGSSVDL PSAEFLSSNL TDALYSGSSI CYSLIFSHSL
LDLTFQYVDI ASLLSQFLLC VYDPSNVGHS FALASFPYVK SHYDAHKYFP IVFDVLMNIS
NMAPHVKVFP FNTNQKRLII HGCLLWLKEI SDTKLNQLEN KPFFVTDKLR YYSSKILAMT
AKTKLTSKNW IPLSGLLFSL RAHDTFMFDG LLDRLNEESR TKLVSSWSKQ DAFDYSKSST
HQEHLSKNLP TLNTSSSSNS SQTDLLVPHG KGETKETEMQ SPIESKEGLL SKDTHIESPQ
GTSLEKENEE EGKNPVESNC SEESLDDHNI DQTLVNKKET LAQDSESLLQ KNNALNEKGF
ENQFGLSSSA AKVLNKDTLD HVSGPISNSV SSSFKDFTRT PFKEINGERE TGFELTSYVN
ALSKKDDINV QKTENVDESV GLNAMFMDNV NQDSLNSVDQ SSGKDKLLLT SSTPNKPTTF
FMPANEEILG SPAKDYDIHD QSYSVHELHS ENMRENVGQS SLIYNNRDYM NTPMNDFSLS
FSEIKGGILE SPVESPMTGT ISPIDADESV LHDIPAYESL NKSESNKYQE QAYSTPLHHT
LNVLPKNKWI LSRMHKMENG SPINVDKNLD DAVAALEAAV KELNDGSVNT KTLKFCIKVC
KETPSMLYHS HGLLPAILHY IESNNSAMHI SDCLILLHEF LVQGYQGVDM HTYHNIICIL
IEKAEKCKDE PVILAGIEDN ITLIAEIADL QGLYEFTQQR LQSLNTETGE KSAPLLLMLL
SAILMRLKDL EFLETKDLLR HVVLKYIDHT NPEIRKATFN VCLAVNTIVN NVDETFSILG
GLNEGQRLLF MHYLKMKSDE KN
