ACT_SCHPO
ID ACT_SCHPO Reviewed; 375 AA.
AC P10989; Q10288;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Actin;
GN Name=act1; Synonyms=cps8; ORFNames=pi012, SPBC32H8.12c;
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 [GENOMIC DNA].
RX PubMed=3309892; DOI=10.1093/nar/15.18.7369;
RA Mertins P., Gallwitz D.;
RT "A single intronless action gene in the fission yeast Schizosaccharomyces
RT pombe: nucleotide sequence and transcripts formed in homologous and
RT heterologous yeast.";
RL Nucleic Acids Res. 15:7369-7379(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF GLY-273.
RC STRAIN=972 / ATCC 24843;
RX PubMed=8774852; DOI=10.1016/0014-5793(96)00819-8;
RA Ishiguro J., Kobayashi W.;
RT "An actin point-mutation neighboring the 'hydrophobic plug' causes defects
RT in the maintenance of cell polarity and septum organization in the fission
RT yeast Schizosaccharomyces pombe.";
RL FEBS Lett. 392:237-241(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=10620777;
RX DOI=10.1002/(sici)1097-0061(20000115)16:1<71::aid-yea505>3.0.co;2-5;
RA Machida M., Yamazaki S., Kunihiro S., Tanaka T., Kushida N., Jinno K.,
RA Haikawa Y., Yamazaki J., Yamamoto S., Sekine M., Oguchi A., Nagai Y.,
RA Sakai M., Aoki K., Ogura K., Kudoh Y., Kikuchi H., Zhang M.Q., Yanagida M.;
RT "A 38 kb segment containing the cdc2 gene from the left arm of fission
RT yeast chromosome II: sequence analysis and characterization of the genomic
RT DNA and cDNAs encoded on the segment.";
RL Yeast 16:71-80(2000).
RN [4]
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-202 AND SER-324, 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: Actins are highly conserved proteins that are involved in
CC various types of cell motility and are ubiquitously expressed in all
CC eukaryotic cells.
CC -!- INTERACTION:
CC P10989; O14188: rng2; NbExp=3; IntAct=EBI-617028, EBI-1152490;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
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DR EMBL; Y00447; CAA68501.1; -; Genomic_DNA.
DR EMBL; D84318; BAA12315.1; -; Genomic_DNA.
DR EMBL; AB004534; BAA21389.1; -; Genomic_DNA.
DR EMBL; CU329671; CAC37502.1; -; Genomic_DNA.
DR PIR; A26836; A26836.
DR RefSeq; NP_595618.1; NM_001021513.2.
DR AlphaFoldDB; P10989; -.
DR SMR; P10989; -.
DR BioGRID; 276589; 43.
DR IntAct; P10989; 4.
DR MINT; P10989; -.
DR STRING; 4896.SPBC32H8.12c.1; -.
DR iPTMnet; P10989; -.
DR MaxQB; P10989; -.
DR PaxDb; P10989; -.
DR PRIDE; P10989; -.
DR EnsemblFungi; SPBC32H8.12c.1; SPBC32H8.12c.1:pep; SPBC32H8.12c.
DR GeneID; 2540051; -.
DR KEGG; spo:SPBC32H8.12c; -.
DR PomBase; SPBC32H8.12c; act1.
DR VEuPathDB; FungiDB:SPBC32H8.12c; -.
DR eggNOG; KOG0676; Eukaryota.
DR HOGENOM; CLU_027965_0_2_1; -.
DR InParanoid; P10989; -.
DR OMA; FHTTAER; -.
DR PhylomeDB; P10989; -.
DR Reactome; R-SPO-114608; Platelet degranulation.
DR Reactome; R-SPO-196025; Formation of annular gap junctions.
DR Reactome; R-SPO-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-SPO-5626467; RHO GTPases activate IQGAPs.
DR Reactome; R-SPO-5663213; RHO GTPases Activate WASPs and WAVEs.
DR Reactome; R-SPO-8856828; Clathrin-mediated endocytosis.
DR PRO; PR:P10989; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0030479; C:actin cortical patch; IDA:PomBase.
DR GO; GO:0005884; C:actin filament; TAS:PomBase.
DR GO; GO:0032153; C:cell division site; HDA:PomBase.
DR GO; GO:0051286; C:cell tip; HDA:PomBase.
DR GO; GO:0031011; C:Ino80 complex; IDA:PomBase.
DR GO; GO:0043332; C:mating projection tip; IDA:PomBase.
DR GO; GO:0120106; C:mitotic actomyosin contractile ring, distal actin filament layer; IDA:PomBase.
DR GO; GO:0120105; C:mitotic actomyosin contractile ring, intermediate layer; IDA:PomBase.
DR GO; GO:0120104; C:mitotic actomyosin contractile ring, proximal layer; IDA:PomBase.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:PomBase.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:PomBase.
DR GO; GO:0005628; C:prospore membrane; IDA:PomBase.
DR GO; GO:0000812; C:Swr1 complex; IDA:PomBase.
DR GO; GO:0003786; F:actin lateral binding; IPI:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006338; P:chromatin remodeling; IDA:PomBase.
DR GO; GO:0006897; P:endocytosis; IMP:PomBase.
DR GO; GO:1902404; P:mitotic actomyosin contractile ring contraction; EXP:PomBase.
DR InterPro; IPR004000; Actin.
DR InterPro; IPR020902; Actin/actin-like_CS.
DR InterPro; IPR004001; Actin_CS.
DR InterPro; IPR043129; ATPase_NBD.
DR PANTHER; PTHR11937; PTHR11937; 1.
DR Pfam; PF00022; Actin; 1.
DR PRINTS; PR00190; ACTIN.
DR SMART; SM00268; ACTIN; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS00406; ACTINS_1; 1.
DR PROSITE; PS00432; ACTINS_2; 1.
DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Cytoskeleton; Nucleotide-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..375
FT /note="Actin"
FT /id="PRO_0000089007"
FT MOD_RES 202
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MUTAGEN 273
FT /note="G->D: Causes a defect in the maintenance of cell
FT polarity and septum organization."
FT /evidence="ECO:0000269|PubMed:8774852"
SQ SEQUENCE 375 AA; 41765 MW; 372C0B2CDBAE1B68 CRC64;
MEEEIAALVI DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH HGIMVGMGQK DSYVGDEAQS
KRGILTLKYP IEHGIVNNWD DMEKIWHHTF YNELRVAPEE HPCLLTEAPL NPKSNREKMT
QIIFETFNAP AFYVAIQAVL SLYASGRTTG IVLDSGDGVT HTVPIYEGYA LPHAIMRLDL
AGRDLTDYLM KILMERGYTF STTAEREIVR DIKEKLCYVA LDFEQELQTA AQSSSLEKSY
ELPDGQVITI GNERFRAPEA LFQPSALGLE NAGIHEATYN SIMKCDVDIR KDLYGNVVMS
GGTTMYPGIA DRMQKEIQAL APSSMKVKIV APPERKYSVW IGGSILASLS TFQQMWISKQ
EYDESGPGIV YRKCF
