VRP1_SCHPO
ID VRP1_SCHPO Reviewed; 309 AA.
AC Q9P6R1;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Verprolin {ECO:0000312|EMBL:CAB89884.1};
GN Name=vrp1 {ECO:0000312|EMBL:CAB89884.1}; ORFNames=SPBC13E7.09;
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] {ECO:0000312|EMBL:CAB89884.1}
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] {ECO:0000305}
RP SUBCELLULAR LOCATION, INTERACTION WITH WSP1, AND DISRUPTION PHENOTYPE.
RX PubMed=12939254; DOI=10.1083/jcb.200305012;
RA Carnahan R.H., Gould K.L.;
RT "The PCH family protein, Cdc15p, recruits two F-actin nucleation pathways
RT to coordinate cytokinetic actin ring formation in Schizosaccharomyces
RT pombe.";
RL J. Cell Biol. 162:851-862(2003).
RN [3] {ECO:0000305}
RP FUNCTION, INTERACTION WITH MYO1 AND ACTIN MONOMERS, SUBCELLULAR LOCATION,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=16087707; DOI=10.1083/jcb.200502053;
RA Sirotkin V., Beltzner C.C., Marchand J.-B., Pollard T.D.;
RT "Interactions of WASp, myosin-I, and verprolin with Arp2/3 complex during
RT actin patch assembly in fission yeast.";
RL J. Cell Biol. 170:637-648(2005).
RN [4] {ECO:0000305}
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).
CC -!- FUNCTION: Involved in cytoskeletal organization and cellular growth.
CC May exert its effects on the cytoskeleton directly, or indirectly via
CC proline-binding proteins such as profilin or proteins possessing SH3
CC domains. Plays a role in actin patch assembly by enhancing the ability
CC of myo1 to stimulate actin polymerization by the Arp2/3 complex.
CC {ECO:0000269|PubMed:16087707}.
CC -!- SUBUNIT: Interacts with wsp1. Interacts with myo1 (via SH3 domain).
CC Interacts with actin monomers. {ECO:0000269|PubMed:12939254,
CC ECO:0000269|PubMed:16087707}.
CC -!- INTERACTION:
CC Q9P6R1; O36027: wsp1; NbExp=3; IntAct=EBI-1148131, EBI-1148109;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:12939254, ECO:0000269|PubMed:16087707,
CC ECO:0000269|PubMed:16823372}. Note=Localized to patches at the tips of
CC growing interphase cells. These patches form prior to patches of myo1,
CC but in cells lacking myo1, they are less intense and may be short
CC lived. Detected in the medial region of mitotic cells, and this
CC requires cdc15.
CC -!- DISRUPTION PHENOTYPE: Grows normally at 25 degrees Celsius. Displays
CC morphological defects at high temperatures and is cold sensitive. At 18
CC degrees Celsius, becomes rounded, characteristic of a polarity defect.
CC Synthetically lethal with deletion of myo1.
CC {ECO:0000269|PubMed:12939254, ECO:0000269|PubMed:16087707}.
CC -!- SIMILARITY: Belongs to the verprolin family. {ECO:0000255}.
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DR EMBL; CU329671; CAB89884.1; -; Genomic_DNA.
DR RefSeq; NP_596264.1; NM_001022184.2.
DR AlphaFoldDB; Q9P6R1; -.
DR BioGRID; 276638; 82.
DR IntAct; Q9P6R1; 3.
DR STRING; 4896.SPBC13E7.09.1; -.
DR iPTMnet; Q9P6R1; -.
DR MaxQB; Q9P6R1; -.
DR PaxDb; Q9P6R1; -.
DR EnsemblFungi; SPBC13E7.09.1; SPBC13E7.09.1:pep; SPBC13E7.09.
DR PomBase; SPBC13E7.09; vrp1.
DR VEuPathDB; FungiDB:SPBC13E7.09; -.
DR eggNOG; KOG4462; Eukaryota.
DR HOGENOM; CLU_049614_0_0_1; -.
DR InParanoid; Q9P6R1; -.
DR OMA; QFRTMRP; -.
DR PRO; PR:Q9P6R1; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0030479; C:actin cortical patch; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0031097; C:medial cortex; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0035840; C:old growing cell tip; IDA:PomBase.
DR GO; GO:0003785; F:actin monomer binding; IDA:PomBase.
DR GO; GO:0000147; P:actin cortical patch assembly; IGI:PomBase.
DR GO; GO:0006897; P:endocytosis; ISO:PomBase.
DR GO; GO:2000601; P:positive regulation of Arp2/3 complex-mediated actin nucleation; IDA:PomBase.
DR InterPro; IPR003124; WH2_dom.
DR Pfam; PF02205; WH2; 1.
DR SMART; SM00246; WH2; 1.
DR PROSITE; PS51082; WH2; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Cytoplasm; Cytoskeleton; Reference proteome.
FT CHAIN 1..309
FT /note="Verprolin"
FT /id="PRO_0000364026"
FT DOMAIN 27..44
FT /note="WH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 1..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..209
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 309 AA; 31225 MW; 47B68086BD93B7D5 CRC64;
MAPAPPPPPP APAPAAAAPA PPLMTGDRSA LLNSIQKGKK LKKATTNDRS APVVGGGVVG
ERKSNTPKSF AAPPVPTGAP SLPTSSNNTQ QAEERPSMPA LGGLFAGGMP KLRHIGKSSA
SAAPPSAPAP PTPQSELRPP TSAPPRPSIP PPSPASAPPI PSKAPPIPSS LPPPAQPAAP
VKSPPSAPSL PSAVPPMPPK VPPPPLSQAP VANTSSRPSS FAPPAGHAPN VTSESPKFPN
RGPSIPSASV PPVPPSSYVL QQRPNRVDDH GRFHFKDDSY LPIPHPFLGV PKVYRGGSGT
TVPLNLSSF
