WSP1_SCHPO
ID WSP1_SCHPO Reviewed; 574 AA.
AC O36027;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 3.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Actin-binding protein wsp1 {ECO:0000305};
DE AltName: Full=Wiskott-Aldrich syndrome protein homolog 1;
GN Name=wsp1; ORFNames=SPAC4F10.15c;
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].
RA Zankel T.C., Ow D.W.;
RT "A Wiskott-Aldrich Syndrome protein homolog in Schizosaccharomyces pombe,
RT Wsp1p, is implicated in stress-response pathways and control of the actin
RT cytoskeleton.";
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP FUNCTION.
RX PubMed=11076964; DOI=10.1083/jcb.151.4.789;
RA Lee W.-L., Bezanilla M., Pollard T.D.;
RT "Fission yeast myosin-I, Myo1p, stimulates actin assembly by Arp2/3 complex
RT and shares functions with WASp.";
RL J. Cell Biol. 151:789-800(2000).
RN [4]
RP INTERACTION WITH VRP1.
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386, AND IDENTIFICATION BY
RP 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: Has a role in regulating actin assembly, so regulating
CC polarized growth. {ECO:0000269|PubMed:11076964}.
CC -!- SUBUNIT: Interacts with vrp1. {ECO:0000269|PubMed:12939254}.
CC -!- INTERACTION:
CC O36027; Q9Y7Z8: myo1; NbExp=4; IntAct=EBI-1148109, EBI-1148082;
CC O36027; Q9P6R1: vrp1; NbExp=3; IntAct=EBI-1148109, EBI-1148131;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
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DR EMBL; AF038575; AAB92587.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB11718.1; -; Genomic_DNA.
DR PIR; T38819; T38819.
DR PIR; T43556; T43556.
DR RefSeq; NP_594758.1; NM_001020185.2.
DR AlphaFoldDB; O36027; -.
DR BioGRID; 280004; 13.
DR IntAct; O36027; 9.
DR STRING; 4896.SPAC4F10.15c.1; -.
DR iPTMnet; O36027; -.
DR MaxQB; O36027; -.
DR PaxDb; O36027; -.
DR PRIDE; O36027; -.
DR EnsemblFungi; SPAC4F10.15c.1; SPAC4F10.15c.1:pep; SPAC4F10.15c.
DR GeneID; 2543589; -.
DR KEGG; spo:SPAC4F10.15c; -.
DR PomBase; SPAC4F10.15c; wsp1.
DR VEuPathDB; FungiDB:SPAC4F10.15c; -.
DR eggNOG; KOG3671; Eukaryota.
DR HOGENOM; CLU_015385_1_1_1; -.
DR InParanoid; O36027; -.
DR OMA; VGNTYWI; -.
DR PRO; PR:O36027; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0030479; C:actin cortical patch; IDA:PomBase.
DR GO; GO:0043332; C:mating projection tip; IDA:PomBase.
DR GO; GO:0031097; C:medial cortex; IDA:PomBase.
DR GO; GO:0003785; F:actin monomer binding; IDA:PomBase.
DR GO; GO:0071933; F:Arp2/3 complex binding; IDA:PomBase.
DR GO; GO:0000147; P:actin cortical patch assembly; IMP:PomBase.
DR GO; GO:0051666; P:actin cortical patch localization; IMP:PomBase.
DR GO; GO:1904670; P:actin filament polymerization involved in mitotic actomyosin contractile ring assembly; IMP:PomBase.
DR GO; GO:0006897; P:endocytosis; IMP:PomBase.
DR GO; GO:0071963; P:establishment or maintenance of cell polarity regulating cell shape; IGI:PomBase.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:PomBase.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IDA:PomBase.
DR GO; GO:2000601; P:positive regulation of Arp2/3 complex-mediated actin nucleation; IDA:PomBase.
DR CDD; cd01205; EVH1_WASP-like; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR027641; WASP.
DR InterPro; IPR033927; WASPfam_EVH1.
DR InterPro; IPR000697; WH1/EVH1_dom.
DR InterPro; IPR003124; WH2_dom.
DR PANTHER; PTHR23202:SF79; PTHR23202:SF79; 1.
DR Pfam; PF00568; WH1; 1.
DR SMART; SM00461; WH1; 1.
DR PROSITE; PS50229; WH1; 1.
DR PROSITE; PS51082; WH2; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome.
FT CHAIN 1..574
FT /note="Actin-binding protein wsp1"
FT /id="PRO_0000189003"
FT DOMAIN 19..130
FT /note="WH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00410"
FT DOMAIN 499..518
FT /note="WH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 144..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..278
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..322
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..373
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..400
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..485
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..540
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 386
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 248
FT /note="L -> V (in Ref. 1; AAB92587)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 574 AA; 59606 MW; C6E5EFCA6A02F0E4 CRC64;
MPPSSSITQE DKATIRKYIP KSTNKIIAAA VVKLYVAYPD PNKWNYTGLC GALVLSYDTT
AKCCWFKLVD VVNNSGIIWD QELYQNMDYR QDRTFFHSFE LDKCLAGFSF ANETDAQKFY
KKVLDKGCHP ESIENPVLSF ITRKGSSRHA PNNSNIQPPS AAPPVPGKEN YNAVGSKSPN
EPELLNSLDP SLIDSLMKMG ISQDQIAENA DFVKAYLNES AGTPTSTSAP PIPPSIPSSR
PPERVPSLSA PAPPPIPPPS NGTVSSPPNS PPRPIAPVSM NPAINSTSKP PLPPPSSRVS
AAALAANKKR PPPPPPPSRR NRGKPPIGNG SSNSSLPPPP PPPRSNAAGS IPLPPQGRSA
PPPPPPRSAP STGRQPPPLS SSRAVSNPPA PPPAIPGRSA PALPPLGNAS RTSTPPVPTP
PSLPPSAPPS LPPSAPPSLP MGAPAAPPLP PSAPIAPPLP AGMPAAPPLP PAAPAPPPAP
APAPAAPVAS IAELPQQDGR ANLMASIRAS GGMDLLKSRK VSASPSVAST KTSNPPVEAP
PSNNLMDALA SALNQRKTKV AQSDEEDEDD DEWD
