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Q9HGP5 (CAPZB_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
F-actin-capping protein subunit beta
Gene names
Name:acp2
ORF Names:SPAC631.01c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length268 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

F-actin-capping proteins bind in a Ca2+-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. Competes with formin cdc12 for attachment to the actin filaments barbed ends. Slowly replaces cdc12 on the barbed ends in preparation for filament disassembly during contractile ring constriction. Ref.2

Subunit structure

Heterodimer of an alpha and a beta subunit. Ref.2

Subcellular location

Cytoplasmcytoskeleton. Nucleus. Note: Septum. Localizes to cell tips during interphase. Ref.2 Ref.3

Sequence similarities

Belongs to the F-actin-capping protein beta subunit family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 268268F-actin-capping protein subunit beta
PRO_0000204641

Sequences

Sequence LengthMass (Da)Tools
Q9HGP5 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 7E781ADB7B275BEE

FASTA26829,845
        10         20         30         40         50         60 
MNSEDAALDL LRRLNPKDIS KNLDTILSVA PDLADVLLSS VDQPLKVNTC SESGNQYLLC 

        70         80         90        100        110        120 
DFNRDGDSYR SPWSNKYDPP LEDGLVSTDR VRKLEVSLNE AIRVYLDLYY EGGVSSVYLW 

       130        140        150        160        170        180 
DQDDSYAGAV LIKKASTSNS SGWDSIHVFE CLPTTETNVY DYRLTSTIIL FLSSGSEEQS 

       190        200        210        220        230        240 
ALPSKALNLS GHLTRQTSQR LPAADDDTEI ANVGKLVEEM ETRMRNFLQD VYFGKTKDII 

       250        260 
NQTRSIQPVS DAQPNDSALR SVLNDLSI 

« Hide

References

« Hide 'large scale' references
[1]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed: 11859360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[2]"Profilin-mediated competition between capping protein and formin Cdc12p during cytokinesis in fission yeast."
Kovar D.R., Wu J.-Q., Pollard T.D.
Mol. Biol. Cell 16:2313-2324(2005) [PubMed: 15743909] [Abstract]
Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
[3]"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
Nat. Biotechnol. 24:841-847(2006) [PubMed: 16823372] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329670 Genomic DNA. Translation: CAC05483.1.
RefSeqNP_593619.3. NM_001019050.2.

3D structure databases

ProteinModelPortalQ9HGP5.
SMRQ9HGP5. Positions 4-266.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9HGP5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC631.01c.1; SPAC631.01c.1:pep; SPAC631.01c.
GeneID2543390.
GenomeReviewsGene locus acp2 in contig CU329670_GR.
KEGGspo:SPAC631.01c.
NMPDRfig|4896.1.peg.3589.

Organism-specific databases

GeneDB_SpombeSPAC631.01c.

Phylogenomic databases

eggNOGfuNOG06099.
GeneTreeEFGT00050000005894.
HOGENOMHBG445391.
OMANLLQEVY.
OrthoDBEOG4XWK6P.

Enzyme and pathway databases

BioCycSPOM-XXX-01:SPOM-XXX-01-001289-MONOMER.

Gene expression databases

ArrayExpressQ9HGP5.

Family and domain databases

InterProIPR019771. F-actin_capping_bsu_CS.
IPR001698. WASH_F-actin_cap_beta.
[Graphical view]
KOK10365.
PANTHERPTHR10619. Factin_cap_beta. 1 hit.
PfamPF01115. F_actin_cap_B. 1 hit.
[Graphical view]
PRINTSPR00192. FACTINCAPB.
PROSITEPS00231. F_ACTIN_CAPPING_BETA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCAPZB_SCHPO
AccessionPrimary (citable) accession number: Q9HGP5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: March 1, 2001
Last modified: December 14, 2011
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

SIMILARITY comments

Index of protein domains and families