Reviewed, UniProtKB/Swiss-Prot Q10434 (CAPZA_SCHPO)

Names and origin

Protein names

Recommended name:
    F-actin-capping protein subunit alpha

Gene names

Name:	acp1
ORF Names:	SPAC12B10.07

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	256 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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	Cytoplasm. Note: Septum. Localizes to cell tips during interphase. Ref.2 Ref.3
Sequence similarities	Belongs to the F-actin-capping protein alpha subunit family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Actin-binding
Molecular function	Actin capping
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	actin cytoskeleton organization Inferred from genetic interaction. Source: GeneDB_SPombe barbed-end actin filament capping Ref.2 Inferred from direct assay. Source: GeneDB_SPombe cell morphogenesis Inferred from genetic interaction. Source: GeneDB_SPombe cellular protein localization Ref.2 Inferred from genetic interaction. Source: GeneDB_SPombe cytokinesis Ref.2 Inferred from genetic interaction. Source: GeneDB_SPombe
Cellular component	F-actin capping protein complex Ref.2 Inferred from direct assay. Source: GeneDB_SPombe actin cortical patch Ref.2 Inferred from direct assay. Source: GeneDB_SPombe actin filament Ref.2 Inferred from direct assay. Source: GeneDB_SPombe cell division site Ref.3 Inferred from direct assay. Source: GeneDB_SPombe cell tip Ref.2 Ref.3 Inferred from direct assay. Source: GeneDB_SPombe
Molecular function	actin filament binding Ref.2 Inferred from direct assay. Source: GeneDB_SPombe
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 256	256	F-actin-capping protein subunit alpha		PRO_0000208645
Amino acid modifications
	Modified residue	31	1	Phosphoserine Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q10434-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 2B54706CF31C9E4B	FASTA	256	29,808
	10 20 30 40 50 60 MEKEAIYKLI RESPPGEVNQ VVHDIRDIGL SDEEAIHEQL KLYHEDYNSS VSISDDEKVI 70 80 90 100 110 120 ISADNRLEGN RYYDQVLQKS FTINYETMEA ENVEDYTEAI KIPDEIVKQI KKVASDHYLS 130 140 150 160 170 180 DVTFGIIKKS DEVESFTIVL VSSKYNPKNY WNGSWRCICN YNVSEKKLEG RSHIRVHYYE 190 200 210 220 230 240 DGNVWLDASR PISATVEETS KLYEVLAQVE NGIQQSFNVE LSSLNDKKFK ELRRQLPVTR 250 QKINWENVSG IRMRNT

References

	« Hide 'large scale' referencesShow '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. , 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: ATCC 38366 / 972.
[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].
[4]	"Phosphoproteome analysis of fission yeast." Wilson-Grady J.T., Villen J., Gygi S.P. J. Proteome Res. 7:1088-1097(2008) [PubMed: 18257517] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CU329670 Genomic DNA. Translation: CAA94697.1.
PIR	T37574.
RefSeq	NP_594639.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q10434.
Genome annotation databases
GeneID	2542679.
GenomeReviews	Gene locus acp1 in contig CU329670_GR.
KEGG	spo:SPAC12B10.07.
NMPDR	fig|4896.1.peg.4609.
Organism-specific databases
GeneDB_Spombe	SPAC12B10.07.
Phylogenomic databases
OMA	CESALRA
OrthoDB	EOG99618C
Gene expression databases
ArrayExpress	Q10434.
Family and domain databases
InterPro	IPR002189. F-actin_cap_asu. IPR018315. F-actin_cap_asu_actin_bd. IPR017865. F-actin_cap_asu_CS. [Graphical view]
PANTHER	PTHR10653. F-actin_cap_A. 1 hit.
Pfam	PF01267. F-actin_cap_A. 1 hit. [Graphical view]
PRINTS	PR00191. FACTINCAPA.
PROSITE	PS00748. F_ACTIN_CAPPING_A_1. 1 hit. PS00749. F_ACTIN_CAPPING_A_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CAPZA_SCHPO

Accession

Primary (citable) accession number: Q10434

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	November 24, 2009
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)