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Protein

F-actin-capping protein subunit alpha

Gene

CAP1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  • actin filament binding Source: SGD

GO - Biological processi

  • barbed-end actin filament capping Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Actin capping

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-31817-MONOMER.
ReactomeiREACT_312184. Factors involved in megakaryocyte development and platelet production.

Names & Taxonomyi

Protein namesi
Recommended name:
F-actin-capping protein subunit alpha
Gene namesi
Name:CAP1
Ordered Locus Names:YKL007W
ORF Names:YKL155
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XI

Organism-specific databases

CYGDiYKL007w.
EuPathDBiFungiDB:YKL007W.
SGDiS000001490. CAP1.

Subcellular locationi

GO - Cellular componenti

  • actin cortical patch Source: SGD
  • actin filament Source: SGD
  • F-actin capping protein complex Source: SGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 268267F-actin-capping protein subunit alphaPRO_0000208646Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei17 – 171Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP28495.
PaxDbiP28495.
PeptideAtlasiP28495.

Expressioni

Gene expression databases

GenevestigatoriP28495.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta subunit.

Binary interactionsi

WithEntry#Exp.IntActNotes
CAP2P135175EBI-4003,EBI-4013

Protein-protein interaction databases

BioGridi34125. 92 interactions.
DIPiDIP-2696N.
IntActiP28495. 12 interactions.
MINTiMINT-500609.
STRINGi4932.YKL007W.

Structurei

3D structure databases

ProteinModelPortaliP28495.
SMRiP28495. Positions 12-262.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG261759.
GeneTreeiENSGT00390000006476.
HOGENOMiHOG000036539.
InParanoidiP28495.
KOiK10364.
OMAiKKTIIAC.
OrthoDBiEOG7CZKHC.

Family and domain databases

InterProiIPR002189. CapZ_alpha.
IPR017865. F-actin_cap_asu_CS.
[Graphical view]
PANTHERiPTHR10653. PTHR10653. 1 hit.
PfamiPF01267. F-actin_cap_A. 1 hit.
[Graphical view]
PRINTSiPR00191. FACTINCAPA.
PROSITEiPS00748. F_ACTIN_CAPPING_A_1. 1 hit.
PS00749. F_ACTIN_CAPPING_A_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P28495-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSSKFEEVI NKIINDSPPG ELREVYDDLI KITSENSKNT ILDAIENYNV
60 70 80 90 100
QNCIPIEVNG NSVIISKYNK EGAKFFDPVN SVIFSVNHLE RKGLDIEPYE
110 120 130 140 150
FTHAKIEKGQ LKELHDKLHE YLLQSFPGDV SFAVYPVPEE ISKISIIIVS
160 170 180 190 200
TKYNPNNFWN GHWRSSYIYD LETRELSGQI STQVHYYEDG NVSFQSGKDI
210 220 230 240 250
NQSNVDDVVC TIRDIETNFE NDLDLSFFDL NEKQFKALRR RLPVTRSKIN
260
WGSAIGSYRL GKNAAEGK
Length:268
Mass (Da):30,699
Last modified:December 1, 1992 - v1
Checksum:i6FBD3130B55B0C5C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S59773 Genomic DNA. Translation: AAC60553.1.
X61398 Genomic DNA. Translation: CAA43669.1.
Z28007 Genomic DNA. Translation: CAA81841.1.
AY558093 Genomic DNA. Translation: AAS56419.1.
BK006944 Genomic DNA. Translation: DAA09149.1.
PIRiS30135.
RefSeqiNP_012918.1. NM_001179573.1.

Genome annotation databases

EnsemblFungiiYKL007W; YKL007W; YKL007W.
GeneIDi853862.
KEGGisce:YKL007W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S59773 Genomic DNA. Translation: AAC60553.1.
X61398 Genomic DNA. Translation: CAA43669.1.
Z28007 Genomic DNA. Translation: CAA81841.1.
AY558093 Genomic DNA. Translation: AAS56419.1.
BK006944 Genomic DNA. Translation: DAA09149.1.
PIRiS30135.
RefSeqiNP_012918.1. NM_001179573.1.

3D structure databases

ProteinModelPortaliP28495.
SMRiP28495. Positions 12-262.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34125. 92 interactions.
DIPiDIP-2696N.
IntActiP28495. 12 interactions.
MINTiMINT-500609.
STRINGi4932.YKL007W.

Proteomic databases

MaxQBiP28495.
PaxDbiP28495.
PeptideAtlasiP28495.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYKL007W; YKL007W; YKL007W.
GeneIDi853862.
KEGGisce:YKL007W.

Organism-specific databases

CYGDiYKL007w.
EuPathDBiFungiDB:YKL007W.
SGDiS000001490. CAP1.

Phylogenomic databases

eggNOGiNOG261759.
GeneTreeiENSGT00390000006476.
HOGENOMiHOG000036539.
InParanoidiP28495.
KOiK10364.
OMAiKKTIIAC.
OrthoDBiEOG7CZKHC.

Enzyme and pathway databases

BioCyciYEAST:G3O-31817-MONOMER.
ReactomeiREACT_312184. Factors involved in megakaryocyte development and platelet production.

Miscellaneous databases

NextBioi975115.
PROiP28495.

Gene expression databases

GenevestigatoriP28495.

Family and domain databases

InterProiIPR002189. CapZ_alpha.
IPR017865. F-actin_cap_asu_CS.
[Graphical view]
PANTHERiPTHR10653. PTHR10653. 1 hit.
PfamiPF01267. F-actin_cap_A. 1 hit.
[Graphical view]
PRINTSiPR00191. FACTINCAPA.
PROSITEiPS00748. F_ACTIN_CAPPING_A_1. 1 hit.
PS00749. F_ACTIN_CAPPING_A_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Effects of null mutations and overexpression of capping protein on morphogenesis, actin distribution and polarized secretion in yeast."
    Amatruda J.F., Gattermeir D.J., Karpova T.S., Cooper J.A.
    J. Cell Biol. 119:1151-1162(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
  2. "Sequence of a 7.8 kb segment on the left arm of yeast chromosome XI reveals four open reading frames, including the CAP1 gene, an intron-containing gene and a gene encoding a homolog to the mammalian UOG-1 gene."
    Boyer J., Pascolo S., Richard G.-F., Dujon B.
    Yeast 9:279-287(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Complete DNA sequence of yeast chromosome XI."
    Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C.
    , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
    Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCAPZA_YEAST
AccessioniPrimary (citable) accession number: P28495
Secondary accession number(s): D6VXS9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: April 29, 2015
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 4380 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XI
    Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.