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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: -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.

Miscellaneous

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

GO - Molecular functioni

  • actin filament binding Source: SGD

GO - Biological processi

  • barbed-end actin filament capping Source: SGD

Keywordsi

Molecular functionActin capping, Actin-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-31817-MONOMER
ReactomeiR-SCE-983231 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
Proteomesi
  • UP000002311 Componenti: Chromosome XI

Organism-specific databases

EuPathDBiFungiDB:YKL007W
SGDiS000001490 CAP1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00002086462 – 268F-actin-capping protein subunit alphaAdd BLAST267

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1
Modified residuei17PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP28495
PaxDbiP28495
PRIDEiP28495

PTM databases

iPTMnetiP28495

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta subunit.

Binary interactionsi

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

GO - Molecular functioni

  • actin filament binding Source: SGD

Protein-protein interaction databases

BioGridi34125, 133 interactors
DIPiDIP-2696N
IntActiP28495, 13 interactors
MINTiP28495
STRINGi4932.YKL007W

Structurei

3D structure databases

ProteinModelPortaliP28495
SMRiP28495
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00390000006476
HOGENOMiHOG000036539
InParanoidiP28495
KOiK10364
OMAiWDKVLGY
OrthoDBiEOG092C4FP8

Family and domain databases

InterProiView protein in InterPro
IPR002189 CapZ_alpha
IPR037282 CapZ_alpha/beta
IPR017865 F-actin_cap_asu_CS
PANTHERiPTHR10653 PTHR10653, 1 hit
PfamiView protein in Pfam
PF01267 F-actin_cap_A, 1 hit
PRINTSiPR00191 FACTINCAPA
SUPFAMiSSF90096 SSF90096, 1 hit
PROSITEiView protein in PROSITE
PS00748 F_ACTIN_CAPPING_A_1, 1 hit
PS00749 F_ACTIN_CAPPING_A_2, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiCAPZA_YEAST
AccessioniPrimary (citable) accession number: P28495
Secondary accession number(s): D6VXS9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: May 23, 2018
This is version 162 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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

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