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Protein

F-actin-capping protein subunit alpha-1

Gene

CAPZA1

Organism
Homo sapiens (Human)
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. May play a role in the formation of epithelial cell junctions.1 Publication

GO - Molecular functioni

  • actin binding Source: ProtInc
  • cadherin binding Source: BHF-UCL

GO - Biological processi

Keywordsi

Molecular functionActin capping, Actin-binding

Enzyme and pathway databases

ReactomeiR-HSA-2132295 MHC class II antigen presentation
R-HSA-3371497 HSP90 chaperone cycle for steroid hormone receptors (SHR)
R-HSA-6807878 COPI-mediated anterograde transport
R-HSA-6811436 COPI-independent Golgi-to-ER retrograde traffic
R-HSA-879415 Advanced glycosylation endproduct receptor signaling
R-HSA-8950505 Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation
R-HSA-983231 Factors involved in megakaryocyte development and platelet production
SIGNORiP52907

Names & Taxonomyi

Protein namesi
Recommended name:
F-actin-capping protein subunit alpha-1
Alternative name(s):
CapZ alpha-1
Gene namesi
Name:CAPZA1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

EuPathDBiHostDB:ENSG00000116489.12
HGNCiHGNC:1488 CAPZA1
MIMi601580 gene
neXtProtiNX_P52907

Subcellular locationi

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

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Organism-specific databases

DisGeNETi829
OpenTargetsiENSG00000116489
PharmGKBiPA26069

Polymorphism and mutation databases

BioMutaiCAPZA1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00002086242 – 286F-actin-capping protein subunit alpha-1Add BLAST285

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1 Publication1
Modified residuei9PhosphoserineCombined sources1
Modified residuei19N6-acetyllysineCombined sources1
Modified residuei97N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP52907
MaxQBiP52907
PaxDbiP52907
PeptideAtlasiP52907
PRIDEiP52907
ProteomicsDBi56550
TopDownProteomicsiP52907

2D gel databases

OGPiP52907
REPRODUCTION-2DPAGEiIPI00005969
P52907
SWISS-2DPAGEiP52907

PTM databases

iPTMnetiP52907
PhosphoSitePlusiP52907
SwissPalmiP52907

Expressioni

Gene expression databases

BgeeiENSG00000116489
CleanExiHS_CAPZA1
ExpressionAtlasiP52907 baseline and differential
GenevisibleiP52907 HS

Organism-specific databases

HPAiCAB045963

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta subunit. Interacts with S100A (By similarity). Component of the WASH complex, composed of F-actin-capping protein subunit alpha (CAPZA1, CAPZA2 or CAPZA3), F-actin-capping protein subunit beta (CAPZB), WASH (WASHC1, WASH2P, WASH3P, WASH4P, WASH5P or WASH6P), WASHC2 (WASHC2A or WASHC2C), WASHC3, WASHC4 and WASHC5. Interacts with S100B. Interacts with SH3BP1; recruits CAPZA1 to forming cell junctions (PubMed:22891260). Interacts with CD2AP (PubMed:22891260).By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SH3KBP1Q96B972EBI-355586,EBI-346595

GO - Molecular functioni

  • actin binding Source: ProtInc
  • cadherin binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi107279, 115 interactors
CORUMiP52907
IntActiP52907, 75 interactors
MINTiP52907
STRINGi9606.ENSP00000263168

Structurei

Secondary structure

1286
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi271 – 275Combined sources5

3D structure databases

ProteinModelPortaliP52907
SMRiP52907
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP52907

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0836 Eukaryota
ENOG410ZAWX LUCA
GeneTreeiENSGT00390000006476
HOGENOMiHOG000036539
HOVERGENiHBG050810
InParanoidiP52907
KOiK10364
OMAiACDSALR
OrthoDBiEOG091G0KST
PhylomeDBiP52907
TreeFamiTF314822

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.

P52907-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADFDDRVSD EEKVRIAAKF ITHAPPGEFN EVFNDVRLLL NNDNLLREGA
60 70 80 90 100
AHAFAQYNMD QFTPVKIEGY EDQVLITEHG DLGNSRFLDP RNKISFKFDH
110 120 130 140 150
LRKEASDPQP EEADGGLKSW RESCDSALRA YVKDHYSNGF CTVYAKTIDG
160 170 180 190 200
QQTIIACIES HQFQPKNFWN GRWRSEWKFT ITPPTAQVVG VLKIQVHYYE
210 220 230 240 250
DGNVQLVSHK DVQDSLTVSN EAQTAKEFIK IIENAENEYQ TAISENYQTM
260 270 280
SDTTFKALRR QLPVTRTKID WNKILSYKIG KEMQNA
Length:286
Mass (Da):32,923
Last modified:January 23, 2007 - v3
Checksum:i0F47ADAB6A3689DD
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti192L → P in BAD96946 (Ref. 4) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_073834219S → L1 PublicationCorresponds to variant dbSNP:rs555597264Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U56637 mRNA Translation: AAC00533.1
CR407657 mRNA Translation: CAG28585.1
CR541819 mRNA Translation: CAG46618.1
BT019364 mRNA Translation: AAV38171.1
AK223226 mRNA Translation: BAD96946.1
AL603832 Genomic DNA No translation available.
AL929470 Genomic DNA No translation available.
BC000144 mRNA Translation: AAH00144.1
CCDSiCCDS30805.1
PIRiG02639
RefSeqiNP_006126.1, NM_006135.2
UniGeneiHs.744974

Genome annotation databases

EnsembliENST00000263168; ENSP00000263168; ENSG00000116489
GeneIDi829
KEGGihsa:829
UCSCiuc001ecj.2 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiCAZA1_HUMAN
AccessioniPrimary (citable) accession number: P52907
Secondary accession number(s): Q53FQ6, Q6FHD5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: July 18, 2018
This is version 182 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

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