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Protein

F-actin-capping protein subunit alpha-1

Gene

CAPZA1

Organism
Homo sapiens (Human)
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. 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.

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.
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. 111 interactors.
CORUMiP52907.
IntActiP52907. 58 interactors.
MINTiMINT-5001076.
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

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1MQ1NMR-C/D265-276[»]
1MWNNMR-X/Y265-276[»]
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: November 22, 2017
This is version 175 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