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Protein

F-actin-capping protein subunit alpha-1

Gene

CAPZA1

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 3 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. CapZ may mediate the attachment of the barbed ends of actin filaments to the Z-line.

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Actin capping

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiR-GGA-879415. Advanced glycosylation endproduct receptor signaling.
R-GGA-983231. Factors involved in megakaryocyte development and platelet production.

Names & Taxonomyi

Protein namesi
Recommended name:
F-actin-capping protein subunit alpha-1
Alternative name(s):
Beta-actinin subunit I
CapZ 36/32
Gene namesi
Name:CAPZA1
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Chromosome 26

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • F-actin capping protein complex Source: InterPro
  • plasma membrane Source: AgBase
  • WASH complex Source: UniProtKB
  • Z disc Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002086341 – 286F-actin-capping protein subunit alpha-1Add BLAST286

Proteomic databases

PaxDbiP13127.
PRIDEiP13127.

Expressioni

Tissue specificityi

Present in all tissues examined.

Gene expression databases

BgeeiENSGALG00000001547.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta subunit. Component of the WASH complex (By similarity).By similarity

Protein-protein interaction databases

DIPiDIP-35364N.
IntActiP13127. 3 interactors.
MINTiMINT-3390680.
STRINGi9031.ENSGALP00000039390.

Structurei

Secondary structure

1286
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi10 – 22Combined sources13
Helixi29 – 40Combined sources12
Helixi43 – 49Combined sources7
Helixi51 – 60Combined sources10
Beta strandi63 – 65Combined sources3
Beta strandi70 – 72Combined sources3
Beta strandi74 – 76Combined sources3
Helixi78 – 80Combined sources3
Beta strandi81 – 83Combined sources3
Beta strandi86 – 89Combined sources4
Turni90 – 93Combined sources4
Beta strandi94 – 99Combined sources6
Turni100 – 103Combined sources4
Beta strandi104 – 110Combined sources7
Beta strandi115 – 117Combined sources3
Helixi118 – 135Combined sources18
Beta strandi136 – 138Combined sources3
Beta strandi140 – 148Combined sources9
Beta strandi151 – 164Combined sources14
Helixi165 – 167Combined sources3
Beta strandi169 – 182Combined sources14
Beta strandi185 – 198Combined sources14
Beta strandi202 – 217Combined sources16
Helixi221 – 252Combined sources32
Helixi254 – 258Combined sources5
Helixi271 – 274Combined sources4
Turni277 – 279Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IZNX-ray2.10A/C1-286[»]
2KXPNMR-A7-281[»]
2KZ7NMR-A1-286[»]
3AA0X-ray1.70A1-286[»]
3AA1X-ray1.90A1-286[»]
3AA6X-ray1.90A1-286[»]
3AA7X-ray1.90A1-286[»]
3AAAX-ray2.20A1-286[»]
3AAEX-ray3.30A/C/E/G/I1-286[»]
3LK2X-ray2.20A1-286[»]
3LK3X-ray2.68A1-286[»]
3LK4X-ray1.991/4/7/A/D/G/J/M/P/S/V/Y1-286[»]
ProteinModelPortaliP13127.
SMRiP13127.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13127.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0836. Eukaryota.
ENOG410ZAWX. LUCA.
GeneTreeiENSGT00390000006476.
HOGENOMiHOG000036539.
HOVERGENiHBG050810.
InParanoidiP13127.
KOiK10364.
OMAiSHAFSQY.
OrthoDBiEOG091G0KST.
PhylomeDBiP13127.

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.

P13127-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADFEDRVSD EEKVRIAAKF ITHAPPGEFN EVFNDVRLLL NNDNLLREGA
60 70 80 90 100
AHAFAQYNMD QFTPVKIEGY DDQVLITEHG DLGNGRFLDP RNKISFKFDH
110 120 130 140 150
LRKEASDPQP EDTESALKQW RDACDSALRA YVKDHYPNGF CTVYGKSIDG
160 170 180 190 200
QQTIIACIES HQFQPKNFWN GRWRSEWKFT ITPPTAQVAA VLKIQVHYYE
210 220 230 240 250
DGNVQLVSHK DIQDSVQVSS DVQTAKEFIK IIENAENEYQ TAISENYQTM
260 270 280
SDTTFKALRR QLPVTRTKID WNKILSYKIG KEMQNA
Length:286
Mass (Da):32,960
Last modified:January 1, 1990 - v1
Checksum:i187E7C51541665DE
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti221D → S AA sequence (PubMed:2341404).Curated1
Sequence conflicti232I → V AA sequence (PubMed:2341404).Curated1
Sequence conflicti234N → A AA sequence (PubMed:2341404).Curated1
Sequence conflicti245E → Q AA sequence (PubMed:2341404).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti163F → I.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M25534 mRNA. Translation: AAA48657.1.
PIRiA33546.
RefSeqiNP_990846.1. NM_205515.1.
UniGeneiGga.2783.

Genome annotation databases

EnsembliENSGALT00000056559; ENSGALP00000056898; ENSGALG00000001547.
GeneIDi396521.
KEGGigga:396521.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M25534 mRNA. Translation: AAA48657.1.
PIRiA33546.
RefSeqiNP_990846.1. NM_205515.1.
UniGeneiGga.2783.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IZNX-ray2.10A/C1-286[»]
2KXPNMR-A7-281[»]
2KZ7NMR-A1-286[»]
3AA0X-ray1.70A1-286[»]
3AA1X-ray1.90A1-286[»]
3AA6X-ray1.90A1-286[»]
3AA7X-ray1.90A1-286[»]
3AAAX-ray2.20A1-286[»]
3AAEX-ray3.30A/C/E/G/I1-286[»]
3LK2X-ray2.20A1-286[»]
3LK3X-ray2.68A1-286[»]
3LK4X-ray1.991/4/7/A/D/G/J/M/P/S/V/Y1-286[»]
ProteinModelPortaliP13127.
SMRiP13127.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-35364N.
IntActiP13127. 3 interactors.
MINTiMINT-3390680.
STRINGi9031.ENSGALP00000039390.

Proteomic databases

PaxDbiP13127.
PRIDEiP13127.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSGALT00000056559; ENSGALP00000056898; ENSGALG00000001547.
GeneIDi396521.
KEGGigga:396521.

Organism-specific databases

CTDi829.

Phylogenomic databases

eggNOGiKOG0836. Eukaryota.
ENOG410ZAWX. LUCA.
GeneTreeiENSGT00390000006476.
HOGENOMiHOG000036539.
HOVERGENiHBG050810.
InParanoidiP13127.
KOiK10364.
OMAiSHAFSQY.
OrthoDBiEOG091G0KST.
PhylomeDBiP13127.

Enzyme and pathway databases

ReactomeiR-GGA-879415. Advanced glycosylation endproduct receptor signaling.
R-GGA-983231. Factors involved in megakaryocyte development and platelet production.

Miscellaneous databases

EvolutionaryTraceiP13127.
PROiP13127.

Gene expression databases

BgeeiENSGALG00000001547.

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...

Entry informationi

Entry nameiCAZA1_CHICK
AccessioniPrimary (citable) accession number: P13127
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: November 30, 2016
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Was originally thought to have an internal disulfide bond.1 Publication

Keywords - Technical termi

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

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.