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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

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 286286F-actin-capping protein subunit alpha-1PRO_0000208634Add
BLAST

Proteomic databases

PaxDbiP13127.
PRIDEiP13127.

Expressioni

Tissue specificityi

Present in all tissues examined.

Gene expression databases

BgeeiENSGALG00000001547.
ExpressionAtlasiP13127. baseline and differential.

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 interactions.
MINTiMINT-3390680.
STRINGi9031.ENSGALP00000039390.

Structurei

Secondary structure

1
286
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 2213Combined sources
Helixi29 – 4012Combined sources
Helixi43 – 497Combined sources
Helixi51 – 6010Combined sources
Beta strandi63 – 653Combined sources
Beta strandi70 – 723Combined sources
Beta strandi74 – 763Combined sources
Helixi78 – 803Combined sources
Beta strandi81 – 833Combined sources
Beta strandi86 – 894Combined sources
Turni90 – 934Combined sources
Beta strandi94 – 996Combined sources
Turni100 – 1034Combined sources
Beta strandi104 – 1107Combined sources
Beta strandi115 – 1173Combined sources
Helixi118 – 13518Combined sources
Beta strandi136 – 1383Combined sources
Beta strandi140 – 1489Combined sources
Beta strandi151 – 16414Combined sources
Helixi165 – 1673Combined sources
Beta strandi169 – 18214Combined sources
Beta strandi185 – 19814Combined sources
Beta strandi202 – 21716Combined sources
Helixi221 – 25232Combined sources
Helixi254 – 2585Combined sources
Helixi271 – 2744Combined sources
Turni277 – 2793Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 7-281.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti221 – 2211D → S AA sequence (PubMed:2341404).Curated
Sequence conflicti232 – 2321I → V AA sequence (PubMed:2341404).Curated
Sequence conflicti234 – 2341N → A AA sequence (PubMed:2341404).Curated
Sequence conflicti245 – 2451E → Q AA sequence (PubMed:2341404).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti163 – 1631F → I.

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

EnsembliENSGALT00000002351; ENSGALP00000002349; 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
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. Positions 7-281.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Proteomic databases

PaxDbiP13127.
PRIDEiP13127.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSGALT00000002351; ENSGALP00000002349; 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.
ExpressionAtlasiP13127. baseline and differential.

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: September 7, 2016
This is version 127 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.