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Protein

F-actin-capping protein subunit alpha-2

Gene

Capza2

Organism
Rattus norvegicus (Rat)
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 (By similarity).By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Actin capping

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
F-actin-capping protein subunit alpha-2
Alternative name(s):
CapZ alpha-2
Gene namesi
Name:Capza2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 4

Organism-specific databases

RGDi1549770. Capza2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 286285F-actin-capping protein subunit alpha-2PRO_0000288478Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei9 – 91PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ3T1K5.
PRIDEiQ3T1K5.

PTM databases

iPTMnetiQ3T1K5.
PhosphoSiteiQ3T1K5.

Expressioni

Gene expression databases

BgeeiENSRNOG00000028549.
GenevisibleiQ3T1K5. RN.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta subunit. Component of the WASH complex, composed of F-actin-capping protein subunit alpha (CAPZA1, CAPZA2 or CAPZA3), F-actin-capping protein subunit beta (CAPZB), WASH1, FAM21, KIAA1033, KIAA0196 and CCDC53. Interacts with RCSD1/CAPZIP (By similarity).By similarity

Protein-protein interaction databases

BioGridi268810. 1 interaction.
IntActiQ3T1K5. 1 interaction.
STRINGi10116.ENSRNOP00000037217.

Structurei

Secondary structure

1
286
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi271 – 2755Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KBMNMR-X/Y265-276[»]
ProteinModelPortaliQ3T1K5.
SMRiQ3T1K5. Positions 9-275.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ3T1K5.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0836. Eukaryota.
ENOG410ZAWX. LUCA.
GeneTreeiENSGT00390000006476.
HOGENOMiHOG000036539.
HOVERGENiHBG050810.
InParanoidiQ3T1K5.
KOiK10364.
OMAiTAMKAYV.
OrthoDBiEOG091G0KST.
PhylomeDBiQ3T1K5.
TreeFamiTF314822.

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q3T1K5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADLEEQLSD EEKVRIAAKF IIHAPPGEFN EVFNDVRLLL NNDNLLREGA
60 70 80 90 100
AHAFAQYNLD QFTPVKIEGY EDQVLITEHG DLGNGKFLDP KNRICFKFDH
110 120 130 140 150
LRKEATDPRP YEAENAIESW RTSVETALRA YVKEHYPNGV CTVYGKKVDG
160 170 180 190 200
QQTIIACIES HQFQAKNFWN GRWRSEWKFT VTPSTTQVVG ILKIQVHYYE
210 220 230 240 250
DGNVQLVSHK DIQDSLTVSN EVQTAKEFIK IVEAAENEYQ TAISENYQTM
260 270 280
SDTTFKALRR QLPVTRTKID WNKILSYKIG KEMQNA
Length:286
Mass (Da):32,967
Last modified:October 11, 2005 - v1
Checksum:iE706A9BC1830E70B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DP000027 Genomic DNA. Translation: AAR16310.1.
BC101867 mRNA. Translation: AAI01868.1.
RefSeqiNP_001009180.1. NM_001009180.2.
UniGeneiRn.17868.

Genome annotation databases

EnsembliENSRNOT00000090451; ENSRNOP00000072041; ENSRNOG00000056207.
GeneIDi493810.
KEGGirno:493810.
UCSCiRGD:1549770. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DP000027 Genomic DNA. Translation: AAR16310.1.
BC101867 mRNA. Translation: AAI01868.1.
RefSeqiNP_001009180.1. NM_001009180.2.
UniGeneiRn.17868.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KBMNMR-X/Y265-276[»]
ProteinModelPortaliQ3T1K5.
SMRiQ3T1K5. Positions 9-275.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi268810. 1 interaction.
IntActiQ3T1K5. 1 interaction.
STRINGi10116.ENSRNOP00000037217.

PTM databases

iPTMnetiQ3T1K5.
PhosphoSiteiQ3T1K5.

Proteomic databases

PaxDbiQ3T1K5.
PRIDEiQ3T1K5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000090451; ENSRNOP00000072041; ENSRNOG00000056207.
GeneIDi493810.
KEGGirno:493810.
UCSCiRGD:1549770. rat.

Organism-specific databases

CTDi830.
RGDi1549770. Capza2.

Phylogenomic databases

eggNOGiKOG0836. Eukaryota.
ENOG410ZAWX. LUCA.
GeneTreeiENSGT00390000006476.
HOGENOMiHOG000036539.
HOVERGENiHBG050810.
InParanoidiQ3T1K5.
KOiK10364.
OMAiTAMKAYV.
OrthoDBiEOG091G0KST.
PhylomeDBiQ3T1K5.
TreeFamiTF314822.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiQ3T1K5.
PROiQ3T1K5.

Gene expression databases

BgeeiENSRNOG00000028549.
GenevisibleiQ3T1K5. RN.

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 nameiCAZA2_RAT
AccessioniPrimary (citable) accession number: Q3T1K5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: October 11, 2005
Last modified: September 7, 2016
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.