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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 - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionActin capping, Actin-binding

Enzyme and pathway databases

ReactomeiR-RNO-2132295. MHC class II antigen presentation.
R-RNO-3371497. HSP90 chaperone cycle for steroid hormone receptors (SHR).
R-RNO-6807878. COPI-mediated anterograde transport.
R-RNO-6811436. COPI-independent Golgi-to-ER retrograde traffic.
R-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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 4

Organism-specific databases

RGDi1549770. Capza2.

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00002884782 – 286F-actin-capping protein subunit alpha-2Add BLAST285

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanine1 Publication1
Modified residuei9PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ3T1K5.
PRIDEiQ3T1K5.

PTM databases

iPTMnetiQ3T1K5.
PhosphoSitePlusiQ3T1K5.

Expressioni

Gene expression databases

BgeeiENSRNOG00000056207.
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), WASHC1, WASHC2, WASHC3, WASHC4 and WASHC5. Interacts with RCSD1/CAPZIP (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi268810. 1 interactor.
IntActiQ3T1K5. 2 interactors.
STRINGi10116.ENSRNOP00000037217.

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
2KBMNMR-X/Y265-276[»]
ProteinModelPortaliQ3T1K5.
SMRiQ3T1K5.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ3T1K5.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

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

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.

Similar proteinsi

Entry informationi

Entry nameiCAZA2_RAT
AccessioniPrimary (citable) accession number: Q3T1K5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: October 11, 2005
Last modified: November 22, 2017
This is version 94 of the entry and version 1 of the sequence. See 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