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44  structures 972  species 9  interactions 1439  sequences 27  architectures

Family: F-actin_cap_A (PF01267)

Summary: F-actin capping protein alpha subunit

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This is the Wikipedia entry entitled "F-actin capping protein". More...

F-actin capping protein Edit Wikipedia article

F-actin capping protein alpha subunit
PDB 1mwn EBI.jpg
solution nmr structure of s100b bound to the high-affinity target peptide trtk-12
Identifiers
Symbol F-actin_cap_A
Pfam PF01267
InterPro IPR018315
PROSITE PDOC00609
SCOP 1izn
SUPERFAMILY 1izn
F-actin capping protein, beta subunit
Identifiers
Symbol F_actin_cap_B
Pfam PF01115
InterPro IPR001698
PROSITE PDOC00203
SCOP 1izn
SUPERFAMILY 1izn

In molecular biology, the F-actin capping protein is a protein which binds in a calcium-independent manner to the fast-growing ends of actin filaments (barbed end), thereby blocking the exchange of subunits at these ends. Unlike gelsolin and severin this protein does not sever actin filaments. The F-actin capping protein is a heterodimer composed of two unrelated subunits: alpha and beta. Neither of the subunits shows sequence similarity to other filament-capping proteins.[1] The alpha subunit is a protein of about 268 to 286 amino acid residues and the beta subunit is approximately 280 amino acids, their sequences are well conserved in eukaryotic species.[2]

The actin filament system, a prominent part of the cytoskeleton in eukaryotic cells, is both a static structure and a dynamic network that can undergo rearrangements: it is thought to be involved in processes such as cell movement and phagocytosis, as well as muscle contraction.[1]

References

  1. ^ a b Maruyama K, Kurokawa H, Oosawa M, Shimaoka S, Yamamoto H, Ito M, Maruyama K (May 1990). "Beta-actinin is equivalent to Cap Z protein". J. Biol. Chem. 265 (15): 8712–5. PMID 2341404. 
  2. ^ Cooper JA, Caldwell JE, Gattermeir DJ, Torres MA, Amatruda JF, Casella JF (1991). "Variant cDNAs encoding proteins similar to the alpha subunit of chicken CapZ". Cell Motil. Cytoskeleton. 18 (3): 204–14. doi:10.1002/cm.970180306. PMID 1711931. 

This article incorporates text from the public domain Pfam and InterPro IPR018315

This article incorporates text from the public domain Pfam and InterPro IPR001698

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

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Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR002189

The F-actin capping protein binds in a calcium-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike gelsolin and severin this protein does not sever actin filaments. The F-actin capping protein is a heterodimer composed of two unrelated subunits: alpha and beta (see INTERPRO). Neither of the subunits shows sequence similarity to other filament-capping proteins [PUBMED:2341404].

This entry represent the alpha subunit (CAPZA), which is a protein of about 268 to 286 amino acid residues whose sequence is well conserved in eukaryotic species [PUBMED:1711931]. In Drosophila mutations in the alpha and beta subunits cause actin accumulation and subsequent retinal degeneration [PUBMED:16143599]. In humans CAPZA is part of the WASH complex that controls the fission of endosomes [PUBMED:19922875].

Gene Ontology

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Domain organisation

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Alignments

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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

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(154)
Full
(1439)
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(2126)
NCBI
(2390)
Meta
(1)
RP15
(342)
RP35
(719)
RP55
(1084)
RP75
(1367)
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  Seed
(154)
Full
(1439)
Representative proteomes UniProt
(2126)
NCBI
(2390)
Meta
(1)
RP15
(342)
RP35
(719)
RP55
(1084)
RP75
(1367)
Alignment:
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  Seed
(154)
Full
(1439)
Representative proteomes UniProt
(2126)
NCBI
(2390)
Meta
(1)
RP15
(342)
RP35
(719)
RP55
(1084)
RP75
(1367)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download   Download   Download  

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

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This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

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Curation and family details

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Seed source: Prosite
Previous IDs: none
Type: Family
Sequence Ontology: SO:0100021
Author: Finn RD , Bateman A
Number in seed: 154
Number in full: 1439
Average length of the domain: 243.50 aa
Average identity of full alignment: 35 %
Average coverage of the sequence by the domain: 84.80 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 45638612 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 24.2 24.2
Trusted cut-off 24.8 24.7
Noise cut-off 24.0 24.0
Model length: 266
Family (HMM) version: 17
Download: download the raw HMM for this family

Species distribution

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Interactions

There are 9 interactions for this family. More...

F_actin_cap_B F_actin_cap_B Ank_4 F-actin_cap_A S_100 EF-hand_1 EF-hand_1 Ank_2 S_100

Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the F-actin_cap_A domain has been found. There are 44 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.

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