Capzb capping actin protein of muscle Z-line subunit beta [Rattus norvegicus (Norway rat)] - Gene

Summary

Official Symbol: Capzbprovided by RGD
Official Full Name: capping actin protein of muscle Z-line subunit betaprovided by RGD
Primary source: RGD:1359099
See related: Ensembl:ENSRNOG00000007330 AllianceGenome:RGD:1359099
Gene type: protein coding
RefSeq status: PROVISIONAL
Organism: Rattus norvegicus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus
Summary: Predicted to enable actin filament binding activity and beta-tubulin binding activity. Predicted to be involved in several processes, including barbed-end actin filament capping; regulation of cell morphogenesis; and regulation of plasma membrane bounded cell projection assembly. Predicted to act upstream of or within several processes, including actin polymerization or depolymerization; negative regulation of microtubule polymerization; and plasma membrane bounded cell projection organization. Located in dendritic spine and neuronal cell body. Biomarker of dementia. Orthologous to human CAPZB (capping actin protein of muscle Z-line subunit beta). [provided by Alliance of Genome Resources, Apr 2022]
Expression: Biased expression in Muscle (RPKM 274.4), Spleen (RPKM 247.3) and 9 other tissues See more
Orthologs: human mouse all
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Genomic context

Location:: 5q36

Exon count:: 12

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCr8 (GCF_036323735.1)	5	NC_086023.1 (156718619..156818623)
RS_2023_06	previous assembly	mRatBN7.2 (GCF_015227675.2)	5	NC_051340.1 (151435600..151535409)
106	previous assembly	Rnor_6.0 (GCF_000001895.5)	5	NC_005104.4 (157642742..157742487)

Chromosome 5 - NC_086023.1 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: A rat RNA-Seq transcriptomic BodyMap across 11 organs and 4 developmental stages
Description: 320 RNA samples isolated from 11 organs (adrenal gland, brain, heart, kidney, liver, lung, muscle, spleen, thymus, and testes or uterus) from both sexes of Fischer 344 rats across four developmental stages (2-, 6-, 21-, and 104-weeks-old)
BioProject: PRJNA238328
Publication: PMID 24510058
Analysis date: Mon Jun 6 17:44:12 2016

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

The goal of this study was to test the hypothesis that actin filament assembly during cardiomyocyte growth is regulated by post-translational modifications (PTMs) of CapZbeta1.
Title: Myofibril growth during cardiac hypertrophy is regulated through dual phosphorylation and acetylation of the actin capping protein CapZ.
with strain there was significant PKCepsilon translocation to the Z-disc and co-localization with CapZbeta1 or alpha-actinin, which was quantified on confocal images.
Title: Cyclic mechanical strain of myocytes modifies CapZβ1 post translationally via PKCε.
Binding of CapZ to PtdIns(3)P, which is enriched in omegasomes, stimulates actin polymerization.
Title: CapZ regulates autophagosomal membrane shaping by promoting actin assembly inside the isolation membrane.
findings reveal a novel role for neuronal clathrin-independent endocytosis controlled by actin dynamics.
Title: Clathrin-independent trafficking of AMPA receptors.
Although ADF and cofilin-1 have many redundant functions, each of these isoforms has functional differences that affect F-actin structures, cell adhesion and lamellipodial dynamics, all of which are important determinants of cell migration.
Title: Non-overlapping activities of ADF and cofilin-1 during the migration of metastatic breast tumor cells.
Suggest that after many hours of cyclic strain, a possible mechanism for cell hypertrophy is the accumulation of thin filament assembly triggered partially by the increased PIP2 level and its binding to CapZbeta1.
Title: Phosphatidylinositol 4,5-bisphosphate regulates CapZβ1 and actin dynamics in response to mechanical strain.
Thus it is possible that mechanical stimulation alters the dynamics for CapZ capping of the actin filament through the CapZbeta1 COOH terminus, known as the beta tentacle, thereby remodeling sarcomeres in cardiac myocytes.
Title: CapZ and actin capping dynamics increase in myocytes after a bout of exercise and abates in hours after stimulation ends.
Nebulin interacts with CapZ to from a thin filament of an adjacent sarcomere, thus providing a structural link between sarcomeres.
Title: Nebulin interacts with CapZ and regulates thin filament architecture within the Z-disc.
BAG3 and Hsc70 interact with actin capping protein CapZ to maintain myofibrillar integrity under mechanical stress.
Title: BAG3 and Hsc70 interact with actin capping protein CapZ to maintain myofibrillar integrity under mechanical stress.
Hence, the CapZ-NAP-22 complex could work as the nucleation site of actin polymerization or as the actin filament-anchoring site on the membrane microdomain.
Title: Biochemical interaction of an actin-capping protein, CapZ, with NAP-22.

Submit: New GeneRIF Correction See all GeneRIFs (11)

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

RH143222 (e-PCR)
- UniSTS:232469

RH128327 (e-PCR)
- UniSTS:211635

Gene Ontology Provided by RGD

Function	Evidence Code	Pubs
enables actin binding	IEA Inferred from Electronic Annotation more info
enables actin binding	ISO Inferred from Sequence Orthology more info
enables actin binding	ISS Inferred from Sequence or Structural Similarity more info
enables actin filament binding	IBA Inferred from Biological aspect of Ancestor more info
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed

Process	Evidence Code	Pubs
involved_in actin cytoskeleton organization	IEA Inferred from Electronic Annotation more info
involved_in actin polymerization or depolymerization	IEA Inferred from Electronic Annotation more info
acts_upstream_of_or_within actin polymerization or depolymerization	ISO Inferred from Sequence Orthology more info
involved_in barbed-end actin filament capping	IBA Inferred from Biological aspect of Ancestor more info
involved_in barbed-end actin filament capping	IEA Inferred from Electronic Annotation more info
involved_in biological_process	ND No biological Data available more info
involved_in cell morphogenesis	IBA Inferred from Biological aspect of Ancestor more info
acts_upstream_of_or_within cell projection organization	ISO Inferred from Sequence Orthology more info
involved_in cytoskeleton organization	ISO Inferred from Sequence Orthology more info
involved_in cytoskeleton organization	ISS Inferred from Sequence or Structural Similarity more info
involved_in lamellipodium assembly	IEA Inferred from Electronic Annotation more info
acts_upstream_of_or_within lamellipodium assembly	ISO Inferred from Sequence Orthology more info
involved_in negative regulation of filopodium assembly	IBA Inferred from Biological aspect of Ancestor more info
involved_in regulation of cell morphogenesis	IEA Inferred from Electronic Annotation more info
involved_in regulation of cell morphogenesis	ISO Inferred from Sequence Orthology more info
involved_in regulation of cell morphogenesis	ISS Inferred from Sequence or Structural Similarity more info
involved_in regulation of lamellipodium assembly	IBA Inferred from Biological aspect of Ancestor more info

Component	Evidence Code	Pubs
part_of F-actin capping protein complex	IBA Inferred from Biological aspect of Ancestor more info
part_of F-actin capping protein complex	IEA Inferred from Electronic Annotation more info
located_in Schaffer collateral - CA1 synapse	IEA Inferred from Electronic Annotation more info
is_active_in Schaffer collateral - CA1 synapse	ISO Inferred from Sequence Orthology more info
part_of WASH complex	IEA Inferred from Electronic Annotation more info
part_of WASH complex	ISO Inferred from Sequence Orthology more info
part_of WASH complex	ISS Inferred from Sequence or Structural Similarity more info
is_active_in asymmetric synapse	ISO Inferred from Sequence Orthology more info
located_in brush border	IEA Inferred from Electronic Annotation more info
located_in brush border	ISO Inferred from Sequence Orthology more info
located_in cortical cytoskeleton	IEA Inferred from Electronic Annotation more info
located_in cortical cytoskeleton	ISO Inferred from Sequence Orthology more info
located_in dendritic spine	IDA Inferred from Direct Assay more info	PubMed
located_in hippocampal mossy fiber to CA3 synapse	IEA Inferred from Electronic Annotation more info
is_active_in hippocampal mossy fiber to CA3 synapse	ISO Inferred from Sequence Orthology more info
located_in lamellipodium	IEA Inferred from Electronic Annotation more info
located_in lamellipodium	ISO Inferred from Sequence Orthology more info
located_in membrane	IEA Inferred from Electronic Annotation more info
located_in membrane	ISO Inferred from Sequence Orthology more info
located_in neuronal cell body	IDA Inferred from Direct Assay more info	PubMed
located_in postsynaptic density	IEA Inferred from Electronic Annotation more info
is_active_in postsynaptic density	ISO Inferred from Sequence Orthology more info
located_in sarcomere	IEA Inferred from Electronic Annotation more info
located_in sperm connecting piece	IEA Inferred from Electronic Annotation more info
located_in sperm connecting piece	ISO Inferred from Sequence Orthology more info

General protein information

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Preferred Names: F-actin-capping protein subunit beta

Names: F-actin capping protein beta subunit; capZ beta; capping actin protein of muscle Z-line beta subunit; capping protein (actin filament) muscle Z-line, beta

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_001005903.1 → NP_001005903.1 F-actin-capping protein subunit beta

See identical proteins and their annotated locations for NP_001005903.1

Status: PROVISIONAL

Source sequence(s)

BC083861

UniProtKB/Swiss-Prot

Q5XI32

UniProtKB/TrEMBL

A0A8I6AWP4, A6ITK5

Related

ENSRNOP00000086771.1, ENSRNOT00000101104.1

Conserved Domains (1) summary

pfam01115
Location:11 → 239

F_actin_cap_B; F-actin capping protein, beta subunit

RefSeqs of Annotated Genomes: GCF_036323735.1-RS_2024_02

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCr8

Genomic

NC_086023.1 Reference GRCr8

Range

156718619..156818623

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_006239177.5 → XP_006239239.2 F-actin-capping protein subunit beta isoform X6

UniProtKB/TrEMBL

A0A8I6AWP4

Conserved Domains (1) summary

pfam01115
Location:68 → 296

F_actin_cap_B; F-actin capping protein, beta subunit
XM_006239175.5 → XP_006239237.1 F-actin-capping protein subunit beta isoform X4

UniProtKB/TrEMBL

A0A8I6A3B7, A0A8I6AWP4

Related

ENSRNOP00000085427.1

Conserved Domains (1) summary

pfam01115
Location:41 → 269

F_actin_cap_B; F-actin capping protein, beta subunit
XM_039109681.2 → XP_038965609.1 F-actin-capping protein subunit beta isoform X3

UniProtKB/TrEMBL

A0A8I6AWP4

Conserved Domains (1) summary

pfam01115
Location:41 → 269

F_actin_cap_B; F-actin capping protein, beta subunit
XM_039109682.2 → XP_038965610.1 F-actin-capping protein subunit beta isoform X5

UniProtKB/TrEMBL

A0A8I6AWP4

Conserved Domains (1) summary

pfam01115
Location:1 → 227

F_actin_cap_B; F-actin capping protein, beta subunit
XM_006239172.5 → XP_006239234.1 F-actin-capping protein subunit beta isoform X2

UniProtKB/TrEMBL

A0A8I6AG02, A0A8L2Q5I8

Related

ENSRNOP00000092671.1

Conserved Domains (1) summary

pfam01115
Location:65 → 293

F_actin_cap_B; F-actin capping protein, beta subunit
XM_039109680.2 → XP_038965608.1 F-actin-capping protein subunit beta isoform X1

UniProtKB/TrEMBL

A0A8L2Q5I8

Conserved Domains (1) summary

pfam01115
Location:65 → 293

F_actin_cap_B; F-actin capping protein, beta subunit