Mybpc3 myosin binding protein C3 [Rattus norvegicus (Norway rat)] - Gene

Summary

Official Symbol: Mybpc3provided by RGD
Official Full Name: myosin binding protein C3provided by RGD
Primary source: RGD:1305950
See related: EnsemblRapid:ENSRNOG00000012307 AllianceGenome:RGD:1305950
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 identical protein binding activity and myosin heavy chain binding activity. Predicted to be a structural constituent of muscle. Involved in cardiac muscle contraction and regulation of striated muscle contraction. Located in striated muscle myosin thick filament. Human ortholog(s) of this gene implicated in dilated cardiomyopathy 1MM; familial hypertrophic cardiomyopathy; hypertrophic cardiomyopathy; and hypertrophic cardiomyopathy 4. Orthologous to human MYBPC3 (myosin binding protein C3). [provided by Alliance of Genome Resources, Nov 2024]
Expression: Restricted expression toward (RPKM 5513.3) See more
Orthologs: human mouse all
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Genomic context

Location:: 3q24

Exon count:: 34

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCr8 (GCF_036323735.1)	3	NC_086021.1 (97550974..97569216)
RS_2023_06	previous assembly	mRatBN7.2 (GCF_015227675.2)	3	NC_051338.1 (77095165..77113406)
106	previous assembly	Rnor_6.0 (GCF_000001895.5)	3	NC_005102.4 (79940509..79958731)

Chromosome 3 - NC_086021.1 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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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?

cMyBP-C acts as a sarcomeric integrator of multiple signaling pathways that determines downstream physiological function.
Title: Site-specific phosphorylation of myosin binding protein-C coordinates thin and thick filament activation in cardiac muscle.
Serine 302 in cardiac myosin binding protein-C was identified as a PKCepsilon substrate that when phosphorylated contributed to the suppression of contraction and Ca(2+) transients by PKCepsilon following ET-1 stimulation.
Title: Contractile responses to endothelin-1 are regulated by PKC phosphorylation of cardiac myosin binding protein-C in rat ventricular myocytes.
Both tris-phosphorylation and Ser-Asp substitutions abolished the interaction between C1mC2 and myosin sub-fragment 2 (myosin S2) in vitro, but yielded different effects on thin filament binding.
Title: Structural and functional effects of myosin-binding protein-C phosphorylation in heart muscle are not mimicked by serine-to-aspartate substitutions.
Phosphorylation of myosin regulatory light chain (RLC) increased and remained elevated post-MI, while phosphorylation of myosin binding protein-C (MyBP-C) was initially depressed but then increased as the hearts became decompensated.
Title: A post-MI power struggle: adaptations in cardiac power occur at the sarcomere level alongside MyBP-C and RLC phosphorylation.
Data show that expression of mutant protein cMyBP-C (cMyBP-C(C10mut)) in cultured adult rat cardiomyocytes led to improper localization and contractile dysfunction.
Title: A hypertrophic cardiomyopathy-associated MYBPC3 mutation common in populations of South Asian descent causes contractile dysfunction.
These results show that the N-terminal region of MyBP-C stabilizes the ON state of thin filaments and the OFF state of thick filaments and lead to a novel hypothesis for the physiological role of MyBP-C in the regulation of cardiac contractility.
Title: Myosin binding protein-C activates thin filaments and inhibits thick filaments in heart muscle cells.
Expression of an actin binding-deficient cMyBP-C resulted in abnormal cytosolic distribution of the protein, indicating that interaction with actin is essential for the formation and/or maintenance of normal cMyBP-C sarcomeric distribution.
Title: Determination of the critical residues responsible for cardiac myosin binding protein C's interactions.
N' region of cMyBP-C is toxic to cardiomyocytes and able to induce cell death.
Title: Pathogenic properties of the N-terminal region of cardiac myosin binding protein-C in vitro.
this study suggests that cMyBP-C is an easily releasable myofilament protein that is dephosphorylated, degraded and released into the circulation post-MI.
Title: Cardiac myosin binding protein-C is a potential diagnostic biomarker for myocardial infarction.

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Gene Ontology Provided by RGD

Function	Evidence Code	Pubs
enables actin binding	IEA Inferred from Electronic Annotation more info
enables identical protein binding	IEA Inferred from Electronic Annotation more info
enables identical protein binding	ISO Inferred from Sequence Orthology more info
enables metal ion binding	IEA Inferred from Electronic Annotation more info
enables myosin binding	ISO Inferred from Sequence Orthology more info
enables myosin heavy chain binding	IBA Inferred from Biological aspect of Ancestor more info
enables myosin heavy chain binding	IEA Inferred from Electronic Annotation more info
enables myosin heavy chain binding	ISO Inferred from Sequence Orthology more info
enables structural constituent of muscle	IEA Inferred from Electronic Annotation more info
enables structural constituent of muscle	ISO Inferred from Sequence Orthology more info

Process	Evidence Code	Pubs
involved_in cardiac muscle contraction	IEP Inferred from Expression Pattern more info	PubMed
acts_upstream_of_or_within cardiac muscle contraction	ISO Inferred from Sequence Orthology more info
involved_in cell adhesion	IEA Inferred from Electronic Annotation more info
acts_upstream_of_or_within heart morphogenesis	ISO Inferred from Sequence Orthology more info
involved_in heart morphogenesis	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within myosin filament assembly	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within regulation of heart contraction	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within regulation of heart rate	ISO Inferred from Sequence Orthology more info
involved_in regulation of striated muscle contraction	IEP Inferred from Expression Pattern more info	PubMed
involved_in sarcomere organization	IBA Inferred from Biological aspect of Ancestor more info
acts_upstream_of_or_within sarcomere organization	ISO Inferred from Sequence Orthology more info
involved_in ventricular cardiac muscle tissue morphogenesis	IBA Inferred from Biological aspect of Ancestor more info
involved_in ventricular cardiac muscle tissue morphogenesis	IEA Inferred from Electronic Annotation more info
involved_in ventricular cardiac muscle tissue morphogenesis	ISO Inferred from Sequence Orthology more info

Component	Evidence Code	Pubs
located_in A band	IEA Inferred from Electronic Annotation more info
located_in A band	ISO Inferred from Sequence Orthology more info
is_active_in M band	IBA Inferred from Biological aspect of Ancestor more info
located_in cardiac myofibril	IEA Inferred from Electronic Annotation more info
located_in cardiac myofibril	ISO Inferred from Sequence Orthology more info
located_in intracellular membraneless organelle	IEA Inferred from Electronic Annotation more info
located_in myofibril	ISO Inferred from Sequence Orthology more info
located_in myosin filament	IEA Inferred from Electronic Annotation more info
located_in sarcomere	ISO Inferred from Sequence Orthology more info
located_in striated muscle myosin thick filament	IDA Inferred from Direct Assay more info	PubMed
located_in striated muscle myosin thick filament	IEA Inferred from Electronic Annotation more info
located_in striated muscle myosin thick filament	ISO Inferred from Sequence Orthology more info

General protein information

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Preferred Names: myosin-binding protein C, cardiac-type

Names: cardiac MyBP-C; myosin binding protein C, cardiac

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_001106490.1 → NP_001099960.1 myosin-binding protein C, cardiac-type

See identical proteins and their annotated locations for NP_001099960.1

Status: PROVISIONAL

Source sequence(s)

CH473949

UniProtKB/Swiss-Prot

P56741

UniProtKB/TrEMBL

A0A8I5ZRN0

Related

ENSRNOP00000016652.8, ENSRNOT00000016652.8

Conserved Domains (8) summary

cd05748
Location:990 → 1062

Ig_Titin_like; Immunoglobulin (Ig)-like domain of titin and similar proteins

cd05894
Location:656 → 768

Ig_C5_MyBP-C; C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C)

smart00408
Location:1195 → 1257

IGc2; Immunoglobulin C-2 Type

smart00410
Location:981 → 1062

IG_like; Immunoglobulin like

cd00063
Location:772 → 862

FN3; Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all ...

pfam07679
Location:1181 → 1270

I-set; Immunoglobulin I-set domain

pfam00047
Location:165 → 249

ig; Immunoglobulin domain

cl11960
Location:40 → 92

Ig; Immunoglobulin domain