MYL1 myosin light chain 1 [Oryctolagus cuniculus (rabbit)] - Gene

Summary

Gene symbol: MYL1
Gene description: myosin light chain 1
See related: Ensembl:ENSOCUG00000014182
Gene type: protein coding
RefSeq status: PROVISIONAL
Organism: Oryctolagus cuniculus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus
Orthologs: all
: Try the new Gene page
Try the new Transcripts and proteins table

Genomic context

Location:: chromosome: 3

Exon count:: 9

Annotation release	Status	Assembly	Chr	Location
RS_2024_11	current	mOryCun1.1 (GCF_964237555.1)	3	NC_091434.1 (29532529..29554902)
RS_2023_02	previous assembly	UM_NZW_1.0 (GCF_009806435.1)	7	NC_067380.1 (22446326..22468378)

Chromosome 3 - NC_091434.1 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

Go to the top of the page Help

Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Bibliography

Go to the top of the page Help

GeneRIFs: Gene References Into Functions

What's a GeneRIF?

altered TM-actin contacts destabilized the thin filament and affected the actin-myosin interactions
Title: Abnormal movement of tropomyosin and response of myosin heads and actin during the ATPase cycle caused by the Arg167His, Arg167Gly and Lys168Glu mutations in TPM1 gene.
changes in thermal unfolding and the domain structure of myosin subfragment 1, were studied.
Title: Does Interaction between the Motor and Regulatory Domains of the Myosin Head Occur during ATPase Cycle? Evidence from Thermal Unfolding Studies on Myosin Subfragment 1.
Data indicate that the W-to-S structural transition in the actomyosin complex during the ATPase cycle is strongly modulated by myosin essential light chains (ELCs) isoforms, with implications for contractile function.
Title: Amplitude of the actomyosin power stroke depends strongly on the isoform of the myosin essential light chain.
Data indicate that phosphorylation of skeletal myosin regulatory light chain (RLC) plays a role in regulation of skeletal muscle contraction.
Title: Comparison of orientation and rotational motion of skeletal muscle cross-bridges containing phosphorylated and dephosphorylated myosin regulatory light chain.
During the active interaction of actin and ATP with myosin, myosin light chain A1 is more effective at stabilizing the strong-binding state of actomyosin, while myosin light chain A2 tends to stabilize the weak-binding W state.
Title: The structural dynamics of actin during active interaction with myosin depends on the isoform of the essential light chain.
Independently of the thick filament backbone, the velocity of skeletal muscle myosin is decreased upon phosphorylation of the myosin regulatory light chain due to an increase in the myosin duty cycle.
Title: The molecular effects of skeletal muscle myosin regulatory light chain phosphorylation.
The orientation of the essential light chain region of myosin in skeletal muscle was determined by polarized fluorescence.
Title: Orientation of the essential light chain region of myosin in relaxed, active, and rigor muscle.

Submit: New GeneRIF Correction

General gene information

Go to the top of the page Help

Gene Ontology Provided by RefSeq

Function	Evidence Code	Pubs
enables calcium ion binding	IEA Inferred from Electronic Annotation more info	PubMed

Component	Evidence Code	Pubs
located_in contractile muscle fiber	IEA Inferred from Electronic Annotation more info	PubMed
part_of myosin II complex	IEA Inferred from Electronic Annotation more info	PubMed

General protein information

Go to the top of the page Help

Preferred Names: myosin light chain 1/3, skeletal muscle isoform

Names: A1 catalytic; A2 catalytic; MLC1/MLC3; MLC1F; MLC1F/MLC3F; MLC3F; alkali myosin light chain 1; alkali myosin light chain 3; myosin light chain A1/A2; myosin light chain alkali 1/2; myosin, light chain 1, alkali; skeletal, fast

NCBI Reference Sequences (RefSeq)

Go to the top of the page Help

NEW Try the new Transcript table

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_001101713.1 → NP_001095183.1 myosin light chain 1/3, skeletal muscle isoform

See identical proteins and their annotated locations for NP_001095183.1

Status: PROVISIONAL

Source sequence(s)

X54041

UniProtKB/Swiss-Prot

P02602, P02603

UniProtKB/TrEMBL

A0A5F9D774

Related

ENSOCUP00000049094.1, ENSOCUT00000061230.1

Conserved Domains (1) summary

PTZ00184
Location:43 → 191

PTZ00184; calmodulin; Provisional

RefSeqs of Annotated Genomes: GCF_964237555.1-RS_2024_11

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

Reference mOryCun1.1

Genomic

NC_091434.1 Reference mOryCun1.1

Range

29532529..29554902

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_008258923.3 → XP_008257145.1 myosin light chain 1/3, skeletal muscle isoform isoform X1

See identical proteins and their annotated locations for XP_008257145.1

UniProtKB/Swiss-Prot

P02602

Related

ENSOCUP00000022702.2

Conserved Domains (4) summary

PTZ00184
Location:4 → 149

PTZ00184; calmodulin; Provisional

cd00051
Location:87 → 148

EFh; EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to ...

pfam13405
Location:10 → 39

EF-hand_6; EF-hand domain

cl08302
Location:10 → 74

EFh; EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to ...