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P02609 (MLRS_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Myosin regulatory light chain 2, skeletal muscle isoform
Alternative name(s):
DTNB
Fast skeletal myosin light chain 2
Short name=MLC-2
G2
LC2f
Gene names
Name:MYLPF
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length168 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Subunit structure

Myosin is a hexamer of 2 heavy chains and 4 light chains.

Post-translational modification

The N-terminus is blocked. N,N,N-trimethylalanine, found in other myosin light chains would not have been detected in the N-terminal tryptic peptide in Ref.2 because it would remain trimethylated and ninhydrin negative after hydrolysis. Ref.3

Miscellaneous

This chain binds calcium.

Sequence similarities

Contains 3 EF-hand domains.

Ontologies

Keywords
   DomainRepeat
   LigandCalcium
Metal-binding
   Molecular functionMotor protein
Muscle protein
Myosin
   PTMMethylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Cellular_componentmyosin complex

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 168167Myosin regulatory light chain 2, skeletal muscle isoform
PRO_0000019308

Regions

Domain24 – 5936EF-hand 1
Domain94 – 12936EF-hand 2
Domain130 – 16536EF-hand 3
Calcium binding37 – 4812

Amino acid modifications

Modified residue21N,N,N-trimethylalanine Probable
Modified residue151Phosphoserine Potential

Experimental info

Sequence conflict611V → L in AAA48980. Ref.1
Sequence conflict1031F → L in AAA48980. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P02609 [UniParc].

Last modified July 19, 2004. Version 2.
Checksum: FF5913861D2795F1

FASTA16818,839
        10         20         30         40         50         60 
MAPKKAKRRA AEGSSNVFSM FDQTQIQEFK EAFTVIDQNR DGIIDKDDLR ETFAAMGRLN 

        70         80         90        100        110        120 
VKNEELDAMI KEASGPINFT VFLTMFGEKL KGADPEDVIM GAFKVLDPDG KGSIKKSFLE 

       130        140        150        160 
ELLTTQCDRF TPEEIKNMWA AFPPDVAGNV DYKNICYVIT HGEDKEGE 

« Hide

References

[1]"Recombinant DNA approach for defining the primary structure of monoclonal antibody epitopes."
Reinach F.C., Fischman D.A.
J. Mol. Biol. 181:411-422(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The amino acid sequence of the L-2 light chain of chicken skeletal muscle myosin."
Suzuyama Y., Umegane T., Maita T., Matsuda G.
Hoppe-Seyler's Z. Physiol. Chem. 361:119-127(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 3-168.
[3]"The widespread distribution of alpha-N-trimethylalanine as the N-terminal amino acid of light chains from vertebrate striated muscle myosins."
Henry G.D., Trayer I.P., Brewer S., Levine B.A.
Eur. J. Biochem. 148:75-82(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT ALA-2.
[4]"Three-dimensional structure of myosin subfragment-1: a molecular motor."
Rayment I., Rypniewski W.R., Schmidt-Base K., Smith R., Tomchick D.R., Benning M.M., Winkelmann D.A., Wesenberg G., Holden H.M.
Science 261:50-58(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M11030 mRNA. Translation: AAA48980.1.
PIRMOCHLS. I50393.
RefSeqNP_001185673.1. NM_001198744.1.
UniGeneGga.839.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ALMmodel-B3-168[»]
1I84electron microscopy20.00U/Z3-164[»]
1M8Qelectron microscopy70.00B/E/H/Q29-164[»]
1MVWelectron microscopy70.00B/E/H/K/N/Q29-164[»]
1O18electron microscopy70.00E/H/K/N/Q29-164[»]
1O19electron microscopy70.00B/E/H/K/N/T29-164[»]
1O1Aelectron microscopy70.00B/E/H/K/N/Q29-164[»]
1O1Belectron microscopy70.00B/E/H/K29-164[»]
1O1Celectron microscopy70.00B/E/H/K/Q29-164[»]
1O1Delectron microscopy70.00B/E/H/K/N/Q29-164[»]
1O1Eelectron microscopy70.00B/E/H/K/N/Q29-164[»]
1O1Felectron microscopy70.00B/E/H/K29-164[»]
1O1Gelectron microscopy70.00B/E/H/K/N/Q29-164[»]
2MYSX-ray2.80B3-168[»]
2W4Aelectron microscopy35.00B16-165[»]
2W4Gelectron microscopy35.00B16-165[»]
2W4Helectron microscopy35.00B16-165[»]
ProteinModelPortalP02609.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP02609.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID776775.
KEGGgga:776775.

Organism-specific databases

CTD29895.

Phylogenomic databases

HOVERGENHBG012180.
KOK12758.
PhylomeDBP02609.

Family and domain databases

Gene3D1.10.238.10. 2 hits.
InterProIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PfamPF13405. EF-hand_6. 1 hit.
[Graphical view]
SMARTSM00054. EFh. 2 hits.
[Graphical view]
PROSITEPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP02609.
NextBio20923396.

Entry information

Entry nameMLRS_CHICK
AccessionPrimary (citable) accession number: P02609
Secondary accession number(s): Q90915
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 19, 2004
Last modified: April 16, 2014
This is version 102 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references