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Protein

Myosin regulatory light chain 2, skeletal muscle isoform

Gene

MYLPF

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi37 – 4812Add
BLAST

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Motor protein, Muscle protein, Myosin

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:MYLPF
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. myosin complex Source: UniProtKB-KW
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 168167Myosin regulatory light chain 2, skeletal muscle isoformPRO_0000019308Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N,N,N-trimethylalanine1 Publication
Modified residuei15 – 151PhosphoserineSequence Analysis

Post-translational modificationi

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 PubMed:7358336 because it would remain trimethylated and ninhydrin negative after hydrolysis.

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

PRIDEiP02609.

Interactioni

Subunit structurei

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

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ALMmodel-B3-168[»]
1I84electron microscopy20.00U/Z3-168[»]
1M8Qelectron microscopy70.00B/E/H/Q21-164[»]
1MVWelectron microscopy70.00B/E/H/K/N/Q26-164[»]
1O18electron microscopy70.00E/H/K/N/Q26-164[»]
1O19electron microscopy70.00B/E/H/K/N/T26-164[»]
1O1Aelectron microscopy70.00B/E/H/K/N/Q26-164[»]
1O1Belectron microscopy70.00B/E/H/K26-164[»]
1O1Celectron microscopy70.00B/E/H/K/Q26-164[»]
1O1Delectron microscopy70.00B/E/H/K/N/Q26-164[»]
1O1Eelectron microscopy70.00B/E/H/K/N/Q26-164[»]
1O1Felectron microscopy70.00B/E/H/K26-164[»]
1O1Gelectron microscopy70.00B/E/H/K/N/Q26-164[»]
2MYSX-ray2.80B3-168[»]
2W4Aelectron microscopy35.00B16-165[»]
2W4Gelectron microscopy35.00B16-165[»]
2W4Helectron microscopy35.00B16-165[»]
ProteinModelPortaliP02609.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02609.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 5936EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini94 – 12936EF-hand 2PROSITE-ProRule annotationAdd
BLAST
Domaini130 – 16536EF-hand 3PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 3 EF-hand domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

HOVERGENiHBG012180.
InParanoidiP02609.
KOiK12758.
PhylomeDBiP02609.

Family and domain databases

Gene3Di1.10.238.10. 2 hits.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PfamiPF13405. EF-hand_6. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 2 hits.
[Graphical view]
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P02609-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPKKAKRRA AEGSSNVFSM FDQTQIQEFK EAFTVIDQNR DGIIDKDDLR
60 70 80 90 100
ETFAAMGRLN VKNEELDAMI KEASGPINFT VFLTMFGEKL KGADPEDVIM
110 120 130 140 150
GAFKVLDPDG KGSIKKSFLE ELLTTQCDRF TPEEIKNMWA AFPPDVAGNV
160
DYKNICYVIT HGEDKEGE
Length:168
Mass (Da):18,839
Last modified:July 18, 2004 - v2
Checksum:iFF5913861D2795F1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti61 – 611V → L in AAA48980 (PubMed:2580100).Curated
Sequence conflicti103 – 1031F → L in AAA48980 (PubMed:2580100).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M11030 mRNA. Translation: AAA48980.1.
PIRiI50393. MOCHLS.
RefSeqiNP_001185673.1. NM_001198744.1.
UniGeneiGga.839.

Genome annotation databases

GeneIDi776775.
KEGGigga:776775.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M11030 mRNA. Translation: AAA48980.1.
PIRiI50393. MOCHLS.
RefSeqiNP_001185673.1. NM_001198744.1.
UniGeneiGga.839.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ALMmodel-B3-168[»]
1I84electron microscopy20.00U/Z3-168[»]
1M8Qelectron microscopy70.00B/E/H/Q21-164[»]
1MVWelectron microscopy70.00B/E/H/K/N/Q26-164[»]
1O18electron microscopy70.00E/H/K/N/Q26-164[»]
1O19electron microscopy70.00B/E/H/K/N/T26-164[»]
1O1Aelectron microscopy70.00B/E/H/K/N/Q26-164[»]
1O1Belectron microscopy70.00B/E/H/K26-164[»]
1O1Celectron microscopy70.00B/E/H/K/Q26-164[»]
1O1Delectron microscopy70.00B/E/H/K/N/Q26-164[»]
1O1Eelectron microscopy70.00B/E/H/K/N/Q26-164[»]
1O1Felectron microscopy70.00B/E/H/K26-164[»]
1O1Gelectron microscopy70.00B/E/H/K/N/Q26-164[»]
2MYSX-ray2.80B3-168[»]
2W4Aelectron microscopy35.00B16-165[»]
2W4Gelectron microscopy35.00B16-165[»]
2W4Helectron microscopy35.00B16-165[»]
ProteinModelPortaliP02609.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP02609.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi776775.
KEGGigga:776775.

Organism-specific databases

CTDi29895.

Phylogenomic databases

HOVERGENiHBG012180.
InParanoidiP02609.
KOiK12758.
PhylomeDBiP02609.

Miscellaneous databases

EvolutionaryTraceiP02609.
NextBioi20923396.

Family and domain databases

Gene3Di1.10.238.10. 2 hits.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PfamiPF13405. EF-hand_6. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 2 hits.
[Graphical view]
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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(1984) [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(1979) [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(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT ALA-2.
  4. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).

Entry informationi

Entry nameiMLRS_CHICK
AccessioniPrimary (citable) accession number: P02609
Secondary accession number(s): Q90915
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 20, 1986
Last sequence update: July 18, 2004
Last modified: February 3, 2015
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

This chain binds calcium.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.