Skip Header

Contribute Send feedback
Read comments (?) or add your own

P13543 (MLR_AEQIR) Reviewed, UniProtKB/Swiss-Prot

Last modified July 27, 2011. Version 83. 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, striated adductor muscle

Short name=R-LC
OrganismAequipecten irradians (Bay scallop) (Argopecten irradians)
Taxonomic identifier31199 [NCBI]
Taxonomic lineageEukaryotaMetazoaMolluscaBivalviaPteriomorphiaPectinoidaPectinoideaPectinidaeArgopecten

Protein attributes

Sequence length157 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

In molluscan muscle, calcium regulation is associated with myosin rather than with actin. Muscle myosin contains two types of light chains: the catalytic light chain, essential for ATPase activity, and the regulatory light chain, a calcium-binding protein responsible for Ca2+ dependent binding and Ca2+ dependent Mg-ATPase activity.

Miscellaneous

This chain binds calcium.

Sequence similarities

Contains 2 EF-hand domains.

Ontologies

Keywords
   DomainRepeat
   LigandCalcium
   Molecular functionMotor protein
Muscle protein
Myosin
   Technical term3D-structure
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 – 157156Myosin regulatory light chain, striated adductor muscle
PRO_0000198751

Regions

Domain16 – 5136EF-hand 1
Domain85 – 12036EF-hand 2
Calcium binding29 – 4012

Secondary structure

.................... 157
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P13543 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 243CE69DB02A7772

FASTA15717,671
        10         20         30         40         50         60 
MADKAASGVL TKLPQKQIQE MKEAFSMIDV DRDGFVSKED IKAISEQLGR APDDKELTAM 

        70         80         90        100        110        120 
LKEAPGPLNF TMFLSIFSDK LSGTDSEETI RNAFAMFDEQ ETKKLNIEYI KDLLENMGDN 

       130        140        150 
FNKDEMRMTF KEAPVEGGKF DYVKFTAMIK GSGEEEA 

« Hide

References

[1]"Cloning and characterization of the scallop essential and regulatory myosin light chain cDNAs."
Goodwin E.B., Szent-Gyorgyi A.G., Leinwand L.A.
J. Biol. Chem. 262:11052-11056(1987) [PubMed: 2440882] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Regulation of scallop myosin by mutant regulatory light chains."
Goodwin E.B., Leinwand L.A., Szent-Gyorgyi A.G.
J. Mol. Biol. 216:85-93(1990) [PubMed: 2146399] [Abstract]
Cited for: SEQUENCE REVISION, MUTAGENESIS.
[3]"Structure of the regulatory domain of scallop myosin at 2.8-A resolution."
Xie X., Harrison D.H., Schlichting I., Sweet R.M., Kalabokis V.N., Szent-Gyorgyi A.G., Cohen C.
Nature 368:306-312(1994) [PubMed: 8127365] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[4]"Structure of the regulatory domain of scallop myosin at 2-A resolution: implications for regulation."
Houdusse A., Cohen C.
Structure 4:21-32(1996) [PubMed: 8805510] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M17208 mRNA. Translation: AAA27715.1. Sequence problems.
PIRB29786.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1B7TX-ray2.50Y2-157[»]
1DFKX-ray4.20Y13-151[»]
1DFLX-ray4.20W/Y13-151[»]
1KK7X-ray3.20Y2-156[»]
1KK8X-ray2.30B14-151[»]
1KQMX-ray3.00B2-156[»]
1KWOX-ray3.80B2-156[»]
1L2OX-ray2.80B2-156[»]
1QVIX-ray2.54Y2-156[»]
1S5GX-ray3.10Y2-156[»]
1SCMX-ray2.80B13-157[»]
1SR6X-ray2.75B2-156[»]
1WDCX-ray2.00B2-157[»]
2W4Telectron microscopy35.00Y16-151[»]
2W4Velectron microscopy35.00Y16-151[»]
2W4Welectron microscopy35.00Y16-151[»]
3JTDX-ray2.57B2-157[»]
3JVTX-ray2.10B2-157[»]
ProteinModelPortalP13543.
SMRP13543. Positions 12-155.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR011992. EF-hand-like_dom.
IPR018247. EF_Hand_1_Ca_BS.
IPR018249. EF_HAND_2.
IPR002048. EF_hand_Ca-bd.
[Graphical view]
Gene3DG3DSA:1.10.238.10. EF-Hand_type. 2 hits.
SMARTSM00054. EFh. 2 hits.
[Graphical view]
PROSITEPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMLR_AEQIR
AccessionPrimary (citable) accession number: P13543
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: July 27, 2011
This is version 83 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families