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Protein

Myosin regulatory light chain 12B

Gene

Myl12b

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Myosin regulatory subunit that plays an important role in regulation of both smooth muscle and nonmuscle cell contractile activity via its phosphorylation. Phosphorylation triggers actin polymerization in vascular smooth muscle. Implicated in cytokinesis, receptor capping, and cell locomotion (By similarity).By similarity

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Calcium bindingi42 – 53PROSITE-ProRule annotationAdd BLAST12

GO - Molecular functioni

  • calcium ion binding Source: InterPro
  • myosin heavy chain binding Source: MGI

GO - Biological processi

  • platelet aggregation Source: MGI
  • regulation of cell shape Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Motor protein, Muscle protein, Myosin

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-MMU-445355. Smooth Muscle Contraction.
R-MMU-5627123. RHO GTPases activate PAKs.

Names & Taxonomyi

Protein namesi
Recommended name:
Myosin regulatory light chain 12B
Alternative name(s):
Myosin regulatory light chain 2-B, smooth muscle isoform
Myosin regulatory light chain 20 kDa
Short name:
MLC20
Myosin regulatory light chain MRLC2
Gene namesi
Name:Myl12b
Synonyms:Mrlc2, Mylc2b
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:107494. Myl12b.

Subcellular locationi

GO - Cellular componenti

  • apical part of cell Source: MGI
  • brush border Source: UniProtKB
  • extracellular exosome Source: MGI
  • myosin II complex Source: MGI
  • stress fiber Source: MGI
  • Z disc Source: MGI
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002843831 – 172Myosin regulatory light chain 12BAdd BLAST172

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei19Phosphothreonine; by MLCK and ZIPK/DAPK3By similarity1
Modified residuei20Phosphoserine; by MLCK and ZIPK/DAPK3By similarity1

Post-translational modificationi

Phosphorylation increases the actin-activated myosin ATPase activity and thereby regulates the contractile activity. It is required to generate the driving force in the migration of the cells but not necessary for localization of myosin-2 at the leading edge. Phosphorylation is reduced following epigallocatechin-3-O-gallate treatment (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ3THE2.
MaxQBiQ3THE2.
PaxDbiQ3THE2.
PeptideAtlasiQ3THE2.
PRIDEiQ3THE2.
TopDownProteomicsiQ3THE2.

PTM databases

iPTMnetiQ3THE2.
PhosphoSitePlusiQ3THE2.
SwissPalmiQ3THE2.

Expressioni

Gene expression databases

BgeeiENSMUSG00000034868.
CleanExiMM_MYLC2B.
GenevisibleiQ3THE2. MM.

Interactioni

Subunit structurei

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

GO - Molecular functioni

  • myosin heavy chain binding Source: MGI

Protein-protein interaction databases

BioGridi212551. 4 interactors.
DIPiDIP-31955N.
IntActiQ3THE2. 20 interactors.
MINTiMINT-1953638.
STRINGi10090.ENSMUSP00000042364.

Structurei

3D structure databases

ProteinModelPortaliQ3THE2.
SMRiQ3THE2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini29 – 64EF-hand 1PROSITE-ProRule annotationAdd BLAST36
Domaini98 – 133EF-hand 2PROSITE-ProRule annotationAdd BLAST36
Domaini134 – 169EF-hand 3PROSITE-ProRule annotationAdd BLAST36

Sequence similaritiesi

Contains 3 EF-hand domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0031. Eukaryota.
COG5126. LUCA.
GeneTreeiENSGT00760000119196.
HOGENOMiHOG000233018.
InParanoidiQ3THE2.
KOiK12757.
OMAiNGQFDYV.
OrthoDBiEOG091G0QF6.
PhylomeDBiQ3THE2.
TreeFamiTF314218.

Family and domain databases

CDDicd00051. EFh. 1 hit.
Gene3Di1.10.238.10. 2 hits.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR015070. EF_hand_DJBP.
IPR002048. EF_hand_dom.
[Graphical view]
PfamiPF08976. EF-hand_11. 1 hit.
PF13405. EF-hand_6. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 2 hits.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q3THE2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSKKAKTKT TKKRPQRATS NVFAMFDQSQ IQEFKEAFNM IDQNRDGFID
60 70 80 90 100
KEDLHDMLAS LGKNPTDAYL DAMMNEAPGP INFTMFLTMF GEKLNGTDPE
110 120 130 140 150
DVIRNAFACF DEEATGTIQE DYLRELLTTM GDRFTDEEVD ELYREAPIDK
160 170
KGNFNYIEFT RILKHGAKDK DD
Length:172
Mass (Da):19,779
Last modified:April 17, 2007 - v2
Checksum:i78FF911630F3870B
GO

Sequence cautioni

The sequence BAE35646 differs from that shown. Reason: Frameshift at position 159.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti45R → Q in BAE40255 (PubMed:16141072).Curated1
Sequence conflicti79G → A in BAE35646 (PubMed:16141072).Curated1
Sequence conflicti159F → V in BAE35646 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002885 mRNA. Translation: BAB22432.1.
AK005133 mRNA. Translation: BAB23832.1.
AK146115 mRNA. Translation: BAE26912.1.
AK160123 mRNA. Translation: BAE35646.1. Frameshift.
AK168316 mRNA. Translation: BAE40255.1.
BC028878 mRNA. Translation: AAH28878.1.
BC099425 mRNA. Translation: AAH99425.1.
BC131925 mRNA. Translation: AAI31926.1.
BC131927 mRNA. Translation: AAI31928.1.
CCDSiCCDS28954.1.
RefSeqiNP_075891.1. NM_023402.2.
UniGeneiMm.261329.

Genome annotation databases

EnsembliENSMUST00000038446; ENSMUSP00000042364; ENSMUSG00000034868.
GeneIDi67938.
KEGGimmu:67938.
UCSCiuc008dlv.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002885 mRNA. Translation: BAB22432.1.
AK005133 mRNA. Translation: BAB23832.1.
AK146115 mRNA. Translation: BAE26912.1.
AK160123 mRNA. Translation: BAE35646.1. Frameshift.
AK168316 mRNA. Translation: BAE40255.1.
BC028878 mRNA. Translation: AAH28878.1.
BC099425 mRNA. Translation: AAH99425.1.
BC131925 mRNA. Translation: AAI31926.1.
BC131927 mRNA. Translation: AAI31928.1.
CCDSiCCDS28954.1.
RefSeqiNP_075891.1. NM_023402.2.
UniGeneiMm.261329.

3D structure databases

ProteinModelPortaliQ3THE2.
SMRiQ3THE2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi212551. 4 interactors.
DIPiDIP-31955N.
IntActiQ3THE2. 20 interactors.
MINTiMINT-1953638.
STRINGi10090.ENSMUSP00000042364.

PTM databases

iPTMnetiQ3THE2.
PhosphoSitePlusiQ3THE2.
SwissPalmiQ3THE2.

Proteomic databases

EPDiQ3THE2.
MaxQBiQ3THE2.
PaxDbiQ3THE2.
PeptideAtlasiQ3THE2.
PRIDEiQ3THE2.
TopDownProteomicsiQ3THE2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000038446; ENSMUSP00000042364; ENSMUSG00000034868.
GeneIDi67938.
KEGGimmu:67938.
UCSCiuc008dlv.1. mouse.

Organism-specific databases

CTDi103910.
MGIiMGI:107494. Myl12b.

Phylogenomic databases

eggNOGiKOG0031. Eukaryota.
COG5126. LUCA.
GeneTreeiENSGT00760000119196.
HOGENOMiHOG000233018.
InParanoidiQ3THE2.
KOiK12757.
OMAiNGQFDYV.
OrthoDBiEOG091G0QF6.
PhylomeDBiQ3THE2.
TreeFamiTF314218.

Enzyme and pathway databases

ReactomeiR-MMU-445355. Smooth Muscle Contraction.
R-MMU-5627123. RHO GTPases activate PAKs.

Miscellaneous databases

PROiQ3THE2.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000034868.
CleanExiMM_MYLC2B.
GenevisibleiQ3THE2. MM.

Family and domain databases

CDDicd00051. EFh. 1 hit.
Gene3Di1.10.238.10. 2 hits.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR015070. EF_hand_DJBP.
IPR002048. EF_hand_dom.
[Graphical view]
PfamiPF08976. EF-hand_11. 1 hit.
PF13405. EF-hand_6. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 2 hits.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 3 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiML12B_MOUSE
AccessioniPrimary (citable) accession number: Q3THE2
Secondary accession number(s): Q3TVH2, Q9CQL8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: April 17, 2007
Last modified: November 30, 2016
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.By similarity

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.