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Protein

Myosin regulatory light chain 12B

Gene

Myl12b

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 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 similarity1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi42 – 5312Add
BLAST

GO - Molecular functioni

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 12B
Alternative name(s):
Myosin RLC-B
Myosin regulatory light chain 2-B, smooth muscle isoform
Short name:
MLC-2
Myosin regulatory light chain 20 kDa
Short name:
MLC20
Myosin regulatory light chain MRLC2
Gene namesi
Name:Myl12b
Synonyms:Mrlc2, Mrlcb, Mylc2b
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi628855. Myl12b.

Subcellular locationi

GO - Cellular componenti

  • myosin complex Source: UniProtKB-KW
  • protein complex Source: RGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 172172Myosin regulatory light chain 12BPRO_0000198740Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei19 – 191Phosphothreonine; by MLCK and ZIPK/DAPK31 Publication
Modified residuei20 – 201Phosphoserine; by MLCK and ZIPK/DAPK31 Publication

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 tratment (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP18666.
PRIDEiP18666.

PTM databases

iPTMnetiP18666.
PhosphoSiteiP18666.

Expressioni

Gene expression databases

BgeeiENSRNOG00000015733.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi248423. 1 interaction.
IntActiP18666. 1 interaction.
STRINGi10116.ENSRNOP00000045992.

Structurei

3D structure databases

ProteinModelPortaliP18666.
SMRiP18666. Positions 28-164.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini29 – 6436EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini98 – 13336EF-hand 2PROSITE-ProRule annotationAdd
BLAST
Domaini134 – 16936EF-hand 3PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 3 EF-hand domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0031. Eukaryota.
COG5126. LUCA.
HOGENOMiHOG000233018.
InParanoidiP18666.
KOiK12757.
PhylomeDBiP18666.
TreeFamiTF314218.

Family and domain databases

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.

P18666-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSKKAKTKT TKKRPQRATS NVFAMFDQSQ IQEFKEAFNM IDQNRDGFID
60 70 80 90 100
KEDLHDMLAS LGKNPTDAYL DAMMNEAPGR INFTMFLTMF GEKLNGTDPE
110 120 130 140 150
DVIRNAFACF DEEATGTIQE DYLRELLTTM GDRFTDEEVD ELYREAPIDK
160 170
KGNFNYIEFT RILKHGAKDK DD
Length:172
Mass (Da):19,838
Last modified:January 23, 2007 - v3
Checksum:i4D9CC47632D1852B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti80 – 801R → P in AAH60577 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52840 mRNA. Translation: CAA37024.1.
BC060577 mRNA. Translation: AAH60577.1.
PIRiB37100.
S11632.
RefSeqiNP_059039.2. NM_017343.2.
UniGeneiRn.103179.
Rn.214633.

Genome annotation databases

GeneIDi50685.
KEGGirno:50685.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52840 mRNA. Translation: CAA37024.1.
BC060577 mRNA. Translation: AAH60577.1.
PIRiB37100.
S11632.
RefSeqiNP_059039.2. NM_017343.2.
UniGeneiRn.103179.
Rn.214633.

3D structure databases

ProteinModelPortaliP18666.
SMRiP18666. Positions 28-164.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248423. 1 interaction.
IntActiP18666. 1 interaction.
STRINGi10116.ENSRNOP00000045992.

PTM databases

iPTMnetiP18666.
PhosphoSiteiP18666.

Proteomic databases

PaxDbiP18666.
PRIDEiP18666.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi50685.
KEGGirno:50685.

Organism-specific databases

CTDi103910.
RGDi628855. Myl12b.

Phylogenomic databases

eggNOGiKOG0031. Eukaryota.
COG5126. LUCA.
HOGENOMiHOG000233018.
InParanoidiP18666.
KOiK12757.
PhylomeDBiP18666.
TreeFamiTF314218.

Miscellaneous databases

PROiP18666.

Gene expression databases

BgeeiENSRNOG00000015733.

Family and domain databases

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_RAT
AccessioniPrimary (citable) accession number: P18666
Secondary accession number(s): Q6P9V4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 141 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

This chain binds calcium.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.