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Protein

Myosin regulatory light polypeptide 9

Gene

MYL9

Organism
Sus scrofa (Pig)
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. Implicated in cytokinesis, receptor capping, and cell locomotion (By similarity).By similarity

Regions

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Motor protein, Muscle protein, Myosin

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Myosin regulatory light polypeptide 9
Alternative name(s):
20 kDa myosin light chain
Short name:
LC20
Myosin regulatory light chain 2, smooth muscle isoform
Myosin regulatory light chain 9
Gene namesi
Name:MYL9
Synonyms:MYRL2
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Chromosome 17

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 172171Myosin regulatory light polypeptide 9PRO_0000198737Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei19 – 191Phosphothreonine; by MLCK, CIT and ROCK2By similarity
Modified residuei20 – 201Phosphoserine; by CDC42BP, CIT, MLCK, PAK1, ROCK1, ROCK2, DAPK1; DAPK2 and ZIPK/DAPK3By similarity

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 (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP29269.
PRIDEiP29269.

Expressioni

Tissue specificityi

Smooth muscle tissues and in some, but not all, nonmuscle cells.

Gene expression databases

GenevisibleiP29269. SS.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000026757.

Structurei

3D structure databases

ProteinModelPortaliP29269.
SMRiP29269. Positions 26-168.
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.
GeneTreeiENSGT00760000119196.
HOGENOMiHOG000233018.
HOVERGENiHBG012180.
InParanoidiP29269.
KOiK12755.
OMAiRINADNE.
OrthoDBiEOG7992RX.
TreeFamiTF314218.

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.
PF13833. EF-hand_8. 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.

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

P29269-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSKRAKAKT TKKRPQRATS NVFAMFDQSQ IQEFKEAFNM IDQNRDGFID
60 70 80 90 100
KEDLHDMLAS LGKNPTDEYL EGMMSEAPGP INFTMFLTMF GEKLNGTDPE
110 120 130 140 150
DVIRNAFACF DEEASGFIHE DHLRELLTTM GDRFTDEEVD EMYREAPIDK
160 170
KGNFNYVEFT RILKHGAKDK DD
Length:172
Mass (Da):19,827
Last modified:September 2, 2008 - v2
Checksum:i4C9839E85154CDA8
GO

Sequence databases

PIRiJX0232.
RefSeqiNP_001231401.1. NM_001244472.1.
UniGeneiSsc.54244.

Genome annotation databases

EnsembliENSSSCT00000023008; ENSSSCP00000026757; ENSSSCG00000024230.
GeneIDi100157760.
KEGGissc:100157760.

Cross-referencesi

Sequence databases

PIRiJX0232.
RefSeqiNP_001231401.1. NM_001244472.1.
UniGeneiSsc.54244.

3D structure databases

ProteinModelPortaliP29269.
SMRiP29269. Positions 26-168.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000026757.

Proteomic databases

PaxDbiP29269.
PRIDEiP29269.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSSSCT00000023008; ENSSSCP00000026757; ENSSSCG00000024230.
GeneIDi100157760.
KEGGissc:100157760.

Organism-specific databases

CTDi10398.

Phylogenomic databases

eggNOGiKOG0031. Eukaryota.
COG5126. LUCA.
GeneTreeiENSGT00760000119196.
HOGENOMiHOG000233018.
HOVERGENiHBG012180.
InParanoidiP29269.
KOiK12755.
OMAiRINADNE.
OrthoDBiEOG7992RX.
TreeFamiTF314218.

Enzyme and pathway databases

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

Gene expression databases

GenevisibleiP29269. SS.

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.
PF13833. EF-hand_8. 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...

Publicationsi

  1. "Amino acid sequence of the 20-kDa regulatory light chain of porcine aorta media smooth muscle myosin."
    Watanabe M., Hasegawa Y., Katoh T., Morita F.
    J. Biochem. 112:431-432(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, ACETYLATION AT SER-2.
    Tissue: Aorta.

Entry informationi

Entry nameiMYL9_PIG
AccessioniPrimary (citable) accession number: P29269
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: September 2, 2008
Last modified: January 20, 2016
This is version 115 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

Complete proteome, Direct protein sequencing, 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.