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Protein

Myosin light chain 3

Gene

Myl3

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

Functioni

Regulatory light chain of myosin. Does not bind calcium.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Motor protein, Muscle protein, Myosin

Enzyme and pathway databases

ReactomeiR-MMU-390522. Striated Muscle Contraction.

Names & Taxonomyi

Protein namesi
Recommended name:
Myosin light chain 3Curated
Alternative name(s):
Myosin alkali light chain 1, ventricular/slow skeletal muscle isoform1 Publication
Myosin light chain 1, slow-twitch muscle B/ventricular isoformBy similarity
Short name:
MLC1SBBy similarity
Gene namesi
Name:Myl3Imported
Synonyms:Mlc1vImported, MylcImported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:97268. Myl3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 204203Myosin light chain 3PRO_0000198697Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N,N,N-trimethylalanine; by NTM11 Publication
Modified residuei97 – 971PhosphothreonineBy similarity
Modified residuei136 – 1361PhosphothreonineCombined sources
Modified residuei138 – 1381PhosphothreonineBy similarity
Modified residuei139 – 1391PhosphotyrosineBy similarity
Modified residuei188 – 1881PhosphoserineCombined sources

Post-translational modificationi

N-terminus is methylated by METTL11A/NTM1.1 Publication

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

EPDiP09542.
MaxQBiP09542.
PaxDbiP09542.
PRIDEiP09542.

2D gel databases

UCD-2DPAGEP09542.

PTM databases

iPTMnetiP09542.
PhosphoSiteiP09542.

Expressioni

Gene expression databases

BgeeiP09542.
CleanExiMM_MYL3.
ExpressionAtlasiP09542. baseline and differential.
GenevisibleiP09542. MM.

Interactioni

Subunit structurei

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

GO - Molecular functioni

Protein-protein interaction databases

BioGridi201654. 1 interaction.
IntActiP09542. 2 interactions.
MINTiMINT-4102127.
STRINGi10090.ENSMUSP00000078715.

Structurei

3D structure databases

ProteinModelPortaliP09542.
SMRiP09542. Positions 58-203.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini58 – 9538EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini137 – 17236EF-hand 2PROSITE-ProRule annotationAdd
BLAST
Domaini172 – 20433EF-hand 3PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 3 EF-hand domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0030. Eukaryota.
COG5126. LUCA.
GeneTreeiENSGT00590000082921.
HOGENOMiHOG000233018.
HOVERGENiHBG012180.
InParanoidiP09542.
KOiK12749.
OMAiRPKEAEF.
OrthoDBiEOG7HQN9N.
PhylomeDBiP09542.
TreeFamiTF351553.

Family and domain databases

Gene3Di1.10.238.10. 2 hits.
InterProiIPR011992. EF-hand-dom_pair.
IPR002048. EF_hand_dom.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS50222. EF_HAND_2. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P09542-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPKKPEPKK DDAKAAAPKA APAPAAAPAA APAAAPEPER PKEAEFDASK
60 70 80 90 100
IKIEFTPEQI EEFKEAFLLF DRTPKGEMKI TYGQCGDVLR ALGQNPTQAE
110 120 130 140 150
VLRVLGKPKQ EELNSKMMDF ETFLPMLQHI SKNKDTGTYE DFVEGLRVFD
160 170 180 190 200
KEGNGTVMGA ELRHVLATLG ERLTEDEVEK LMAGQEDSNG CINYEAFVKH

IMAS
Length:204
Mass (Da):22,422
Last modified:January 23, 2007 - v4
Checksum:i3DF39389FF5BAB41
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002312 mRNA. Translation: BAB22006.1.
AK011518 mRNA. Translation: BAB27672.1.
AK146943 mRNA. Translation: BAE27552.1.
BC061222 mRNA. Translation: AAH61222.1.
X12972 Genomic DNA. Translation: CAA31415.1.
CCDSiCCDS23571.1.
PIRiS01945.
RefSeqiNP_034989.1. NM_010859.2.
UniGeneiMm.7353.

Genome annotation databases

EnsembliENSMUST00000079784; ENSMUSP00000078715; ENSMUSG00000059741.
GeneIDi17897.
KEGGimmu:17897.
UCSCiuc009rur.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002312 mRNA. Translation: BAB22006.1.
AK011518 mRNA. Translation: BAB27672.1.
AK146943 mRNA. Translation: BAE27552.1.
BC061222 mRNA. Translation: AAH61222.1.
X12972 Genomic DNA. Translation: CAA31415.1.
CCDSiCCDS23571.1.
PIRiS01945.
RefSeqiNP_034989.1. NM_010859.2.
UniGeneiMm.7353.

3D structure databases

ProteinModelPortaliP09542.
SMRiP09542. Positions 58-203.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201654. 1 interaction.
IntActiP09542. 2 interactions.
MINTiMINT-4102127.
STRINGi10090.ENSMUSP00000078715.

PTM databases

iPTMnetiP09542.
PhosphoSiteiP09542.

2D gel databases

UCD-2DPAGEP09542.

Proteomic databases

EPDiP09542.
MaxQBiP09542.
PaxDbiP09542.
PRIDEiP09542.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000079784; ENSMUSP00000078715; ENSMUSG00000059741.
GeneIDi17897.
KEGGimmu:17897.
UCSCiuc009rur.1. mouse.

Organism-specific databases

CTDi4634.
MGIiMGI:97268. Myl3.

Phylogenomic databases

eggNOGiKOG0030. Eukaryota.
COG5126. LUCA.
GeneTreeiENSGT00590000082921.
HOGENOMiHOG000233018.
HOVERGENiHBG012180.
InParanoidiP09542.
KOiK12749.
OMAiRPKEAEF.
OrthoDBiEOG7HQN9N.
PhylomeDBiP09542.
TreeFamiTF351553.

Enzyme and pathway databases

ReactomeiR-MMU-390522. Striated Muscle Contraction.

Miscellaneous databases

PROiP09542.
SOURCEiSearch...

Gene expression databases

BgeeiP09542.
CleanExiMM_MYL3.
ExpressionAtlasiP09542. baseline and differential.
GenevisibleiP09542. MM.

Family and domain databases

Gene3Di1.10.238.10. 2 hits.
InterProiIPR011992. EF-hand-dom_pair.
IPR002048. EF_hand_dom.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS50222. EF_HAND_2. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryo, Heart and Kidney.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Heart and Lung.
  3. "Promoter analysis of myosin alkali light chain genes expressed in mouse striated muscle."
    Cohen A., Barton P.J.R., Robert B., Garner I., Alonso S., Buckingham M.E.
    Nucleic Acids Res. 16:10037-10052(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-52.
    Strain: C3H/HeJ.
    Tissue: Spleen.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-136 AND SER-188, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Heart, Kidney and Lung.
  5. "NRMT is an alpha-N-methyltransferase that methylates RCC1 and retinoblastoma protein."
    Tooley C.E., Petkowski J.J., Muratore-Schroeder T.L., Balsbaugh J.L., Shabanowitz J., Sabat M., Minor W., Hunt D.F., Macara I.G.
    Nature 466:1125-1128(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE OF INITIATOR METHIONINE, METHYLATION AT ALA-2.

Entry informationi

Entry nameiMYL3_MOUSE
AccessioniPrimary (citable) accession number: P09542
Secondary accession number(s): Q3UIF4, Q9CQZ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 128 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, 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.