Reviewed, UniProtKB/Swiss-Prot P10916 (MLRV_HUMAN)

Names and origin

Protein names

Recommended name:
    Myosin regulatory light chain 2, ventricular/cardiac muscle isoform
      Short name=MLC-2v
      Short name=MLC-2

Gene names

Name:

MYL2

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	166 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Subunit structure	Myosin is an hexamer of 2 heavy chains and 4 light chains.
Involvement in disease	Defects in MYL2 are the cause of cardiomyopathy familial hypertrophic type 10 (CMH10) [MIM:608758]. Familial hypertrophic cardiomyopathy is a hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death. Ref.8 Ref.9 Ref.10 Ref.12 Defects in MYL2 are the cause of cardiomyopathy familial hypertrophic with mid-left ventricular chamber type 2 (MVC2) [MIM:608758]. MVC2 is a very rare variant of familial hypertrophic cardiomyopathy, characterized by mid-left ventricular chamber thickening.
Miscellaneous	This chain binds calcium.
Sequence similarities	Contains 3 EF-hand domains.

Ontologies

Keywords
Coding sequence diversity	Polymorphism
Disease	Cardiomyopathy Disease mutation
Domain	Repeat
Ligand	Calcium
Molecular function	Motor protein Muscle protein Myosin
PTM	Methylation
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	cardiac myofibril assembly Inferred from sequence or structural similarity. Source: UniProtKB heart contraction Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of cell growth Inferred from mutant phenotype. Source: UniProtKB regulation of striated muscle contraction Ref.7 Traceable author statement. Source: ProtInc ventricular cardiac muscle tissue morphogenesis Ref.7 Inferred from mutant phenotype. Source: UniProtKB
Cellular component	myosin complex Traceable author statement. Source: UniProtKB sarcomere Traceable author statement. Source: UniProtKB
Molecular function	actin monomer binding Inferred from direct assay. Source: UniProtKB calcium ion binding Inferred from direct assay. Source: MGI motor activity Inferred from electronic annotation. Source: UniProtKB-KW myosin heavy chain binding Ref.4 Non-traceable author statement. Source: UniProtKB structural constituent of muscle Ref.7 Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
USP6	P35125-3	2	EBI-725770,EBI-954590

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 166	165	Myosin regulatory light chain 2, ventricular/cardiac muscle isoform		PRO_0000198727
Regions
	Domain	24 – 59	36	EF-hand 1
	Domain	94 – 129	36	EF-hand 2
	Domain	130 – 165	36	EF-hand 3
	Calcium binding	37 – 48	12
Amino acid modifications
	Modified residue	2	1	N,N,N-trimethylalanine By similarity
Natural variations
	Natural variant	13	1	A → T in MVC2. Ref.7		VAR_004601
	Natural variant	18	1	F → L in CMH10. dbSNP rs28932774.		VAR_004602
	Natural variant	22	1	E → K in CMH10 and MVC2. Ref.9 Ref.7		VAR_004603
	Natural variant	57	1	G → R: dbSNP rs2428140.		VAR_029449
	Natural variant	58	1	R → Q in CMH10. dbSNP rs28933099.		VAR_004604
	Natural variant	95	1	P → A in MVC2. Ref.7		VAR_004605
	Natural variant	166	1	D → V in CMH10. Ref.10		VAR_019844

Sequences

	Sequence		Length	Mass (Da)
	P10916-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: EA0BEF886AA3FAF5	FASTA	166	18,789
	10 20 30 40 50 60 MAPKKAKKRA GGANSNVFSM FEQTQIQEFK EAFTIMDQNR DGFIDKNDLR DTFAALGRVN 70 80 90 100 110 120 VKNEEIDEMI KEAPGPINFT VFLTMFGEKL KGADPEETIL NAFKVFDPEG KGVLKADYVR 130 140 150 160 EMLTTQAERF SKEEVDQMFA AFPPDVTGNL DYKNLVHIIT HGEEKD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and nucleotide sequence of the cDNA encoding human ventricular myosin light chain 2." Libera L.D., Hoffmann E., Floroff M., Jackowski G. Nucleic Acids Res. 17:2360-2360(1989) [PubMed: 2704627] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Heart.
[2]	Wu Q.L. Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Muscle.
[3]	Margossian S.S., Umeda P.K., Sciaky D., Anderson P.A.W. Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Interaction of a conserved peptide domain in recombinant human ventricular myosin light chain-2 with myosin heavy chain." Wadgaonkar R., Shafiq S., Rajmanickam C., Siddiqui M.A. Cell. Mol. Biol. Res. 39:13-26(1993) [PubMed: 8287067] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Prostate and Skeletal muscle.
[6]	"The major protein expression profile and two-dimensional protein database of human heart." Kovalyov L.I., Shishkin S.S., Efimochkin A.S., Kovalyova M.A., Ershova E.S., Egorov T.A., Musalyamov A.K. Electrophoresis 16:1160-1169(1995) [PubMed: 7498159] [Abstract] Cited for: PROTEIN SEQUENCE OF 138-144. Tissue: Heart.
[7]	"Mutations in either the essential or regulatory light chains of myosin are associated with a rare myopathy in human heart and skeletal muscle." Poetter K., Jiang H., Hassanzadeh S., Master S.R., Chang A., Dalakas M.C., Rayment I., Sellers J.R., Fananapazir L., Epstein N.D. Nat. Genet. 13:63-69(1996) [PubMed: 8673105] [Abstract] Cited for: VARIANTS MVC2 THR-13; LYS-22 AND ALA-95.
[8]	"Identification of two novel mutations in the ventricular regulatory myosin light chain gene (MYL2) associated with familial and classical forms of hypertrophic cardiomyopathy." Flavigny J., Richard P., Isnard R., Carrier L., Charron P., Bonne G., Forissier J.F., Desnos M., Dubourg O., Komajda M., Schwartz K., Hainque B. J. Mol. Med. 76:208-214(1998) [PubMed: 9535554] [Abstract] Cited for: VARIANTS CMH10 LEU-18 AND GLN-58.
[9]	"Systematic analysis of the regulatory and essential myosin light chain genes: genetic variants and mutations in hypertrophic cardiomyopathy." Kabaeva Z.T., Perrot A., Wolter B., Dietz R., Cardim N., Correia J.M., Schulte H.D., Aldashev A.A., Mirrakhimov M.M., Osterziel K.J. Eur. J. Hum. Genet. 10:741-748(2002) [PubMed: 12404107] [Abstract] Cited for: VARIANTS CMH10 LYS-22 AND GLN-58.
[10]	"Hypertrophic cardiomyopathy: distribution of disease genes, spectrum of mutations, and implications for a molecular diagnosis strategy." Richard P., Charron P., Carrier L., Ledeuil C., Cheav T., Pichereau C., Benaiche A., Isnard R., Dubourg O., Burban M., Gueffet J.-P., Millaire A., Desnos M., Schwartz K., Hainque B., Komajda M. Circulation 107:2227-2232(2003) [PubMed: 12707239] [Abstract] Cited for: VARIANT CMH10 VAL-166.
[11]	Erratum Richard P., Charron P., Carrier L., Ledeuil C., Cheav T., Pichereau C., Benaiche A., Isnard R., Dubourg O., Burban M., Gueffet J.-P., Millaire A., Desnos M., Schwartz K., Hainque B., Komajda M. Circulation 109:3258-3258(2004)
[12]	"Identification of the genotypes causing hypertrophic cardiomyopathy in northern Sweden." Moerner S., Richard P., Kazzam E., Hellman U., Hainque B., Schwartz K., Waldenstroem A. J. Mol. Cell. Cardiol. 35:841-849(2003) [PubMed: 12818575] [Abstract] Cited for: VARIANT CMH10 GLN-58.
+	Additional computationally mapped references.

Web resources

Familial hypertrophic cardiomyopathy mutation database

GeneReviews

Cross-references

Sequence databases
EMBLGenBankDDBJ	X14332 mRNA. Translation: CAA32510.1. M22815 mRNA. Translation: AAA91832.1. AF020768 mRNA. Translation: AAB91993.1. S69022 mRNA. Translation: AAB29658.2. BC015821 mRNA. Translation: AAH15821.1. BC031006 mRNA. Translation: AAH31006.1. BC031008 mRNA. Translation: AAH31008.1.
IPI	IPI00216798.
RefSeq	NP_000423.2.
UniGene	Hs.75535
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	P10916. 2 interactions.
STRING	P10916.
PTM databases
PhosphoSite	P10916.
2-D gel databases
HSC-2DPAGE	P10916.
Proteomic databases
PRIDE	P10916.
Genome annotation databases
Ensembl	ENST00000228841; ENSP00000228841; ENSG00000111245; Homo sapiens. [Genome view]
GeneID	4633.
KEGG	hsa:4633.
UCSC	uc001try.2. human.
Organism-specific databases
CTD	4633.
GeneCards	GC12M109811.
HGNC	HGNC:7583. MYL2.
HPA	HPA019763.
MIM	160781. gene. 608758. phenotype.
Orphanet	155. Cardiomyopathy, hypertrophic, primary or idiopathic.
PharmGKB	PA31380.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	P10916.
HOVERGEN	P10916.
OMA	EIDQMFA
OrthoDB	EOG9DNHPR
Enzyme and pathway databases
Reactome	REACT_17044. Muscle contraction.
Gene expression databases
ArrayExpress	P10916.
Bgee	P10916.
CleanEx	HS_MYL2.
Genevestigator	P10916.
GermOnline	ENSG00000111245. Homo sapiens.
Family and domain databases
InterPro	IPR011992. EF-Hand_type. IPR018247. EF_Hand_1_Ca_BS. IPR018249. EF_HAND_2. IPR002048. EF_hand_Ca_bd. IPR018248. EF_Hand_dom. [Graphical view]
Gene3D	G3DSA:1.10.238.10. EF-Hand_type. 1 hit.
Pfam	PF00036. efhand. 1 hit. [Graphical view]
SMART	SM00054. EFh. 3 hits. [Graphical view]
PROSITE	PS00018. EF_HAND_1. 1 hit. PS50222. EF_HAND_2. 3 hits. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	17836.
SOURCE	Search...

Entry information

Entry name

MLRV_HUMAN

Accession

Primary (citable) accession number: P10916
Secondary accession number(s): Q16123

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	January 23, 2007
Last modified:	November 24, 2009
This is version 107 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.