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Protein

Leiomodin-2

Gene

Lmod2

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

Functioni

Mediates nucleation of actin filaments and thereby promotes actin polymerization (By similarity). Plays a role in the regulation of actin filament length (PubMed:26487682). Required for normal sarcomere organization in the heart, and for normal heart function (PubMed:26487682, PubMed:27274810).By similarity2 Publications

GO - Molecular functioni

GO - Biological processi

  • actin filament organization Source: GO_Central
  • actin filament polymerization Source: UniProtKB
  • actin nucleation Source: UniProtKB
  • muscle contraction Source: GO_Central
  • myofibril assembly Source: GO_Central
  • pointed-end actin filament capping Source: InterPro
  • positive regulation of actin filament polymerization Source: UniProtKB
  • sarcomere organization Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Leiomodin-2
Alternative name(s):
Cardiac leiomodin
Short name:
C-LMOD
LeiomodinCurated
Gene namesi
Name:Lmod2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:2135672. Lmod2.

Subcellular locationi

  • Cytoplasmmyofibrilsarcomere By similarity
  • Cytoplasmmyofibril By similarity
  • CytoplasmmyofibrilsarcomereM line By similarity
  • Cytoplasmcytoskeleton By similarity

  • Note: Colocalizes with actin filaments in sarcomeres. Detected close to the M line.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Disruption phenotypei

Mutant mice are born at the expected Mendelian rate. All die between 15 to 33 days after birth due to early-onset dilated cardiomyopathy. Cardiac muscle thin filaments are shorter than in wild-type, both in embryonic heart and in pups 6 or 15 days after birth. Hearts appear grossly normal at birth, but after 15 days, they display enlarged left ventricles with thin ventricle walls and resuced systolic performance. In contrast, there are no differences in thin filament length in skeletal muscle (PubMed:26487682). Insertion of a transposon in the first, non-coding exon decreases Lmod2 expression by 90% in females and by over 95% in males and gives rise to a phenotype that is closely similar to that of complete gene disruption, except that mutant mice die between three and nine weeks after birth (PubMed:27274810).1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003113411 – 550Leiomodin-2Add BLAST550

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei11PhosphoserineCombined sources1
Modified residuei15PhosphoserineCombined sources1
Modified residuei24PhosphoserineBy similarity1
Modified residuei407PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ3UHZ5.
PaxDbiQ3UHZ5.
PRIDEiQ3UHZ5.

PTM databases

iPTMnetiQ3UHZ5.
PhosphoSitePlusiQ3UHZ5.

Expressioni

Tissue specificityi

Detected in neonate heart (at protein level) (PubMed:26487682). Detected in embryonic heart and in pharyngeal arches (PubMed:26487682). Detected in adult heart (PubMed:27274810).2 Publications

Gene expression databases

BgeeiENSMUSG00000029683.
CleanExiMM_LMOD2.
GenevisibleiQ3UHZ5. MM.

Interactioni

Subunit structurei

Can bind at least three actin monomers and thereby provides a nucleus for actin filament formation. Interacts (via N-terminus) with tropomyosin alpha (TPM1) (via N-terminus). May also interact with TPM2 (via N-terminus) (PubMed:17572376).By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000031694.

Structurei

3D structure databases

ProteinModelPortaliQ3UHZ5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini524 – 543WH2Add BLAST20

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 165Interaction with actin 1By similarityAdd BLAST165
Regioni1 – 47Interaction with tropomyosin alphaBy similarityAdd BLAST47
Regioni166 – 500Interaction with actin 2By similarityAdd BLAST335
Regioni524 – 543Interaction with actin 3By similarityAdd BLAST20

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili91 – 147Sequence analysisAdd BLAST57

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi14 – 146Glu-richAdd BLAST133
Compositional biasi392 – 453Pro-richAdd BLAST62

Sequence similaritiesi

Belongs to the tropomodulin family.Curated
Contains 1 WH2 domain.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG3735. Eukaryota.
ENOG410YAHM. LUCA.
GeneTreeiENSGT00760000119226.
HOGENOMiHOG000261624.
HOVERGENiHBG056172.
InParanoidiQ3UHZ5.
OMAiKVNQHIT.
OrthoDBiEOG091G0C3H.
PhylomeDBiQ3UHZ5.
TreeFamiTF315841.

Family and domain databases

Gene3Di3.80.10.10. 1 hit.
InterProiIPR032675. L_dom-like.
IPR030132. LMOD2.
IPR004934. TMOD.
[Graphical view]
PANTHERiPTHR10901. PTHR10901. 1 hit.
PTHR10901:SF12. PTHR10901:SF12. 1 hit.
PfamiPF03250. Tropomodulin. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q3UHZ5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTFGYRRGL SKYESIDEDE LLASLSPEEL KELERELEDI EPDRNLPVGL
60 70 80 90 100
RQKSLTEKTP TGNFSREALM AYWEKESQKL LEKERLGECG KVAEEDKEES
110 120 130 140 150
EEELIFTESN SEVSEEVCTE DEEESQEEEE DSEEEEDSEE EEETTEATKH
160 170 180 190 200
INGTVSYNSV NTDNSKPKTF KSQIENINLT NGNSGRTQRN SESPAAIHPC
210 220 230 240 250
GNPTVIEDAL EKIRNNDPDT TEVNLNNIEN ITTQTLSRFA EALKENTVVK
260 270 280 290 300
TFSLANTHAD DAAAIAIADM LKVNEHITSV NVESNFITGK GILAIMRALQ
310 320 330 340 350
HNTVLTELRF HNQRHIMGSQ VEMEIVKLLK ENTTLLRLGY HFELPGPRMS
360 370 380 390 400
MTSILTRNMD KQRQKRMQEQ KQQEGHDGGA ALRTKVWQRG TPGSSPYASP
410 420 430 440 450
RQSPWSSPKV SKKVHTGRSR PPSPVAPPPP PPPPPLPPHM LPPPPPPPAP
460 470 480 490 500
PLPEKKLITR NIAEVIKQQE SAQRALQNGQ RKKKGKKVKK QPNNILKEIK
510 520 530 540 550
NSLRSVQEKK MEDSSRPSTP QRSVHENLME AIRGSSIRQL RRVEVPEALR
Length:550
Mass (Da):62,018
Last modified:October 11, 2005 - v1
Checksum:iBFA34F7BDFF25A1D
GO

Sequence cautioni

The sequence AAK00789 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti223V → F in AAK00789 (PubMed:11318603).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK147141 mRNA. Translation: BAE27711.1.
AF237628 mRNA. Translation: AAK00789.1. Different initiation.
CCDSiCCDS19944.1.
RefSeqiNP_444328.1. NM_053098.2.
UniGeneiMm.332941.

Genome annotation databases

EnsembliENSMUST00000031694; ENSMUSP00000031694; ENSMUSG00000029683.
GeneIDi93677.
KEGGimmu:93677.
UCSCiuc009bbu.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK147141 mRNA. Translation: BAE27711.1.
AF237628 mRNA. Translation: AAK00789.1. Different initiation.
CCDSiCCDS19944.1.
RefSeqiNP_444328.1. NM_053098.2.
UniGeneiMm.332941.

3D structure databases

ProteinModelPortaliQ3UHZ5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000031694.

PTM databases

iPTMnetiQ3UHZ5.
PhosphoSitePlusiQ3UHZ5.

Proteomic databases

MaxQBiQ3UHZ5.
PaxDbiQ3UHZ5.
PRIDEiQ3UHZ5.

Protocols and materials databases

DNASUi93677.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000031694; ENSMUSP00000031694; ENSMUSG00000029683.
GeneIDi93677.
KEGGimmu:93677.
UCSCiuc009bbu.1. mouse.

Organism-specific databases

CTDi442721.
MGIiMGI:2135672. Lmod2.

Phylogenomic databases

eggNOGiKOG3735. Eukaryota.
ENOG410YAHM. LUCA.
GeneTreeiENSGT00760000119226.
HOGENOMiHOG000261624.
HOVERGENiHBG056172.
InParanoidiQ3UHZ5.
OMAiKVNQHIT.
OrthoDBiEOG091G0C3H.
PhylomeDBiQ3UHZ5.
TreeFamiTF315841.

Miscellaneous databases

PROiQ3UHZ5.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000029683.
CleanExiMM_LMOD2.
GenevisibleiQ3UHZ5. MM.

Family and domain databases

Gene3Di3.80.10.10. 1 hit.
InterProiIPR032675. L_dom-like.
IPR030132. LMOD2.
IPR004934. TMOD.
[Graphical view]
PANTHERiPTHR10901. PTHR10901. 1 hit.
PTHR10901:SF12. PTHR10901:SF12. 1 hit.
PfamiPF03250. Tropomodulin. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLMOD2_MOUSE
AccessioniPrimary (citable) accession number: Q3UHZ5
Secondary accession number(s): Q99PM7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: October 11, 2005
Last modified: November 2, 2016
This is version 76 of the entry and version 1 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.