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Protein

Leiomodin-2

Gene

Lmod2

Organism
Rattus norvegicus (Rat)
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 (PubMed:18403713). Plays a role in the regulation of actin filament length (By similarity). Required for normal sarcomere organization in the heart, and for normal heart function (PubMed:18403713).By similarity1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Leiomodin-2
Alternative name(s):
Cardiac leiomodin
Short name:
C-LMOD
Leiomodin1 Publication
Gene namesi
Name:Lmod2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi1592092. Lmod2.

Subcellular locationi

GO - Cellular componenti

  • actin filament Source: UniProtKB
  • cardiac myofibril Source: UniProtKB
  • M band Source: UniProtKB-SubCell
  • sarcomere Source: UniProtKB
  • striated muscle thin filament Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003113421 – 549Leiomodin-2Add BLAST549

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei11PhosphoserineCombined sources1
Modified residuei15PhosphoserineCombined sources1
Modified residuei24PhosphoserineCombined sources1
Modified residuei406PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiA1A5Q0.
PeptideAtlasiA1A5Q0.
PRIDEiA1A5Q0.

PTM databases

iPTMnetiA1A5Q0.
PhosphoSitePlusiA1A5Q0.

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).By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000067847.

Structurei

3D structure databases

ProteinModelPortaliA1A5Q0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini523 – 542WH2Add BLAST20

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 164Interaction with actin 1By similarityAdd BLAST164
Regioni1 – 47Interaction with tropomyosin alphaBy similarityAdd BLAST47
Regioni1 – 42Tropomyosin-bindingBy similarityAdd BLAST42
Regioni165 – 499Interaction with actin 2By similarityAdd BLAST335
Regioni523 – 542Interaction with actin 3By similarityAdd BLAST20

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili457 – 515Sequence analysisAdd BLAST59

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi14 – 145Glu-richAdd BLAST132
Compositional biasi391 – 452Pro-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.
HOVERGENiHBG056172.
InParanoidiA1A5Q0.
PhylomeDBiA1A5Q0.

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.

A1A5Q0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTFGYRRGL SKYESIDEDE LLASLTAEEL KELERELEDI EPDRNLPVGL
60 70 80 90 100
RQKSLTEKTP TGNFSREALM AYWEKESQKL LEKERLGECG KLAEEDKEES
110 120 130 140 150
EEELIFTESN SEVSEEVCTE EEEESTEEEE EEEEEDSEEE EVTTEVTKHI
160 170 180 190 200
NGTVSHNGVN PDNSKPKTFK SQIENINLTN GNSGGTQRNT ESPAAIHPCG
210 220 230 240 250
NPTVIEDALE KIKNNDPDTT EVNLNNIENI TTQTLSRFAE ALKENTVVKT
260 270 280 290 300
FSLANTHADD AAAIAIAEML KVNEHITSVN VESNFITGKG ILAIMRALQH
310 320 330 340 350
NTVLTELRFH NQRHIMGSQV EMEIVKLLKE NTTLLRLGYH FELPGPRMSM
360 370 380 390 400
TSILTRNMDK QRQKRMQEQK QQEGHDGGAT LRTKVWQRGT PGSSPYASPR
410 420 430 440 450
QSPWSSPKVS KKVHTGRSRP PSPVAPPPPP PPPPLPPHML PPPPPPPAPP
460 470 480 490 500
LPGKKLITRN IAEVIKQQES AQRALQNGQR KKKGKKVKKQ PNNILKEIKN
510 520 530 540
SLRSVQEKKM EESSRPSTPQ RSAHENLMEA IRGSSIRQLR RVEVPEALR
Length:549
Mass (Da):61,717
Last modified:January 23, 2007 - v1
Checksum:i3494F88AEA5C395C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC128755 mRNA. Translation: AAI28756.1.
RefSeqiNP_001094434.1. NM_001100964.1.
UniGeneiRn.16210.

Genome annotation databases

GeneIDi296935.
KEGGirno:296935.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC128755 mRNA. Translation: AAI28756.1.
RefSeqiNP_001094434.1. NM_001100964.1.
UniGeneiRn.16210.

3D structure databases

ProteinModelPortaliA1A5Q0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000067847.

PTM databases

iPTMnetiA1A5Q0.
PhosphoSitePlusiA1A5Q0.

Proteomic databases

PaxDbiA1A5Q0.
PeptideAtlasiA1A5Q0.
PRIDEiA1A5Q0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi296935.
KEGGirno:296935.

Organism-specific databases

CTDi442721.
RGDi1592092. Lmod2.

Phylogenomic databases

eggNOGiKOG3735. Eukaryota.
ENOG410YAHM. LUCA.
HOVERGENiHBG056172.
InParanoidiA1A5Q0.
PhylomeDBiA1A5Q0.

Miscellaneous databases

PROiA1A5Q0.

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_RAT
AccessioniPrimary (citable) accession number: A1A5Q0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 44 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. 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.