Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Tropomodulin-1

Gene

Tmod1

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

Functioni

Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton (By similarity).By similarity

GO - Molecular functioni

  • tropomyosin binding Source: MGI

GO - Biological processi

  • adult locomotory behavior Source: MGI
  • lens fiber cell development Source: CACAO
  • muscle contraction Source: MGI
  • myofibril assembly Source: MGI
  • pointed-end actin filament capping Source: InterPro
Complete GO annotation...

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiR-MMU-390522. Striated Muscle Contraction.

Names & Taxonomyi

Protein namesi
Recommended name:
Tropomodulin-1
Alternative name(s):
Erythrocyte tropomodulin
Short name:
E-Tmod
Gene namesi
Name:Tmod1
Synonyms:Tmod
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:98775. Tmod1.

Subcellular locationi

  • Cytoplasmcytoskeleton By similarity

  • Note: In myofibrils with sarcomeric structure, localizes to the pointed end of actin thin filaments.By similarity

GO - Cellular componenti

  • COP9 signalosome Source: Ensembl
  • cortical cytoskeleton Source: MGI
  • cytoskeleton Source: MGI
  • membrane Source: MGI
  • myofibril Source: MGI
  • sarcomere Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 359359Tropomodulin-1PRO_0000186129Add
BLAST

Proteomic databases

MaxQBiP49813.
PaxDbiP49813.
PRIDEiP49813.
TopDownProteomicsiP49813.

PTM databases

iPTMnetiP49813.
PhosphoSiteiP49813.

Expressioni

Tissue specificityi

Highly expressed in the erythrocyte, heart and skeletal muscle.

Gene expression databases

BgeeiP49813.
CleanExiMM_TMOD1.
ExpressionAtlasiP49813. baseline and differential.
GenevisibleiP49813. MM.

Interactioni

Subunit structurei

Binds to the N-terminus of tropomyosin and to actin.

GO - Molecular functioni

  • tropomyosin binding Source: MGI

Protein-protein interaction databases

BioGridi204233. 1 interaction.
IntActiP49813. 2 interactions.
MINTiMINT-4138079.
STRINGi10090.ENSMUSP00000103402.

Structurei

3D structure databases

ProteinModelPortaliP49813.
SMRiP49813. Positions 59-99, 170-349.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni39 – 138100Tropomyosin-bindingSequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the tropomodulin family.Curated

Phylogenomic databases

eggNOGiKOG3735. Eukaryota.
ENOG410YAHM. LUCA.
GeneTreeiENSGT00760000119226.
HOGENOMiHOG000261624.
HOVERGENiHBG056172.
InParanoidiP49813.
KOiK10370.
OMAiSTIVNKQ.
OrthoDBiEOG7D59Q1.
TreeFamiTF315841.

Family and domain databases

Gene3Di3.80.10.10. 1 hit.
InterProiIPR032675. L_dom-like.
IPR004934. TMOD.
IPR030135. TMOD1.
[Graphical view]
PANTHERiPTHR10901. PTHR10901. 1 hit.
PTHR10901:SF8. PTHR10901:SF8. 1 hit.
PfamiPF03250. Tropomodulin. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P49813-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSYRRELEKY RDLDEDEILG ALTEEELRTL ENELDELDPD NALLPAGLRQ
60 70 80 90 100
KDQTTKAPTG PFKREELLDH LEKQAKEFKD REDLVPYTGE KRGKVWVPKQ
110 120 130 140 150
KPMDPVLESV TLEPELEEAL ANASDAELCD IAAILGMHTL MSNQQYYQAL
160 170 180 190 200
GSSSIVNKEG LNSVIKPTQY KPVPDEEPNS TDVEETLERI KNNDPELEEV
210 220 230 240 250
NLNNIRNIPI PTLKAYAEAL KENSYVKKFS IVGTRSNDPV AFALAEMLKV
260 270 280 290 300
NKVLKTLNVE SNFISGAGIL RLVEALPHNT SLVELKIDNQ SQPLGNKVEM
310 320 330 340 350
EIVNMLEKNT TLLKFGYHFT QQGPRLRASN AMMSNNDLVR KRRLADLTGP

IIPKCRSGV
Length:359
Mass (Da):40,466
Last modified:July 27, 2011 - v2
Checksum:iEAE340B83048823B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti352 – 3521I → M in AAB33388 (PubMed:7851652).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S76831 mRNA. Translation: AAB33388.1.
AF287746
, AF287738, AF287739, AF287740, AF287741, AF287742, AF287743, AF287744, AF287745 Genomic DNA. Translation: AAF91487.1.
AL732615 Genomic DNA. Translation: CAM17028.1.
CH466565 Genomic DNA. Translation: EDL02383.1.
BC106849 mRNA. Translation: AAI06850.1.
BC106850 mRNA. Translation: AAI06851.1.
CCDSiCCDS18143.1.
RefSeqiNP_068683.1. NM_021883.2.
UniGeneiMm.249594.
Mm.331588.

Genome annotation databases

EnsembliENSMUST00000107773; ENSMUSP00000103402; ENSMUSG00000028328.
GeneIDi21916.
KEGGimmu:21916.
UCSCiuc008ste.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S76831 mRNA. Translation: AAB33388.1.
AF287746
, AF287738, AF287739, AF287740, AF287741, AF287742, AF287743, AF287744, AF287745 Genomic DNA. Translation: AAF91487.1.
AL732615 Genomic DNA. Translation: CAM17028.1.
CH466565 Genomic DNA. Translation: EDL02383.1.
BC106849 mRNA. Translation: AAI06850.1.
BC106850 mRNA. Translation: AAI06851.1.
CCDSiCCDS18143.1.
RefSeqiNP_068683.1. NM_021883.2.
UniGeneiMm.249594.
Mm.331588.

3D structure databases

ProteinModelPortaliP49813.
SMRiP49813. Positions 59-99, 170-349.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204233. 1 interaction.
IntActiP49813. 2 interactions.
MINTiMINT-4138079.
STRINGi10090.ENSMUSP00000103402.

PTM databases

iPTMnetiP49813.
PhosphoSiteiP49813.

Proteomic databases

MaxQBiP49813.
PaxDbiP49813.
PRIDEiP49813.
TopDownProteomicsiP49813.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000107773; ENSMUSP00000103402; ENSMUSG00000028328.
GeneIDi21916.
KEGGimmu:21916.
UCSCiuc008ste.1. mouse.

Organism-specific databases

CTDi7111.
MGIiMGI:98775. Tmod1.

Phylogenomic databases

eggNOGiKOG3735. Eukaryota.
ENOG410YAHM. LUCA.
GeneTreeiENSGT00760000119226.
HOGENOMiHOG000261624.
HOVERGENiHBG056172.
InParanoidiP49813.
KOiK10370.
OMAiSTIVNKQ.
OrthoDBiEOG7D59Q1.
TreeFamiTF315841.

Enzyme and pathway databases

ReactomeiR-MMU-390522. Striated Muscle Contraction.

Miscellaneous databases

ChiTaRSiTmod1. mouse.
PROiP49813.
SOURCEiSearch...

Gene expression databases

BgeeiP49813.
CleanExiMM_TMOD1.
ExpressionAtlasiP49813. baseline and differential.
GenevisibleiP49813. MM.

Family and domain databases

Gene3Di3.80.10.10. 1 hit.
InterProiIPR032675. L_dom-like.
IPR004934. TMOD.
IPR030135. TMOD1.
[Graphical view]
PANTHERiPTHR10901. PTHR10901. 1 hit.
PTHR10901:SF8. PTHR10901:SF8. 1 hit.
PfamiPF03250. Tropomodulin. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of tropomodulin cDNA and localization of gene transcripts during mouse embryogenesis."
    Ito M., Swanson B., Sussman M.A., Kedes L., Lyons G.
    Dev. Biol. 167:317-328(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Genomic organization of mouse and human erythrocyte tropomodulin genes encoding the pointed end capping protein for the actin filaments."
    Chu X., Thompson D., Yee L.J., Sung L.A.
    Gene 256:271-281(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Spleen.

Entry informationi

Entry nameiTMOD1_MOUSE
AccessioniPrimary (citable) accession number: P49813
Secondary accession number(s): Q3KP84, Q9ERR9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 27, 2011
Last modified: June 8, 2016
This is version 116 of the entry and version 2 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.