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Q7TPR4 (ACTN1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-actinin-1
Alternative name(s):
Alpha-actinin cytoskeletal isoform
F-actin cross-linking protein
Non-muscle alpha-actinin-1
Gene names
Name:Actn1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length892 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein By similarity.

Subunit structure

Homodimer; antiparallel. Interacts with DDN, MYOZ2, PDLIM2, TTID and LPP By similarity. Interacts with PSD. Interacts with MICALL2. Ref.3 Ref.4

Subcellular location

Cytoplasmcytoskeleton. CytoplasmmyofibrilsarcomereZ line. Cell membrane. Cell junction. Cell projectionruffle. Note: Colocalizes with MYOZ2 and PPP3CA at the Z-line of heart and skeletal muscle. Colocalizes with PSD in membrane ruffles and central reticular structures. Ref.2 Ref.3 Ref.4

Sequence similarities

Belongs to the alpha-actinin family.

Contains 1 actin-binding domain.

Contains 2 CH (calponin-homology) domains.

Contains 2 EF-hand domains.

Contains 4 spectrin repeats.

Ontologies

Keywords
   Cellular componentCell junction
Cell membrane
Cell projection
Cytoplasm
Cytoskeleton
Membrane
   DomainRepeat
   LigandActin-binding
Calcium
Metal-binding
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin filament bundle assembly

Inferred from direct assay PubMed 16043482. Source: UniProtKB

cortical cytoskeleton organization

Traceable author statement PubMed 15841212. Source: UniProtKB

focal adhesion assembly

Inferred from electronic annotation. Source: Ensembl

negative regulation of cellular component movement

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentZ disc

Inferred from direct assay PubMed 15665106PubMed 18332105PubMed 20215401PubMed 20368620. Source: MGI

cortical cytoskeleton

Traceable author statement PubMed 15841212. Source: UniProtKB

dendritic spine

Inferred from electronic annotation. Source: Ensembl

dense core granule membrane

Traceable author statement PubMed 16043482. Source: UniProtKB

extracellular vesicular exosome

Inferred from electronic annotation. Source: Ensembl

fascia adherens

Inferred from direct assay PubMed 11732910. Source: MGI

focal adhesion

Traceable author statement PubMed 15841212. Source: UniProtKB

nucleus

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

ruffle

Inferred from electronic annotation. Source: UniProtKB-SubCell

secretory granule

Non-traceable author statement PubMed 16043482. Source: UniProtKB

stress fiber

Traceable author statement PubMed 15841212. Source: UniProtKB

   Molecular_functionactin filament binding

Inferred from direct assay PubMed 15465019. Source: MGI

calcium ion binding

Inferred from electronic annotation. Source: InterPro

double-stranded RNA binding

Inferred from sequence orthology PubMed 21266579. Source: MGI

protein homodimerization activity

Traceable author statement PubMed 15841212. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 892892Alpha-actinin-1
PRO_0000073432

Regions

Domain1 – 247247Actin-binding
Domain31 – 135105CH 1
Domain144 – 247104CH 2
Repeat274 – 384111Spectrin 1
Repeat394 – 499106Spectrin 2
Repeat509 – 620112Spectrin 3
Repeat630 – 733104Spectrin 4
Domain746 – 78136EF-hand 1
Domain787 – 82236EF-hand 2
Calcium binding759 – 770121 Potential
Calcium binding800 – 811122 Potential
Region274 – 733460Interaction with DDN By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue61Phosphoserine By similarity
Modified residue121Phosphotyrosine; by FAK1 By similarity
Modified residue951N6-acetyllysine By similarity
Modified residue1951N6-acetyllysine By similarity
Modified residue6761N6-acetyllysine By similarity

Experimental info

Mutagenesis321Q → K: Shows less organization of the circumferential actin-filament network compared to controls. Ref.5
Mutagenesis1051V → I: Shows less organization of the circumferential actin-filament network compared to controls. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q7TPR4 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 652DA065A5F38E7C

FASTA892103,068
        10         20         30         40         50         60 
MDHYDSQQTN DYMQPEEDWD RDLLLDPAWE KQQRKTFTAW CNSHLRKAGT QIENIEEDFR 

        70         80         90        100        110        120 
DGLKLMLLLE VISGERLAKP ERGKMRVHKI SNVNKALDFI ASKGVKLVSI GAEEIVDGNV 

       130        140        150        160        170        180 
KMTLGMIWTI ILRFAIQDIS VEETSAKEGL LLWCQRKTAP YKNVNIQNFH ISWKDGLGFC 

       190        200        210        220        230        240 
ALIHRHRPEL IDYGKLRKDD PLTNLNTAFD VAERFLDIPK MLDAEDIVGT ARPDEKAIMT 

       250        260        270        280        290        300 
YVSSFYHAFS GAQKAETAAN RICKVLAVNQ ENEQLMEDYE KLASDLLEWI RRTIPWLENR 

       310        320        330        340        350        360 
VPENTMHAMQ QKLEDFRDYR RLHKPPKVQE KCQLEINFNT LQTKLRLSNR PAFMPSEGRM 

       370        380        390        400        410        420 
VSDINNAWGC LEQAEKGYEE WLLNEIRRLE RLDHLAEKFR QKASIHEAWT DGKEAMLRQK 

       430        440        450        460        470        480 
DYETATLSEI KALLKKHEAF ESDLAAHQDR VEQIAAIAQE LNELDYYDSP SVNARCQKIC 

       490        500        510        520        530        540 
DQWDNLGALT QKRREALERT EKLLETIDQL YLEYAKRAAP FNNWMEGAME DLQDTFIVHT 

       550        560        570        580        590        600 
IEEIQGLTTA HEQFKATLPD ADKERLAILG IHNEVSKIVQ TYHVNMAGTN PYTTITPQEI 

       610        620        630        640        650        660 
NGKWDHVRQL VPRRDQALTE EHARQQHNER LRKQFGAQAN VIGPWIQTKM EEIGRISIEM 

       670        680        690        700        710        720 
HGTLEDQLSH LRQYEKSIVN YKPKIDQLEC DHQLIQEALI FDNKHTNYNM EHIRVGWEQL 

       730        740        750        760        770        780 
LTTIARTINE VENQILTRDA KGISQEQMNE FRASFNHFDR DHSGTLGPEE FKACLISLGY 

       790        800        810        820        830        840 
DIGNDPQGEA EFARIMSIVD PNRLGVVTFQ AFIDFMSRET ADTDTADQVM ASFKILAGDK 

       850        860        870        880        890 
NYITEDELRR ELPPDQAEYC IARMAPYAGP DSVPGALDYM SFSTALYGES DL 

« Hide

References

« Hide 'large scale' references
[1]"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: Olfactory epithelium.
[2]"Calsarcins, a novel family of sarcomeric calcineurin-binding proteins."
Frey N., Richardson J.A., Olson E.N.
Proc. Natl. Acad. Sci. U.S.A. 97:14632-14637(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[3]"Somatodendritic localization of EFA6A, a guanine nucleotide exchange factor for ADP-ribosylation factor 6, and its possible interaction with alpha-actinin in dendritic spines."
Sakagami H., Honma T., Sukegawa J., Owada Y., Yanagisawa T., Kondo H.
Eur. J. Neurosci. 25:618-628(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PSD, SUBCELLULAR LOCATION.
[4]"Rab13 small G protein and junctional Rab13-binding protein (JRAB) orchestrate actin cytoskeletal organization during epithelial junctional development."
Sakane A., Abdallah A.A., Nakano K., Honda K., Ikeda W., Nishikawa Y., Matsumoto M., Matsushita N., Kitamura T., Sasaki T.
J. Biol. Chem. 287:42455-42468(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MICALL2, SUBCELLULAR LOCATION.
[5]"ACTN1 mutations cause congenital macrothrombocytopenia."
Kunishima S., Okuno Y., Yoshida K., Shiraishi Y., Sanada M., Muramatsu H., Chiba K., Tanaka H., Miyazaki K., Sakai M., Ohtake M., Kobayashi R., Iguchi A., Niimi G., Otsu M., Takahashi Y., Miyano S., Saito H., Kojima S., Ogawa S.
Am. J. Hum. Genet. 92:431-438(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF GLN-32 AND VAL-105.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC054830 mRNA. Translation: AAH54830.1.
RefSeqNP_598917.1. NM_134156.2.
UniGeneMm.253564.
Mm.403477.

3D structure databases

ProteinModelPortalQ7TPR4.
SMRQ7TPR4. Positions 30-254, 267-892.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid224977. 11 interactions.
IntActQ7TPR4. 7 interactions.
MINTMINT-1869732.
STRING10090.ENSMUSP00000021554.

PTM databases

PhosphoSiteQ7TPR4.

Proteomic databases

PaxDbQ7TPR4.
PRIDEQ7TPR4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000021554; ENSMUSP00000021554; ENSMUSG00000015143.
GeneID109711.
KEGGmmu:109711.
UCSCuc007oap.2. mouse.

Organism-specific databases

CTD87.
MGIMGI:2137706. Actn1.

Phylogenomic databases

eggNOGCOG5069.
GeneTreeENSGT00670000097825.
HOGENOMHOG000263418.
HOVERGENHBG050453.
InParanoidQ7TPR4.
KOK05699.
OMAWIRRTMP.
OrthoDBEOG72C4ZJ.
PhylomeDBQ7TPR4.
TreeFamTF352676.

Gene expression databases

ArrayExpressQ7TPR4.
BgeeQ7TPR4.
CleanExMM_ACTN1.
GenevestigatorQ7TPR4.

Family and domain databases

Gene3D1.10.238.10. 2 hits.
1.10.418.10. 2 hits.
InterProIPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR011992. EF-hand-dom_pair.
IPR014837. EF-hand_Ca_insen.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR018159. Spectrin/alpha-actinin.
IPR002017. Spectrin_repeat.
[Graphical view]
PfamPF00307. CH. 2 hits.
PF13405. EF-hand_6. 1 hit.
PF08726. EFhand_Ca_insen. 1 hit.
PF00435. Spectrin. 4 hits.
[Graphical view]
SMARTSM00033. CH. 2 hits.
SM00054. EFh. 2 hits.
SM00150. SPEC. 2 hits.
[Graphical view]
SUPFAMSSF47576. SSF47576. 1 hit.
PROSITEPS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
PS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSACTN1. mouse.
NextBio362623.
PROQ7TPR4.
SOURCESearch...

Entry information

Entry nameACTN1_MOUSE
AccessionPrimary (citable) accession number: Q7TPR4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: October 1, 2003
Last modified: April 16, 2014
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot