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Q9JI91 (ACTN2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 120. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-actinin-2
Alternative name(s):
Alpha-actinin skeletal muscle isoform 2
F-actin cross-linking protein
Gene names
Name:Actn2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length894 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. Also forms heterodimers with ACTN3. Interacts with ADAM12, MYOZ1, MYOZ2 and MYOZ3. Interacts via its C-terminal region with the LDB3 PDZ domain. Interacts with XIRP2. Interacts with DST (via N-terminus). Interacts with PARVB By similarity. Ref.4

Subcellular location

CytoplasmmyofibrilsarcomereZ line. Note: Colocalizes with MYOZ1 and FLNC at the Z-lines of skeletal muscle. Ref.5

Post-translational modification

Ubiquitinated by FBXL22, leading to proteasomal degradation By similarity.

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 componentCytoplasm
   DomainRepeat
   LigandActin-binding
Calcium
Metal-binding
   PTMUbl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processfocal adhesion assembly

Inferred from electronic annotation. Source: Ensembl

microspike assembly

Inferred from electronic annotation. Source: Ensembl

muscle contraction

Inferred from direct assay PubMed 8618961. Source: MGI

negative regulation of potassium ion transmembrane transporter activity

Inferred from electronic annotation. Source: Ensembl

negative regulation of potassium ion transport

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein localization to cell surface

Inferred from electronic annotation. Source: Ensembl

positive regulation of potassium ion transmembrane transporter activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of potassium ion transport

Inferred from electronic annotation. Source: Ensembl

positive regulation of receptor activity

Inferred from direct assay PubMed 15072553. Source: GOC

protein homotetramerization

Inferred from electronic annotation. Source: Ensembl

regulation of RNA biosynthetic process

Inferred from direct assay PubMed 15072553. Source: GOC

regulation of membrane potential

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentZ disc

Inferred from direct assay Ref.5. Source: UniProtKB

filopodium

Inferred from electronic annotation. Source: Ensembl

focal adhesion

Inferred from electronic annotation. Source: Ensembl

sarcomere

Inferred from direct assay PubMed 16585392. Source: MGI

striated muscle thin filament

Traceable author statement PubMed 8618961. Source: MGI

   Molecular_functionLIM domain binding

Inferred from physical interaction PubMed 10391924. Source: MGI

actin filament binding

Inferred from direct assay PubMed 15465019. Source: MGI

calcium ion binding

Inferred from electronic annotation. Source: InterPro

cytoskeletal protein binding

Inferred from direct assay PubMed 10391924. Source: UniProtKB

ligand-dependent nuclear receptor transcription coactivator activity

Inferred from direct assay PubMed 15072553. Source: MGI

protein binding

Inferred from physical interaction PubMed 10391924. Source: UniProtKB

protein binding, bridging

Traceable author statement PubMed 8618961. Source: MGI

protein homodimerization activity

Traceable author statement PubMed 15841212. Source: UniProtKB

thyroid hormone receptor coactivator activity

Inferred from direct assay PubMed 15072553. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Camk2aP117983EBI-299169,EBI-400384
Grin2bQ010974EBI-299169,EBI-400125

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 894894Alpha-actinin-2
PRO_0000073436

Regions

Domain1 – 254254Actin-binding
Domain38 – 142105CH 1
Domain151 – 254104CH 2
Repeat281 – 391111Spectrin 1
Repeat401 – 506106Spectrin 2
Repeat516 – 627112Spectrin 3
Repeat637 – 740104Spectrin 4
Domain753 – 78836EF-hand 1
Domain789 – 82436EF-hand 2
Calcium binding766 – 777121; possibly ancestral
Calcium binding802 – 813122; possibly ancestral

Experimental info

Sequence conflict2721V → G in AAF76325. Ref.1
Sequence conflict3581P → A in AAF76325. Ref.1
Sequence conflict3751W → C in AAF76325. Ref.1
Sequence conflict7051A → G in AAF76325. Ref.1
Sequence conflict7321A → G in AAF76325. Ref.1
Sequence conflict7531E → K in AAF76325. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9JI91 [UniParc].

Last modified October 3, 2012. Version 2.
Checksum: 79FCDC9C85B3949C

FASTA894103,834
        10         20         30         40         50         60 
MNQIEPGVQY NYVYDEDEYM IQEEEWDRDL LLDPAWEKQQ RKTFTAWCNS HLRKAGTQIE 

        70         80         90        100        110        120 
NIEEDFRNGL KLMLLLEVIS GERLPKPDRG KMRFHKIANV NKALDYIASK GVKLVSIGAE 

       130        140        150        160        170        180 
EIVDGNVKMT LGMIWTIILR FAIQDISVEE TSAKEGLLLW CQRKTAPYRN VNIQNFHTSW 

       190        200        210        220        230        240 
KDGLGLCALI HRHRPDLIDY SKLNKDDPIG NINLAMEIAE KHLDIPKMLD AEDIVNTPKP 

       250        260        270        280        290        300 
DERAIMTYVS CFYHAFAGAE QAETAANRIC KVLAVNQENE RLMEEYERLA SELLEWIRRT 

       310        320        330        340        350        360 
IPWLENRTPE KTMQAMQKKL EDFRDYRRKH KPPKVQEKCQ LEINFNTLQT KLRISNRPAF 

       370        380        390        400        410        420 
MPSEGKMVSD IAGAWQRLEQ AEKGYEEWLL NEIRRLERLE HLAEKFRQKA STHETWAYGK 

       430        440        450        460        470        480 
EQILLQKDYE SASLTEVRAL LRKHEAFESD LAAHQDRVEQ IAAIAQELNE LDYHDAVNVN 

       490        500        510        520        530        540 
DRCQKICDQW DRLGTLTQKR REALERTEKL LETIDQLHLE FAKRAAPFNN WMEGAMEDLQ 

       550        560        570        580        590        600 
DMFIVHSIEE IQSLITAHEQ FKATLPEADG ERQSILAIQN EVEKVIQSYS IRISSSNPYS 

       610        620        630        640        650        660 
TVTMDELRNK WDKVKQLVPV RDQSLQEELA RQHANERLRR QFAAQANAIG PWIQNKMEEI 

       670        680        690        700        710        720 
ARSSIQITGA LEDQMNQLKQ YEHNIINYKN NIDKLEGDHQ LIQEALVFDN KHTNYTMEHI 

       730        740        750        760        770        780 
RVGWELLLTT IARTINEVET QILTRDAKGI TQEQMNEFRA SFNHFDRRKN GLMDHEDFRA 

       790        800        810        820        830        840 
CLISMGYDLG EAEFARIMTL VDPNGQGTVT FQSFIDFMTR ETADTDTAEQ VIASFRILAS 

       850        860        870        880        890 
DKPYILAEEL RRELPPDQAQ YCIKRMPPYS GPGSVPGALD YTAFSSALYG ESDL 

« Hide

References

« Hide 'large scale' references
[1]"Differential expression of the actin-binding proteins, alpha-actinin-2 and -3, in different species: implications for the evolution of functional redundancy."
Mills M., Yang N., Weinberger R., Vander Woude D.L., Beggs A.H., Easteal S., North K.N.
Hum. Mol. Genet. 10:1335-1346(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Skeletal muscle.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Binding of ADAM12, a marker of skeletal muscle regeneration, to the muscle-specific actin-binding protein, alpha-actinin-2, is required for myoblast fusion."
Galliano M.-F., Huet C., Frygelius J., Polgren A., Wewer U.M., Engvall E.
J. Biol. Chem. 275:13933-13939(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ADAM12.
[5]"BPAG1 isoform-b: complex distribution pattern in striated and heart muscle and association with plectin and alpha-actinin."
Steiner-Champliaud M.F., Schneider Y., Favre B., Paulhe F., Praetzel-Wunder S., Faulkner G., Konieczny P., Raith M., Wiche G., Adebola A., Liem R.K., Langbein L., Sonnenberg A., Fontao L., Borradori L.
Exp. Cell Res. 316:297-313(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF248643 mRNA. Translation: AAF76325.1.
AC154523 Genomic DNA. No translation available.
CH466588 Genomic DNA. Translation: EDL32304.1.
CCDSCCDS26239.1.
RefSeqNP_150371.4. NM_033268.4.
UniGeneMm.37638.

3D structure databases

ProteinModelPortalQ9JI91.
SMRQ9JI91. Positions 35-261, 274-894.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid197950. 7 interactions.
IntActQ9JI91. 10 interactions.
MINTMINT-97958.

PTM databases

PhosphoSiteQ9JI91.

Proteomic databases

MaxQBQ9JI91.
PaxDbQ9JI91.
PRIDEQ9JI91.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000064204; ENSMUSP00000067708; ENSMUSG00000052374.
ENSMUST00000168193; ENSMUSP00000129609; ENSMUSG00000052374.
GeneID11472.
KEGGmmu:11472.
UCSCuc007pli.1. mouse.

Organism-specific databases

CTD88.
MGIMGI:109192. Actn2.

Phylogenomic databases

eggNOGCOG5069.
GeneTreeENSGT00670000097825.
HOGENOMHOG000263418.
HOVERGENHBG050453.
InParanoidQ9JI91.
KOK05699.
OMARAKWDKV.
OrthoDBEOG72C4ZJ.
TreeFamTF352676.

Gene expression databases

ArrayExpressQ9JI91.
CleanExMM_ACTN2.
GenevestigatorQ9JI91.

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.
IPR002048. EF_hand_dom.
IPR018159. Spectrin/alpha-actinin.
IPR002017. Spectrin_repeat.
[Graphical view]
PfamPF00307. CH. 2 hits.
PF08726. EFhand_Ca_insen. 1 hit.
PF00435. Spectrin. 4 hits.
[Graphical view]
SMARTSM00033. CH. 2 hits.
SM00054. EFh. 2 hits.
SM00150. SPEC. 3 hits.
[Graphical view]
SUPFAMSSF47576. SSF47576. 1 hit.
PROSITEPS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
PS50222. EF_HAND_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSACTN2. mouse.
NextBio278808.
PROQ9JI91.
SOURCESearch...

Entry information

Entry nameACTN2_MOUSE
AccessionPrimary (citable) accession number: Q9JI91
Secondary accession number(s): G3UW84
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: October 3, 2012
Last modified: July 9, 2014
This is version 120 of the entry and version 2 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