Alpha-actinin-2 - Mus musculus (Mouse)

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Q9JI91 (ACTN2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 109. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Alpha-actinin-2

Alternative name(s):
Alpha-actinin skeletal muscle isoform 2
F-actin cross-linking protein

Gene names

Name:

Actn2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	894 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Cytoplasm › myofibril › sarcomere › Z line. Note: Colocalizes with MYOZ1 and FLNC at the Z-lines of skeletal muscle. Ref.6
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 component	Cytoplasm
Domain	Repeat
Ligand	Actin-binding Calcium Metal-binding
PTM	Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin crosslink formation Inferred from electronic annotation. Source: InterPro actin filament bundle assembly Inferred from electronic annotation. Source: InterPro focal adhesion assembly Inferred from electronic annotation. Source: Compara microspike assembly Inferred from electronic annotation. Source: Compara muscle contraction Inferred from direct assay PubMed 8618961. Source: MGI negative regulation of potassium ion transmembrane transporter activity Inferred from electronic annotation. Source: Compara negative regulation of potassium ion transport Inferred from electronic annotation. Source: Compara negative regulation of protein localization to cell surface Inferred from electronic annotation. Source: Compara positive regulation of potassium ion transmembrane transporter activity Inferred from electronic annotation. Source: Compara positive regulation of potassium ion transport Inferred from electronic annotation. Source: Compara protein homotetramerization Inferred from electronic annotation. Source: Compara regulation of membrane potential Inferred from electronic annotation. Source: Compara
Cellular_component	Z disc Inferred from direct assay Ref.6. Source: UniProtKB filopodium Inferred from electronic annotation. Source: Compara focal adhesion Inferred from electronic annotation. Source: Compara striated muscle thin filament Traceable author statement PubMed 8618961. Source: MGI
Molecular_function	actin filament binding Inferred from direct assay PubMed 15465019. Source: MGI calcium ion binding Inferred from electronic annotation. Source: InterPro 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...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 894

894

Alpha-actinin-2

PRO_0000073436

Regions

Domain

1 – 254

254

Actin-binding

Domain

38 – 142

105

CH 1

Domain

151 – 254

104

CH 2

Repeat

281 – 391

111

Spectrin 1

Repeat

401 – 506

106

Spectrin 2

Repeat

516 – 627

112

Spectrin 3

Repeat

637 – 740

104

Spectrin 4

Domain

753 – 788

EF-hand 1

Domain

789 – 824

EF-hand 2

Calcium binding

766 – 777

1; possibly ancestral

Calcium binding

802 – 813

2; possibly ancestral

Amino acid modifications

Modified residue

237

Phosphothreonine Ref.5

Experimental info

Sequence conflict

272

V → G in AAF76325. Ref.1

Sequence conflict

358

P → A in AAF76325. Ref.1

Sequence conflict

375

W → C in AAF76325. Ref.1

Sequence conflict

705

A → G in AAF76325. Ref.1

Sequence conflict

732

A → G in AAF76325. Ref.1

Sequence conflict

753

E → K in AAF76325. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Q9JI91 [UniParc].

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

FASTA

894

103,834

        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' referencesShow '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. 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]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-237, MASS SPECTROMETRY. Tissue: Melanoma.
[6]	"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.
IPI	IPI00331664.
RefSeq	NP_150371.4. NM_033268.4.
UniGene	Mm.37638.
3D structure databases
ProteinModelPortal	Q9JI91.
SMR	Q9JI91. Positions 35-261, 274-746, 751-894.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9JI91. 5 interactions.
MINT	MINT-97958.
PTM databases
PhosphoSite	Q9JI91.
Proteomic databases
PaxDb	Q9JI91.
PRIDE	Q9JI91.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000064204; ENSMUSP00000067708; ENSMUSG00000052374. ENSMUST00000168193; ENSMUSP00000129609; ENSMUSG00000052374.
GeneID	11472.
KEGG	mmu:11472.
Organism-specific databases
CTD	88.
MGI	MGI:109192. Actn2.
Phylogenomic databases
eggNOG	COG5069.
GeneTree	ENSGT00670000097825.
HOGENOM	HOG000263418.
HOVERGEN	HBG050453.
InParanoid	Q9JI91.
KO	K05699.
OMA	ELRTKWD.
OrthoDB	EOG44F68D.
Gene expression databases
CleanEx	MM_ACTN2.
Genevestigator	Q9JI91.
GermOnline	ENSMUSG00000052374. Mus musculus.
Family and domain databases
Gene3D	1.10.238.10. 2 hits. 1.10.418.10. 2 hits.
InterPro	IPR001589. Actinin_actin-bd_CS. IPR026921. Alpha-actinin. IPR001715. CH-domain. IPR011992. EF-hand-like_dom. IPR014837. EF-hand_Ca_insen. IPR002048. EF_hand_dom. IPR018159. Spectrin/alpha-actinin. IPR002017. Spectrin_repeat. [Graphical view]
PANTHER	PTHR11915:SF47. PTHR11915:SF47. 1 hit.
Pfam	PF00307. CH. 2 hits. PF08726. efhand_Ca_insen. 1 hit. PF00435. Spectrin. 4 hits. [Graphical view]
SMART	SM00033. CH. 2 hits. SM00054. EFh. 2 hits. SM00150. SPEC. 3 hits. [Graphical view]
SUPFAM	SSF47576. Calponin-homology. 1 hit.
PROSITE	PS00019. ACTININ_1. 1 hit. PS00020. ACTININ_2. 1 hit. PS50021. CH. 2 hits. PS50222. EF_HAND_2. 2 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	ACTN2. mouse.
NextBio	278808.
SOURCE	Search...

Entry information

Entry name

ACTN2_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 109 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents