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P05094 (ACTN1_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 137. 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·Alt products·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
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length893 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

Homodimer; antiparallel.

Subcellular location

Cytoplasmcytoskeleton By similarity. CytoplasmmyofibrilsarcomereZ line By similarity. Cell membrane By similarity. Cell junction By similarity. Cell projectionruffle 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 componentCell junction
Cell membrane
Cell projection
Cytoplasm
Cytoskeleton
Membrane
   Coding sequence diversityAlternative splicing
   DomainRepeat
   LigandActin-binding
Calcium
Metal-binding
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentZ disc

Inferred from electronic annotation. Source: UniProtKB-SubCell

cell junction

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

ruffle

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ICAM5Q9UMF03EBI-5847257,EBI-6398041From a different organism.
ITGB1P072284EBI-5847257,EBI-5606437
ITGB3P051062EBI-5847257,EBI-702847From a different organism.
VCLP120035EBI-6049246,EBI-1039563
ZYXQ045844EBI-6049246,EBI-6222189

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Note: Isoforms only differ in the region of the first EF-hand calcium-binding motif.
Isoform 1 (identifier: P05094-1)

Also known as: Brain;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P05094-2)

Also known as: Smooth muscle;

The sequence of this isoform differs from the canonical sequence as follows:
     762-773: DHSGTLGPEEFK → KKTGMMDCEDFR
     779-788: LGYDIGNDAQ → MGYNM

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 893893Alpha-actinin-1
PRO_0000073434

Regions

Domain1 – 248248Actin-binding
Domain32 – 136105CH 1
Domain145 – 248104CH 2
Repeat275 – 385111Spectrin 1
Repeat395 – 500106Spectrin 2
Repeat510 – 621112Spectrin 3
Repeat631 – 734104Spectrin 4
Domain747 – 78236EF-hand 1
Domain788 – 82336EF-hand 2
Calcium binding760 – 771121 Potential
Calcium binding801 – 812122 Potential

Amino acid modifications

Modified residue131Phosphotyrosine; by FAK1 By similarity

Natural variations

Alternative sequence762 – 77312DHSGT…PEEFK → KKTGMMDCEDFR in isoform 2.
VSP_000710
Alternative sequence779 – 78810LGYDIGNDAQ → MGYNM in isoform 2.
VSP_000711

Experimental info

Sequence conflict1551C → Y in AAA48567. Ref.2
Sequence conflict5011T → S in AAA48570. Ref.1
Sequence conflict852 – 8532EL → DV in CAA32079. Ref.3

Secondary structure

.............................................................................................................. 893
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Brain) [UniParc].

Last modified February 21, 2001. Version 3.
Checksum: B9D1CE5A2C6F8821

FASTA893103,162
        10         20         30         40         50         60 
MDHHYDPQQT NDYMQPEEDW DRDLLLDPAW EKQQRKTFTA WCNSHLRKAG TQIENIEEDF 

        70         80         90        100        110        120 
RDGLKLMLLL EVISGERLAK PERGKMRVHK ISNVNKALDF IASKGVKLVS IGAEEIVDGN 

       130        140        150        160        170        180 
VKMTLGMIWT IILRFAIQDI SVEETSAKEG LLLWCQRKTA PYKNVNIQNF HISWKDGLGF 

       190        200        210        220        230        240 
CALIHRHRPE LIDYGKLRKD DPLTNLNTAF DVAEKYLDIP KMLDAEDIVG TARPDEKAIM 

       250        260        270        280        290        300 
TYVSSFYHAF SGAQKAETAA NRICKVLAVN QENEQLMEDY EKLASDLLEW IRRTIPWLEN 

       310        320        330        340        350        360 
RAPENTMQAM QQKLEDFRDY RRLHKPPKVQ EKCQLEINFN TLQTKLRLSN RPAFMPSEGK 

       370        380        390        400        410        420 
MVSDINNAWG GLEQAEKGYE EWLLNEIRRL ERLDHLAEKF RQKASIHESW TDGKEAMLQQ 

       430        440        450        460        470        480 
KDYETATLSE IKALLKKHEA FESDLAAHQD RVEQIAAIAQ ELNELDYYDS PSVNARCQKI 

       490        500        510        520        530        540 
CDQWDNLGAL TQKRREALER TEKLLETIDQ LYLEYAKRAA PFNNWMEGAM EDLQDTFIVH 

       550        560        570        580        590        600 
TIEEIQGLTT AHEQFKATLP DADKERQAIL GIHNEVSKIV QTYHVNMAGT NPYTTITPQE 

       610        620        630        640        650        660 
INGKWEHVRQ LVPRRDQALM EEHARQQQNE RLRKQFGAQA NVIGPWIQTK MEEIGRISIE 

       670        680        690        700        710        720 
MHGTLEDQLN HLRQYEKSIV NYKPKIDQLE GDHQQIQEAL IFDNKHTNYT MEHIRVGWEQ 

       730        740        750        760        770        780 
LLTTIARTIN EVENQILTRD AKGISQEQMN EFRASFNHFD RDHSGTLGPE EFKACLISLG 

       790        800        810        820        830        840 
YDIGNDAQGE AEFARIMSIV DPNRMGVVTF QAFIDFMSRE TADTDTADQV MASFKILAGD 

       850        860        870        880        890 
KNYITVDELR RELPPDQAEY CIARMAPYNG RDAVPGALDY MSFSTALYGE SDL 

« Hide

Isoform 2 (Smooth muscle) [UniParc].

Checksum: 5F2485A047EA644C
Show »

FASTA888102,855

References

[1]"The sequence of chick alpha-actinin reveals homologies to spectrin and calmodulin."
Baron M.D., Davison M.D., Jones P., Critchley D.R.
J. Biol. Chem. 262:17623-17629(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Mutually exclusive splicing of calcium-binding domain exons in chick alpha-actinin."
Waites G.T., Graham I.R., Jackson P., Millake D.B., Patel B., Blanchard A.D., Weller P., Eperon I.C., Critchley D.R.
J. Biol. Chem. 267:6263-6271(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Brain.
[3]"Primary structure of chicken skeletal muscle and fibroblast alpha-actinins deduced from cDNA sequences."
Arimura C., Suzuki T., Yanagisawa M., Imamura M., Hamada Y., Masaki T.
Eur. J. Biochem. 177:649-655(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 38-893 (ISOFORM 1).
Tissue: Fibroblast.
[4]"Isolation and characterization of a cDNA encoding a chick alpha-actinin."
Baron M.D., Davison M.D., Jones P., Patel B., Critchley D.R.
J. Biol. Chem. 262:2558-2561(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 62-769 (ISOFORM 1).
Tissue: Fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M74143 mRNA. Translation: AAA48570.1.
X13875 mRNA. Translation: CAA32079.1.
J02666 mRNA. Translation: AAA48566.1.
J03486 mRNA. Translation: AAA48567.1.
PIRA42162.
RefSeqNP_989458.1. NM_204127.1.
UniGeneGga.4993.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1SJJelectron microscopy20.00A/B26-893[»]
ProteinModelPortalP05094.
SMRP05094. Positions 31-255, 268-740, 822-893.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid674968. 1 interaction.
IntActP05094. 7 interactions.

Proteomic databases

PaxDbP05094.
PRIDEP05094.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID373918.
KEGGgga:373918.

Organism-specific databases

CTD87.

Phylogenomic databases

eggNOGCOG5069.
HOGENOMHOG000263418.
HOVERGENHBG050453.
InParanoidP05094.
KOK05699.
OMAWIRRTMP.
OrthoDBEOG72C4ZJ.
PhylomeDBP05094.
TreeFamTF352676.

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. 3 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

EvolutionaryTraceP05094.
NextBio20813450.
PROP05094.

Entry information

Entry nameACTN1_CHICK
AccessionPrimary (citable) accession number: P05094
Secondary accession number(s): Q99001
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: February 21, 2001
Last modified: April 16, 2014
This is version 137 of the entry and version 3 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references