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Protein

Alpha-actinin-1

Gene

ACTN1

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi760 – 771121PROSITE-ProRule annotationAdd
BLAST
Calcium bindingi801 – 812122PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • alpha-actinin binding Source: AgBase
  • calcium ion binding Source: InterPro
  • LIM domain binding Source: AgBase
  • phosphoprotein binding Source: AgBase
  • protein homodimerization activity Source: AgBase
  • vinculin binding Source: AgBase

GO - Biological processi

  • actin crosslink formation Source: InterPro
  • actin filament bundle assembly Source: InterPro
  • sarcomere organization Source: AgBase
  • skeletal muscle fiber development Source: AgBase
Complete GO annotation...

Keywords - Ligandi

Actin-binding, Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-actinin-1
Alternative name(s):
Alpha-actinin cytoskeletal isoform
F-actin cross-linking protein
Non-muscle alpha-actinin-1
Gene namesi
Name:ACTN1
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

  • cell Source: AgBase
  • cell leading edge Source: AgBase
  • dense body Source: AgBase
  • focal adhesion Source: AgBase
  • lamellipodium Source: AgBase
  • ruffle Source: UniProtKB-SubCell
  • sarcolemma Source: AgBase
  • stress fiber Source: AgBase
  • Z disc Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 893893Alpha-actinin-1PRO_0000073434Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei13 – 131Phosphotyrosine; by FAK1By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP05094.
PRIDEiP05094.

Interactioni

Subunit structurei

Homodimer; antiparallel.

Binary interactionsi

WithEntry#Exp.IntActNotes
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

Protein-protein interaction databases

BioGridi674968. 1 interaction.
IntActiP05094. 7 interactions.
STRINGi9031.ENSGALP00000015409.

Structurei

Secondary structure

1
893
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi31 – 4919
Helixi64 – 729
Helixi87 – 10317
Helixi114 – 1174
Helixi121 – 13212
Turni148 – 1514
Helixi152 – 1598
Beta strandi169 – 1713
Helixi172 – 1743
Helixi178 – 1858
Beta strandi190 – 1923
Helixi195 – 1984
Helixi203 – 2053
Helixi208 – 21710
Helixi225 – 2284
Helixi236 – 24510
Turni246 – 2505
Turni267 – 2693
Helixi270 – 29425
Helixi295 – 2973
Helixi307 – 32216
Helixi326 – 33712
Turni338 – 3403
Helixi341 – 3455
Turni346 – 3494
Helixi362 – 3643
Helixi365 – 37612
Turni377 – 3793
Helixi380 – 3878
Helixi390 – 41930
Turni422 – 4243
Helixi428 – 44518
Helixi448 – 46417
Helixi470 – 51849
Turni519 – 5224
Helixi523 – 53412
Beta strandi540 – 5423
Helixi543 – 5453
Helixi546 – 55611
Helixi559 – 58123
Beta strandi592 – 5954
Helixi598 – 61922
Helixi620 – 6223
Helixi623 – 65331
Turni661 – 6633
Helixi666 – 68015
Helixi683 – 6853
Helixi686 – 69712
Turni698 – 7003
Helixi712 – 73827
Helixi746 – 75611
Turni757 – 7593
Beta strandi761 – 7699
Helixi772 – 7798
Helixi791 – 80010
Beta strandi806 – 8094
Helixi812 – 8154
Helixi817 – 8204
Beta strandi825 – 8273
Helixi828 – 8358
Helixi836 – 8383
Beta strandi840 – 8456
Helixi846 – 8527
Helixi855 – 86410
Beta strandi865 – 8673
Beta strandi877 – 8804
Helixi881 – 8877

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SJJelectron microscopy20.00A/B26-893[»]
ProteinModelPortaliP05094.
SMRiP05094. Positions 31-255, 268-740, 822-893.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05094.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 248248Actin-bindingAdd
BLAST
Domaini32 – 136105CH 1PROSITE-ProRule annotationAdd
BLAST
Domaini145 – 248104CH 2PROSITE-ProRule annotationAdd
BLAST
Repeati275 – 385111Spectrin 1Add
BLAST
Repeati395 – 500106Spectrin 2Add
BLAST
Repeati510 – 621112Spectrin 3Add
BLAST
Repeati631 – 734104Spectrin 4Add
BLAST
Domaini747 – 78236EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini788 – 82336EF-hand 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the alpha-actinin family.Curated
Contains 1 actin-binding domain.Curated
Contains 2 CH (calponin-homology) domains.PROSITE-ProRule annotation
Contains 2 EF-hand domains.PROSITE-ProRule annotation
Contains 4 spectrin repeats.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5069.
HOGENOMiHOG000263418.
HOVERGENiHBG050453.
InParanoidiP05094.
KOiK05699.
OrthoDBiEOG72C4ZJ.
PhylomeDBiP05094.
TreeFamiTF352676.

Family and domain databases

Gene3Di1.10.238.10. 2 hits.
1.10.418.10. 2 hits.
InterProiIPR001589. Actinin_actin-bd_CS.
IPR026921. Alpha-actinin_1.
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]
PANTHERiPTHR11915:SF241. PTHR11915:SF241. 1 hit.
PfamiPF00307. CH. 2 hits.
PF13405. EF-hand_6. 1 hit.
PF08726. EFhand_Ca_insen. 1 hit.
PF00435. Spectrin. 4 hits.
[Graphical view]
SMARTiSM00033. CH. 2 hits.
SM00054. EFh. 2 hits.
SM00150. SPEC. 3 hits.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 1 hit.
PROSITEiPS00019. 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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Isoforms only differ in the region of the first EF-hand calcium-binding motif.

Isoform 1 (identifier: P05094-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MDHHYDPQQT NDYMQPEEDW DRDLLLDPAW EKQQRKTFTA WCNSHLRKAG
60 70 80 90 100
TQIENIEEDF RDGLKLMLLL EVISGERLAK PERGKMRVHK ISNVNKALDF
110 120 130 140 150
IASKGVKLVS IGAEEIVDGN VKMTLGMIWT IILRFAIQDI SVEETSAKEG
160 170 180 190 200
LLLWCQRKTA PYKNVNIQNF HISWKDGLGF CALIHRHRPE LIDYGKLRKD
210 220 230 240 250
DPLTNLNTAF DVAEKYLDIP KMLDAEDIVG TARPDEKAIM TYVSSFYHAF
260 270 280 290 300
SGAQKAETAA NRICKVLAVN QENEQLMEDY EKLASDLLEW IRRTIPWLEN
310 320 330 340 350
RAPENTMQAM QQKLEDFRDY RRLHKPPKVQ EKCQLEINFN TLQTKLRLSN
360 370 380 390 400
RPAFMPSEGK MVSDINNAWG GLEQAEKGYE EWLLNEIRRL ERLDHLAEKF
410 420 430 440 450
RQKASIHESW TDGKEAMLQQ KDYETATLSE IKALLKKHEA FESDLAAHQD
460 470 480 490 500
RVEQIAAIAQ ELNELDYYDS PSVNARCQKI CDQWDNLGAL TQKRREALER
510 520 530 540 550
TEKLLETIDQ LYLEYAKRAA PFNNWMEGAM EDLQDTFIVH TIEEIQGLTT
560 570 580 590 600
AHEQFKATLP DADKERQAIL GIHNEVSKIV QTYHVNMAGT NPYTTITPQE
610 620 630 640 650
INGKWEHVRQ LVPRRDQALM EEHARQQQNE RLRKQFGAQA NVIGPWIQTK
660 670 680 690 700
MEEIGRISIE MHGTLEDQLN HLRQYEKSIV NYKPKIDQLE GDHQQIQEAL
710 720 730 740 750
IFDNKHTNYT MEHIRVGWEQ LLTTIARTIN EVENQILTRD AKGISQEQMN
760 770 780 790 800
EFRASFNHFD RDHSGTLGPE EFKACLISLG YDIGNDAQGE AEFARIMSIV
810 820 830 840 850
DPNRMGVVTF QAFIDFMSRE TADTDTADQV MASFKILAGD KNYITVDELR
860 870 880 890
RELPPDQAEY CIARMAPYNG RDAVPGALDY MSFSTALYGE SDL
Length:893
Mass (Da):103,162
Last modified:February 21, 2001 - v3
Checksum:iB9D1CE5A2C6F8821
GO
Isoform 2 (identifier: P05094-2) [UniParc]FASTAAdd to basket

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

Show »
Length:888
Mass (Da):102,855
Checksum:i5F2485A047EA644C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti155 – 1551C → Y in AAA48567 (PubMed:1556133).Curated
Sequence conflicti501 – 5011T → S in AAA48570 (PubMed:2826427).Curated
Sequence conflicti852 – 8532EL → DV in CAA32079 (PubMed:3197725).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei762 – 77312DHSGT…PEEFK → KKTGMMDCEDFR in isoform 2. 1 PublicationVSP_000710Add
BLAST
Alternative sequencei779 – 78810LGYDIGNDAQ → MGYNM in isoform 2. 1 PublicationVSP_000711

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M74143 mRNA. Translation: AAA48570.1.
X13875 mRNA. Translation: CAA32079.1.
J02666 mRNA. Translation: AAA48566.1.
J03486 mRNA. Translation: AAA48567.1.
PIRiA42162.
RefSeqiNP_989458.1. NM_204127.1.
UniGeneiGga.4993.

Genome annotation databases

GeneIDi373918.
KEGGigga:373918.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M74143 mRNA. Translation: AAA48570.1.
X13875 mRNA. Translation: CAA32079.1.
J02666 mRNA. Translation: AAA48566.1.
J03486 mRNA. Translation: AAA48567.1.
PIRiA42162.
RefSeqiNP_989458.1. NM_204127.1.
UniGeneiGga.4993.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SJJelectron microscopy20.00A/B26-893[»]
ProteinModelPortaliP05094.
SMRiP05094. Positions 31-255, 268-740, 822-893.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi674968. 1 interaction.
IntActiP05094. 7 interactions.
STRINGi9031.ENSGALP00000015409.

Proteomic databases

PaxDbiP05094.
PRIDEiP05094.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi373918.
KEGGigga:373918.

Organism-specific databases

CTDi87.

Phylogenomic databases

eggNOGiCOG5069.
HOGENOMiHOG000263418.
HOVERGENiHBG050453.
InParanoidiP05094.
KOiK05699.
OrthoDBiEOG72C4ZJ.
PhylomeDBiP05094.
TreeFamiTF352676.

Miscellaneous databases

EvolutionaryTraceiP05094.
NextBioi20813450.
PROiP05094.

Family and domain databases

Gene3Di1.10.238.10. 2 hits.
1.10.418.10. 2 hits.
InterProiIPR001589. Actinin_actin-bd_CS.
IPR026921. Alpha-actinin_1.
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]
PANTHERiPTHR11915:SF241. PTHR11915:SF241. 1 hit.
PfamiPF00307. CH. 2 hits.
PF13405. EF-hand_6. 1 hit.
PF08726. EFhand_Ca_insen. 1 hit.
PF00435. Spectrin. 4 hits.
[Graphical view]
SMARTiSM00033. CH. 2 hits.
SM00054. EFh. 2 hits.
SM00150. SPEC. 3 hits.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 1 hit.
PROSITEiPS00019. 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]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiACTN1_CHICK
AccessioniPrimary (citable) accession number: P05094
Secondary accession number(s): Q99001
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: February 21, 2001
Last modified: June 24, 2015
This is version 146 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.