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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)DescriptionActionsGraphical viewLength
Calcium bindingi760 – 7711PROSITE-ProRule annotationAdd BLAST12
Calcium bindingi801 – 8122PROSITE-ProRule annotationAdd BLAST12

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

Enzyme and pathway databases

SABIO-RKP05094.

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
Proteomesi
  • UP000000539 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

  • bicellular tight junction Source: AgBase
  • cell Source: AgBase
  • cell leading edge Source: AgBase
  • dense body Source: AgBase
  • focal adhesion Source: AgBase
  • inner dense plaque of desmosome Source: AgBase
  • lamellipodium Source: AgBase
  • lateral plasma membrane Source: AgBase
  • outer dense plaque of desmosome Source: AgBase
  • ruffle Source: UniProtKB-SubCell
  • sarcolemma Source: AgBase
  • smooth muscle dense body Source: AgBase
  • stress fiber Source: AgBase
  • terminal web Source: AgBase
  • Z disc Source: UniProtKB-SubCell
  • zonula adherens Source: AgBase
Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000734341 – 893Alpha-actinin-1Add BLAST893

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei13Phosphotyrosine; by FAK1By similarity1

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

GO - Molecular functioni

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

Protein-protein interaction databases

BioGridi674968. 1 interactor.
IntActiP05094. 7 interactors.
STRINGi9031.ENSGALP00000015409.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SJJelectron microscopy20.00A/B26-893[»]
ProteinModelPortaliP05094.
SMRiP05094.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05094.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 248Actin-bindingAdd BLAST248
Domaini32 – 136CH 1PROSITE-ProRule annotationAdd BLAST105
Domaini145 – 248CH 2PROSITE-ProRule annotationAdd BLAST104
Repeati275 – 385Spectrin 1Add BLAST111
Repeati395 – 500Spectrin 2Add BLAST106
Repeati510 – 621Spectrin 3Add BLAST112
Repeati631 – 734Spectrin 4Add BLAST104
Domaini747 – 782EF-hand 1PROSITE-ProRule annotationAdd BLAST36
Domaini788 – 823EF-hand 2PROSITE-ProRule annotationAdd BLAST36

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

eggNOGiKOG0035. Eukaryota.
COG5069. LUCA.
GeneTreeiENSGT00760000118813.
HOGENOMiHOG000263418.
HOVERGENiHBG050453.
InParanoidiP05094.
KOiK05699.
PhylomeDBiP05094.
TreeFamiTF352676.

Family and domain databases

CDDicd00014. CH. 2 hits.
cd00051. EFh. 1 hit.
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.
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]
SUPFAMiSSF47473. SSF47473. 1 hit.
SSF47576. 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)DescriptionActionsGraphical viewLength
Sequence conflicti155C → Y in AAA48567 (PubMed:1556133).Curated1
Sequence conflicti501T → S in AAA48570 (PubMed:2826427).Curated1
Sequence conflicti852 – 853EL → DV in CAA32079 (PubMed:3197725).Curated2

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_000710762 – 773DHSGT…PEEFK → KKTGMMDCEDFR in isoform 2. 1 PublicationAdd BLAST12
Alternative sequenceiVSP_000711779 – 788LGYDIGNDAQ → MGYNM in isoform 2. 1 Publication10

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.
XP_015142744.1. XM_015287258.1. [P05094-1]
UniGeneiGga.4993.

Genome annotation databases

EnsembliENSGALT00000061392; ENSGALP00000051864; ENSGALG00000042458. [P05094-2]
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.
XP_015142744.1. XM_015287258.1. [P05094-1]
UniGeneiGga.4993.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SJJelectron microscopy20.00A/B26-893[»]
ProteinModelPortaliP05094.
SMRiP05094.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi674968. 1 interactor.
IntActiP05094. 7 interactors.
STRINGi9031.ENSGALP00000015409.

Proteomic databases

PaxDbiP05094.
PRIDEiP05094.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSGALT00000061392; ENSGALP00000051864; ENSGALG00000042458. [P05094-2]
GeneIDi373918.
KEGGigga:373918.

Organism-specific databases

CTDi87.

Phylogenomic databases

eggNOGiKOG0035. Eukaryota.
COG5069. LUCA.
GeneTreeiENSGT00760000118813.
HOGENOMiHOG000263418.
HOVERGENiHBG050453.
InParanoidiP05094.
KOiK05699.
PhylomeDBiP05094.
TreeFamiTF352676.

Enzyme and pathway databases

SABIO-RKP05094.

Miscellaneous databases

EvolutionaryTraceiP05094.
PROiP05094.

Family and domain databases

CDDicd00014. CH. 2 hits.
cd00051. EFh. 1 hit.
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.
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]
SUPFAMiSSF47473. SSF47473. 1 hit.
SSF47576. 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...

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: November 30, 2016
This is version 158 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

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 one 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.