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Q08043

- ACTN3_HUMAN

UniProt

Q08043 - ACTN3_HUMAN

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Protein

Alpha-actinin-3

Gene

ACTN3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi773 – 784121; possibly ancestralAdd
BLAST
Calcium bindingi809 – 820122; possibly ancestralAdd
BLAST

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. integrin binding Source: UniProtKB
  3. protein homodimerization activity Source: UniProtKB
  4. structural constituent of muscle Source: ProtInc

GO - Biological processi

  1. focal adhesion assembly Source: UniProtKB
  2. muscle filament sliding Source: Reactome
  3. regulation of apoptotic process Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Actin-binding, Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_16969. Striated Muscle Contraction.
REACT_23832. Nephrin interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-actinin-3
Alternative name(s):
Alpha-actinin skeletal muscle isoform 3
F-actin cross-linking protein
Gene namesi
Name:ACTN3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:165. ACTN3.

Subcellular locationi

GO - Cellular componenti

  1. actin filament Source: ProtInc
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: UniProtKB
  4. focal adhesion Source: UniProtKB
  5. pseudopodium Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

MIMi102574. gene+phenotype.
PharmGKBiPA24485.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 901901Alpha-actinin-3PRO_0000073438Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ08043.
PRIDEiQ08043.

PTM databases

PhosphoSiteiQ08043.

Expressioni

Tissue specificityi

Expressed only in a subset of type 2 skeletal muscle fibers.1 Publication

Gene expression databases

CleanExiHS_ACTN3.
ExpressionAtlasiQ08043. baseline and differential.
GenevestigatoriQ08043.

Interactioni

Subunit structurei

Homodimer; antiparallel. Also forms heterodimers with ACTN2. Interacts with MYOZ1.1 Publication

Protein-protein interaction databases

BioGridi106604. 4 interactions.
IntActiQ08043. 4 interactions.
MINTiMINT-269455.

Structurei

Secondary structure

1
901
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi43 – 5917Combined sources
Helixi60 – 623Combined sources
Turni69 – 757Combined sources
Helixi77 – 8711Combined sources
Helixi100 – 11516Combined sources
Turni116 – 1183Combined sources
Helixi126 – 1316Combined sources
Helixi134 – 14916Combined sources
Turni150 – 1523Combined sources
Helixi160 – 17213Combined sources
Beta strandi182 – 1843Combined sources
Helixi185 – 1873Combined sources
Helixi191 – 20010Combined sources
Turni202 – 2043Combined sources
Helixi207 – 2093Combined sources
Helixi215 – 22915Combined sources
Helixi238 – 2436Combined sources
Beta strandi244 – 2463Combined sources
Helixi249 – 26517Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TJTX-ray2.19A26-273[»]
1WKUX-ray1.60A/B26-273[»]
3LUEelectron microscopy-K/L/M/N/O/P/Q/R/S/T42-150[»]
ProteinModelPortaliQ08043.
SMRiQ08043. Positions 42-268, 281-901.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ08043.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 261261Actin-bindingAdd
BLAST
Domaini45 – 149105CH 1PROSITE-ProRule annotationAdd
BLAST
Domaini158 – 261104CH 2PROSITE-ProRule annotationAdd
BLAST
Repeati288 – 398111Spectrin 1Add
BLAST
Repeati408 – 513106Spectrin 2Add
BLAST
Repeati523 – 634112Spectrin 3Add
BLAST
Repeati644 – 747104Spectrin 4Add
BLAST
Domaini760 – 79536EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini796 – 83136EF-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

GeneTreeiENSGT00760000118813.
HOVERGENiHBG050453.
InParanoidiQ08043.
KOiK05699.
PhylomeDBiQ08043.

Family and domain databases

Gene3Di1.10.238.10. 2 hits.
1.10.418.10. 2 hits.
InterProiIPR001589. 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]
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. 2 hits.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 1 hit.
PROSITEiPS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
PS50222. EF_HAND_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q08043-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MMMVMQPEGL GAGEGRFAGG GGGGEYMEQE EDWDRDLLLD PAWEKQQRKT
60 70 80 90 100
FTAWCNSHLR KAGTQIENIE EDFRNGLKLM LLLEVISGER LPRPDKGKMR
110 120 130 140 150
FHKIANVNKA LDFIASKGVK LVSIGAEEIV DGNLKMTLGM IWTIILRFAI
160 170 180 190 200
QDISVEETSA KEGLLLWCQR KTAPYRNVNV QNFHTSWKDG LALCALIHRH
210 220 230 240 250
RPDLIDYAKL RKDDPIGNLN TAFEVAEKYL DIPKMLDAED IVNTPKPDEK
260 270 280 290 300
AIMTYVSCFY HAFAGAEQAE TAANRICKVL AVNQENEKLM EEYEKLASEL
310 320 330 340 350
LEWIRRTVPW LENRVGEPSM SAMQRKLEDF RDYRRLHKPP RIQEKCQLEI
360 370 380 390 400
NFNTLQTKLR LSHRPAFMPS EGKLVSDIAN AWRGLEQVEK GYEDWLLSEI
410 420 430 440 450
RRLQRLQHLA EKFRQKASLH EAWTRGKEEM LSQRDYDSAL LQEVRALLRR
460 470 480 490 500
HEAFESDLAA HQDRVEHIAA LAQELNELDY HEAASVNSRC QAICDQWDNL
510 520 530 540 550
GTLTQKRRDA LERMEKLLET IDRLQLEFAR RAAPFNNWLD GAVEDLQDVW
560 570 580 590 600
LVHSVEETQS LLTAHDQFKA TLPEADRERG AIMGIQGEIQ KICQTYGLRP
610 620 630 640 650
CSTNPYITLS PQDINTKWDM VRKLVPSCDQ TLQEELARQQ VNERLRRQFA
660 670 680 690 700
AQANAIGPWI QAKVEEVGRL AAGLAGSLEE QMAGLRQQEQ NIINYKTNID
710 720 730 740 750
RLEGDHQLLQ ESLVFDNKHT VYSMEHIRVG WEQLLTSIAR TINEVENQVL
760 770 780 790 800
TRDAKGLSQE QLNEFRASFN HFDRKQNGMM EPDDFRACLI SMGYDLGEVE
810 820 830 840 850
FARIMTMVDP NAAGVVTFQA FIDFMTRETA ETDTTEQVVA SFKILAGDKN
860 870 880 890 900
YITPEELRRE LPAKQAEYCI RRMVPYKGSG APAGALDYVA FSSALYGESD

L
Length:901
Mass (Da):103,241
Last modified:November 25, 2008 - v2
Checksum:iC49B7885E7E1EDA7
GO

Sequence cautioni

The sequence AP002748 differs from that shown. Reason: According to the human genome assembly there is a stop codon in position 577 which is only found in 18% of the world population.Curated

Polymorphismi

About 18% of the world population lack a functional ACTN3 due to a stop codon polymorphism at position 577. The absence of a functional ACTN3 expression is not correlated with a disease state [MIMi:102574].

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti523 – 5231R → Q.3 Publications
Corresponds to variant rs1671064 [ dbSNP | Ensembl ].
VAR_012705
Natural varianti628 – 6281C → R.2 Publications
Corresponds to variant rs618838 [ dbSNP | Ensembl ].
VAR_047528
Natural varianti635 – 6351E → A.
Corresponds to variant rs2229456 [ dbSNP | Ensembl ].
VAR_033488
Natural varianti776 – 7761Q → R.2 Publications
Corresponds to variant rs540874 [ dbSNP | Ensembl ].
VAR_047529

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M86407 mRNA. Translation: AAA51585.1.
AP002748 Genomic DNA. No translation available.
BC099647 mRNA. Translation: AAH99647.1.
BC099649 mRNA. Translation: AAH99649.1.
PIRiB40199. FAHUA3.
RefSeqiNP_001095.2. NM_001104.3.
NP_001245300.2. NM_001258371.2.
UniGeneiHs.654432.
Hs.737862.

Genome annotation databases

EnsembliENST00000513398; ENSP00000426797; ENSG00000248746.
GeneIDi89.
KEGGihsa:89.

Polymorphism databases

DMDMi215273967.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M86407 mRNA. Translation: AAA51585.1 .
AP002748 Genomic DNA. No translation available.
BC099647 mRNA. Translation: AAH99647.1 .
BC099649 mRNA. Translation: AAH99649.1 .
PIRi B40199. FAHUA3.
RefSeqi NP_001095.2. NM_001104.3.
NP_001245300.2. NM_001258371.2.
UniGenei Hs.654432.
Hs.737862.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1TJT X-ray 2.19 A 26-273 [» ]
1WKU X-ray 1.60 A/B 26-273 [» ]
3LUE electron microscopy - K/L/M/N/O/P/Q/R/S/T 42-150 [» ]
ProteinModelPortali Q08043.
SMRi Q08043. Positions 42-268, 281-901.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106604. 4 interactions.
IntActi Q08043. 4 interactions.
MINTi MINT-269455.

PTM databases

PhosphoSitei Q08043.

Polymorphism databases

DMDMi 215273967.

Proteomic databases

MaxQBi Q08043.
PRIDEi Q08043.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000513398 ; ENSP00000426797 ; ENSG00000248746 .
GeneIDi 89.
KEGGi hsa:89.

Organism-specific databases

CTDi 89.
GeneCardsi GC11P066314.
HGNCi HGNC:165. ACTN3.
MIMi 102574. gene+phenotype.
neXtProti NX_Q08043.
PharmGKBi PA24485.
GenAtlasi Search...

Phylogenomic databases

GeneTreei ENSGT00760000118813.
HOVERGENi HBG050453.
InParanoidi Q08043.
KOi K05699.
PhylomeDBi Q08043.

Enzyme and pathway databases

Reactomei REACT_16969. Striated Muscle Contraction.
REACT_23832. Nephrin interactions.

Miscellaneous databases

EvolutionaryTracei Q08043.
GeneWikii ACTN3.
GenomeRNAii 89.
NextBioi 331.
PROi Q08043.
SOURCEi Search...

Gene expression databases

CleanExi HS_ACTN3.
ExpressionAtlasi Q08043. baseline and differential.
Genevestigatori Q08043.

Family and domain databases

Gene3Di 1.10.238.10. 2 hits.
1.10.418.10. 2 hits.
InterProi IPR001589. 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 ]
Pfami PF00307. CH. 2 hits.
PF08726. EFhand_Ca_insen. 1 hit.
PF00435. Spectrin. 4 hits.
[Graphical view ]
SMARTi SM00033. CH. 2 hits.
SM00054. EFh. 2 hits.
SM00150. SPEC. 2 hits.
[Graphical view ]
SUPFAMi SSF47576. SSF47576. 1 hit.
PROSITEi PS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
PS50222. EF_HAND_2. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of two human skeletal muscle alpha-actinin genes located on chromosomes 1 and 11."
    Beggs A.H., Byers T.J., Knoll J.H.M., Boyce F.M., Bruns G.A.P., Kunkel L.M.
    J. Biol. Chem. 267:9281-9288(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS GLN-523; ARG-628 AND ARG-776.
    Tissue: Skeletal muscle.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS GLN-523; ARG-628 AND ARG-776.
  4. "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: TISSUE SPECIFICITY, POLYMORPHISM.
  5. "Myozenin: an alpha-actinin- and gamma-filamin-binding protein of skeletal muscle Z lines."
    Takada F., Vander Woude D.L., Tong H.-Q., Thompson T.G., Watkins S.C., Kunkel L.M., Beggs A.H.
    Proc. Natl. Acad. Sci. U.S.A. 98:1595-1600(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MYOZ1.
  6. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "The crystal structure of the actin binding domain from alpha-actinin in its closed conformation: structural insight into phospholipid regulation of alpha-actinin."
    Franzot G., Sjoblom B., Gautel M., Djinovic Carugo K.
    J. Mol. Biol. 348:151-165(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 26-273.
  8. "A common nonsense mutation results in alpha-actinin-3 deficiency in the general population."
    North K.N., Yang N., Wattanasirichaigoon D., Mills M., Easteal S., Beggs A.H.
    Nat. Genet. 21:353-354(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT GLN-523, POLYMORPHISM.

Entry informationi

Entry nameiACTN3_HUMAN
AccessioniPrimary (citable) accession number: Q08043
Secondary accession number(s): A6NP77, Q4KKV2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: November 25, 2008
Last modified: November 26, 2014
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3