Alpha-actinin-1

Protein-coding gene in the species Homo sapiens
ACTN1
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2EYI, 2EYN, 2N8Z, 2N8Y

Identifiers
AliasesACTN1, BDPLT15, actinin alpha 1
External IDsOMIM: 102575; MGI: 2137706; HomoloGene: 55553; GeneCards: ACTN1; OMA:ACTN1 - orthologs
Gene location (Human)
Chromosome 14 (human)
Chr.Chromosome 14 (human)[1]
Chromosome 14 (human)
Genomic location for ACTN1
Genomic location for ACTN1
Band14q24.1|14q22-q24Start68,874,128 bp[1]
End68,979,440 bp[1]
Gene location (Mouse)
Chromosome 12 (mouse)
Chr.Chromosome 12 (mouse)[2]
Chromosome 12 (mouse)
Genomic location for ACTN1
Genomic location for ACTN1
Band12 C3|12 36.49 cMStart80,214,321 bp[2]
End80,307,145 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • saphenous vein

  • ascending aorta

  • right coronary artery

  • popliteal artery

  • tibial arteries

  • stromal cell of endometrium

  • Descending thoracic aorta

  • smooth muscle tissue

  • myometrium

  • gastric mucosa
Top expressed in
  • vestibular membrane of cochlear duct

  • Ileal epithelium

  • granulocyte

  • stria vascularis

  • tunica media of zone of aorta

  • endothelial cell of lymphatic vessel

  • ascending aorta

  • external carotid artery

  • internal carotid artery

  • ciliary body
More reference expression data
BioGPS




More reference expression data
Gene ontology
Molecular function
  • calcium ion binding
  • protein homodimerization activity
  • transmembrane transporter binding
  • vinculin binding
  • metal ion binding
  • integrin binding
  • actin filament binding
  • protein binding
  • nuclear receptor coactivator activity
  • double-stranded RNA binding
  • actin binding
  • structural constituent of postsynapse
Cellular component
  • cytoplasm
  • cytosol
  • cell projection
  • pseudopodium
  • membrane
  • cell-cell junction
  • focal adhesion
  • ruffle
  • plasma membrane
  • intracellular anatomical structure
  • stress fiber
  • extracellular region
  • cell junction
  • Z disc
  • brush border
  • actin filament
  • fascia adherens
  • extracellular exosome
  • cytoskeleton
  • platelet alpha granule lumen
  • sarcomere
  • extracellular space
  • glutamatergic synapse
Biological process
  • regulation of apoptotic process
  • actin filament organization
  • actin filament network formation
  • platelet degranulation
  • platelet formation
  • actin filament bundle assembly
  • focal adhesion assembly
  • actin crosslink formation
  • platelet morphogenesis
  • platelet aggregation
  • platelet activation
  • regulation of nucleic acid-templated transcription
  • postsynapse organization
  • positive regulation of nucleic acid-templated transcription
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

87

109711

Ensembl

ENSG00000072110

ENSMUSG00000015143

UniProt

P12814

Q7TPR4

RefSeq (mRNA)

NM_001102
NM_001130004
NM_001130005

NM_134156
NM_001346669
NM_001379075
NM_001379076

RefSeq (protein)

NP_001093
NP_001123476
NP_001123477
NP_001093.1

NP_001333598
NP_598917
NP_001366004
NP_001366005

Location (UCSC)Chr 14: 68.87 – 68.98 MbChr 12: 80.21 – 80.31 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Alpha-actinin-1 is a protein that in humans is encoded by the ACTN1 gene.[5]

Function

Alpha actinins belong to the spectrin gene superfamily which represents a diverse group of cytoskeletal proteins, including the alpha and beta spectrins and dystrophins. Alpha-actinin-1 is an F-actin cross-linking protein – a bundling protein that is thought to anchor actin to a number of intracellular structures.[6] Alpha-actinin-1 is a non-muscle cytoskeletal isoform found along microfilament bundles and adherens-type junctions, where it is involved in binding actin to the membrane. In contrast, skeletal, cardiac, and smooth muscle isoforms are localized to the Z-disc and analogous dense bodies, where they help anchor the myofibrillar actin filaments.[7]

Interactions

Alpha-actinin-1 has been shown to interact with:

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000072110 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000015143 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Youssoufian H, McAfee M, Kwiatkowski DJ (Jul 1990). "Cloning and chromosomal localization of the human cytoskeletal alpha-actinin gene reveals linkage to the beta-spectrin gene". Am J Hum Genet. 47 (1): 62–72. PMC 1683765. PMID 2349951.
  6. ^ "ACTN2 - Alpha-actinin-2 - Homo sapiens (Human) - ACTN2 gene & protein". www.uniprot.org. Retrieved 5 December 2021.
  7. ^ "Entrez Gene: ACTN1 actinin, alpha 1".
  8. ^ a b Dhavan R, Greer PL, Morabito MA, Orlando LR, Tsai LH (September 2002). "The cyclin-dependent kinase 5 activators p35 and p39 interact with the alpha-subunit of Ca2+/calmodulin-dependent protein kinase II and alpha-actinin-1 in a calcium-dependent manner". J. Neurosci. 22 (18): 7879–91. doi:10.1523/JNEUROSCI.22-18-07879.2002. PMC 6758084. PMID 12223541.
  9. ^ Gonzalez AM, Otey C, Edlund M, Jones JC (December 2001). "Interactions of a hemidesmosome component and actinin family members". J. Cell Sci. 114 (Pt 23): 4197–206. doi:10.1242/jcs.114.23.4197. PMID 11739652.
  10. ^ Bunn RC, Jensen MA, Reed BC (April 1999). "Protein interactions with the glucose transporter binding protein GLUT1CBP that provide a link between GLUT1 and the cytoskeleton". Mol. Biol. Cell. 10 (4): 819–32. doi:10.1091/mbc.10.4.819. PMC 25204. PMID 10198040.
  11. ^ Vallenius T, Luukko K, Mäkelä TP (April 2000). "CLP-36 PDZ-LIM protein associates with nonmuscle alpha-actinin-1 and alpha-actinin-4". J. Biol. Chem. 275 (15): 11100–5. doi:10.1074/jbc.275.15.11100. PMID 10753915.
  12. ^ Bauer K, Kratzer M, Otte M, de Quintana KL, Hagmann J, Arnold GJ, Eckerskorn C, Lottspeich F, Siess W (December 2000). "Human CLP36, a PDZ-domain and LIM-domain protein, binds to alpha-actinin-1 and associates with actin filaments and stress fibers in activated platelets and endothelial cells". Blood. 96 (13): 4236–45. doi:10.1182/blood.V96.13.4236. PMID 11110697.
  13. ^ Feng S, Reséndiz JC, Christodoulides N, Lu X, Arboleda D, Berndt MC, Kroll MH (January 2002). "Pathological shear stress stimulates the tyrosine phosphorylation of alpha-actinin associated with the glycoprotein Ib-IX complex". Biochemistry. 41 (4): 1100–8. doi:10.1021/bi0156005. PMID 11802708.
  14. ^ Asada M, Irie K, Morimoto K, Yamada A, Ikeda W, Takeuchi M, Takai Y (February 2003). "ADIP, a novel Afadin- and alpha-actinin-binding protein localized at cell-cell adherens junctions". J. Biol. Chem. 278 (6): 4103–11. doi:10.1074/jbc.M209832200. PMID 12446711.
  15. ^ Reinhard M, Zumbrunn J, Jaquemar D, Kuhn M, Walter U, Trueb B (May 1999). "An alpha-actinin binding site of zyxin is essential for subcellular zyxin localization and alpha-actinin recruitment". J. Biol. Chem. 274 (19): 13410–8. doi:10.1074/jbc.274.19.13410. PMID 10224105.
  16. ^ Li B, Trueb B (September 2001). "Analysis of the alpha-actinin/zyxin interaction". J. Biol. Chem. 276 (36): 33328–35. doi:10.1074/jbc.M100789200. PMID 11423549.
  17. ^ Besco JA, Hooft van Huijsduijnen R, Frostholm A, Rotter A (2006). "Intracellular substrates of brain-enriched receptor protein tyrosine phosphatase rho (RPTPrho/PTPRT)". Brain Res. 1116 (1): 50–7. doi:10.1016/j.brainres.2006.07.122. PMID 16973135. S2CID 23343123.

Further reading

  • Snásel J, Pichová I (1997). "The cleavage of host cell proteins by HIV-1 protease". Folia Biol. (Praha). 42 (5): 227–30. doi:10.1007/BF02818986. PMID 8997639. S2CID 7617882.
  • Menko S, Philp N, Veneziale B, Walker J (1998). "Integrins and development: how might these receptors regulate differentiation of the lens". Ann. N. Y. Acad. Sci. 842 (1): 36–41. Bibcode:1998NYASA.842...36M. doi:10.1111/j.1749-6632.1998.tb09629.x. PMID 9599291. S2CID 31836557.
  • Yürüker B, Niggli V (1992). "Alpha-actinin and vinculin in human neutrophils: reorganization during adhesion and relation to the actin network". J. Cell Sci. 101 (2): 403–14. doi:10.1242/jcs.101.2.403. PMID 1629252.
  • Tokuue Y, Goto S, Imamura M, et al. (1992). "Transfection of chicken skeletal muscle alpha-actinin cDNA into nonmuscle and myogenic cells: dimerization is not essential for alpha-actinin to bind to microfilaments". Exp. Cell Res. 197 (2): 158–67. doi:10.1016/0014-4827(91)90418-T. PMID 1720388.
  • Shoeman RL, Kesselmier C, Mothes E, et al. (1991). "Non-viral cellular substrates for human immunodeficiency virus type 1 protease". FEBS Lett. 278 (2): 199–203. doi:10.1016/0014-5793(91)80116-K. PMID 1991513.
  • Nishiyama M, Ozturk M, Frohlich M, et al. (1990). "Expression of human alpha-actinin in human hepatocellular carcinoma". Cancer Res. 50 (19): 6291–4. PMID 2169343.
  • Millake DB, Blanchard AD, Patel B, Critchley DR (1989). "The cDNA sequence of a human placental alpha-actinin". Nucleic Acids Res. 17 (16): 6725. doi:10.1093/nar/17.16.6725. PMC 318366. PMID 2780298.
  • Dubernard V, Faucher D, Launay JM, Legrand C (1995). "Identification of the cytoskeletal protein alpha-actinin as a platelet thrombospondin-binding protein". FEBS Lett. 364 (2): 109–14. doi:10.1016/0014-5793(95)00362-D. PMID 7750553. S2CID 44955001.
  • Knudsen KA, Soler AP, Johnson KR, Wheelock MJ (1995). "Interaction of alpha-actinin with the cadherin/catenin cell-cell adhesion complex via alpha-catenin". J. Cell Biol. 130 (1): 67–77. doi:10.1083/jcb.130.1.67. PMC 2120515. PMID 7790378.
  • Glück U, Ben-Ze'ev A (1995). "Modulation of alpha-actinin levels affects cell motility and confers tumorigenicity on 3T3 cells". J. Cell Sci. 107 (7): 1773–82. doi:10.1242/jcs.107.7.1773. PMID 7983147.
  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
  • Egerton M, Moritz RL, Druker B, et al. (1996). "Identification of the 70kD heat shock cognate protein (Hsc70) and alpha-actinin-1 as novel phosphotyrosine-containing proteins in T lymphocytes". Biochem. Biophys. Res. Commun. 224 (3): 666–74. doi:10.1006/bbrc.1996.1082. PMID 8713105.
  • Mukai H, Toshimori M, Shibata H, et al. (1997). "Interaction of PKN with alpha-actinin". J. Biol. Chem. 272 (8): 4740–6. doi:10.1074/jbc.272.8.4740. PMID 9030526.
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
  • Hazan RB, Norton L (1998). "The epidermal growth factor receptor modulates the interaction of E-cadherin with the actin cytoskeleton". J. Biol. Chem. 273 (15): 9078–84. doi:10.1074/jbc.273.15.9078. PMID 9535896.
  • Bunn RC, Jensen MA, Reed BC (1999). "Protein interactions with the glucose transporter binding protein GLUT1CBP that provide a link between GLUT1 and the cytoskeleton". Mol. Biol. Cell. 10 (4): 819–32. doi:10.1091/mbc.10.4.819. PMC 25204. PMID 10198040.
  • Reinhard M, Zumbrunn J, Jaquemar D, et al. (1999). "An alpha-actinin binding site of zyxin is essential for subcellular zyxin localization and alpha-actinin recruitment". J. Biol. Chem. 274 (19): 13410–8. doi:10.1074/jbc.274.19.13410. PMID 10224105.

External links

  • Actinin, alpha 1 Info with links in the Cell Migration Gateway
  • Human ACTN1 genome location and ACTN1 gene details page in the UCSC Genome Browser.
  • v
  • t
  • e
  • 1sjj: Cryo-EM Structure of Chicken Gizzard Smooth Muscle alpha-Actinin
    1sjj: Cryo-EM Structure of Chicken Gizzard Smooth Muscle alpha-Actinin
  • 2eyi: Crystal structure of the actin-binding domain of human alpha-actinin 1 at 1.7 Angstrom resolution
    2eyi: Crystal structure of the actin-binding domain of human alpha-actinin 1 at 1.7 Angstrom resolution
  • 2eyn: Crystal structure of the actin-binding domain of human alpha-actinin 1 at 1.8 Angstrom resolution
    2eyn: Crystal structure of the actin-binding domain of human alpha-actinin 1 at 1.8 Angstrom resolution
  • v
  • t
  • e
Human
Microfilaments
and ABPs
Myofilament
Actins
Myosins
Other
Other
Intermediate
filaments
Type 1/2
(Keratin,
Cytokeratin)
Epithelial keratins
(soft alpha-keratins)
Hair keratins
(hard alpha-keratins)
Ungrouped alpha
Not alpha
Type 3
Type 4
Type 5
Microtubules
and MAPs
Tubulins
MAPs
Kinesins
Dyneins
Microtubule organising proteins
Microtubule severing proteins
Other
Catenins
Membrane
Other
Nonhuman
See also: cytoskeletal defects