Alpha-actinin-1

ACTN1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2EYI, 2EYN, 2N8Z, 2N8Y
Identifiers
Aliases	ACTN1, BDPLT15, actinin alpha 1
External IDs	OMIM: 102575 MGI: 2137706 HomoloGene: 55553 GeneCards: ACTN1
Gene location (Human) Chr. Chromosome 14 (human) Band 14q24.1|14q22-q24 Start 68,874,128 bp End 68,979,440 bp
Gene location (Mouse) Chr. Chromosome 12 (mouse) Band 12 C3|12 36.49 cM Start 80,214,321 bp End 80,307,145 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in saphenous vein ascending aorta right coronary artery popliteal artery stromal cell of endometrium smooth muscle tissue myometrium gastric mucosa left coronary artery seminal vesicula Top expressed in stria vascularis ascending aorta external carotid artery internal carotid artery ciliary body uterus belly cord cervix calvaria semi-lunar valve 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 Species Human Mouse 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 Mb Chr 12: 80.21 – 80.31 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

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

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. 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.

Interactions

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

• CDK5R1,
• CDK5R2,
• Collagen, type XVII, alpha 1,
• GIPC1,
• PDLIM1,
• Protein kinase N1,
• SSX2IP, and
• Zyxin.
• PTPRT (PTPrho)

See also

• Actinin

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.