ADD1

ADD1
Identificadores
Nomes alternativos	ADD1, alfa-aducina
IDs externos	OMIM: 102680 HomoloGene: 22758 GeneCards: ADD1
Ontologia genética
Função molecular	• spectrin binding; • protein homodimerization activity; • transcription factor binding; • structural molecule activity; • calmodulin binding; • actin filament binding; • GO:0001948, GO:0016582 ligação a proteínas plasmáticas; • protein heterodimerization activity; • actin binding; • RNA binding; • cadherin binding;
Componente celular	• F-actin capping protein complex; • citosol; • membrane; • focal adhesion; • membrana plasmática; • cariolinfa; • citoesqueleto; • núcleo celular; • nuclear body; • citoplasma; • GO:0097483, GO:0097481 postsynaptic density; • plasma membrane raft;
Processo biológico	• cell volume homeostasis; • multicellular organism growth; • barbed-end actin filament capping; • in utero embryonic development; • actin filament bundle assembly; • IRE1-mediated unfolded protein response; • transmembrane transport; • GO:0000767 cell morphogenesis; • erythrocyte differentiation; • homeostasis of number of cells within a tissue; • positive regulation of protein binding; • actin cytoskeleton organization; • hemoglobin metabolic process; • cellular response to calcium ion; • positive regulation of establishment of endothelial barrier; • positive regulation of adherens junction organization;
	Sources:Amigo / QuickGO
Padrão de expressão RNA
	; ; ; ;
	Mais dados de referência de expressão
Ortólogos
	118
	n/a
	ENSG00000087274
	n/a
	P35611
	n/a
NM_001119; NM_001286645; NM_014189; NM_014190; NM_176801;
	NM_001354754; NM_001354755; NM_001354756; NM_001354757; NM_001354759; NM_001354761; NM_001354762; NM_001354758
	n/a
NP_001110; NP_001273574; NP_054908; NP_054909; NP_789771;
	NP_001341683; NP_001341684; NP_001341685; NP_001341686; NP_001341688; NP_001341690; NP_001341691; NP_001341687
	n/a
	Wikidata
Ver/Editar Humano

A alfa-aducina é uma proteína que em humanos é codificada pelo gene ADD1.

As adducinas são uma família de proteínas do citoesqueleto codificadas por três genes (alfa, beta, gama). A adducina é uma proteína heterodimérica que consiste em subunidades relacionadas, produzidas a partir de genes distintos, mas que compartilham uma estrutura semelhante. A alfa e a beta-adducina incluem uma região N-terminal resistente a protease e uma região C-terminal hidrofílica sensível a protease. As alfa e gama-adducinas são expressas em toda a parte. Por outro lado, a beta-adducina é expressa em altos níveis no cérebro e nos tecidos hematopoiéticos. A aducina se liga com alta afinidade ao Ca²⁺/calmodulina e é um substrato para as proteínas cinases A e C. A emenda alternativa resulta em múltiplas variantes que codificam isoformas distintas; no entanto, nem todas as variantes foram totalmente descritas. O polimorfismo no ADD1 está associado à hipertensão.

Referências

↑ «Human PubMed Reference:»
↑ Joshi R, Gilligan DM, Otto E, McLaughlin T, Bennett V (novembro de 1991). «Primary structure and domain organization of human alpha and beta adducin». J Cell Biol. 115 (3): 665–75. PMC 2289184. PMID 1840603. doi:10.1083/jcb.115.3.665
1 2 «Entrez Gene: ADD1 adducin 1 (alpha)»
↑ Hirata R, Ohsumk Y, Nakano A, Kawasaki H, Suzuki K, Anraku Y (abril de 1990). «Molecular structure of a gene, VMA1, encoding the catalytic subunit of H(+)-translocating adenosine triphosphatase from vacuolar membranes of Saccharomyces cerevisiae». J. Biol. Chem. 265 (12): 6726–33. PMID 2139027
↑ Schlüter H, Apweiler R, Holzhütter HG, Jungblut PR (setembro de 2009). «Finding one's way in proteomics: a protein species nomenclature». Chemistry Central Journal. 3. 11 páginas. PMC 2758878. PMID 19740416. doi:10.1186/1752-153X-3-11

Leitura adicional

Mangeat PH (1989). «Interaction of biological membranes with the cytoskeletal framework of living cells». Biol. Cell. 64 (3): 261–81. PMID 2976282. doi:10.1016/0248-4900(88)90001-9
Matsuoka Y, Li X, Bennett V (2000). «Adducin: structure, function and regulation». Cell. Mol. Life Sci. 57 (6): 884–95. PMID 10950304. doi:10.1007/PL00000731
Goldberg YP, Lin BY, Andrew SE, et al. (1993). «Cloning and mapping of the alpha-adducin gene close to D4S95 and assessment of its relationship to Huntington disease». Hum. Mol. Genet. 1 (9): 669–75. PMID 1284592. doi:10.1093/hmg/1.9.669
Taylor SA, Snell RG, Buckler A, et al. (1994). «Cloning of the alpha-adducin gene from the Huntington's disease candidate region of chromosome 4 by exon amplification». Nat. Genet. 2 (3): 223–7. PMID 1345173. doi:10.1038/ng1192-223
Gardner K, Bennett V (1987). «Modulation of spectrin-actin assembly by erythrocyte adducin». Nature. 328 (6128): 359–62. Bibcode:1987Natur.328..359G. PMID 3600811. doi:10.1038/328359a0
Gilligan DM, Lieman J, Bennett V (1996). «Assignment of the human beta-adducin gene (ADD2) to 2p13-p14 by in situ hybridization». Genomics. 28 (3): 610–2. PMID 7490111. doi:10.1006/geno.1995.1205
Lin B, Nasir J, McDonald H, et al. (1995). «Genomic organization of the human alpha-adducin gene and its alternately spliced isoforms». Genomics. 25 (1): 93–9. PMID 7774961. doi:10.1016/0888-7543(95)80113-Z
Nasir J, Lin B, Bucan M, et al. (1994). «The murine homologues of the Huntington disease gene (Hdh) and the alpha-adducin gene (Add1) map to mouse chromosome 5 within a region of conserved synteny with human chromosome 4p16.3». Genomics. 22 (1): 198–201. PMID 7959767. doi:10.1006/geno.1994.1361
Kuhlman PA, Hughes CA, Bennett V, Fowler VM (1996). «A new function for adducin. Calcium/calmodulin-regulated capping of the barbed ends of actin filaments». J. Biol. Chem. 271 (14): 7986–91. PMID 8626479. doi:10.1074/jbc.271.14.7986
Li X, Bennett V (1996). «Identification of the spectrin subunit and domains required for formation of spectrin/adducin/actin complexes». J. Biol. Chem. 271 (26): 15695–702. PMID 8663089. doi:10.1074/jbc.271.26.15695
Matsuoka Y, Hughes CA, Bennett V (1996). «Adducin regulation. Definition of the calmodulin-binding domain and sites of phosphorylation by protein kinases A and C». J. Biol. Chem. 271 (41): 25157–66. PMID 8810272. doi:10.1074/jbc.271.41.25157
Hadano S, Ishida Y, Tomiyasu H, et al. (1997). «Transcript map of the human chromosome 4p16.3 consisting of 627 cDNA clones derived from 1 Mb of the Huntington's disease locus». DNA Res. 3 (4): 239–55. PMID 8946164. doi:10.1093/dnares/3.4.239
Cusi D, Barlassina C, Azzani T, et al. (1997). «Polymorphisms of alpha-adducin and salt sensitivity in patients with essential hypertension». Lancet. 349 (9062): 1353–7. PMID 9149697. doi:10.1016/S0140-6736(97)01029-5
Kamitani A, Wong ZY, Fraser R, et al. (1998). «Human alpha-adducin gene, blood pressure, and sodium metabolism». Hypertension. 32 (1): 138–43. PMID 9674650. doi:10.1161/01.HYP.32.1.138
Matsuoka Y, Li X, Bennett V (1998). «Adducin is an in vivo substrate for protein kinase C: phosphorylation in the MARCKS-related domain inhibits activity in promoting spectrin-actin complexes and occurs in many cells, including dendritic spines of neurons». J. Cell Biol. 142 (2): 485–97. PMC 2133059. PMID 9679146. doi:10.1083/jcb.142.2.485
Fukata Y, Oshiro N, Kinoshita N, et al. (1999). «Phosphorylation of adducin by Rho-kinase plays a crucial role in cell motility». J. Cell Biol. 145 (2): 347–61. PMC 2133101. PMID 10209029. doi:10.1083/jcb.145.2.347
Halushka MK, Fan JB, Bentley K, et al. (1999). «Patterns of single-nucleotide polymorphisms in candidate genes for blood-pressure homeostasis». Nat. Genet. 22 (3): 239–47. PMID 10391210. doi:10.1038/10297
Ferrandi M, Salardi S, Tripodi G, et al. (1999). «Evidence for an interaction between adducin and Na(+)-K(+)-ATPase: relation to genetic hypertension». Am. J. Physiol. 277 (4 Pt 2): H1338–49. PMID 10516168. doi:10.1152/ajpheart.1999.277.4.H1338

[1] «Human PubMed Reference:»

[pmid1840603-2] Joshi R, Gilligan DM, Otto E, McLaughlin T, Bennett V (novembro de 1991). «Primary structure and domain organization of human alpha and beta adducin». J Cell Biol. 115 (3): 665–75. PMC 2289184. PMID 1840603. doi:10.1083/jcb.115.3.665

[entrez-3] 1 2 «Entrez Gene: ADD1 adducin 1 (alpha)»

[4] Hirata R, Ohsumk Y, Nakano A, Kawasaki H, Suzuki K, Anraku Y (abril de 1990). «Molecular structure of a gene, VMA1, encoding the catalytic subunit of H(+)-translocating adenosine triphosphatase from vacuolar membranes of Saccharomyces cerevisiae». J. Biol. Chem. 265 (12): 6726–33. PMID 2139027

[5] Schlüter H, Apweiler R, Holzhütter HG, Jungblut PR (setembro de 2009). «Finding one's way in proteomics: a protein species nomenclature». Chemistry Central Journal. 3. 11 páginas. PMC 2758878. PMID 19740416. doi:10.1186/1752-153X-3-11

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