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ACTR2
Dostupne strukture
PDB	Pretraga ortologa: PDBe RCSB
Spisak PDB ID kodova
	2P9N, 1TYQ, 1U2V, 4JD2, 3DXK, 3UKU, 3UKR, 2P9P, 2P9U, 3ULE, 3RSE, 2P9S, 2P9I, 4XF2, 2P9L, 1K8K, 3DXM, 4XEI
Identifikatori
Aliasi	ACTR2
Vanjski ID-jevi	OMIM: 604221 MGI: 1913963 HomoloGene: 4181 GeneCards: ACTR2
Lokacija gena (čovjek)
Hrom.	Hromosom 2 (čovjek)
Kraj	65,271,253 bp
Lokacija gena (miš)
Hrom.	Hromosom 11 (miš)
Kraj	20,062,913 bp
Ontologija gena
Molekularna funkcija	• nucleotide binding; • actin filament binding; • structural constituent of cytoskeleton; • actin binding; • ATP binding; • cytoskeletal protein binding;
Ćelijska komponenta	• citoplazma; • citosol; • projekcija ćelije; • membrana; • focal adhesion; • arp2/3 protein complex; • cell cortex; • actin cytoskeleton; • actin cap; • Egzosom; • citoskelet; • extracellular region; • GO:0097483, GO:0097481 postsynaptic density; • lamellipodium; • azurophil granule lumen; • ficolin-1-rich granule lumen; • podosome core;
Biološki proces	• cytosolic transport; • Fc-gamma receptor signaling pathway involved in phagocytosis; • actin filament organization; • ephrin receptor signaling pathway; • meiotic chromosome movement towards spindle pole; • meiotic cytokinesis; • establishment or maintenance of cell polarity; • GO:0007126 Mejoza; • asymmetric cell division; • Arp2/3 complex-mediated actin nucleation; • spindle localization; • actin cytoskeleton organization; • associative learning; • response to immobilization stress; • cellular response to trichostatin A; • neutrophil degranulation; • response to ethanol; • cilium assembly; • positive regulation of dendritic spine morphogenesis; • membrane organization;
	Izvori:Amigo / QuickGO
Ortolozi
	10097
	66713
	ENSG00000138071
	ENSMUSG00000020152
	P61160
	P61161
	NM_005722; NM_001005386
	NM_146243; NM_001362899
	NP_001005386; NP_005713
	NP_666355; NP_001349828
	Wikipodaci
Pogledaj/uredi – čovjek	Pogledaj/uredi – miš

Aktinu-srodni protein 2 jest protein koji je kod ljudi kodiran genom ACTR2 sa hromosoma 3.^[5]

Aminokiselinska sekvenca

Dužina polipeptidnog lanca je 394 aminokiseline, а molekulska težina 44.761 Da.^[6]

C: Cistein

D: Asparaginska kiselina

E: Glutaminska kiselina

F: Fenilalanin

G: Glicin

H: Histidin

I: Izoleucin

K: Lizin

L: Leucin

M: Metionin

N: Asparagin

P: Prolin

Q: Glutamin

R: Arginin

S: Serin

T: Treonin

V: Valin

W: Triptofan

Y: Tirozin

10	20	30	40	50
MDSQGRKVVV	CDNGTGFVKC	GYAGSNFPEH	IFPALVGRPI	IRSTTKVGNI
EIKDLMVGDE	ASELRSMLEV	NYPMENGIVR	NWDDMKHLWD	YTFGPEKLNI
DTRNCKILLT	EPPMNPTKNR	EKIVEVMFET	YQFSGVYVAI	QAVLTLYAQG
LLTGVVVDSG	DGVTHICPVY	EGFSLPHLTR	RLDIAGRDIT	RYLIKLLLLR
GYAFNHSADF	ETVRMIKEKL	CYVGYNIEQE	QKLALETTVL	VESYTLPDGR
IIKVGGERFE	APEALFQPHL	INVEGVGVAE	LLFNTIQAAD	IDTRSEFYKH
IVLSGGSTMY	PGLPSRLERE	LKQLYLERVL	KGDVEKLSKF	KIRIEDPPRR
KHMVFLGGAV	LADIMKDKDN	FWMTRQEYQE	KGVRVLEKLG	VTVR

Funkcija

Specifična funkcija ACTR2 još nije utvrđena. Međutim, poznato je da je glavni sastojak ARP2/3- kompleksa. Ovaj kompleks nalazi se na površini ćelije i neophodan je za oblik ćelije i pokretljivost kroz lamelipodijski aktinski sklop i izbočenje. Za ovaj genro, pnađene su dvije varijante transkripta koje kodiraju različite izoforme.^[7]

Reference

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000138071 - Ensembl, maj 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000020152 - Ensembl, maj 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Welch MD, DePace AH, Verma S, Iwamatsu A, Mitchison TJ (Aug 1997). "The human Arp2/3 complex is composed of evolutionarily conserved subunits and is localized to cellular regions of dynamic actin filament assembly". J Cell Biol. 138 (2): 375–84. doi:10.1083/jcb.138.2.375. PMC 2138188. PMID 9230079.
^ "UniProt, P61160" (jezik: en.). Pristupljeno 9. 11. 2021.CS1 održavanje: nepoznati jezik (link)
^ "Entrez Gene: ACTR2 ARP2 actin-related protein 2 homolog (yeast)".

Dopunska literatura

Bearer EL, Prakash JM, Li Z (2002). "Actin dynamics in platelets". Int. Rev. Cytol. International Review of Cytology. 217: 137–82. doi:10.1016/S0074-7696(02)17014-8. ISBN 9780123646217. PMC 3376087. PMID 12019562.
Welch MD, Iwamatsu A, Mitchison TJ (1997). "Actin polymerization is induced by Arp2/3 protein complex at the surface of Listeria monocytogenes". Nature. 385 (6613): 265–9. Bibcode:1997Natur.385..265W. doi:10.1038/385265a0. PMID 9000076. S2CID 4358529.
Winter D, Podtelejnikov AV, Mann M, Li R (1997). "The complex containing actin-related proteins Arp2 and Arp3 is required for the motility and integrity of yeast actin patches". Curr. Biol. 7 (7): 519–29. doi:10.1016/S0960-9822(06)00223-5. PMID 9210376. S2CID 52837402.
Machesky LM, Reeves E, Wientjes F, et al. (1998). "Mammalian actin-related protein 2/3 complex localizes to regions of lamellipodial protrusion and is composed of evolutionarily conserved proteins". Biochem. J. 328. ( Pt 1): 105–12. doi:10.1042/bj3280105. PMC 1218893. PMID 9359840.
Machesky LM, Insall RH (1999). "Scar1 and the related Wiskott-Aldrich syndrome protein, WASP, regulate the actin cytoskeleton through the Arp2/3 complex". Curr. Biol. 8 (25): 1347–56. doi:10.1016/S0960-9822(98)00015-3. PMID 9889097. S2CID 16661755.
Suetsugu S, Miki H, Takenawa T (1999). "Identification of two human WAVE/SCAR homologues as general actin regulatory molecules which associate with the Arp2/3 complex". Biochem. Biophys. Res. Commun. 260 (1): 296–302. doi:10.1006/bbrc.1999.0894. PMID 10381382.
May RC, Hall ME, Higgs HN, et al. (1999). "The Arp2/3 complex is essential for the actin-based motility of Listeria monocytogenes". Curr. Biol. 9 (14): 759–62. doi:10.1016/S0960-9822(99)80337-6. PMID 10421578. S2CID 17030983.
Loisel TP, Boujemaa R, Pantaloni D, Carlier MF (1999). "Reconstitution of actin-based motility of Listeria and Shigella using pure proteins". Nature. 401 (6753): 613–6. Bibcode:1999Natur.401..613L. doi:10.1038/44183. PMID 10524632. S2CID 4313372.
Higgs HN, Blanchoin L, Pollard TD (1999). "Influence of the C terminus of Wiskott-Aldrich syndrome protein (WASp) and the Arp2/3 complex on actin polymerization". Biochemistry. 38 (46): 15212–22. doi:10.1021/bi991843. PMID 10563804.
Carlier MF, Nioche P, Broutin-L'Hermite I, et al. (2000). "GRB2 links signaling to actin assembly by enhancing interaction of neural Wiskott-Aldrich syndrome protein (N-WASp) with actin-related protein (ARP2/3) complex". J. Biol. Chem. 275 (29): 21946–52. doi:10.1074/jbc.M000687200. PMID 10781580.
Weed SA, Karginov AV, Schafer DA, et al. (2000). "Cortactin localization to sites of actin assembly in lamellipodia requires interactions with F-actin and the Arp2/3 complex". J. Cell Biol. 151 (1): 29–40. doi:10.1083/jcb.151.1.29. PMC 2189811. PMID 11018051.
Prehoda KE, Scott JA, Mullins RD, Lim WA (2000). "Integration of multiple signals through cooperative regulation of the N-WASP-Arp2/3 complex". Science. 290 (5492): 801–6. Bibcode:2000Sci...290..801P. doi:10.1126/science.290.5492.801. PMID 11052943.
Marchand JB, Kaiser DA, Pollard TD, Higgs HN (2001). "Interaction of WASP/Scar proteins with actin and vertebrate Arp2/3 complex". Nat. Cell Biol. 3 (1): 76–82. doi:10.1038/35050590. PMID 11146629. S2CID 30437883.
Zhao X, Yang Z, Qian M, Zhu X (2001). "Interactions among subunits of human Arp2/3 complex: p20-Arc as the hub". Biochem. Biophys. Res. Commun. 280 (2): 513–7. doi:10.1006/bbrc.2000.4151. PMID 11162547.
Flanagan LA, Chou J, Falet H, et al. (2001). "Filamin A, the Arp2/3 complex, and the morphology and function of cortical actin filaments in human melanoma cells". J. Cell Biol. 155 (4): 511–7. doi:10.1083/jcb.200105148. PMC 2198874. PMID 11706047.
Robinson RC, Turbedsky K, Kaiser DA, et al. (2001). "Crystal structure of Arp2/3 complex". Science. 294 (5547): 1679–84. Bibcode:2001Sci...294.1679R. doi:10.1126/science.1066333. PMID 11721045. S2CID 18088124.
Gournier H, Goley ED, Niederstrasser H, et al. (2002). "Reconstitution of human Arp2/3 complex reveals critical roles of individual subunits in complex structure and activity". Mol. Cell. 8 (5): 1041–52. doi:10.1016/S1097-2765(01)00393-8. PMID 11741539.
Li Z, Kim ES, Bearer EL (2002). "Arp2/3 complex is required for actin polymerization during platelet shape change". Blood. 99 (12): 4466–74. doi:10.1182/blood.V99.12.4466. PMC 3376088. PMID 12036877.

Vanjski linkovi

ACTR2 lokacija ljudskog genoma UCSC Genome Browser.

ACTR2 detalji ljudskog genoma u UCSC Genome Browser.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000138071 - Ensembl, maj 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000020152 - Ensembl, maj 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.

[pmid9230079-5] Welch MD, DePace AH, Verma S, Iwamatsu A, Mitchison TJ (Aug 1997). "The human Arp2/3 complex is composed of evolutionarily conserved subunits and is localized to cellular regions of dynamic actin filament assembly". J Cell Biol. 138 (2): 375–84. doi:10.1083/jcb.138.2.375. PMC 2138188. PMID 9230079.

[UniProt-6] "UniProt, P61160" (jezik: en.). Pristupljeno 9. 11. 2021.CS1 održavanje: nepoznati jezik (link)

[entrez-7] "Entrez Gene: ACTR2 ARP2 actin-related protein 2 homolog (yeast)".

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