ARPC3

Podjedinica ARPC3 (21 kDa) kompleksa ARP2/3
Podjedinica ARPC3 (21 kDa) kompleksa ARP2/3
	Kristalna struktura kompleksa arp2/3 sa vezanim adp i kalcijem
Identifikatori
Simbol	P21-Arc

ARPC3
Dostupne strukture
PDB	Pretraga ortologa: PDBe RCSB
Spisak PDB ID kodova
	2P9N, 1TYQ, 1U2V, 4JD2, 3DXK, 3UKU, 3UKR, 2P9P, 2P9K, 2P9U, 3ULE, 3RSE, 2P9S, 2P9I, 4XF2, 2P9L, 1K8K, 3DXM, 4XEI
Identifikatori
Aliasi	ARPC3
Vanjski ID-jevi	OMIM: 604225 MGI: 1928375 HomoloGene: 4178 GeneCards: ARPC3
Lokacija gena (čovjek)
Hrom.	Hromosom 12 (čovjek)
Kraj	110,450,422 bp
Lokacija gena (miš)
Hrom.	Hromosom 5 (miš)
Kraj	122,552,247 bp
Obrazac RNK ekspresije
	Više referentnih podataka o ekspresiji
Ontologija gena
Molekularna funkcija	• actin filament binding; • structural constituent of cytoskeleton; • GO:0001948, GO:0016582 vezivanje za proteine; • actin binding;
Ćelijska komponenta	• citoplazma; • citosol; • projekcija ćelije; • membrana; • focal adhesion; • arp2/3 protein complex; • actin cytoskeleton; • Egzosom; • citoskelet; • lamellipodium; • cell leading edge; • filamentous actin; • growth cone leading edge; • jedro; • site of double-strand break;
Biološki proces	• Fc-gamma receptor signaling pathway involved in phagocytosis; • ephrin receptor signaling pathway; • regulation of actin filament polymerization; • Arp2/3 complex-mediated actin nucleation; • cellular response to nerve growth factor stimulus; • membrane organization; • actin polymerization-dependent cell motility;
	Izvori:Amigo / QuickGO
Ortolozi
	10094
	56378
	ENSG00000111229
	ENSMUSG00000029465
	O15145
	Q9JM76
	NM_001287222; NM_001278556
	NM_019824
	NP_001265485; NP_001274151
	NP_062798
	Wikipodaci
Pogledaj/uredi – čovjek	Pogledaj/uredi – miš

Podjedinica 3 aktinu-srodnog dvotrećinskog proteinskog kompleksa je protein koji je kod ljudi kodiran genom ARPC3.^[5]^[6]^[7]

Ovaj gen kodira jednu od sedam podjedinica Arp2/3 proteinskog kompleksa. Proteinski kompleks Arp2/3 uključen je u kontrolu polimerizacije aktina i evolucijski je konzerviran. Tačna uloga podjedinice p21 proteina kodiranog ovim genom, tek treba biti utvrđena.^[7]

Aminokiselinska sekvenca

Dužina polipeptidnog lanca je 178 aminokiselina, a molekulska težina 20.547 Da.^[8].

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
MPAYHSSLMD	PDTKLIGNMA	LLPIRSQFKG	PAPRETKDTD	IVDEAIYYFK
ANVFFKNYEI	KNEADRTLIY	ITLYISECLK	KLQKCNSKSQ	GEKEMYTLGI
TNFPIPGEPG	FPLNAIYAKP	ANKQEDEVMR	AYLQQLRQET	GLRLCEKVFD
PQNDKPSKWW	TCFVKRQFMN	KSLSGPGQ

Reference

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000111229 - Ensembl, maj 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000029465 - 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.
^ Machesky LM, Reeves E, Wientjes F, Mattheyse FJ, Grogan A, Totty NF, Burlingame AL, Hsuan JJ, Segal AW (Jan 1998). "Mammalian actin-related protein 2/3 complex localizes to regions of lamellipodial protrusion and is composed of evolutionarily conserved proteins". Biochem J. 328 (1): 105–12. doi:10.1042/bj3280105. PMC 1218893. PMID 9359840.
^ ^a ^b "Entrez Gene: ARPC3 actin related protein 2/3 complex, subunit 3, 21kDa".
^ "UniProt, O15145". Pristupljeno 6. 8. 2021.

Dopunska literatura

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. doi:10.1038/385265a0. PMID 9000076. S2CID 4358529.
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.
Robinson RC, Turbedsky K, Kaiser DA, et al. (2001). "Crystal structure of Arp2/3 complex". Science. 294 (5547): 1679–84. 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.
Andersen JS, Lyon CE, Fox AH, et al. (2002). "Directed proteomic analysis of the human nucleolus". Curr. Biol. 12 (1): 1–11. doi:10.1016/S0960-9822(01)00650-9. PMID 11790298. S2CID 14132033.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Gevaert K, Goethals M, Martens L, et al. (2004). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nat. Biotechnol. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801. S2CID 23783563.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Andersen JS, Lam YW, Leung AK, et al. (2005). "Nucleolar proteome dynamics". Nature. 433 (7021): 77–83. doi:10.1038/nature03207. PMID 15635413. S2CID 4344740.
Dubois T, Paléotti O, Mironov AA, et al. (2005). "Golgi-localized GAP for Cdc42 functions downstream of ARF1 to control Arp2/3 complex and F-actin dynamics". Nat. Cell Biol. 7 (4): 353–64. doi:10.1038/ncb1244. PMID 15793564. S2CID 37000096.
Stelzl U, Worm U, Lalowski M, et al. (2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. hdl:11858/00-001M-0000-0010-8592-0. PMID 16169070. S2CID 8235923.
Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.

Vanjski linkovi

ARPC3 lokacija ljudskog genoma UCSC Genome Browser.

ARPC3 detalji ljudskog genoma u UCSC Genome Browser.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000111229 - Ensembl, maj 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000029465 - 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.

[pmid9359840-6] Machesky LM, Reeves E, Wientjes F, Mattheyse FJ, Grogan A, Totty NF, Burlingame AL, Hsuan JJ, Segal AW (Jan 1998). "Mammalian actin-related protein 2/3 complex localizes to regions of lamellipodial protrusion and is composed of evolutionarily conserved proteins". Biochem J. 328 (1): 105–12. doi:10.1042/bj3280105. PMC 1218893. PMID 9359840.

[entrez-7] "Entrez Gene: ARPC3 actin related protein 2/3 complex, subunit 3, 21kDa".

[UniProt-8] "UniProt, O15145". Pristupljeno 6. 8. 2021.

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