DICDI:ACT1

Species (Taxon ID)	Dictyostelium discoideum (Slime mold). (44689)
Gene Name(s)	act21 (synonyms: actM6)
Protein Name(s)	Major actin Actin A1 Actin A12 Actin A8 Actin III Actin M6 Actin-1 Actin-11 Actin-12 Actin-13 Actin-14 Actin-15 Actin-16 Actin-19 Actin-2 Actin-2-sub 1 Actin-20 Actin-21 Actin-3a Actin-4 Actin-5 Actin-6 Actin-7 Actin-8 Actin-9 Actin-IEL1
External Links
UniProt	P07830
EMBL	X03281 X03282 M14146 AAFI02000005 AAFI02000008 AAFI02000008 AAFI02000012 AAFI02000012 AAFI02000012 AAFI02000012 AAFI02000012 AAFI02000012 AAFI02000012 AAFI02000012 AAFI02000012 AAFI02000037 AAFI02000126 AAFI02000129 AAFI02000142 AAFI02000148 U25660 V00183 V00186 V00188 J01267 J01273 J01274 J01276 J01279 J01265 J01270 J01272 K02954 K02958 K02960 J01278
PIR	A25084 A39239 A93223 B23412
RefSeq	XP_636088.1 XP_636169.1 XP_636425.1 XP_636507.1 XP_641146.1 XP_643986.1 XP_643988.1 XP_643989.1 XP_643990.1 XP_644132.1 XP_644146.1 XP_644157.1 XP_644244.1 XP_644246.1 XP_645099.1 XP_645262.1 XP_646688.1
PDB	1C0F 1C0G 1DEJ 1NLV 1NM1 1NMD 3A5L 3A5M 3A5N 3A5O 3CHW 3CI5 3CIP
PDBsum	1C0F 1C0G 1DEJ 1NLV 1NM1 1NMD 3A5L 3A5M 3A5N 3A5O 3CHW 3CI5 3CIP
ProteinModelPortal	P07830
DIP	DIP-40989N
MINT	MINT-121645
SWISS-2DPAGE	P07830
PRIDE	P07830
EnsemblProtists	DDB0185015 DDB0185124 DDB0185126 DDB0185127 DDB0216213 DDB0216214 DDB0220444 DDB0220445 DDB0220446 DDB0220447 DDB0220448 DDB0220449 DDB0220450 DDB0220451 DDB0220454 DDB0220455 DDB0220456
GeneID	8617663 8618428 8618493 8619412 8619414 8619415 8619416 8619562 8619575 8619586 8619672 8619674 8622703 8626890 8626916 8627198 8627300
KEGG	ddi:DDB_G0269234 ddi:DDB_G0272248 ddi:DDB_G0272520 ddi:DDB_G0274129 ddi:DDB_G0274133 ddi:DDB_G0274135 ddi:DDB_G0274137 ddi:DDB_G0274285 ddi:DDB_G0274561 ddi:DDB_G0274599 ddi:DDB_G0274601 ddi:DDB_G0274727 ddi:DDB_G0280545 ddi:DDB_G0288879 ddi:DDB_G0289005 ddi:DDB_G0289553 ddi:DDB_G0289663
dictyBase	DDB_G0289553 DDB_G0288879 DDB_G0274129 DDB_G0274599 DDB_G0274137 DDB_G0272520 DDB_G0272248 DDB_G0274727 DDB_G0274133 DDB_G0274285 DDB_G0274561 DDB_G0289005 DDB_G0289663 DDB_G0274135 DDB_G0280545 DDB_G0269234 DDB_G0274601
InParanoid	P07830
KO	K10355
OMA	TANASRW
PhylomeDB	P07830
EvolutionaryTrace	P07830
Proteomes	UP000002195 UP000002195 UP000002195 UP000002195 UP000002195
GO	GO:0015629 GO:0005884 GO:0031252 GO:0060187 GO:0032009 GO:0001891 GO:0045335 GO:0032010 GO:0031143 GO:0005524 GO:0017022 GO:0005200 GO:0000902 GO:0006928 GO:0006935 GO:0006897 GO:0006972 GO:0000281 GO:0006909 GO:0042331 GO:0016192
InterPro	IPR004000 IPR020902 IPR004001
PANTHER	PTHR11937
Pfam	PF00022
PRINTS	PR00190
SMART	SM00268
PROSITE	PS00406 PS00432 PS01132

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
part_of	GO:0030139	endocytic vesicle	PMID:7593293^[1]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0031252	cell leading edge	PMID:29118357^[2]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(GO:0043327)	Seeded From UniProt	complete
part_of	GO:0005938	cell cortex	PMID:28409084^[3]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(GO:0016477)	Seeded From UniProt	complete
part_of	GO:0030027	lamellipodium	PMID:28409084^[3]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(GO:0016477)	Seeded From UniProt	complete
part_of	GO:0061836	intranuclear rod	PMID:28074884^[4]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0051591	response to cAMP	PMID:2543508^[5]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0030864	cortical actin cytoskeleton	PMID:9484954^[6]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005811	lipid droplet	PMID:24036346^[7]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0060187	cell pole	PMID:20530573^[8]	ECO:0000314	direct assay evidence used in manual assertion		C	exists_during:(GO:0000910)	Seeded From UniProt	complete
part_of	GO:0045335	phagocytic vesicle	PMID:22008230^[9]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
colocalizes_with	GO:0044291	cell-cell contact zone	PMID:11278598^[10]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0032010	phagolysosome	PMID:20052281^[11]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0032009	early phagosome	PMID:20052281^[11]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0017022	myosin binding	PMID:1057168^[12]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0015629	actin cytoskeleton	PMID:1057168^[12]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0006972	hyperosmotic response	PMID:17517120^[13]	ECO:0000270	expression pattern evidence used in manual assertion		P		Seeded From UniProt	complete
acts_upstream_of_or_within	GO:0006909	phagocytosis	PMID:21190565^[14]	ECO:0000270	expression pattern evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005884	actin filament	PMID:1057168^[12]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0005200	structural constituent of cytoskeleton	PMID:1057168^[12]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0001891	phagocytic cup	PMID:21190565^[14]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0001891	phagocytic cup	PMID:20052281^[11]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0007010	cytoskeleton organization	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0005200	P		Seeded From UniProt	complete
involved_in	GO:0042331	phototaxis	PMID:15726806^[15]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0031143	pseudopodium	PMID:11257435^[16]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0016192	vesicle-mediated transport	PMID:15726806^[15]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006935	chemotaxis	PMID:15726806^[15]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006897	endocytosis	PMID:15726806^[15]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0000902	cell morphogenesis	PMID:15726806^[15]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0000281	mitotic cytokinesis	PMID:15726806^[15]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0067	F		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963	C		Seeded From UniProt	complete
part_of	GO:0005856	cytoskeleton	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0206 UniProtKB-SubCell:SL-0090	C		Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F		Seeded From UniProt	complete
edit table

Notes

References

See Help:References for how to manage references in GONUTS.

↑ Adessi, C et al. (1995) Identification of major proteins associated with Dictyostelium discoideum endocytic vesicles. J. Cell. Sci. 108 ( Pt 10) 3331-7 PubMed GONUTS page
↑ Hotz, M & Nelson, WJ (2017) Pumilio-dependent localization of mRNAs at the cell front coordinates multiple pathways required for chemotaxis. Nat Commun 8 1366 PubMed GONUTS page
↑ ^3.0 ^3.1 Shibata, K et al. (2016) Actin binding domain of filamin distinguishes posterior from anterior actin filaments in migrating cells. Biophys Physicobiol 13 321-331 PubMed GONUTS page
↑ Ishikawa-Ankerhold, HC et al. (2017) Actin-Interacting Protein 1 Contributes to Intranuclear Rod Assembly in Dictyostelium discoideum. Sci Rep 7 40310 PubMed GONUTS page
↑ Dharmawardhane, S et al. (1989) Changes in the association of actin-binding proteins with the actin cytoskeleton during chemotactic stimulation of Dictyostelium discoideum. Cell Motil. Cytoskeleton 13 57-63 PubMed GONUTS page
↑ Lee, E et al. (1998) Formation of F-actin aggregates in cells treated with actin stabilizing drugs. Cell Motil. Cytoskeleton 39 122-33 PubMed GONUTS page
↑ Du, X et al. (2013) Dictyostelium lipid droplets host novel proteins. Eukaryotic Cell 12 1517-29 PubMed GONUTS page
↑ King, JS et al. (2010) SCAR/WAVE is activated at mitosis and drives myosin-independent cytokinesis. J. Cell. Sci. 123 2246-55 PubMed GONUTS page
↑ Gopaldass, N et al. (2012) Dynamin A, Myosin IB and Abp1 couple phagosome maturation to F-actin binding. Traffic 13 120-30 PubMed GONUTS page
↑ Harris, TJ et al. (2001) Involvement of a triton-insoluble floating fraction in Dictyostelium cell-cell adhesion. J. Biol. Chem. 276 18640-8 PubMed GONUTS page
↑ ^11.0 ^11.1 ^11.2 Clarke, M et al. (2010) Retrieval of the vacuolar H-ATPase from phagosomes revealed by live cell imaging. PLoS ONE 5 e8585 PubMed GONUTS page
↑ ^12.0 ^12.1 ^12.2 ^12.3 Clarke, M et al. (1975) Visualization of actin fibers associated with the cell membrane in amoebae of Dictyostelium discoideum. Proc. Natl. Acad. Sci. U.S.A. 72 1758-62 PubMed GONUTS page
↑ Na, J et al. (2007) STATc is a key regulator of the transcriptional response to hyperosmotic shock. BMC Genomics 8 123 PubMed GONUTS page
↑ ^14.0 ^14.1 Clarke, M et al. (2010) Curvature recognition and force generation in phagocytosis. BMC Biol. 8 154 PubMed GONUTS page
↑ ^15.0 ^15.1 ^15.2 ^15.3 ^15.4 ^15.5 Cvrcková, F et al. (2004) Evolutionarily conserved modules in actin nucleation: lessons from Dictyostelium discoideum and plants. Review article. Protoplasma 224 15-31 PubMed GONUTS page
↑ Lee, E et al. (2001) The regulation of actin polymerization and cross-linking in Dictyostelium. Biochim. Biophys. Acta 1525 217-27 PubMed GONUTS page

[PMID:7593293-1] Adessi, C et al. (1995) Identification of major proteins associated with Dictyostelium discoideum endocytic vesicles. J. Cell. Sci. 108 ( Pt 10) 3331-7 PubMed GONUTS page

[PMID:29118357-2] Hotz, M & Nelson, WJ (2017) Pumilio-dependent localization of mRNAs at the cell front coordinates multiple pathways required for chemotaxis. Nat Commun 8 1366 PubMed GONUTS page

[PMID:28409084-3] 3.0 ^3.1 Shibata, K et al. (2016) Actin binding domain of filamin distinguishes posterior from anterior actin filaments in migrating cells. Biophys Physicobiol 13 321-331 PubMed GONUTS page

[PMID:28074884-4] Ishikawa-Ankerhold, HC et al. (2017) Actin-Interacting Protein 1 Contributes to Intranuclear Rod Assembly in Dictyostelium discoideum. Sci Rep 7 40310 PubMed GONUTS page

[PMID:2543508-5] Dharmawardhane, S et al. (1989) Changes in the association of actin-binding proteins with the actin cytoskeleton during chemotactic stimulation of Dictyostelium discoideum. Cell Motil. Cytoskeleton 13 57-63 PubMed GONUTS page

[PMID:9484954-6] Lee, E et al. (1998) Formation of F-actin aggregates in cells treated with actin stabilizing drugs. Cell Motil. Cytoskeleton 39 122-33 PubMed GONUTS page

[PMID:24036346-7] Du, X et al. (2013) Dictyostelium lipid droplets host novel proteins. Eukaryotic Cell 12 1517-29 PubMed GONUTS page

[PMID:20530573-8] King, JS et al. (2010) SCAR/WAVE is activated at mitosis and drives myosin-independent cytokinesis. J. Cell. Sci. 123 2246-55 PubMed GONUTS page

[PMID:22008230-9] Gopaldass, N et al. (2012) Dynamin A, Myosin IB and Abp1 couple phagosome maturation to F-actin binding. Traffic 13 120-30 PubMed GONUTS page

[PMID:11278598-10] Harris, TJ et al. (2001) Involvement of a triton-insoluble floating fraction in Dictyostelium cell-cell adhesion. J. Biol. Chem. 276 18640-8 PubMed GONUTS page

[PMID:20052281-11] 11.0 ^11.1 ^11.2 Clarke, M et al. (2010) Retrieval of the vacuolar H-ATPase from phagosomes revealed by live cell imaging. PLoS ONE 5 e8585 PubMed GONUTS page

[PMID:1057168-12] 12.0 ^12.1 ^12.2 ^12.3 Clarke, M et al. (1975) Visualization of actin fibers associated with the cell membrane in amoebae of Dictyostelium discoideum. Proc. Natl. Acad. Sci. U.S.A. 72 1758-62 PubMed GONUTS page

[PMID:17517120-13] Na, J et al. (2007) STATc is a key regulator of the transcriptional response to hyperosmotic shock. BMC Genomics 8 123 PubMed GONUTS page

[PMID:21190565-14] 14.0 ^14.1 Clarke, M et al. (2010) Curvature recognition and force generation in phagocytosis. BMC Biol. 8 154 PubMed GONUTS page

[PMID:15726806-15] 15.0 ^15.1 ^15.2 ^15.3 ^15.4 ^15.5 Cvrcková, F et al. (2004) Evolutionarily conserved modules in actin nucleation: lessons from Dictyostelium discoideum and plants. Review article. Protoplasma 224 15-31 PubMed GONUTS page

[PMID:11257435-16] Lee, E et al. (2001) The regulation of actin polymerization and cross-linking in Dictyostelium. Biochim. Biophys. Acta 1525 217-27 PubMed GONUTS page

[1]

[2]

[3]

[4]

[5]

[6]

[7]

[8]

[9]

[10]

[11]

[12]

[13]

[14]

[15]

[16]

DICDI:ACT1

Contents

Annotations

Notes

References

a

c

d

e

h

i

l

m

n

p

r

s

v

Navigation menu

Personal tools

Namespaces

Variants

Views

More

Search

Navigation

Cacao

Links

Tools