ARP3_DICDI
ID ARP3_DICDI Reviewed; 418 AA.
AC P42528; Q54QJ1;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=Actin-related protein 3;
DE AltName: Full=Actin-like protein 3;
DE AltName: Full=Actin-related protein C;
GN Name=arpC; Synonyms=aclA, act; ORFNames=DDB_G0283755;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=AX3;
RX PubMed=7883039; DOI=10.1016/0014-5793(95)00111-l;
RA Murgia I., Maciver S.K., Morandini P.;
RT "An actin-related protein from Dictyostelium discoideum is developmentally
RT regulated and associated with mitochondria.";
RL FEBS Lett. 360:235-241(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP PROTEIN SEQUENCE OF 1-20; 199-209 AND 360-374, ACETYLATION AT MET-1, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=AX2;
RA Bienvenut W.V., Ura S., Insall R.H.;
RL Submitted (JUL-2009) to UniProtKB.
RN [4]
RP PROTEIN SEQUENCE OF 276-298, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=11425877; DOI=10.1083/jcb.153.7.1479;
RA Jung G., Remmert K., Wu X., Volosky J.M., Hammer J.A. III;
RT "The Dictyostelium CARMIL protein links capping protein and the Arp2/3
RT complex to type I myosins through their SH3 domains.";
RL J. Cell Biol. 153:1479-1497(2001).
RN [5]
RP IDENTIFICATION IN THE ARP2/3 COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=11807934; DOI=10.1002/cm.10005;
RA Insall R., Mueller-Taubenberger A., Machesky L., Koehler J., Simmeth E.,
RA Atkinson S.J., Weber I., Gerisch G.;
RT "Dynamics of the Dictyostelium Arp2/3 complex in endocytosis, cytokinesis,
RT and chemotaxis.";
RL Cell Motil. Cytoskeleton 50:115-128(2001).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=AX2;
RX PubMed=16926386; DOI=10.1074/mcp.m600113-mcp200;
RA Gotthardt D., Blancheteau V., Bosserhoff A., Ruppert T., Delorenzi M.,
RA Soldati T.;
RT "Proteomics fingerprinting of phagosome maturation and evidence for the
RT role of a Galpha during uptake.";
RL Mol. Cell. Proteomics 5:2228-2243(2006).
RN [7]
RP IDENTIFICATION IN THE ARP2/3 COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=17296313; DOI=10.1016/j.pep.2007.01.001;
RA Meima M.E., Weening K.E., Schaap P.;
RT "Vectors for expression of proteins with single or combinatorial
RT fluorescent protein and tandem affinity purification tags in
RT Dictyostelium.";
RL Protein Expr. Purif. 53:283-288(2007).
CC -!- FUNCTION: Functions as ATP-binding component of the Arp2/3 complex
CC which is involved in regulation of actin polymerization and together
CC with an activating nucleation-promoting factor (NPF) mediates the
CC formation of branched actin networks. Seems to contact the pointed end
CC of the daughter actin filament. The Arp2/3 complex is involved in
CC organizing the actin system in cell motility and chemotaxis, in
CC phagocytosis and macropinocytosis, at late steps of endosome
CC processing, and in mitosis. In concert with a group of other proteins,
CC the Arp2/3 complex plays a general role in the rapid activation and
CC adaptation of the actin system to its multiple functions.
CC -!- SUBUNIT: Component of the Arp2/3 complex composed of arpB/Arp2,
CC arpC/Arp3, arcA/p41-arc, arcB/p34-arc, arcC/p21-arc, arcD/p20-arc and
CC arcE/p16-arc. Interacts with carmil (via the region between the LRR
CC domain and COOH-terminal proline-rich domain); carmil is required for
CC Arp2/3-dependent actin nucleation. Arp2/3 complex, MyoB, MyoC, and the
CC alpha and beta subunits of capping protein all form a larger complex
CC with carmil. {ECO:0000269|PubMed:11425877, ECO:0000269|PubMed:11807934,
CC ECO:0000269|PubMed:17296313}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:11807934}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:11425877}. Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:11425877}. Cell projection, pseudopodium
CC {ECO:0000269|PubMed:11425877}.
CC -!- INDUCTION: By starvation.
CC -!- SIMILARITY: Belongs to the actin family. ARP3 subfamily. {ECO:0000305}.
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DR EMBL; Z46418; CAA86553.1; -; mRNA.
DR EMBL; AAFI02000057; EAL65492.1; -; Genomic_DNA.
DR PIR; S69002; S48844.
DR RefSeq; XP_638880.1; XM_633788.1.
DR AlphaFoldDB; P42528; -.
DR SMR; P42528; -.
DR STRING; 44689.DDB0219936; -.
DR PaxDb; P42528; -.
DR EnsemblProtists; EAL65492; EAL65492; DDB_G0283755.
DR GeneID; 8624278; -.
DR KEGG; ddi:DDB_G0283755; -.
DR dictyBase; DDB_G0283755; arpC.
DR eggNOG; KOG0678; Eukaryota.
DR HOGENOM; CLU_027965_3_0_1; -.
DR InParanoid; P42528; -.
DR OMA; TAEFKSY; -.
DR PhylomeDB; P42528; -.
DR Reactome; R-DDI-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-DDI-5663213; RHO GTPases Activate WASPs and WAVEs.
DR Reactome; R-DDI-8856828; Clathrin-mediated endocytosis.
DR PRO; PR:P42528; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:dictyBase.
DR GO; GO:0005885; C:Arp2/3 protein complex; IDA:dictyBase.
DR GO; GO:0031252; C:cell leading edge; IDA:dictyBase.
DR GO; GO:0060187; C:cell pole; IDA:dictyBase.
DR GO; GO:0042995; C:cell projection; IDA:dictyBase.
DR GO; GO:0005905; C:clathrin-coated pit; IDA:dictyBase.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IDA:dictyBase.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0030175; C:filopodium; IDA:dictyBase.
DR GO; GO:0030027; C:lamellipodium; IDA:dictyBase.
DR GO; GO:0061851; C:leading edge of lamellipodium; IDA:dictyBase.
DR GO; GO:0070685; C:macropinocytic cup; IDA:dictyBase.
DR GO; GO:0005739; C:mitochondrion; IDA:dictyBase.
DR GO; GO:0001891; C:phagocytic cup; IDA:dictyBase.
DR GO; GO:0097203; C:phagocytic cup lip; IDA:dictyBase.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:dictyBase.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IDA:dictyBase.
DR GO; GO:0032195; C:post-lysosomal vacuole; IDA:dictyBase.
DR GO; GO:0031143; C:pseudopodium; IC:dictyBase.
DR GO; GO:0051015; F:actin filament binding; TAS:dictyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0030041; P:actin filament polymerization; TAS:dictyBase.
DR GO; GO:0045010; P:actin nucleation; TAS:dictyBase.
DR GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; IBA:GO_Central.
DR GO; GO:0006887; P:exocytosis; IEP:dictyBase.
DR GO; GO:0006909; P:phagocytosis; IEP:dictyBase.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IGI:dictyBase.
DR GO; GO:0009617; P:response to bacterium; HEP:dictyBase.
DR GO; GO:0046689; P:response to mercury ion; IDA:dictyBase.
DR InterPro; IPR004000; Actin.
DR InterPro; IPR020902; Actin/actin-like_CS.
DR InterPro; IPR015623; Arp3.
DR InterPro; IPR043129; ATPase_NBD.
DR PANTHER; PTHR11937; PTHR11937; 1.
DR PANTHER; PTHR11937:SF175; PTHR11937:SF175; 1.
DR Pfam; PF00022; Actin; 1.
DR SMART; SM00268; ACTIN; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; ATP-binding; Cell projection; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Nucleotide-binding;
KW Reference proteome; Stress response.
FT CHAIN 1..418
FT /note="Actin-related protein 3"
FT /id="PRO_0000089086"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|Ref.3"
SQ SEQUENCE 418 AA; 46698 MW; FFBC49A46CD05806 CRC64;
MNPASGLPAV VIDNGTGYTK MGYAGNNDPS FIIPTTIATQ SSKGKQTAAS QKKGVEDLDF
FIGDEAIANS KTYDMTNPVK HGQIENWTHM EQYWEHCVFK YLRCEPEDHY FLLTEPPLNA
PENREFTAEI MFETFNVPGL YIAVQAVLAL AASWTSKNAE KTLTGTVIDS GDGVTHVIPI
SEGYVIGSSI KHIPIAGRDI SSYVQQIMRE REPNIPPAES LEIAKRVKEQ YSYVCPDIVK
EFGKYDSEPD KWIKTINAQD SVTKKPFSYD VGYERFLGPE LFFNPEIASS DYLTPLPKVV
DDTIQSCPID CRRGLYKNIV LSGGSTMFKD FGKRLQRDVK RSVDYRIKRS EELSGGKIKA
VPLAVNVISH NMQRYAVWFG GSMLASTPEF YNVCHTKAQY DEIGPSICRF NTVIGGIN
