SCAR_DICDI
ID SCAR_DICDI Reviewed; 443 AA.
AC Q54NF8; Q9XYA8;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Protein SCAR;
DE AltName: Full=Suppressor of cAMP receptor;
GN Name=scrA; ORFNames=DDB_G0285253;
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], FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=9732292; DOI=10.1083/jcb.142.5.1325;
RA Bear J.E., Rawls J.F., Saxe C.L. III;
RT "SCAR, a WASP-related protein, isolated as a suppressor of receptor defects
RT in late Dictyostelium development.";
RL J. Cell Biol. 142:1325-1335(1998).
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 FUNCTION.
RX PubMed=11683394; DOI=10.1242/jcs.114.14.2673;
RA Seastone D.J., Harris E., Temesvari L.A., Bear J.E., Saxe C.L.,
RA Cardelli J.;
RT "The WASp-like protein scar regulates macropinocytosis, phagocytosis and
RT endosomal membrane flow in Dictyostelium.";
RL J. Cell Sci. 114:2673-2683(2001).
RN [4]
RP FUNCTION.
RX PubMed=12956949; DOI=10.1016/s0960-9822(03)00580-3;
RA Blagg S.L., Stewart M., Sambles C., Insall R.H.;
RT "PIR121 regulates pseudopod dynamics and SCAR activity in Dictyostelium.";
RL Curr. Biol. 13:1480-1487(2003).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=16822579; DOI=10.1016/j.ejcb.2006.05.014;
RA Pollitt A.Y., Blagg S.L., Ibarra N., Insall R.H.;
RT "Cell motility and SCAR localisation in axenically growing Dictyostelium
RT cells.";
RL Eur. J. Cell Biol. 85:1091-1098(2006).
RN [6]
RP IDENTIFICATION IN THE WAVE COMPLEX, INTERACTION WITH BRICK1 AND ABIA, AND
RP FUNCTION.
RX PubMed=17314411; DOI=10.1091/mbc.e06-06-0518;
RA Caracino D., Jones C., Compton M., Saxe C.L. III;
RT "The N-terminus of Dictyostelium Scar interacts with Abi and HSPC300 and is
RT essential for proper regulation and function.";
RL Mol. Biol. Cell 18:1609-1620(2007).
CC -!- FUNCTION: Involved in regulation of actin and microtubule organization.
CC Regulates phagocytosis and macropinocytosis.
CC {ECO:0000269|PubMed:11683394, ECO:0000269|PubMed:12956949,
CC ECO:0000269|PubMed:17314411, ECO:0000269|PubMed:9732292}.
CC -!- SUBUNIT: Part of a Scar/WAVE complex containing brk1, scrA, abiA, pirA
CC and napA. Interacts with brk1 and abiA. {ECO:0000269|PubMed:17314411}.
CC -!- INTERACTION:
CC Q54NF8; Q55FT9: abiA; NbExp=3; IntAct=EBI-1808146, EBI-1808197;
CC Q54NF8; Q54X65: brk1; NbExp=3; IntAct=EBI-1808146, EBI-1808171;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell
CC projection, pseudopodium tip {ECO:0000269|PubMed:16822579}. Cell
CC projection, filopodium tip {ECO:0000269|PubMed:16822579}. Note=Located
CC at the tips of filopodia and at the tips of pseudopodia. In strains
CC IR1, IR3, NC4A2, AX2, always enriched at the ends of actin protrusions.
CC In strains AX3, AX4, JH8, JH10, DH1, does not seem to associate with
CC actin structures in vegetative cells, but similar to other strains in
CC developed cells.
CC -!- DEVELOPMENTAL STAGE: Expressed at low levels during vegetative growth,
CC and accumulates dramatically by 4 hours of development. Expression
CC levels remain high through 12 hours, and drop off at 16 hours.
CC {ECO:0000269|PubMed:9732292}.
CC -!- DISRUPTION PHENOTYPE: Amoeba grow as very small cells in suspension
CC culture. They have reduced levels of F-actin staining during vegetative
CC growth, and abnormal cell morphology and actin distribution during
CC chemotaxis. {ECO:0000269|PubMed:9732292}.
CC -!- SIMILARITY: Belongs to the SCAR/WAVE family. {ECO:0000305}.
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DR EMBL; AF079805; AAD29083.1; -; mRNA.
DR EMBL; AAFI02000077; EAL64790.1; -; Genomic_DNA.
DR RefSeq; XP_638311.1; XM_633219.1.
DR AlphaFoldDB; Q54NF8; -.
DR SMR; Q54NF8; -.
DR IntAct; Q54NF8; 3.
DR STRING; 44689.DDB0191148; -.
DR PaxDb; Q54NF8; -.
DR PRIDE; Q54NF8; -.
DR EnsemblProtists; EAL64790; EAL64790; DDB_G0285253.
DR GeneID; 8625028; -.
DR KEGG; ddi:DDB_G0285253; -.
DR dictyBase; DDB_G0285253; scrA.
DR eggNOG; KOG1830; Eukaryota.
DR HOGENOM; CLU_036022_1_0_1; -.
DR InParanoid; Q54NF8; -.
DR OMA; QSVHHGA; -.
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-9013149; RAC1 GTPase cycle.
DR Reactome; R-DDI-9013404; RAC2 GTPase cycle.
DR Reactome; R-DDI-9013423; RAC3 GTPase cycle.
DR PRO; PR:Q54NF8; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0015629; C:actin cytoskeleton; TAS:dictyBase.
DR GO; GO:0005938; C:cell cortex; IDA:dictyBase.
DR GO; GO:0031252; C:cell leading edge; IDA:dictyBase.
DR GO; GO:0060187; C:cell pole; IDA:dictyBase.
DR GO; GO:0005911; C:cell-cell junction; IC:dictyBase.
DR GO; GO:0005829; C:cytosol; TAS:dictyBase.
DR GO; GO:0032433; C:filopodium tip; IC:dictyBase.
DR GO; GO:0031143; C:pseudopodium; IDA:dictyBase.
DR GO; GO:0001726; C:ruffle; IDA:dictyBase.
DR GO; GO:0031209; C:SCAR complex; IDA:dictyBase.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0071933; F:Arp2/3 complex binding; IBA:GO_Central.
DR GO; GO:0034237; F:protein kinase A regulatory subunit binding; IBA:GO_Central.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0090630; P:activation of GTPase activity; IMP:dictyBase.
DR GO; GO:0032060; P:bleb assembly; IMP:dictyBase.
DR GO; GO:0031589; P:cell-substrate adhesion; IMP:dictyBase.
DR GO; GO:0043327; P:chemotaxis to cAMP; IMP:dictyBase.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IMP:dictyBase.
DR GO; GO:0006887; P:exocytosis; IMP:dictyBase.
DR GO; GO:1902774; P:late endosome to lysosome transport; IMP:dictyBase.
DR GO; GO:0044351; P:macropinocytosis; IMP:dictyBase.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:dictyBase.
DR GO; GO:0007052; P:mitotic spindle organization; IMP:dictyBase.
DR GO; GO:0006909; P:phagocytosis; IMP:dictyBase.
DR GO; GO:0006907; P:pinocytosis; TAS:dictyBase.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IMP:dictyBase.
DR GO; GO:2000601; P:positive regulation of Arp2/3 complex-mediated actin nucleation; IBA:GO_Central.
DR GO; GO:1903669; P:positive regulation of chemorepellent activity; IMP:dictyBase.
DR GO; GO:0031269; P:pseudopodium assembly; IMP:dictyBase.
DR GO; GO:0008064; P:regulation of actin polymerization or depolymerization; IMP:dictyBase.
DR GO; GO:0031288; P:sorocarp morphogenesis; IMP:dictyBase.
DR InterPro; IPR028288; SCAR/WAVE_fam.
DR InterPro; IPR003124; WH2_dom.
DR PANTHER; PTHR12902; PTHR12902; 2.
DR PROSITE; PS51082; WH2; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Cell projection; Coiled coil; Cytoplasm; Cytoskeleton;
KW Phagocytosis; Reference proteome.
FT CHAIN 1..443
FT /note="Protein SCAR"
FT /id="PRO_0000331405"
FT DOMAIN 382..399
FT /note="WH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 1..96
FT /note="Interaction with brk1 and abiA"
FT REGION 176..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 166..201
FT /evidence="ECO:0000255"
FT COMPBIAS 220..253
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..288
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..325
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..367
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 344
FT /note="A -> G (in Ref. 1; AAD29083)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 443 AA; 48403 MW; 2340250F86A1AEA9 CRC64;
MVLITRYLPS VTDNNQPALE GQSKDQIVDT VITSTTVGII NQLTMLVAHS NSIFTALAND
ANLVTQRIEK LGSRIRPLIQ SIPSIEDYHR NTSIDTMNSK PRAEFHADNS ERNQHFTHAS
IPASINTVYE KCKPPPNLQL LDPYMDDGQK SLKLYTNPDF FMDEWVAEQQ KLHEEARQRK
RERREARLKK KGEKNEVEVK KVKSVTKVRY DPVTGEKITI NIESPHTSSP QIQHQSNNTA
TPQHTTQHFG TNQYQAPPPP PLSQSSPSQQ HSPINSYTPP PPPLNTSTPS PSSSFQGRPP
STGFNTPPPP MSNNNNMPPP PPMQQNGGAA NNRLSVHNSA PIVAAPAPPP PPPPPSAPAP
PPPPMAKAGG GASDIKPKAS GARSDLLSSI MQGMALKPAE ERKVAEAPKK EEALNVADIL
ARRIAWAGDS DSSEDESDDS DWD
