SCAR3_ARATH
ID SCAR3_ARATH Reviewed; 1020 AA.
AC Q9LP46;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Protein SCAR3;
DE Short=AtSCAR3;
DE AltName: Full=Protein WAVE2;
GN Name=SCAR3; OrderedLocusNames=At1g29170; ORFNames=F28N24.14;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INTERACTION WITH BRK1.
RX PubMed=15534215; DOI=10.1073/pnas.0407392101;
RA Frank M., Egile C., Dyachok J., Djakovic S., Nolasco M., Li R., Smith L.G.;
RT "Activation of Arp2/3 complex-dependent actin polymerization by plant
RT proteins distantly related to Scar/WAVE.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:16379-16384(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP FUNCTION, AND IDENTIFICATION.
RX PubMed=15316111; DOI=10.1105/tpc.104.023739;
RA Brembu T., Winge P., Seem M., Bones A.M.;
RT "NAPP and PIRP encode subunits of a putative wave regulatory protein
RT complex involved in plant cell morphogenesis.";
RL Plant Cell 16:2335-2349(2004).
RN [5]
RP INTERACTION WITH SPK1; ABI1; ABI2; ABI3 AND ABI4.
RX PubMed=17267444; DOI=10.1242/dev.02792;
RA Uhrig J.F., Mutondo M., Zimmermann I., Deeks M.J., Machesky L.M.,
RA Thomas P., Uhrig S., Rambke C., Hussey P.J., Huelskamp M.;
RT "The role of Arabidopsis SCAR genes in ARP2-ARP3-dependent cell
RT morphogenesis.";
RL Development 134:967-977(2007).
CC -!- FUNCTION: Involved in regulation of actin and microtubule organization.
CC Part of a WAVE complex that activates the Arp2/3 complex. Regulates
CC trichome branch positioning and expansion.
CC {ECO:0000269|PubMed:15316111}.
CC -!- SUBUNIT: Binds BRK1. Interacts with SPK1, ABI1, ABI2, ABI3 and ABI4.
CC {ECO:0000269|PubMed:15534215, ECO:0000269|PubMed:17267444}.
CC -!- INTERACTION:
CC Q9LP46; Q94JY4: BRK1; NbExp=3; IntAct=EBI-1547699, EBI-1547691;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9LP46-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in expanding cotyledons, expanding leaves
CC and expanding siliques containing developing embryos. Detected in
CC unopened flower buds. Reduced expression in mature leaves and mature
CC cotyledons. {ECO:0000269|PubMed:15534215}.
CC -!- DOMAIN: Activates the Arp2/3 complex and binds actin through the C-
CC terminal VCA (verprolin homology/cofilin homology/acidic) domain
CC consisting of a WH2 domain followed by an Arp2/3-binding acidic motif
CC (A), separated by a conserved linker region (C). Binds BRK1 through the
CC N-terminal Scar homology domain (SHD).
CC -!- SIMILARITY: Belongs to the SCAR/WAVE family. {ECO:0000305}.
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DR EMBL; AY743925; AAU93850.1; -; mRNA.
DR EMBL; AC021043; AAF88121.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31052.1; -; Genomic_DNA.
DR PIR; B86414; B86414.
DR RefSeq; NP_174212.2; NM_102658.3. [Q9LP46-1]
DR AlphaFoldDB; Q9LP46; -.
DR BioGRID; 25026; 10.
DR ELM; Q9LP46; -.
DR IntAct; Q9LP46; 10.
DR STRING; 3702.AT1G29170.1; -.
DR iPTMnet; Q9LP46; -.
DR PaxDb; Q9LP46; -.
DR PRIDE; Q9LP46; -.
DR ProteomicsDB; 226623; -. [Q9LP46-1]
DR EnsemblPlants; AT1G29170.1; AT1G29170.1; AT1G29170. [Q9LP46-1]
DR GeneID; 839791; -.
DR Gramene; AT1G29170.1; AT1G29170.1; AT1G29170. [Q9LP46-1]
DR KEGG; ath:AT1G29170; -.
DR Araport; AT1G29170; -.
DR TAIR; locus:2030000; AT1G29170.
DR eggNOG; ENOG502QSPV; Eukaryota.
DR HOGENOM; CLU_005038_0_0_1; -.
DR InParanoid; Q9LP46; -.
DR OMA; CHTKREV; -.
DR PhylomeDB; Q9LP46; -.
DR PRO; PR:Q9LP46; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LP46; baseline and differential.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0031209; C:SCAR complex; TAS:TAIR.
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:0051127; P:positive regulation of actin nucleation; IMP:TAIR.
DR GO; GO:2000601; P:positive regulation of Arp2/3 complex-mediated actin nucleation; IBA:GO_Central.
DR InterPro; IPR028288; SCAR/WAVE_fam.
DR PANTHER; PTHR12902; PTHR12902; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Cytoplasm; Cytoskeleton;
KW Reference proteome.
FT CHAIN 1..1020
FT /note="Protein SCAR3"
FT /id="PRO_0000189006"
FT DOMAIN 954..972
FT /note="WH2"
FT REGION 167..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 351..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 802..827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..192
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..382
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..817
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1020 AA; 113030 MW; 8082F565A5AA3FD0 CRC64;
MPRNVYGMNQ SEVYRNVDRE DPKAILNGVA VTGLVGVLRQ LGDLAEFAAE IFHGIQEEVM
ATASRSNQLK IRLQHIEATV PPLEKAMLAQ TTHIHFAYTG GLEWHPRIPI TQNHLIYDDL
PHIIMDPYEE CRGPPRLHLL DKFDINGPGS CLKRYSDPTY FRRASSNLSQ GNKKFQKDKK
HCKMKKKKTS SRSRDMSRLA SLANQNARKT FASFSFSGQT SSTKTTSTSD MEKRYDFQDH
HSRSFESRSG SGYNECLSTA TSSLKTGERP KGVFVSSSLT PGSCTIASVL SECETEDAHD
NFQFSPSQGQ AARGSSCVSW DEKAEIVESL GLQTDEASEM VEANSVVDTL DEKPSYGEGI
GGVDFHSKDN ENDKSESGLR KRAGIDEVRE IKNGREIVGE PRDSEQETES EGECFVDALN
TIESESENNQ GLQTSQVSSS CGVADERLEK SVCEQETEQN SYSVEDSCRS MDGLMANSFK
NEENASSENV SVEMHQQNLQ AGSDINRLQK NDLCANKDMR NDSGGKDTIT FTFVPGLENS
LVDSSNPLIH HGLQENQETE AESSGDLEAF KIWTNGGLLG LKPSKPPVLA MPSSLSPDCK
TEERTVGFAE AEKDKADDLV ENASHRHVLN NSSLATPGTQ NPGSSNGIVM GIVDQRESHE
TSSGVFGLSH KFLTSGFRRK DSFAHDRKTV PATIPENDEV TTERRRFCDQ DINEKTFMDP
FRDEAPIDWI TSSPPLQHMK ISLNPADTLQ ASRLKLKFSD GDNTYNTFSS FQLLPETGTS
LPDSYSDDDT FCRSSPYMSD TDYLSDNHSL SNSEPWEESS DSHGRKEQEL YDSFHESRHV
DNNAEASPLG IKSESSCVAV NLSYLQNPAE PLPPPFPPMQ WMVSKTPSEK MEDKTQSLQL
QEALRFAFEK HISLPTAKNE LPSMVTSAPK PEIKAHLKNN VREEKQSANA KETETGDFLQ
QIRTQQFNLR PVVMTTTSSA TATTDPIINT KISAILEKAN SIRQAVASKD GDESDTWSDT
