SCAR2_ARATH
ID SCAR2_ARATH Reviewed; 1399 AA.
AC Q5XPJ9; O80907;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=Protein SCAR2;
DE Short=AtSCAR2;
DE AltName: Full=Protein DISTORTED 3;
DE AltName: Full=Protein IRREGULAR TRICHOME BRANCH 1;
DE AltName: Full=Protein WAVE4;
GN Name=SCAR2; Synonyms=DIS3, ITB1, WAVE4; OrderedLocusNames=At2g38440;
GN ORFNames=T19C21.7;
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], AND TISSUE SPECIFICITY.
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 [MRNA], FUNCTION, TISSUE SPECIFICITY, MUTANT DIS3-4,
RP AND INTERACTION WITH ABIL1 AND ARPC3.
RX PubMed=15659634; DOI=10.1105/tpc.104.027987;
RA Basu D., Le J., El-Din El-Assal S., Huang S., Zhang C., Mallery E.L.,
RA Koliantz G., Staiger C.J., Szymanski D.B.;
RT "DISTORTED3/SCAR2 is a putative Arabidopsis WAVE complex subunit that
RT activates the Arp2/3 complex and is required for epidermal morphogenesis.";
RL Plant Cell 17:502-524(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [4]
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 [5]
RP FUNCTION, AND IDENTIFICATION.
RX PubMed=15296761; DOI=10.1016/j.cub.2004.06.065;
RA Deeks M.J., Kaloriti D., Davies B., Malho R., Hussey P.J.;
RT "Arabidopsis NAP1 is essential for Arp2/3-dependent trichome
RT morphogenesis.";
RL Curr. Biol. 14:1410-1414(2004).
RN [6]
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 [7]
RP FUNCTION, IDENTIFICATION, TISSUE SPECIFICITY, AND INTERACTION WITH BRK1.
RX PubMed=16006582; DOI=10.1105/tpc.104.028670;
RA Zhang X., Dyachok J., Krishnakumar S., Smith L.G., Oppenheimer D.G.;
RT "IRREGULAR TRICHOME BRANCH1 in Arabidopsis encodes a plant homolog of the
RT actin-related protein2/3 complex activator Scar/WAVE that regulates actin
RT and microtubule organization.";
RL Plant Cell 17:2314-2326(2005).
RN [8]
RP INTERACTION WITH SPK1; ABI1; ABI2 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:15296761, ECO:0000269|PubMed:15316111,
CC ECO:0000269|PubMed:15659634, ECO:0000269|PubMed:16006582}.
CC -!- SUBUNIT: Binds BRK1, actin, ABIL1 and ARPC3 (Arp2/3 complex). Interacts
CC with SPK1, ABI1, ABI2 and ABI4. {ECO:0000269|PubMed:15659634,
CC ECO:0000269|PubMed:16006582, ECO:0000269|PubMed:17267444}.
CC -!- INTERACTION:
CC Q5XPJ9; Q8S8M5: ABIL1; NbExp=3; IntAct=EBI-1547795, EBI-1547655;
CC Q5XPJ9; Q1ECJ7: ARPC3; NbExp=4; IntAct=EBI-1547795, EBI-1547752;
CC Q5XPJ9; Q94JY4: BRK1; NbExp=3; IntAct=EBI-1547795, EBI-1547691;
CC Q5XPJ9; Q8SAB7: SPK1; NbExp=3; IntAct=EBI-1547795, EBI-1547917;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- TISSUE SPECIFICITY: Expressed in expanding cotyledons, expanding leaves
CC and expanding siliques containing developing embryos. Lower expression,
CC sometimes not detected, in unopened flower buds and in matures leaves.
CC {ECO:0000269|PubMed:15534215, ECO:0000269|PubMed:15659634,
CC ECO:0000269|PubMed:16006582}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC28760.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY743924; AAU93849.1; -; mRNA.
DR EMBL; AY817016; AAW49260.1; -; mRNA.
DR EMBL; AC004683; AAC28760.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC09537.1; -; Genomic_DNA.
DR PIR; T02501; T02501.
DR RefSeq; NP_181378.2; NM_129400.3.
DR AlphaFoldDB; Q5XPJ9; -.
DR BioGRID; 3767; 12.
DR ELM; Q5XPJ9; -.
DR IntAct; Q5XPJ9; 10.
DR STRING; 3702.AT2G38440.1; -.
DR iPTMnet; Q5XPJ9; -.
DR PaxDb; Q5XPJ9; -.
DR PRIDE; Q5XPJ9; -.
DR ProteomicsDB; 232689; -.
DR EnsemblPlants; AT2G38440.1; AT2G38440.1; AT2G38440.
DR GeneID; 818425; -.
DR Gramene; AT2G38440.1; AT2G38440.1; AT2G38440.
DR KEGG; ath:AT2G38440; -.
DR Araport; AT2G38440; -.
DR TAIR; locus:2057155; AT2G38440.
DR eggNOG; ENOG502QTI6; Eukaryota.
DR HOGENOM; CLU_002411_0_0_1; -.
DR InParanoid; Q5XPJ9; -.
DR OMA; CDDHISH; -.
DR OrthoDB; 594491at2759; -.
DR PhylomeDB; Q5XPJ9; -.
DR PRO; PR:Q5XPJ9; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q5XPJ9; baseline and differential.
DR Genevisible; Q5XPJ9; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0031209; C:SCAR complex; ISS: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; IMP:TAIR.
DR GO; GO:0045010; P:actin nucleation; TAS:TAIR.
DR GO; GO:0098609; P:cell-cell adhesion; IMP:TAIR.
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 GO; GO:0010091; P:trichome branching; IMP:TAIR.
DR GO; GO:0010090; P:trichome morphogenesis; IMP:TAIR.
DR InterPro; IPR028288; SCAR/WAVE_fam.
DR InterPro; IPR003124; WH2_dom.
DR PANTHER; PTHR12902; PTHR12902; 1.
DR PROSITE; PS51082; WH2; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Cytoplasm; Cytoskeleton; Reference proteome.
FT CHAIN 1..1399
FT /note="Protein SCAR2"
FT /id="PRO_0000189005"
FT DOMAIN 1335..1353
FT /note="WH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 178..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 896..961
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1102..1139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1207..1261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..428
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..456
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..611
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 941..955
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1102..1117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1207..1228
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 1231..1399
FT /note="Missing: In dis 3-4; distorded trichomes."
SQ SEQUENCE 1399 AA; 151585 MW; CAC55D7CF3C8AEBC CRC64;
MPLTRYQSRN EYGLADPDLY QAADKDDPEA LLEGVAMAGL VGILRQLGDL AEFAAEMFHD
LHEEVMATAS RSHGLMARVQ QLEAEFPSIE KALLCQTDHS PFFSNKGVEW HPNLQLEQSV
VTSGDLPRCV MDSYEECRGP PRLFLLDKFD ISGAGACLKR YTDPSFVRLE TSSYEESWDD
IQREKKSQKA KRRASQWRNG GTPENALSSH AKLHELFLEE HLEAHHSDPA RVVKLKTRKL
DGCSLISKSG ESYMEKFVQT RVDSKISYEI ITQNPGLLTW NMDSARDVVT DIPEISMVGA
MDKSHGGSRA EVSFPSEQEN VANVNMNGGF IEKDIETVPE STYNEVRGTT ITQDSQTVLN
GKPGFFQQRS YSEDLTSEAD NYVDAPATME SETETDDECR PKSRSDTLKD GNHHIYSDAV
EERMEDPPQF SFSHSNGNTP VSENGRSSFG KKSTSYSYSD TASISIDDQS DGEKLSGCLP
STSSFKSELV DSMSHVTPEA NKVSHDLNVQ ESVSSSNVDG QTSLSSNGTC SSPRPVSQND
QSCSLTVQSL ASEVVETSPE LVRLDLMKGG NDGRKVDPFD SSKSCASFDA KNSDLPSETS
SISSTSEGSR CDSTIEKNCM VASNLVNSGT SPQAFVDSQT GKQLPIADTD FETNSIVACS
EVLANSGSDP EERDGRCLTG KLVPCSAGVG MEVSPDTPSK VCGPSSADGI HLKDTLDDET
DCVSVTNVVV DVDSKNSVAD VGSQSSVADI DSQSSVAEIS DEHSCAFGNT ADVSVSESHE
DTLENGMSVP SDFNSGVEKL AGDASPTCSK CDDHISHEGF HDLSGLDNAT TDIVPNVELD
VSDNDNDTSS GGVNHAVSLS STRGKGSLPW ISTNTYQSSS DAGEIFHDTV VESDGTLLED
NNPESEIKMH KSPLEVSSEG LSTEPDNKDV ESIESTSPKP SLDQRNRDTE TKSPGESILD
DNCIDSTQVY NLNLLESEAI DQAVREQTSY ASHEVADEEL LQSNVFRGLE FEPQSAGLEF
APQSAGIELN RPKQELNLDP TFPSFGFIPE TIPPNPEDMP PLPPMQWLIG KVPHSFPTFM
GESVETSSSA LSAAPPIGSS LNVQIGSPPS ELSVSLGSDE SERLPGGFVH NASEKPLQSS
IQFPTMSTDL NSQYDSSELP TIPYQECIED FGSEENNLLA DHAAQNHELV YSQASSLQLP
QVKHEDFKDD ADVHESQSSS DDHHCPETKS LTPTQSTKVE DKGHSVPDAS NAETAESSNT
SVQKINPVSV GDAMWPVSCF SVAPTLDTYK TEVVPTVRLP RPRSPLVDAV AAHDRRKMKK
VSEMVHPPIK SKQDDKDSLL AQIRNKSVNL KPAVTTRPSI QTGPRTDLRV AAILEKANTI
RMAMAGSDED EDSDSWSDS
