SCAR4_ARATH
ID SCAR4_ARATH Reviewed; 1170 AA.
AC Q5XPJ6; Q9LCZ7;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Protein SCAR4;
DE Short=AtSCAR4;
DE AltName: Full=Protein WAVE3;
GN Name=SCAR4; OrderedLocusNames=At5g01730; ORFNames=F7A7.250;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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.
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: Interacts with SPK1. {ECO:0000269|PubMed:17267444}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- TISSUE SPECIFICITY: Expressed in expanding cotyledons, expanding leaves
CC and expanding siliques containing developing embryos. Detected in
CC unopened flower buds and in the expanding tip region of roots. Reduced
CC expression in mature leaves. {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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB82289.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY743927; AAU93852.1; -; mRNA.
DR EMBL; AL161946; CAB82289.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED90383.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM68918.1; -; Genomic_DNA.
DR PIR; T48194; T48194.
DR RefSeq; NP_001318456.1; NM_001342607.1.
DR RefSeq; NP_195793.3; NM_120251.4.
DR AlphaFoldDB; Q5XPJ6; -.
DR BioGRID; 16963; 3.
DR IntAct; Q5XPJ6; 3.
DR STRING; 3702.AT5G01730.1; -.
DR iPTMnet; Q5XPJ6; -.
DR PaxDb; Q5XPJ6; -.
DR PRIDE; Q5XPJ6; -.
DR ProteomicsDB; 232961; -.
DR EnsemblPlants; AT5G01730.1; AT5G01730.1; AT5G01730.
DR EnsemblPlants; AT5G01730.4; AT5G01730.4; AT5G01730.
DR GeneID; 831687; -.
DR Gramene; AT5G01730.1; AT5G01730.1; AT5G01730.
DR Gramene; AT5G01730.4; AT5G01730.4; AT5G01730.
DR KEGG; ath:AT5G01730; -.
DR Araport; AT5G01730; -.
DR TAIR; locus:2149820; AT5G01730.
DR eggNOG; ENOG502RRIC; Eukaryota.
DR HOGENOM; CLU_274211_0_0_1; -.
DR InParanoid; Q5XPJ6; -.
DR OrthoDB; 594491at2759; -.
DR PhylomeDB; Q5XPJ6; -.
DR PRO; PR:Q5XPJ6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q5XPJ6; baseline and differential.
DR Genevisible; Q5XPJ6; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0010287; C:plastoglobule; HDA:TAIR.
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; Cytoplasm; Cytoskeleton; Reference proteome.
FT CHAIN 1..1170
FT /note="Protein SCAR4"
FT /id="PRO_0000189007"
FT DOMAIN 1105..1123
FT /note="WH2"
FT REGION 180..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 631..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 700..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 783..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 960..980
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1026..1046
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..717
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 964..980
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1028..1046
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1170 AA; 128618 MW; 96522221853ED25D CRC64;
MALTRYQIRN EYGLADKELY QSADKEDPEA LLEAASMAGL VGVLRQLGDL SEFAAEVFHC
LHEQLMTTAA RGHGLAMRLQ HLEADFPSVE IPILSQTDHS TFFYEPGLEW HSDLQTKEDL
ISPRNLPRCI MDSYEECHGP PQLFLLDKFD VAGSGSCLKR YSDPSLLKTH TTSAVVATSK
LGKDKRLRQS KKKGSHTTIK ETPEDSRTSH AKLHQLFFLE HVENGHRNPE FHVKLKRRQL
NGPPINSSSG ASYMEKFLKN SSPYCERVHG TMDQSSPAME TEVTVCSEQE DLPIPSLVYS
NSGGTRKYNE MEIESIAGHE ILEIPFVPHE ITVNEKSPVV CLESSSSVNL CCKTNNDADS
PASTESEVKE AGSDDKAGCD HGFPGFGQPQ ICTNAEVNQT EVLTQFSNVL RHSPEEGESS
LLCTDIQRAS PESKPHKAEE AAVDLDESFS QMTPDIDSAG MGTLEILQTP FSLSCYESPA
NLPEDSGSHL ELQSNKANAE ACEVFEVRRD PMLNISPETH LLKVTQVPQD AYEGGTNDVH
SQHVFSVETA SEISVSALVE DQFSSITNQE IEALESEDIS SEAGHFIPDT KKSLNETSVA
LESDFLLPNH YISTFDNFED LSLSADAQDY AAPKEDETNS QDGSSMNPAQ SKHISTSEIS
SENGTLMSDT PRDLHTGYGS LSASSCLEDG LANPDLAEIS SYSGQEDPQT MSIVSDDSSD
PEVPIPDGTC FAGDVDHDNQ TGLNNKAIET VPQKELETIS DPQESLLGTE ECLSSEYCLQ
IQNQRQESPS ETGSANSRTS SDESPPTQNG SVGVQSSPLD VFPSSITEIE ALHAPYQEIF
TSLNDHISES VLSKGLTDEE DFLNVSPESI LPLSTSLHET PQANPEITPP LPPLPPTQWW
MGKLVESTEM PSLAGSGNNS FNIQRDENTQ NGSVQANEAQ YPSEVSVTDG ENHNFHIYTE
ESKATEEQSP SGVNGTSDTY MESKHKCLNR TPEDSFSLAE SAQGLEADWR TEAMALEWFS
QNLREHNNPH PAKLEEEEPQ VDHPLEKPGQ TKFRQTLRDN NSYNQNQKAG KLKRDEDTLV
IGIDRSMLRK VSEGNRTHVG ARVDENDSLL EIIRSKSFNL RPADASGRPN FQVAVPKTNL
KVAAILEKAN TLRQAMAGSD DEHDSDSWSE
