SCAR1_ARATH
ID SCAR1_ARATH Reviewed; 821 AA.
AC Q6AWX6; O22968; Q56WS5; Q5XPJ7; Q84WP7;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Protein SCAR1;
DE Short=AtSCAR1;
DE AltName: Full=Protein WAVE1;
GN Name=SCAR1; OrderedLocusNames=At2g34150; ORFNames=T14G11.27;
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=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 [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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 523-821.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP IDENTIFICATION, AND INTERACTION WITH ACTIN.
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 [7]
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 [8]
RP INTERACTION WITH SPK1; ABI1 AND ABI2.
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 and actin. Interacts with SPK1, ABI1 and ABI2.
CC {ECO:0000269|PubMed:15296761, ECO:0000269|PubMed:15534215,
CC ECO:0000269|PubMed:17267444}.
CC -!- INTERACTION:
CC Q6AWX6; Q94JY4: BRK1; NbExp=2; IntAct=EBI-1547775, 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=Q6AWX6-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in expanding cotyledons, expanding leaves
CC and expanding siliques containing developing embryos. Detected in
CC unopened flower buds and in the expanding tip region of roots. Reduced
CC expression in mature leaves and mature cotyledons.
CC {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=AAB67636.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAO22743.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY743926; AAU93851.1; -; mRNA.
DR EMBL; AC002341; AAB67636.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC08925.1; -; Genomic_DNA.
DR EMBL; BT002929; AAO22743.1; ALT_FRAME; mRNA.
DR EMBL; AK221958; BAD94455.1; -; mRNA.
DR EMBL; BK005566; DAA05586.1; -; mRNA.
DR PIR; A84753; A84753.
DR RefSeq; NP_001031474.1; NM_001036397.3. [Q6AWX6-1]
DR AlphaFoldDB; Q6AWX6; -.
DR BioGRID; 3323; 9.
DR ELM; Q6AWX6; -.
DR IntAct; Q6AWX6; 8.
DR STRING; 3702.AT2G34150.2; -.
DR iPTMnet; Q6AWX6; -.
DR PaxDb; Q6AWX6; -.
DR ProteomicsDB; 226594; -. [Q6AWX6-1]
DR EnsemblPlants; AT2G34150.2; AT2G34150.2; AT2G34150. [Q6AWX6-1]
DR GeneID; 817976; -.
DR Gramene; AT2G34150.2; AT2G34150.2; AT2G34150. [Q6AWX6-1]
DR KEGG; ath:AT2G34150; -.
DR Araport; AT2G34150; -.
DR TAIR; locus:2055511; AT2G34150.
DR eggNOG; ENOG502QSPV; Eukaryota.
DR HOGENOM; CLU_005038_0_0_1; -.
DR InParanoid; Q6AWX6; -.
DR OMA; DHRSCSF; -.
DR OrthoDB; 594491at2759; -.
DR PhylomeDB; Q6AWX6; -.
DR PRO; PR:Q6AWX6; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q6AWX6; baseline and differential.
DR Genevisible; Q6AWX6; AT.
DR GO; GO:0071944; C:cell periphery; IDA:TAIR.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0043229; C:intracellular organelle; IDA:TAIR.
DR GO; GO:0016020; C:membrane; IDA:TAIR.
DR GO; GO:0031209; C:SCAR complex; TAS:TAIR.
DR GO; GO:0003785; F:actin monomer binding; IDA:TAIR.
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; 3.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Cytoplasm; Cytoskeleton;
KW Reference proteome.
FT CHAIN 1..821
FT /note="Protein SCAR1"
FT /id="PRO_0000189004"
FT DOMAIN 756..774
FT /note="WH2"
FT REGION 168..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 802..821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..625
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 261
FT /note="G -> V (in Ref. 4; AAO22743)"
FT /evidence="ECO:0000305"
FT CONFLICT 646
FT /note="V -> A (in Ref. 1; AAU93851)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 821 AA; 92090 MW; 67DB3E28A60F6115 CRC64;
MPLVRLQVRN VYGLGQKELH TKVDREDPKA ILDDVAVSGL VGILRQLGDL TEFAAEIFHG
IQEEVMITAS RSNKLKMRLK QIEAKVPTIQ KTVLAQTNHI HFAYTGGLEW HPRIPNVQNH
FMYDELPPFI MTPYEDCREP PRLHLLDKFD INGPGSCLKR YSDPTHFKRA SRASKPSEIK
KKKSIQRGRD ISRLASVANQ SDRKTCTSLS FSGRTSTSKT ASTIEIESKS DLQEHRSFSF
DSRSGGEKPK RVSSSSRFTP GSRTIASVLS ESESESDSPS QDLTARGSSS VSWHEKAEIV
ECNVLQCATD EAPEVMETNF VLDAEPVSRL KEHSAVEAVQ DIKPKELEMD NEDETESEGD
DFVDALYTID SESENDEAFQ ATKEVQKNLY NDITEQETEK ISNNFSVDET KCAATSELHL
SSSPVYKSDE LIHQDPWAAS EISSGTHSYS NGFSNPLYDI SGIQEHQESE EVESSCDTES
IKTWTNGNLL GLKPSKPKII AETIPEIVED IDSETFQEHL REDYKAPFDW FTSSPPLDHM
KISFKSSETL PSSELQLKLP DEYTFSSFQL VPETIATSLP DSDSDKDTFC RSSSYISDNS
DNDNRSVSMS EQQWEEESEG IRESKRQQEL YDSFHRVNAE ASSLPVPFPK IETTNGCLVE
NVSYLQNPAE PLPPPLPPLQ WMVSKIPSAG FEDNNKQSLK DALTQAFEKN NNSLTAVKKK
EPHIVTVSDP KLVTKVHLKN NVRDYKQSHG NTNETEAGDF LHQIRTKQFN LRRVVRTKTS
SSETTMNTNI SVILEKANSI RQAVASDDGE GESDTWSDSD T
