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ARC1B_ARATH
ID   ARC1B_ARATH             Reviewed;         378 AA.
AC   Q9SJW6;
DT   29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 141.
DE   RecName: Full=Actin-related protein 2/3 complex subunit 1B;
DE   AltName: Full=Actin-related protein C1;
DE   AltName: Full=Actin-related protein C1B;
DE   AltName: Full=Arp2/3 complex 41 kDa subunit;
DE   AltName: Full=p41-ARC;
GN   Name=ARPC1B; OrderedLocusNames=At2g31300; ORFNames=F16D14.14;
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 [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   [2]
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   [3]
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   [4]
RP   TISSUE SPECIFICITY, AND IDENTIFICATION OF THE ARP2/3 COMPLEX.
RX   PubMed=12913159; DOI=10.1104/pp.103.028563;
RA   Li S., Blanchoin L., Yang Z., Lord E.M.;
RT   "The putative Arabidopsis arp2/3 complex controls leaf cell
RT   morphogenesis.";
RL   Plant Physiol. 132:2034-2044(2003).
RN   [5]
RP   REVIEW.
RX   PubMed=15653407; DOI=10.1016/j.pbi.2004.11.004;
RA   Szymanski D.B.;
RT   "Breaking the WAVE complex: the point of Arabidopsis trichomes.";
RL   Curr. Opin. Plant Biol. 8:103-112(2005).
CC   -!- FUNCTION: Functions as component of the Arp2/3 complex which is
CC       involved in regulation of actin polymerization and together with an
CC       activating nucleation-promoting factor (NPF) mediates the formation of
CC       branched actin networks. Arp2/3 complex plays a critical role in the
CC       control of cell morphogenesis via the modulation of cell polarity
CC       development. {ECO:0000250}.
CC   -!- SUBUNIT: Component of the Arp2/3 complex composed of ARP2, ARP3,
CC       ARPC1/p41-ARC, ARPC2/p34-ARC, ARPC3/p21-ARC, ARPC4/p20-ARC and
CC       ARPC5/p16-ARC.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed at low levels in all tissues with a
CC       relatively highest expression in inflorescences.
CC       {ECO:0000269|PubMed:12913159}.
CC   -!- SIMILARITY: Belongs to the WD repeat ARPC1 family. {ECO:0000305}.
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DR   EMBL; AC006593; AAD20675.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC08524.1; -; Genomic_DNA.
DR   EMBL; AF439845; AAL27513.1; -; mRNA.
DR   EMBL; BT000567; AAN18136.1; -; mRNA.
DR   PIR; A84719; A84719.
DR   RefSeq; NP_180688.1; NM_128686.3.
DR   AlphaFoldDB; Q9SJW6; -.
DR   SMR; Q9SJW6; -.
DR   IntAct; Q9SJW6; 1.
DR   STRING; 3702.AT2G31300.1; -.
DR   PaxDb; Q9SJW6; -.
DR   PRIDE; Q9SJW6; -.
DR   ProteomicsDB; 246981; -.
DR   EnsemblPlants; AT2G31300.1; AT2G31300.1; AT2G31300.
DR   GeneID; 817687; -.
DR   Gramene; AT2G31300.1; AT2G31300.1; AT2G31300.
DR   KEGG; ath:AT2G31300; -.
DR   Araport; AT2G31300; -.
DR   TAIR; locus:2042491; AT2G31300.
DR   eggNOG; KOG1523; Eukaryota.
DR   HOGENOM; CLU_034396_0_0_1; -.
DR   InParanoid; Q9SJW6; -.
DR   OMA; TLKGSTW; -.
DR   PhylomeDB; Q9SJW6; -.
DR   PRO; PR:Q9SJW6; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9SJW6; baseline and differential.
DR   Genevisible; Q9SJW6; AT.
DR   GO; GO:0005885; C:Arp2/3 protein complex; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR   GO; GO:0005634; C:nucleus; HDA:TAIR.
DR   GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR   GO; GO:0007015; P:actin filament organization; TAS:TAIR.
DR   GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; IBA:GO_Central.
DR   GO; GO:0030833; P:regulation of actin filament polymerization; IEA:InterPro.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR017383; ARPC1.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   PANTHER; PTHR10709; PTHR10709; 1.
DR   Pfam; PF00400; WD40; 2.
DR   PIRSF; PIRSF038093; ARP2/3_su1; 1.
DR   SMART; SM00320; WD40; 5.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 2.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   2: Evidence at transcript level;
KW   Actin-binding; Cytoplasm; Cytoskeleton; Reference proteome; Repeat;
KW   WD repeat.
FT   CHAIN           1..378
FT                   /note="Actin-related protein 2/3 complex subunit 1B"
FT                   /id="PRO_0000422527"
FT   REPEAT          8..47
FT                   /note="WD 1"
FT   REPEAT          53..92
FT                   /note="WD 2"
FT   REPEAT          97..138
FT                   /note="WD 3"
FT   REPEAT          143..182
FT                   /note="WD 4"
FT   REPEAT          203..242
FT                   /note="WD 5"
FT   REPEAT          257..295
FT                   /note="WD 6"
FT   REPEAT          331..375
FT                   /note="WD 7"
FT   REGION          319..340
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        319..334
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   378 AA;  41819 MW;  C96E4329C1667ED8 CRC64;
     MAVVDVHRFA ESITCHAWSP DLSMVALCPN NTEVHIYKSL SQDHWERLHV LQKHDQIVSG
     IDWSSKSNKI VTVSHDRNSY VWSLEGAEWV PTLVILRLNR AALCVQWSPK ENKFAVGSGA
     KTVCICYYEQ ENNWWVSKLI RKRHESSVTS VAWHPNNVLL ATTSTDGKCR VFSTFIKGVD
     TKDSKAGSPA ETKFGEQILQ LDLSYSWAFG VKWSPSGNTL AYVGHSSMIY FVDDVGPSPL
     AQSVAFRDLP LRDVLFISEK MVIGVGYDSN PMVFAADDTG IWSFIRYIGE KKAASSGSSY
     SSQFSEAFGK FYGSQSKSTT ANDASDSRGG VHDNSITSIV PLGKGGSPKV MRFSTSGLDG
     KIAIWDLENM QQELGNQF
 
 
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