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ARC5A_ARATH
ID   ARC5A_ARATH             Reviewed;         132 AA.
AC   Q9M117; Q941F3;
DT   29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2013, sequence version 2.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Actin-related protein 2/3 complex subunit 5A;
DE   AltName: Full=Actin-related protein C5A;
DE   AltName: Full=Arp2/3 complex 16 kDa subunit;
DE            Short=p16-ARC;
DE   AltName: Full=Protein CROOKED;
GN   Name=ARPC5A; Synonyms=CRK; OrderedLocusNames=At4g01710; ORFNames=T15B16.22;
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=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(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   FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX   PubMed=12783786; DOI=10.1242/dev.00549;
RA   Mathur J., Mathur N., Kirik V., Kernebeck B., Srinivas B.P., Huelskamp M.;
RT   "Arabidopsis CROOKED encodes for the smallest subunit of the ARP2/3 complex
RT   and controls cell shape by region specific fine F-actin formation.";
RL   Development 130:3137-3146(2003).
RN   [5]
RP   FUNCTION, TISSUE SPECIFICITY, IDENTIFICATION OF THE ARP2/3 COMPLEX, AND
RP   DISRUPTION PHENOTYPE.
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   [6]
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).
RN   [7]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
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 (By similarity). Arp2/3 complex plays a
CC       critical role in the control of cell morphogenesis via the modulation
CC       of cell polarity development. {ECO:0000250,
CC       ECO:0000269|PubMed:12783786, ECO:0000269|PubMed:12913159}.
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}. Cell
CC       projection {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed at low levels in all tissues with a
CC       relatively highest expression in inflorescences.
CC       {ECO:0000269|PubMed:12783786, ECO:0000269|PubMed:12913159}.
CC   -!- DISRUPTION PHENOTYPE: Distorted trichomes and altered epidermal cell
CC       types. {ECO:0000269|PubMed:12783786, ECO:0000269|PubMed:12913159}.
CC   -!- SIMILARITY: Belongs to the ARPC5 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB77741.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AF104919; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL161492; CAB77741.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE82068.1; -; Genomic_DNA.
DR   EMBL; AY052191; AAK97662.1; -; mRNA.
DR   EMBL; AY143806; AAN28745.1; -; mRNA.
DR   PIR; A85022; A85022.
DR   RefSeq; NP_567216.1; NM_116401.3.
DR   AlphaFoldDB; Q9M117; -.
DR   SMR; Q9M117; -.
DR   BioGRID; 13378; 1.
DR   IntAct; Q9M117; 1.
DR   STRING; 3702.AT4G01710.1; -.
DR   iPTMnet; Q9M117; -.
DR   PaxDb; Q9M117; -.
DR   PRIDE; Q9M117; -.
DR   ProteomicsDB; 246491; -.
DR   EnsemblPlants; AT4G01710.1; AT4G01710.1; AT4G01710.
DR   GeneID; 828087; -.
DR   Gramene; AT4G01710.1; AT4G01710.1; AT4G01710.
DR   KEGG; ath:AT4G01710; -.
DR   Araport; AT4G01710; -.
DR   TAIR; locus:2133422; AT4G01710.
DR   eggNOG; KOG3380; Eukaryota.
DR   HOGENOM; CLU_101888_3_0_1; -.
DR   InParanoid; Q9M117; -.
DR   OMA; CKSANWL; -.
DR   OrthoDB; 1565115at2759; -.
DR   PRO; PR:Q9M117; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9M117; baseline and differential.
DR   Genevisible; Q9M117; AT.
DR   GO; GO:0005885; C:Arp2/3 protein complex; IBA:GO_Central.
DR   GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0003779; F:actin binding; TAS:TAIR.
DR   GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IMP:TAIR.
DR   GO; GO:0007015; P:actin filament organization; TAS:TAIR.
DR   GO; GO:0030041; P:actin filament polymerization; IMP:TAIR.
DR   GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; IBA:GO_Central.
DR   GO; GO:0009825; P:multidimensional cell growth; IMP:TAIR.
DR   GO; GO:0030833; P:regulation of actin filament polymerization; IEA:InterPro.
DR   GO; GO:0010090; P:trichome morphogenesis; IMP:TAIR.
DR   Gene3D; 1.25.40.190; -; 1.
DR   InterPro; IPR006789; ARPC5.
DR   InterPro; IPR036743; ARPC5_sf.
DR   PANTHER; PTHR12644; PTHR12644; 1.
DR   Pfam; PF04699; P16-Arc; 1.
DR   SUPFAM; SSF69103; SSF69103; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Actin-binding; Cell projection; Cytoplasm; Cytoskeleton;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   CHAIN           2..132
FT                   /note="Actin-related protein 2/3 complex subunit 5A"
FT                   /id="PRO_0000422532"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:22223895"
SQ   SEQUENCE   132 AA;  14972 MW;  DC3AADCC46390942 CRC64;
     MAEFVEADNA EAIIARIETK SRKIESLLKQ YKHVEALKTA LEGSPPKTRD ERCKSANWIV
     VHRALMAIKD IDGMLNALDV EYYDILMKYL YRGLSTGDRP TCDQCLKIHE KLTERAGLGC
     ILRCLTDTIN TV
 
 
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