ACT7_ARATH
ID ACT7_ARATH Reviewed; 377 AA.
AC P53492; P53495;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 144.
DE RecName: Full=Actin-7 {ECO:0000303|PubMed:8754679};
DE AltName: Full=Actin-2 {ECO:0000303|Ref.1};
GN Name=ACT7 {ECO:0000303|PubMed:8754679};
GN OrderedLocusNames=At5g09810 {ECO:0000312|Araport:AT5G09810};
GN ORFNames=MYH9.2 {ECO:0000312|EMBL:BAB09402.1};
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].
RA Hong Y., Chua N.;
RT "A cDNA sequence encoding a novel actin from Arabidopsis thaliana.";
RL Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC STRAIN=cv. Columbia;
RX PubMed=8754679; DOI=10.1104/pp.111.3.699;
RA McDowell J.M., An Y.-Q., Huang S., McKinney E.C., Meagher R.B.;
RT "The Arabidopsis ACT7 actin gene is expressed in rapidly developing tissues
RT and responds to several external stimuli.";
RL Plant Physiol. 111:699-711(1996).
RN [3]
RP SEQUENCE REVISION.
RA McKinney E.C., An Y.-Q.;
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
RN [5]
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 [6]
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 [7]
RP GENE FAMILY ORGANIZATION, AND CHARACTERIZATION.
RC STRAIN=cv. Columbia;
RX PubMed=8852856; DOI=10.1093/genetics/142.2.587;
RA McDowell J.M., Huang S., McKinney E.C., An Y.-Q., Meagher R.B.;
RT "Structure and evolution of the actin gene family in Arabidopsis
RT thaliana.";
RL Genetics 142:587-602(1996).
RN [8]
RP FUNCTION, AND INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=11449050; DOI=10.2307/3871385;
RA Kandasamy M.K., Gilliland L.U., McKinney E.C., Meagher R.B.;
RT "One plant actin isovariant, ACT7, is induced by auxin and required for
RT normal callus formation.";
RL Plant Cell 13:1541-1554(2001).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLY-15 AND THR-108.
RC STRAIN=cv. Columbia;
RX PubMed=27803190; DOI=10.1104/pp.16.01252;
RA Mao H., Nakamura M., Viotti C., Grebe M.;
RT "A framework for lateral membrane trafficking and polar tethering of the
RT PEN3 ATP-binding cassette transporter.";
RL Plant Physiol. 172:2245-2260(2016).
CC -!- FUNCTION: Actins are highly conserved proteins that are involved in
CC various types of cell motility and are ubiquitously expressed in all
CC eukaryotic cells (PubMed:11449050). Essential component of cell
CC cytoskeleton; plays an important role in cytoplasmic streaming, cell
CC shape determination, cell division, organelle movement and extension
CC growth (PubMed:11449050). This is considered as one of the vegetative
CC actins which is involved in the regulation of hormone-induced plant
CC cell proliferation and callus formation (PubMed:11449050). Required for
CC the trafficking and endocytic recycling of ABCG36/PEN3 between the
CC trans-Golgi network and the plasma membrane in root epidermal and cap
CC cells (PubMed:27803190). {ECO:0000269|PubMed:11449050,
CC ECO:0000269|PubMed:27803190}.
CC -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a
CC structural filament (F-actin) in the form of a two-stranded helix. The
CC binding of profilin to monomeric G-actin cause the sequestration of
CC actin into profilactin complexes, and prevents the polymerization.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- TISSUE SPECIFICITY: Constitutively expressed at high levels in young
CC expanding vegetative tissues. Also strongly expressed in the hypocotyl
CC and seed coat. Little or no expression is detected in mature pollen
CC sacs, ovules, embryos or seeds.
CC -!- INDUCTION: Differentially regulated in response to exogenous hormone
CC treatment. In particular, auxin is a strong inducer.
CC {ECO:0000269|PubMed:11449050}.
CC -!- DISRUPTION PHENOTYPE: Impaired trafficking and endocytic recycling of
CC ABCG36/PEN3 between the trans-Golgi network and the plasma membrane in
CC root epidermal and cap cells. {ECO:0000269|PubMed:27803190}.
CC -!- MISCELLANEOUS: There are 8 actin genes in A.thaliana.
CC -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
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DR EMBL; U37281; AAA80356.1; -; mRNA.
DR EMBL; U27811; AAB52506.1; -; Genomic_DNA.
DR EMBL; AB016893; BAB09402.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91450.1; -; Genomic_DNA.
DR EMBL; AY062702; AAL32780.1; -; mRNA.
DR EMBL; AY063980; AAL36336.1; -; mRNA.
DR EMBL; AY096397; AAM20037.1; -; mRNA.
DR EMBL; AY114679; AAM47998.1; -; mRNA.
DR EMBL; AY120779; AAM53337.1; -; mRNA.
DR PIR; S68107; S68107.
DR RefSeq; NP_196543.1; NM_121018.4.
DR AlphaFoldDB; P53492; -.
DR SMR; P53492; -.
DR BioGRID; 16119; 11.
DR IntAct; P53492; 11.
DR MINT; P53492; -.
DR STRING; 3702.AT5G09810.1; -.
DR iPTMnet; P53492; -.
DR MetOSite; P53492; -.
DR SwissPalm; P53492; -.
DR PaxDb; P53492; -.
DR PRIDE; P53492; -.
DR ProteomicsDB; 244646; -.
DR EnsemblPlants; AT5G09810.1; AT5G09810.1; AT5G09810.
DR GeneID; 830841; -.
DR Gramene; AT5G09810.1; AT5G09810.1; AT5G09810.
DR KEGG; ath:AT5G09810; -.
DR Araport; AT5G09810; -.
DR TAIR; locus:2178128; AT5G09810.
DR eggNOG; KOG0676; Eukaryota.
DR HOGENOM; CLU_027965_0_2_1; -.
DR InParanoid; P53492; -.
DR OMA; FHTTAER; -.
DR OrthoDB; 649708at2759; -.
DR PhylomeDB; P53492; -.
DR PRO; PR:P53492; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P53492; baseline and differential.
DR Genevisible; P53492; AT.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005856; C:cytoskeleton; ISS:TAIR.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; ISS:TAIR.
DR GO; GO:0051301; P:cell division; IMP:TAIR.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; IMP:UniProtKB.
DR GO; GO:0008104; P:protein localization; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0009733; P:response to auxin; IEP:TAIR.
DR GO; GO:0009416; P:response to light stimulus; IEP:TAIR.
DR GO; GO:0009611; P:response to wounding; IEP:TAIR.
DR GO; GO:0048364; P:root development; IMP:TAIR.
DR GO; GO:0010053; P:root epidermal cell differentiation; IMP:TAIR.
DR GO; GO:0048767; P:root hair elongation; IMP:TAIR.
DR GO; GO:0009845; P:seed germination; IMP:TAIR.
DR InterPro; IPR004000; Actin.
DR InterPro; IPR020902; Actin/actin-like_CS.
DR InterPro; IPR004001; Actin_CS.
DR InterPro; IPR043129; ATPase_NBD.
DR PANTHER; PTHR11937; PTHR11937; 1.
DR Pfam; PF00022; Actin; 1.
DR PRINTS; PR00190; ACTIN.
DR SMART; SM00268; ACTIN; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS00406; ACTINS_1; 1.
DR PROSITE; PS00432; ACTINS_2; 1.
DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Cytoplasm; Cytoskeleton; Nucleotide-binding;
KW Protein transport; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q96292"
FT CHAIN 2..377
FT /note="Actin-7"
FT /id="PRO_0000088892"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q96292"
FT MUTAGEN 15
FT /note="G->E: In act7-9; impaired trafficking and endocytic
FT recycling of ABCG36/PEN3 between the trans-Golgi network
FT and the plasma membrane in root epidermal and cap cells."
FT /evidence="ECO:0000269|PubMed:27803190"
FT MUTAGEN 108
FT /note="T->I: In act7-8; impaired trafficking and endocytic
FT recycling of ABCG36/PEN3 between the trans-Golgi network
FT and the plasma membrane in root epidermal and cap cells."
FT /evidence="ECO:0000269|PubMed:27803190"
SQ SEQUENCE 377 AA; 41736 MW; 0BED4053EDA9F916 CRC64;
MADGEDIQPL VCDNGTGMVK AGFAGDDAPR AVFPSIVGRP RHTGVMVGMG QKDAYVGDEA
QSKRGILTLK YPIEHGIVSN WDDMEKIWHH TFYNELRVAP EEHPVLLTEA PLNPKANREK
MTQIMFETFN VPAMYVAIQA VLSLYASGRT TGIVLDSGDG VSHTVPIYEG YALPHAILRL
DLAGRDLTDS LMKILTERGY MFTTTAEREI VRDIKEKLAY VALDYEQELE TAKSSSSVEK
NYELPDGQVI TIGAERFRCP EVLFQPSLIG MEAPGIHETT YNSIMKCDVD IRKDLYGNIV
LSGGSTMFPG IADRMSKEIT ALAPSSMKIK VVAPPERKYS VWIGGSILAS LSTFQQMWIS
KSEYDESGPS IVHRKCF
