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   27-MAR-2024, entry version 152.
DE   RecName: Full=Actin-7 {ECO:0000303|PubMed:8754679};
DE            EC=3.6.4.- {ECO:0000250|UniProtKB:P68137};
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=10.1105/tpc.010026;
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000250|UniProtKB:P68137};
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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.P53492; -.
DR   iPTMnet; P53492; -.
DR   MetOSite; P53492; -.
DR   SwissPalm; P53492; -.
DR   PaxDb; 3702-AT5G09810-1; -.
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; AT5G09810; ACT7.
DR   eggNOG; KOG0676; Eukaryota.
DR   HOGENOM; CLU_027965_0_2_1; -.
DR   InParanoid; P53492; -.
DR   OMA; FHTTAER; -.
DR   OrthoDB; 337309at2759; -.
DR   PhylomeDB; P53492; -.
DR   PRO; PR:P53492; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; P53492; baseline and differential.
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:0016787; F:hydrolase activity; 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   CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   InterPro; IPR004000; Actin.
DR   InterPro; IPR020902; Actin/actin-like_CS.
DR   InterPro; IPR004001; Actin_CS.
DR   InterPro; IPR043129; ATPase_NBD.
DR   PANTHER; PTHR11937; ACTIN; 1.
DR   PANTHER; PTHR11937:SF574; ACTIN FAMILY PROTEIN-RELATED; 1.
DR   Pfam; PF00022; Actin; 1.
DR   PRINTS; PR00190; ACTIN.
DR   SMART; SM00268; ACTIN; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   PROSITE; PS00406; ACTINS_1; 1.
DR   PROSITE; PS00432; ACTINS_2; 1.
DR   PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
DR   Genevisible; P53492; AT.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Cytoplasm; Cytoskeleton; Hydrolase;
KW   Nucleotide-binding; 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
//