ID   ACT2_ARATH              Reviewed;         377 AA.
AC   Q96292; Q42056;
DT   25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   25-MAY-2022, entry version 157.
DE   RecName: Full=Actin-2;
GN   Name=ACT2; OrderedLocusNames=At3g18780; ORFNames=MVE11.16;
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 [GENOMIC DNA].
RX   PubMed=8758981; DOI=10.1046/j.1365-313x.1996.10010107.x;
RA   An Y.-Q., McDowell J.M., Huang S., McKinney E.C., Chambliss S.,
RA   Meagher R.B.;
RT   "Strong, constitutive expression of the Arabidopsis ACT2/ACT8 actin
RT   subclass in vegetative tissues.";
RL   Plant J. 10:107-121(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT   features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:131-135(2000).
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].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-63.
RC   STRAIN=cv. Columbia; TISSUE=Seedling;
RX   PubMed=8281187; DOI=10.1046/j.1365-313x.1993.04061051.x;
RA   Hoefte H., Desprez T., Amselem J., Chiapello H., Rouze P., Caboche M.,
RA   Moisan A., Jourjon M.-F., Charpenteau J.-L., Berthomieu P., Guerrier D.,
RA   Giraudat J., Quigley F., Thomas F., Yu D.-Y., Mache R., Raynal M.,
RA   Cooke R., Grellet F., Delseny M., Parmentier Y., de Marcillac G., Gigot C.,
RA   Fleck J., Philipps G., Axelos M., Bardet C., Tremousaygue D., Lescure B.;
RT   "An inventory of 1152 expressed sequence tags obtained by partial
RT   sequencing of cDNAs from Arabidopsis thaliana.";
RL   Plant J. 4:1051-1061(1993).
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   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: Actins are highly conserved proteins that are involved in
CC       various types of cell motility and are ubiquitously expressed in all
CC       eukaryotic cells. Essential component of cell cytoskeleton; plays an
CC       important role in cytoplasmic streaming, cell shape determination, cell
CC       division, organelle movement and extension growth. This is considered
CC       as one of the vegetative actins.
CC   -!- ACTIVITY REGULATION: Subject to negative translational control in
CC       pollen.
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   -!- INTERACTION:
CC       Q96292; Q42525: HXK1; NbExp=2; IntAct=EBI-1644538, EBI-1644489;
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=Q96292-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Strongly expressed in nearly all vegetative
CC       tissues, and remains high in older tissues. Little or no expression is
CC       detected in mature pollen sacs, ovules, embryos or seeds.
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; U41998; AAB37098.1; -; Genomic_DNA.
DR   EMBL; AB026654; BAB01806.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE76148.1; -; Genomic_DNA.
DR   EMBL; CP002686; ANM65915.1; -; Genomic_DNA.
DR   EMBL; AF428330; AAL16260.1; -; mRNA.
DR   EMBL; AY064043; AAL36399.1; -; mRNA.
DR   EMBL; AY096381; AAM20022.1; -; mRNA.
DR   EMBL; AY087751; AAM65287.1; -; mRNA.
DR   EMBL; Z25952; CAA81112.1; -; mRNA.
DR   RefSeq; NP_001327851.1; NM_001338359.1. [Q96292-1]
DR   RefSeq; NP_188508.1; NM_112764.4. [Q96292-1]
DR   AlphaFoldDB; Q96292; -.
DR   SMR; Q96292; -.
DR   BioGRID; 6744; 15.
DR   IntAct; Q96292; 9.
DR   STRING; 3702.AT3G18780.2; -.
DR   iPTMnet; Q96292; -.
DR   PaxDb; Q96292; -.
DR   PRIDE; Q96292; -.
DR   ProteomicsDB; 244709; -. [Q96292-1]
DR   EnsemblPlants; AT3G18780.2; AT3G18780.2; AT3G18780. [Q96292-1]
DR   EnsemblPlants; AT3G18780.3; AT3G18780.3; AT3G18780. [Q96292-1]
DR   GeneID; 821411; -.
DR   Gramene; AT3G18780.2; AT3G18780.2; AT3G18780. [Q96292-1]
DR   Gramene; AT3G18780.3; AT3G18780.3; AT3G18780. [Q96292-1]
DR   KEGG; ath:AT3G18780; -.
DR   Araport; AT3G18780; -.
DR   TAIR; locus:2093954; AT3G18780.
DR   eggNOG; KOG0676; Eukaryota.
DR   HOGENOM; CLU_027965_0_2_1; -.
DR   InParanoid; Q96292; -.
DR   OMA; AGIHENT; -.
DR   PhylomeDB; Q96292; -.
DR   PRO; PR:Q96292; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q96292; baseline and differential.
DR   Genevisible; Q96292; AT.
DR   GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005634; C:nucleus; HDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:TAIR.
DR   GO; GO:0009735; P:response to cytokinin; IEP:TAIR.
DR   GO; GO:0010218; P:response to far red light; IEP:TAIR.
DR   GO; GO:0009644; P:response to high light intensity; IEP:TAIR.
DR   GO; GO:0010114; P:response to red light; IEP:TAIR.
DR   GO; GO:0010053; P:root epidermal cell differentiation; IMP:TAIR.
DR   GO; GO:0048768; P:root hair cell tip growth; IMP:TAIR.
DR   GO; GO:0048767; P:root hair elongation; 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; Alternative splicing; ATP-binding; Cytoplasm; Cytoskeleton;
KW   Nucleotide-binding; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   CHAIN           2..377
FT                   /note="Actin-2"
FT                   /id="PRO_0000088889"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:22223895"
SQ   SEQUENCE   377 AA;  41877 MW;  F9E53D17F333D786 CRC64;
     MAEADDIQPI VCDNGTGMVK AGFAGDDAPR AVFPSVVGRP RHHGVMVGMN QKDAYVGDEA
     QSKRGILTLK YPIEHGVVSN WDDMEKIWHH TFYNELRIAP EEHPVLLTEA PLNPKANREK
     MTQIMFETFN SPAMYVAIQA VLSLYASGRT TGIVLDSGDG VSHTVPIYEG FSLPHAILRL
     DLAGRDLTDY LMKILTERGY MFTTTAEREI VRDIKEKLSF VAVDYEQEME TSKTSSSIEK
     NYELPDGQVI TIGAERFRCP EVLFQPSFVG MEAAGIHETT YNSIMKCDVD IRKDLYGNIV
     LSGGTTMFSG IADRMSKEIT ALAPSSMKIK VVAPPERKYS VWIGGSILAS LSTFQQMWIS
     KAEYDEAGPG IVHRKCF