ID   ACT1_ARATH              Reviewed;         377 AA.
AC   P0CJ46; P10671; P53493; Q9M351;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 1.
DT   25-MAY-2022, entry version 66.
DE   RecName: Full=Actin-1;
GN   Name=ACT1; Synonyms=AAC1; OrderedLocusNames=At2g37620; ORFNames=F13M22.12;
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=3410320; DOI=10.1016/0378-1119(88)90461-1;
RA   Nairn C.J., Winesett L., Ferl R.J.;
RT   "Nucleotide sequence of an actin gene from Arabidopsis thaliana.";
RL   Gene 65:247-257(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=8597657; DOI=10.2307/3870065;
RA   An Y.-Q., Huang S., McDowell J.M., McKinney E.C., Meagher R.B.;
RT   "Conserved expression of the Arabidopsis ACT1 and ACT3 actin subclass in
RT   organ primordia and mature pollen.";
RL   Plant Cell 8:15-30(1996).
RN   [3]
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   [4]
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   [5]
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   [6]
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).
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 reproductive actins.
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: Preferentially expressed in mature pollen, pollen
CC       tubes, young embryo sac, and organ primordia. Little or no
CC       reproductive-gene expression is detected in vegetative organs, such as
CC       root, stems, leaves, sepals and petals.
CC   -!- MISCELLANEOUS: There are 8 actin genes in A.thaliana.
CC   -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC23632.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; M20016; AAA32727.1; -; Genomic_DNA.
DR   EMBL; U39449; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC004684; AAC23632.2; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002685; AEC09426.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC09427.1; -; Genomic_DNA.
DR   EMBL; CP002685; ANM62357.1; -; Genomic_DNA.
DR   EMBL; CP002685; ANM62358.1; -; Genomic_DNA.
DR   EMBL; AY074873; AAL75893.1; -; mRNA.
DR   EMBL; AY093784; AAM10400.1; -; mRNA.
DR   PIR; JA0066; ATMUM1.
DR   RefSeq; NP_001031504.1; NM_001036427.3.
DR   RefSeq; NP_001324518.1; NM_001336664.1.
DR   RefSeq; NP_001324519.1; NM_001336665.1.
DR   RefSeq; NP_001326881.1; NM_001339629.1.
DR   RefSeq; NP_566988.1; NM_115235.4.
DR   RefSeq; NP_850284.1; NM_179953.3.
DR   AlphaFoldDB; P0CJ46; -.
DR   SMR; P0CJ46; -.
DR   BioGRID; 3683; 8.
DR   BioGRID; 9859; 2.
DR   IntAct; P0CJ46; 6.
DR   STRING; 3702.AT2G37620.1; -.
DR   iPTMnet; P0CJ46; -.
DR   PaxDb; P0CJ46; -.
DR   PRIDE; P0CJ46; -.
DR   EnsemblPlants; AT2G37620.1; AT2G37620.1; AT2G37620.
DR   EnsemblPlants; AT2G37620.2; AT2G37620.2; AT2G37620.
DR   EnsemblPlants; AT2G37620.3; AT2G37620.3; AT2G37620.
DR   EnsemblPlants; AT2G37620.4; AT2G37620.4; AT2G37620.
DR   EnsemblPlants; AT3G53750.1; AT3G53750.1; AT3G53750.
DR   EnsemblPlants; AT3G53750.2; AT3G53750.2; AT3G53750.
DR   GeneID; 818339; -.
DR   GeneID; 824542; -.
DR   Gramene; AT2G37620.1; AT2G37620.1; AT2G37620.
DR   Gramene; AT2G37620.2; AT2G37620.2; AT2G37620.
DR   Gramene; AT2G37620.3; AT2G37620.3; AT2G37620.
DR   Gramene; AT2G37620.4; AT2G37620.4; AT2G37620.
DR   Gramene; AT3G53750.1; AT3G53750.1; AT3G53750.
DR   Gramene; AT3G53750.2; AT3G53750.2; AT3G53750.
DR   KEGG; ath:AT2G37620; -.
DR   KEGG; ath:AT3G53750; -.
DR   Araport; AT2G37620; -.
DR   TAIR; locus:2040656; AT2G37620.
DR   eggNOG; KOG0676; Eukaryota.
DR   HOGENOM; CLU_027965_0_2_1; -.
DR   InParanoid; P0CJ46; -.
DR   OMA; NILPICC; -.
DR   OrthoDB; 649708at2759; -.
DR   PhylomeDB; P0CJ46; -.
DR   PRO; PR:P0CJ46; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; P0CJ46; baseline and differential.
DR   Genevisible; P0CJ46; AT.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005783; C:endoplasmic reticulum; 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:0048589; P:developmental 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; ATP-binding; Cytoplasm; Cytoskeleton; Nucleotide-binding;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q96292"
FT   CHAIN           2..377
FT                   /note="Actin-1"
FT                   /id="PRO_0000088888"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96292"
FT   CONFLICT        354
FT                   /note="F -> L (in Ref. 1; AAA32727 and 2; U39449)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   377 AA;  41798 MW;  44D749AD5A9671BB CRC64;
     MADGEDIQPL VCDNGTGMVK AGFAGDDAPR AVFPSIVGRP RHTGVMVGMG QKDAYVGDEA
     QSKRGILTLK YPIEHGIVNN WDDMEKIWHH TFYNELRVAP EEHPILLTEA PLNPKANREK
     MTQIMFETFN APAMYVAIQA VLSLYASGRT TGIVLDSGDG VSHTVPIYEG YALPHAILRL
     DLAGRDLTDA LMKILTERGY SFTTTAEREI VRDIKEKLCY IALDYEQELE TAKTSSSVEK
     NYELPDGQVI TIGSERFRCP EVLYQPSMIG MENAGIHETT YNSIMKCDVD IRKDLYGNIV
     LSGGTTMFPG IADRMSKEIT ALAPSSMKIK VVAPPERKYS VWIGGSILAS LSTFQQMWIA
     KAEYDESGPS IVHRKCF