ID   ACT8_ARATH              Reviewed;         377 AA.
AC   Q96293; Q41933; Q9M9C2;
DT   25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2002, sequence version 2.
DT   27-MAR-2024, entry version 159.
DE   RecName: Full=Actin-8;
DE            EC=3.6.4.- {ECO:0000250|UniProtKB:P68137};
GN   Name=ACT8; OrderedLocusNames=At1g49240; ORFNames=F27J15.1;
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 [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=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(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] OF 318-377.
RC   STRAIN=cv. Columbia; TISSUE=Green siliques;
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   [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 vegetative actins.
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   -!- 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   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- TISSUE SPECIFICITY: Strongly expressed in nearly all vegetative
CC       tissues, and levels remain high in older tissues. Little or no
CC       expression is 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; U42007; AAC49523.1; -; Genomic_DNA.
DR   EMBL; AC016041; AAF69724.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE32408.1; -; Genomic_DNA.
DR   EMBL; AF370302; AAK44117.1; -; mRNA.
DR   EMBL; AY063089; AAL34263.1; -; mRNA.
DR   EMBL; AY124004; AAM74512.1; -; mRNA.
DR   EMBL; Z17778; CAA79065.1; -; mRNA.
DR   RefSeq; NP_175350.1; NM_103814.4.
DR   AlphaFoldDB; Q96293; -.
DR   SMR; Q96293; -.
DR   BioGRID; 26572; 6.
DR   IntAct; Q96293; 2.
DR   MINT; Q96293; -.
DR   STRING; 3702.Q96293; -.
DR   iPTMnet; Q96293; -.
DR   MetOSite; Q96293; -.
DR   PaxDb; 3702-AT1G49240-1; -.
DR   ProteomicsDB; 244692; -.
DR   EnsemblPlants; AT1G49240.1; AT1G49240.1; AT1G49240.
DR   GeneID; 841347; -.
DR   Gramene; AT1G49240.1; AT1G49240.1; AT1G49240.
DR   KEGG; ath:AT1G49240; -.
DR   Araport; AT1G49240; -.
DR   TAIR; AT1G49240; ACT8.
DR   eggNOG; KOG0676; Eukaryota.
DR   HOGENOM; CLU_027965_0_2_1; -.
DR   InParanoid; Q96293; -.
DR   OMA; ERFCASE; -.
DR   OrthoDB; 337309at2759; -.
DR   PhylomeDB; Q96293; -.
DR   PRO; PR:Q96293; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q96293; 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; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005634; C:nucleus; HDA:TAIR.
DR   GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR   GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005507; F:copper ion binding; HDA:TAIR.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003729; F:mRNA binding; HDA:TAIR.
DR   GO; GO:0048768; P:root hair cell tip growth; 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:SF572; ACTIN-12-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   SWISS-2DPAGE; P99055; -.
DR   Genevisible; Q96293; AT.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Cytoplasm; Cytoskeleton; Hydrolase;
KW   Nucleotide-binding; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q96292"
FT   CHAIN           2..377
FT                   /note="Actin-8"
FT                   /id="PRO_0000088893"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96292"
FT   CONFLICT        309
FT                   /note="S -> L (in Ref. 1; AAC49523)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        320
FT                   /note="T -> R (in Ref. 5; CAA79065)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   377 AA;  41863 MW;  E9553D52F3C6D7B4 CRC64;
     MADADDIQPI 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
//