ACT8_ARATH
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 25-MAY-2022, entry version 151.
DE RecName: Full=Actin-8;
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 -!- 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.AT1G49240.1; -.
DR iPTMnet; Q96293; -.
DR MetOSite; Q96293; -.
DR SWISS-2DPAGE; P99055; -.
DR PaxDb; Q96293; -.
DR PRIDE; Q96293; -.
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; locus:2028416; AT1G49240.
DR eggNOG; KOG0676; Eukaryota.
DR HOGENOM; CLU_027965_0_2_1; -.
DR InParanoid; Q96293; -.
DR OMA; ERFCASE; -.
DR OrthoDB; 649708at2759; -.
DR PhylomeDB; Q96293; -.
DR PRO; PR:Q96293; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q96293; baseline and differential.
DR Genevisible; Q96293; 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; 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:0003729; F:mRNA binding; HDA:TAIR.
DR GO; GO:0048768; P:root hair cell tip growth; 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-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
