ACT3_ARATH
ID ACT3_ARATH Reviewed; 377 AA.
AC P0CJ47; 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 63.
DE RecName: Full=Actin-3;
GN Name=ACT3; OrderedLocusNames=At3g53750; ORFNames=F5K20_50;
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].
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 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=CAB88337.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U39480; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL132960; CAB88337.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE79138.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64878.1; -; Genomic_DNA.
DR EMBL; AY049293; AAK83635.1; -; mRNA.
DR EMBL; BT002257; AAN72268.1; -; mRNA.
DR EMBL; AY086557; AAM63620.1; -; mRNA.
DR PIR; S68112; S68112.
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; P0CJ47; -.
DR SMR; P0CJ47; -.
DR BioGRID; 3683; 8.
DR BioGRID; 9859; 2.
DR IntAct; P0CJ47; 3.
DR PRIDE; P0CJ47; -.
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; AT3G53750; -.
DR TAIR; locus:2084410; AT3G53750.
DR HOGENOM; CLU_027965_0_2_1; -.
DR InParanoid; P0CJ47; -.
DR OMA; NILPICC; -.
DR OrthoDB; 649708at2759; -.
DR PhylomeDB; P0CJ47; -.
DR PRO; PR:P0CJ47; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P0CJ47; baseline and differential.
DR Genevisible; P0CJ47; AT.
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:0009505; C:plant-type cell wall; 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 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-3"
FT /id="PRO_0000403937"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q96292"
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
