ACT11_ARATH
ID ACT11_ARATH Reviewed; 377 AA.
AC P53496;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 139.
DE RecName: Full=Actin-11;
GN Name=ACT11; OrderedLocusNames=At3g12110;
GN ORFNames=T21B14.7, T21B14_108, T23B7.5;
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=9037165; DOI=10.1023/a:1005741514764;
RA Huang S., An Y.-Q., McDowell J.M., McKinney E.C., Meagher R.B.;
RT "The Arabidopsis ACT11 actin gene is strongly expressed in tissues of the
RT emerging inflorescence, pollen, and developing ovules.";
RL Plant Mol. Biol. 33:125-139(1997).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
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 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 [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).
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 young and expanding
CC tissues, floral organ primordia, developing seeds, and emerging
CC inflorescence. Displays a very high expression level in mature pollen
CC and pollen tubes. Little or no reproductive-gene expression is detected
CC in vegetative organs, such as root, stems, leaves, sepals and petals.
CC -!- DEVELOPMENTAL STAGE: Significantly expressed during endosperm, ovule
CC and embryo development.
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; U27981; AAB39404.1; -; Genomic_DNA.
DR EMBL; AC069473; AAG51045.1; -; Genomic_DNA.
DR EMBL; AP002063; BAB01959.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75151.1; -; Genomic_DNA.
DR EMBL; BT005593; AAO64013.1; -; mRNA.
DR EMBL; AY087740; AAM65277.1; -; mRNA.
DR PIR; S68109; S68109.
DR RefSeq; NP_187818.1; NM_112046.4.
DR AlphaFoldDB; P53496; -.
DR SMR; P53496; -.
DR BioGRID; 5719; 7.
DR IntAct; P53496; 6.
DR STRING; 3702.AT3G12110.1; -.
DR iPTMnet; P53496; -.
DR MetOSite; P53496; -.
DR PaxDb; P53496; -.
DR PRIDE; P53496; -.
DR ProteomicsDB; 244672; -.
DR EnsemblPlants; AT3G12110.1; AT3G12110.1; AT3G12110.
DR GeneID; 820385; -.
DR Gramene; AT3G12110.1; AT3G12110.1; AT3G12110.
DR KEGG; ath:AT3G12110; -.
DR Araport; AT3G12110; -.
DR TAIR; locus:2099302; AT3G12110.
DR eggNOG; KOG0676; Eukaryota.
DR HOGENOM; CLU_027965_0_2_1; -.
DR InParanoid; P53496; -.
DR OMA; IMELEWS; -.
DR OrthoDB; 649708at2759; -.
DR PhylomeDB; P53496; -.
DR PRO; PR:P53496; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P53496; baseline and differential.
DR Genevisible; P53496; 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; ISS:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; 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-11"
FT /id="PRO_0000088895"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q96292"
SQ SEQUENCE 377 AA; 41675 MW; 93BAA4D67DA3EE61 CRC64;
MADGEDIQPL VCDNGTGMVK AGFAGDDAPR AVFPSIVGRP RHTGVMVGMG QKDAYVGDEA
QSKRGILTLK YPIEHGIVSN WDDMEKIWHH TFYNELRVAP EEHPVLLTEA PLNPKANREK
MTQIMFETFN TPAMYVAIQA VLSLYASGRT TGIVLDSGDG VSHTVPIYEG YALPHAILRL
DLAGRDLTDY LMKILTERGY SFTTSAEREI VRDVKEKLAY IALDYEQEME TANTSSSVEK
SYELPDGQVI TIGGERFRCP EVLFQPSLVG MEAAGIHETT YNSIMKCDVD IRKDLYGNIV
LSGGTTMFPG IADRMSKEIT ALAPSSMKIK VVAPPERKYS VWIGGSILAS LSTFQQMWIA
KAEYDESGPS IVHRKCF
