ACT12_ARATH
ID ACT12_ARATH Reviewed; 377 AA.
AC P53497;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Actin-12;
GN Name=ACT12; OrderedLocusNames=At3g46520; ORFNames=F12A12.40;
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=8771777; DOI=10.1046/j.1365-313x.1996.10020189.x;
RA Huang S., An Y.-Q., McDowell J.M., McKinney E.C., Meagher R.B.;
RT "The Arabidopsis thaliana ACT4/ACT12 actin gene subclass is strongly
RT expressed throughout pollen development.";
RL Plant J. 10:189-202(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 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: Displays particular expression in the root cap and
CC pericycle tissues associated with lateral root development. Little or
CC no reproductive-gene expression is detected in vegetative organs, such
CC as stems, leaves, sepals and petals.
CC -!- DEVELOPMENTAL STAGE: Expressed primarily in pollen.
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; U27982; AAB39405.1; -; Genomic_DNA.
DR EMBL; AL133314; CAB62322.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78168.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65018.1; -; Genomic_DNA.
DR EMBL; BT003847; AAO41897.1; -; mRNA.
DR EMBL; BT005073; AAO50606.1; -; mRNA.
DR PIR; S68110; S68110.
DR RefSeq; NP_001327017.1; NM_001339262.1.
DR RefSeq; NP_190236.1; NM_114519.3.
DR AlphaFoldDB; P53497; -.
DR SMR; P53497; -.
DR BioGRID; 9125; 17.
DR IntAct; P53497; 12.
DR STRING; 3702.AT3G46520.1; -.
DR PaxDb; P53497; -.
DR PRIDE; P53497; -.
DR ProteomicsDB; 244362; -.
DR EnsemblPlants; AT3G46520.1; AT3G46520.1; AT3G46520.
DR EnsemblPlants; AT3G46520.2; AT3G46520.2; AT3G46520.
DR GeneID; 823805; -.
DR Gramene; AT3G46520.1; AT3G46520.1; AT3G46520.
DR Gramene; AT3G46520.2; AT3G46520.2; AT3G46520.
DR KEGG; ath:AT3G46520; -.
DR Araport; AT3G46520; -.
DR TAIR; locus:2075160; AT3G46520.
DR eggNOG; KOG0676; Eukaryota.
DR HOGENOM; CLU_027965_0_2_1; -.
DR InParanoid; P53497; -.
DR OMA; WICKSEY; -.
DR OrthoDB; 649708at2759; -.
DR PhylomeDB; P53497; -.
DR PRO; PR:P53497; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P53497; baseline and differential.
DR Genevisible; P53497; 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:0005739; C:mitochondrion; 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-12"
FT /id="PRO_0000088896"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q96292"
SQ SEQUENCE 377 AA; 41795 MW; BD1C7C523DBB167B CRC64;
MADGEDIQPL VCDNGTGMVK AGFAGDDAPR AVFPSIVGRP RHTGVMVGMG QKDAYVGDEA
QSKRGILTLK YPIEHGIVNN WDDMEKIWHH TFYNELRVAP EEHPVLLTEA PLNPKANREK
MTQIMFETFN TPAMYVAIQA VLSLYASGRT TGIVLDSGDG VSHTVPIYEG YALPHAILRL
DLAGRDLTDH LMKILTERGY SFTTTAEREI VRDMKEKLSY IALDYEQELE TSKTSSSVEK
SFELPDGQVI TIGAERFRCP EVLFQPSMIG MENPGIHETT YNSIMKCDVD IRKDLYGNIV
LSGGTTMFGG IGDRMSKEIT ALAPSSMKIK VVAPPERKYS VWIGGSILAS LSTFQQMWIA
KAEYDESGPS IVHRKCF
