ID   ACT4_ARATH              Reviewed;         377 AA.
AC   P53494;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   05-MAY-2009, entry version 66.
DE   RecName: Full=Actin-4;
GN   Name=ACT4; OrderedLocusNames=At5g59370; ORFNames=F2O15.3;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC   STRAIN=cv. Columbia;
RX   MEDLINE=96367663; PubMed=8771777;
RX   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;
RA   Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL   Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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   [4]
RP   GENE FAMILY ORGANIZATION, AND CHARACTERIZATION.
RC   STRAIN=cv. Columbia;
RX   MEDLINE=97005557; PubMed=8852856;
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
CC       in various types of cell motility and are ubiquitously expressed
CC       in all eukaryotic cells. Essential component of cell cytoskeleton;
CC       plays an important role in cytoplasmic streaming, cell shape
CC       determination, cell division, organelle movement and extension
CC       growth. This is considered 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.
CC       The binding of profilin to monomeric G-actin cause the
CC       sequestration of actin into profilactin complexes, and prevents
CC       the polymerization.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- TISSUE SPECIFICITY: Little or no reproductive-gene expression is
CC       detected in vegetative organs, such as root, stems, leaves, sepals
CC       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.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U27980; AAB39403.1; -; Genomic_DNA.
DR   EMBL; AB025604; BAA97473.1; -; Genomic_DNA.
DR   EMBL; AY088111; AAM65657.1; -; mRNA.
DR   IPI; IPI00547404; -.
DR   PIR; S68108; S68108.
DR   RefSeq; NP_001078769.1; -.
DR   RefSeq; NP_200745.1; -.
DR   UniGene; At.29229; -.
DR   HSSP; P02568; 1MA9.
DR   SMR; P53494; 10-377.
DR   PRIDE; P53494; -.
DR   GeneID; 836056; -.
DR   GenomeReviews; BA000015_GR; AT5G59370.
DR   KEGG; ath:AT5G59370; -.
DR   NMPDR; fig|3702.1.peg.27930; -.
DR   TAIR; At5g59370; -.
DR   OMA; P53494; DARAPIM.
DR   GermOnline; AT5G59370; Arabidopsis thaliana.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR   GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IEA:InterPro.
DR   InterPro; IPR004001; Actin_CS.
DR   InterPro; IPR004000; Actin_like.
DR   PANTHER; PTHR11937; Actin_like; 1.
DR   Pfam; PF00022; Actin; 1.
DR   PRINTS; PR00190; ACTIN.
DR   SMART; SM00268; ACTIN; 1.
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   ATP-binding; Complete proteome; Cytoplasm; Cytoskeleton;
KW   Nucleotide-binding.
FT   CHAIN         1    377       Actin-4.
FT                                /FTId=PRO_0000088890.
FT   CONFLICT    154    154       V -> F (in Ref. 3; AAM65657).
SQ   SEQUENCE   377 AA;  41779 MW;  3BC5B633D2BB088A CRC64;
     MADGEDIQPL VCDNGTGMVK AGFAGDDAPR AVFPSIVGRP RHTGVMVGMG QKDAYVGDEA
     QSKRGILTLK YPIEHGIVNN WDDMEKIWHH TFYNELRVAP EEHPVLLTEA PLNPKANREK
     MTQIMFETFN TPAMYVAIQA VLSLYASGRT TGIVLDSGDG VSHTVPIYEG YALPHAILRL
     DLAGRDLTDH LMKILTERGY SFTTTAEREI VRDMKEKLSY IALDFEQELE TSKTSSSVEK
     SFELPDGQVI TIGAERFRCP EVLFQPSMIG MENPGIHETT YNSIMKCDVD IRKDLYGNIV
     LSGGTTMFGG IGDRMSKEIT ALAPSSMKIK VVAPPERKYS VWIGGSILAS LSTFQQMWIA
     KAEYDESGPS IVHRKCF
//