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Q96293

- ACT8_ARATH

UniProt

Q96293 - ACT8_ARATH

Protein

Actin-8

Gene

ACT8

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 2 (25 Nov 2002)
      Previous versions | rss
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    Functioni

    Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Essential component of cell cytoskeleton; plays an important role in cytoplasmic streaming, cell shape determination, cell division, organelle movement and extension growth. This is considered as one of the vegetative actins.

    Enzyme regulationi

    Subject to negative translational control in pollen.

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. copper ion binding Source: TAIR

    GO - Biological processi

    1. response to salt stress Source: TAIR
    2. root hair cell tip growth Source: TAIR

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Actin-8
    Gene namesi
    Name:ACT8
    Ordered Locus Names:At1g49240
    ORF Names:F27J15.1
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 1

    Organism-specific databases

    TAIRiAT1G49240.

    Subcellular locationi

    GO - Cellular componenti

    1. chloroplast Source: TAIR
    2. chloroplast envelope Source: TAIR
    3. chloroplast stroma Source: TAIR
    4. cytoskeleton Source: UniProtKB-SubCell
    5. cytosol Source: TAIR
    6. plasma membrane Source: TAIR
    7. plasmodesma Source: TAIR
    8. vacuole Source: TAIR

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 377377Actin-8PRO_0000088893Add
    BLAST

    Proteomic databases

    PaxDbiQ96293.
    PRIDEiQ96293.

    2D gel databases

    SWISS-2DPAGEP99055.

    Expressioni

    Tissue specificityi

    Strongly expressed in nearly all vegetative tissues, and levels remain high in older tissues. Little or no expression is detected in mature pollen sacs, ovules, embryos or seeds.

    Gene expression databases

    GenevestigatoriQ96293.

    Interactioni

    Subunit structurei

    Polymerization of globular actin (G-actin) leads to a structural filament (F-actin) in the form of a two-stranded helix. The binding of profilin to monomeric G-actin cause the sequestration of actin into profilactin complexes, and prevents the polymerization.

    Protein-protein interaction databases

    BioGridi26572. 5 interactions.
    IntActiQ96293. 2 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ96293.
    SMRiQ96293. Positions 10-377.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the actin family.Curated

    Phylogenomic databases

    eggNOGiCOG5277.
    HOGENOMiHOG000233340.
    InParanoidiQ96293.
    KOiK10355.
    OMAiPPFYRIP.
    PhylomeDBiQ96293.

    Family and domain databases

    InterProiIPR004000. Actin-related.
    IPR020902. Actin/actin-like_CS.
    IPR004001. Actin_CS.
    [Graphical view]
    PANTHERiPTHR11937. PTHR11937. 1 hit.
    PfamiPF00022. Actin. 1 hit.
    [Graphical view]
    PRINTSiPR00190. ACTIN.
    SMARTiSM00268. ACTIN. 1 hit.
    [Graphical view]
    PROSITEiPS00406. ACTINS_1. 1 hit.
    PS00432. ACTINS_2. 1 hit.
    PS01132. ACTINS_ACT_LIKE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q96293-1 [UniParc]FASTAAdd to Basket

    « Hide

    MADADDIQPI VCDNGTGMVK AGFAGDDAPR AVFPSVVGRP RHHGVMVGMN    50
    QKDAYVGDEA QSKRGILTLK YPIEHGVVSN WDDMEKIWHH TFYNELRIAP 100
    EEHPVLLTEA PLNPKANREK MTQIMFETFN SPAMYVAIQA VLSLYASGRT 150
    TGIVLDSGDG VSHTVPIYEG FSLPHAILRL DLAGRDLTDY LMKILTERGY 200
    MFTTTAEREI VRDIKEKLSF VAVDYEQEME TSKTSSSIEK NYELPDGQVI 250
    TIGAERFRCP EVLFQPSFVG MEAAGIHETT YNSIMKCDVD IRKDLYGNIV 300
    LSGGTTMFSG IADRMSKEIT ALAPSSMKIK VVAPPERKYS VWIGGSILAS 350
    LSTFQQMWIS KAEYDEAGPG IVHRKCF 377
    Length:377
    Mass (Da):41,863
    Last modified:November 25, 2002 - v2
    Checksum:iE9553D52F3C6D7B4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti309 – 3091S → L in AAC49523. (PubMed:8758981)Curated
    Sequence conflicti320 – 3201T → R in CAA79065. (PubMed:8281187)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U42007 Genomic DNA. Translation: AAC49523.1.
    AC016041 Genomic DNA. Translation: AAF69724.1.
    CP002684 Genomic DNA. Translation: AEE32408.1.
    AF370302 mRNA. Translation: AAK44117.1.
    AY063089 mRNA. Translation: AAL34263.1.
    AY124004 mRNA. Translation: AAM74512.1.
    Z17778 mRNA. Translation: CAA79065.1.
    RefSeqiNP_175350.1. NM_103814.3.
    UniGeneiAt.24689.

    Genome annotation databases

    EnsemblPlantsiAT1G49240.1; AT1G49240.1; AT1G49240.
    GeneIDi841347.
    KEGGiath:AT1G49240.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U42007 Genomic DNA. Translation: AAC49523.1 .
    AC016041 Genomic DNA. Translation: AAF69724.1 .
    CP002684 Genomic DNA. Translation: AEE32408.1 .
    AF370302 mRNA. Translation: AAK44117.1 .
    AY063089 mRNA. Translation: AAL34263.1 .
    AY124004 mRNA. Translation: AAM74512.1 .
    Z17778 mRNA. Translation: CAA79065.1 .
    RefSeqi NP_175350.1. NM_103814.3.
    UniGenei At.24689.

    3D structure databases

    ProteinModelPortali Q96293.
    SMRi Q96293. Positions 10-377.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 26572. 5 interactions.
    IntActi Q96293. 2 interactions.

    2D gel databases

    SWISS-2DPAGE P99055.

    Proteomic databases

    PaxDbi Q96293.
    PRIDEi Q96293.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT1G49240.1 ; AT1G49240.1 ; AT1G49240 .
    GeneIDi 841347.
    KEGGi ath:AT1G49240.

    Organism-specific databases

    TAIRi AT1G49240.

    Phylogenomic databases

    eggNOGi COG5277.
    HOGENOMi HOG000233340.
    InParanoidi Q96293.
    KOi K10355.
    OMAi PPFYRIP.
    PhylomeDBi Q96293.

    Gene expression databases

    Genevestigatori Q96293.

    Family and domain databases

    InterProi IPR004000. Actin-related.
    IPR020902. Actin/actin-like_CS.
    IPR004001. Actin_CS.
    [Graphical view ]
    PANTHERi PTHR11937. PTHR11937. 1 hit.
    Pfami PF00022. Actin. 1 hit.
    [Graphical view ]
    PRINTSi PR00190. ACTIN.
    SMARTi SM00268. ACTIN. 1 hit.
    [Graphical view ]
    PROSITEi PS00406. ACTINS_1. 1 hit.
    PS00432. ACTINS_2. 1 hit.
    PS01132. ACTINS_ACT_LIKE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Strong, constitutive expression of the Arabidopsis ACT2/ACT8 actin subclass in vegetative tissues."
      An Y.-Q., McDowell J.M., Huang S., McKinney E.C., Chambliss S., Meagher R.B.
      Plant J. 10:107-121(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
      Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
      , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
      Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    3. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
      , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 318-377.
      Strain: cv. Columbia.
      Tissue: Green siliques.
    6. "Structure and evolution of the actin gene family in Arabidopsis thaliana."
      McDowell J.M., Huang S., McKinney E.C., An Y.-Q., Meagher R.B.
      Genetics 142:587-602(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENE FAMILY ORGANIZATION, CHARACTERIZATION.
      Strain: cv. Columbia.

    Entry informationi

    Entry nameiACT8_ARATH
    AccessioniPrimary (citable) accession number: Q96293
    Secondary accession number(s): Q41933, Q9M9C2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 25, 2002
    Last sequence update: November 25, 2002
    Last modified: October 1, 2014
    This is version 108 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    There are 8 actin genes in A.thaliana.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3