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P63270

- ACTH_CHICK

UniProt

P63270 - ACTH_CHICK

Protein

Actin, gamma-enteric smooth muscle

Gene

ACTG2

Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 62 (01 Oct 2014)
      Sequence version 1 (11 Oct 2004)
      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.

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW

    Keywords - Molecular functioni

    Muscle protein

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Actin, gamma-enteric smooth muscle
    Alternative name(s):
    Alpha-actin-3
    Gamma-2-actin
    Smooth muscle gamma-actin
    Gene namesi
    Name:ACTG2
    Synonyms:ACTA3, ACTSG
    OrganismiGallus gallus (Chicken)
    Taxonomic identifieri9031 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
    ProteomesiUP000000539: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-KW
    2. cytoskeleton Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei1 – 22Removed in mature formBy similarityPRO_0000000754
    Chaini3 – 376374Actin, gamma-enteric smooth musclePRO_0000000755Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei3 – 31N-acetylglutamateBy similarity
    Modified residuei45 – 451Methionine (R)-sulfoxideBy similarity
    Modified residuei48 – 481Methionine (R)-sulfoxideBy similarity

    Post-translational modificationi

    Oxidation of Met-45 and Met-48 by MICALs (MICAL1, MICAL2 or MICAL3) to form methionine sulfoxide promotes actin filament depolymerization. MICAL1 and MICAL2 produce the (R)-S-oxide form. The (R)-S-oxide form is reverted by MSRB1 and MSRB2, which promote actin repolymerization By similarity.By similarity

    Keywords - PTMi

    Acetylation, Oxidation

    Proteomic databases

    PRIDEiP63270.

    Miscellaneous databases

    PMAP-CutDBP63270.

    Interactioni

    Subunit structurei

    Polymerization of globular actin (G-actin) leads to a structural filament (F-actin) in the form of a two-stranded helix. Each actin can bind to 4 others.

    Protein-protein interaction databases

    BioGridi676350. 1 interaction.

    Structurei

    Secondary structure

    1
    376
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi9 – 135
    Beta strandi15 – 228
    Beta strandi29 – 335
    Beta strandi36 – 416
    Beta strandi43 – 453
    Beta strandi54 – 563
    Helixi57 – 615
    Helixi63 – 653
    Beta strandi66 – 694
    Helixi80 – 9213
    Turni93 – 953
    Helixi99 – 1013
    Beta strandi104 – 1085
    Helixi114 – 12613
    Beta strandi131 – 1377
    Helixi138 – 1458
    Beta strandi151 – 1566
    Beta strandi161 – 1677
    Helixi173 – 1753
    Beta strandi177 – 1793
    Helixi183 – 19614
    Helixi204 – 21714
    Helixi224 – 23310
    Beta strandi239 – 2424
    Beta strandi248 – 2536
    Helixi254 – 2607
    Turni261 – 2633
    Helixi265 – 2684
    Helixi275 – 28511
    Helixi290 – 2956
    Beta strandi298 – 3036
    Helixi304 – 3063
    Helixi310 – 31910
    Turni334 – 3374
    Helixi339 – 34911
    Helixi352 – 3554
    Helixi360 – 3645

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3W3DX-ray1.80A3-376[»]
    ProteinModelPortaliP63270.
    SMRiP63270. Positions 3-376.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the actin family.Curated

    Phylogenomic databases

    HOVERGENiHBG003771.
    KOiK12315.

    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P63270-1 [UniParc]FASTAAdd to Basket

    « Hide

    MCEEETTALV CDNGSGLCKA GFAGDDAPRA VFPSIVGRPR HQGVMVGMGQ    50
    KDSYVGDEAQ SKRGILTLKY PIEHGIITNW DDMEKIWHHS FYNELRVAPE 100
    EHPTLLTEAP LNPKANREKM TQIMFETFNV PAMYVAIQAV LSLYASGRTT 150
    GIVLDSGDGV THNVPIYEGY ALPHAIMRLD LAGRDLTDYL MKILTERGYS 200
    FVTTAEREIV RDIKEKLCYV ALDFENEMAT AASSSSLEKS YELPDGQVIT 250
    IGNERFRCPE TLFQPSFIGM ESAGIHETTY NSIMKCDIDI RKDLYANNVL 300
    SGGTTMYPGI ADRMQKEITA LAPSTMKIKI IAPPERKYSV WIGGSILASL 350
    STFQQMWISK PEYDEAGPSI VHRKCF 376
    Length:376
    Mass (Da):41,877
    Last modified:October 11, 2004 - v1
    Checksum:i6EC08CD5EEAD445E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti221 – 2211A → P in AAC05823. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S63494 mRNA. Translation: AAB27386.1.
    AF012348 Genomic DNA. Translation: AAC05823.1.
    PIRiI51208. ATCHSM.
    RefSeqiNP_990503.1. NM_205172.1.
    UniGeneiGga.644.

    Genome annotation databases

    GeneIDi396084.
    KEGGigga:396084.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S63494 mRNA. Translation: AAB27386.1 .
    AF012348 Genomic DNA. Translation: AAC05823.1 .
    PIRi I51208. ATCHSM.
    RefSeqi NP_990503.1. NM_205172.1.
    UniGenei Gga.644.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3W3D X-ray 1.80 A 3-376 [» ]
    ProteinModelPortali P63270.
    SMRi P63270. Positions 3-376.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 676350. 1 interaction.

    Proteomic databases

    PRIDEi P63270.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 396084.
    KEGGi gga:396084.

    Organism-specific databases

    CTDi 72.

    Phylogenomic databases

    HOVERGENi HBG003771.
    KOi K12315.

    Miscellaneous databases

    NextBioi 20816142.
    PMAP-CutDB P63270.

    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. "Molecular cloning and expression of the chicken smooth muscle gamma-actin mRNA."
      Kovacs A.M., Zimmer W.E.
      Cell Motil. Cytoskeleton 24:67-81(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Smooth muscle.
    2. Kovacs A.M., Zimmer W.E.
      Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Smooth muscle.

    Entry informationi

    Entry nameiACTH_CHICK
    AccessioniPrimary (citable) accession number: P63270
    Secondary accession number(s): O73680, P12718
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 11, 2004
    Last sequence update: October 11, 2004
    Last modified: October 1, 2014
    This is version 62 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    In vertebrates 3 main groups of actin isoforms, alpha, beta and gamma have been identified. The alpha actins are found in muscle tissues and are a major constituent of the contractile apparatus. The beta and gamma actins coexist in most cell types as components of the cytoskeleton and as mediators of internal cell motility.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3