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P63270

- ACTH_CHICK

UniProt

P63270 - ACTH_CHICK

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Protein
Actin, gamma-enteric smooth muscle
Gene
ACTG2, ACTA3, ACTSG
Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 22Removed in mature form By similarity
PRO_0000000754
Chaini3 – 376374Actin, gamma-enteric smooth muscle
PRO_0000000755Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei3 – 31N-acetylglutamate By similarity
Modified residuei45 – 451Methionine (R)-sulfoxide By similarity
Modified residuei48 – 481Methionine (R)-sulfoxide By 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.

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

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.

Family & Domainsi

Sequence similaritiesi

Belongs to the actin family.

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

Sequence conflict

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

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...

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: February 19, 2014
This is version 61 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

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