Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Actin, gamma-enteric smooth muscle

Gene

ACTG2

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539 Componenti: 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 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 – 135Combined sources
Beta strandi15 – 228Combined sources
Beta strandi29 – 335Combined sources
Beta strandi36 – 416Combined sources
Beta strandi43 – 453Combined sources
Beta strandi54 – 563Combined sources
Helixi57 – 615Combined sources
Helixi63 – 653Combined sources
Beta strandi66 – 694Combined sources
Helixi80 – 9213Combined sources
Turni93 – 953Combined sources
Helixi99 – 1013Combined sources
Beta strandi104 – 1085Combined sources
Helixi114 – 12613Combined sources
Beta strandi131 – 1377Combined sources
Helixi138 – 1458Combined sources
Beta strandi151 – 1566Combined sources
Beta strandi161 – 1677Combined sources
Helixi173 – 1753Combined sources
Beta strandi177 – 1793Combined sources
Helixi183 – 19614Combined sources
Helixi204 – 21714Combined sources
Helixi224 – 23310Combined sources
Beta strandi239 – 2424Combined sources
Beta strandi248 – 2536Combined sources
Helixi254 – 2607Combined sources
Turni261 – 2633Combined sources
Helixi265 – 2684Combined sources
Helixi275 – 28511Combined sources
Helixi290 – 2956Combined sources
Beta strandi298 – 3036Combined sources
Helixi304 – 3063Combined sources
Helixi310 – 31910Combined sources
Turni334 – 3374Combined sources
Helixi339 – 34911Combined sources
Helixi352 – 3554Combined sources
Helixi360 – 3645Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiP63270.
KOiK12315.

Family and domain databases

InterProiIPR004000. Actin.
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

        10         20         30         40         50
MCEEETTALV CDNGSGLCKA GFAGDDAPRA VFPSIVGRPR HQGVMVGMGQ
60 70 80 90 100
KDSYVGDEAQ SKRGILTLKY PIEHGIITNW DDMEKIWHHS FYNELRVAPE
110 120 130 140 150
EHPTLLTEAP LNPKANREKM TQIMFETFNV PAMYVAIQAV LSLYASGRTT
160 170 180 190 200
GIVLDSGDGV THNVPIYEGY ALPHAIMRLD LAGRDLTDYL MKILTERGYS
210 220 230 240 250
FVTTAEREIV RDIKEKLCYV ALDFENEMAT AASSSSLEKS YELPDGQVIT
260 270 280 290 300
IGNERFRCPE TLFQPSFIGM ESAGIHETTY NSIMKCDIDI RKDLYANNVL
310 320 330 340 350
SGGTTMYPGI ADRMQKEITA LAPSTMKIKI IAPPERKYSV WIGGSILASL
360 370
STFQQMWISK PEYDEAGPSI VHRKCF
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 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
S63494 mRNA. Translation: AAB27386.1.
AF012348 Genomic DNA. Translation: AAC05823.1.
PIRiI51208. ATCHSM.
RefSeqiNP_990503.1. NM_205172.1.
UniGeneiGga.644.

3D structure databases

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

Protein-protein interaction databases

BioGridi676350. 1 interaction.

Proteomic databases

PRIDEiP63270.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi396084.
KEGGigga:396084.

Organism-specific databases

CTDi72.

Phylogenomic databases

HOVERGENiHBG003771.
InParanoidiP63270.
KOiK12315.

Miscellaneous databases

NextBioi20816142.
PMAP-CutDBP63270.
PROiP63270.

Family and domain databases

InterProiIPR004000. Actin.
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]
ProtoNetiSearch...

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: April 29, 2015
This is version 67 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.