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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

GO - Biological processi

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
Proteomesi
  • UP000000539 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000007541 – 2Removed in mature formBy similarity2
ChainiPRO_00000007553 – 376Actin, gamma-enteric smooth muscleAdd BLAST374

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei3N-acetylglutamateBy similarity1
Modified residuei45Methionine (R)-sulfoxideBy similarity1
Modified residuei48Methionine (R)-sulfoxideBy similarity1

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

PaxDbiP63270.
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 interactor.
STRINGi9031.ENSGALP00000015988.

Structurei

Secondary structure

1376
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi9 – 13Combined sources5
Beta strandi15 – 22Combined sources8
Beta strandi29 – 33Combined sources5
Beta strandi36 – 41Combined sources6
Beta strandi43 – 45Combined sources3
Beta strandi54 – 56Combined sources3
Helixi57 – 61Combined sources5
Helixi63 – 65Combined sources3
Beta strandi66 – 69Combined sources4
Helixi80 – 92Combined sources13
Turni93 – 95Combined sources3
Helixi99 – 101Combined sources3
Beta strandi104 – 108Combined sources5
Helixi114 – 126Combined sources13
Beta strandi131 – 137Combined sources7
Helixi138 – 145Combined sources8
Beta strandi151 – 156Combined sources6
Beta strandi161 – 167Combined sources7
Helixi173 – 175Combined sources3
Beta strandi177 – 179Combined sources3
Helixi183 – 196Combined sources14
Helixi204 – 217Combined sources14
Helixi224 – 233Combined sources10
Beta strandi239 – 242Combined sources4
Beta strandi248 – 253Combined sources6
Helixi254 – 260Combined sources7
Turni261 – 263Combined sources3
Helixi265 – 268Combined sources4
Helixi275 – 285Combined sources11
Helixi290 – 295Combined sources6
Beta strandi298 – 303Combined sources6
Helixi304 – 306Combined sources3
Helixi310 – 319Combined sources10
Turni334 – 337Combined sources4
Helixi339 – 349Combined sources11
Helixi352 – 355Combined sources4
Helixi360 – 364Combined sources5

3D structure databases

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

Family & Domainsi

Sequence similaritiesi

Belongs to the actin family.Curated

Phylogenomic databases

eggNOGiKOG0676. Eukaryota.
COG5277. LUCA.
GeneTreeiENSGT00760000118957.
HOVERGENiHBG003771.
InParanoidiP63270.
KOiK12315.

Family and domain databases

InterProiIPR004000. Actin.
IPR020902. Actin/actin-like_CS.
IPR004001. Actin_CS.
[Graphical view]
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)DescriptionActionsGraphical viewLength
Sequence conflicti221A → P in AAC05823 (Ref. 2) Curated1

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

EnsembliENSGALT00000065171; ENSGALP00000048103; ENSGALG00000041634.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3W3DX-ray1.80A3-376[»]
ProteinModelPortaliP63270.
SMRiP63270.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi676350. 1 interactor.
STRINGi9031.ENSGALP00000015988.

Proteomic databases

PaxDbiP63270.
PRIDEiP63270.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSGALT00000065171; ENSGALP00000048103; ENSGALG00000041634.
GeneIDi396084.
KEGGigga:396084.

Organism-specific databases

CTDi72.

Phylogenomic databases

eggNOGiKOG0676. Eukaryota.
COG5277. LUCA.
GeneTreeiENSGT00760000118957.
HOVERGENiHBG003771.
InParanoidiP63270.
KOiK12315.

Miscellaneous databases

PMAP-CutDBP63270.
PROiP63270.

Family and domain databases

InterProiIPR004000. Actin.
IPR020902. Actin/actin-like_CS.
IPR004001. Actin_CS.
[Graphical view]
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...

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: November 30, 2016
This is version 73 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

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 one 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.