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Protein

Actin, gamma-enteric smooth muscle

Gene

Actg2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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

Enzyme and pathway databases

ReactomeiR-RNO-445355. Smooth Muscle Contraction.

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 4

Organism-specific databases

RGDi2027. Actg2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 22Removed in mature formBy similarityPRO_0000000752
Chaini3 – 376374Actin, gamma-enteric smooth musclePRO_0000000753Add
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
Monomethylation at Lys-85 (K84me1) regulates actin-myosin interaction and actomyosin-dependent processes. Demethylation by ALKBH4 is required for maintaining actomyosin dynamics supporting normal cleavage furrow ingression during cytokinesis and cell migration (By similarity).By similarity

Keywords - PTMi

Acetylation, Oxidation

Proteomic databases

PaxDbiP63269.
PRIDEiP63269.

PTM databases

iPTMnetiP63269.
PhosphoSiteiP63269.

Expressioni

Gene expression databases

GenevisibleiP63269. RN.

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

BioGridi247404. 1 interaction.
IntActiP63269. 1 interaction.
STRINGi10116.ENSRNOP00000050322.

Structurei

3D structure databases

ProteinModelPortaliP63269.
SMRiP63269. Positions 3-376.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the actin family.Curated

Phylogenomic databases

eggNOGiKOG0676. Eukaryota.
COG5277. LUCA.
GeneTreeiENSGT00760000118957.
HOGENOMiHOG000233340.
HOVERGENiHBG003771.
InParanoidiP63269.
KOiK12315.
OMAiKCDESIC.
OrthoDBiEOG72RMZ1.
PhylomeDBiP63269.

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.

P63269-1 [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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22323 mRNA. Translation: AAA40672.1.
BC087689 mRNA. Translation: AAH87689.1.
PIRiA31375.
RefSeqiNP_037025.1. NM_012893.1.
XP_006236790.1. XM_006236728.2.
UniGeneiRn.958.

Genome annotation databases

EnsembliENSRNOT00000042699; ENSRNOP00000050322; ENSRNOG00000029401.
GeneIDi25365.
KEGGirno:25365.
UCSCiRGD:2027. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22323 mRNA. Translation: AAA40672.1.
BC087689 mRNA. Translation: AAH87689.1.
PIRiA31375.
RefSeqiNP_037025.1. NM_012893.1.
XP_006236790.1. XM_006236728.2.
UniGeneiRn.958.

3D structure databases

ProteinModelPortaliP63269.
SMRiP63269. Positions 3-376.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247404. 1 interaction.
IntActiP63269. 1 interaction.
STRINGi10116.ENSRNOP00000050322.

PTM databases

iPTMnetiP63269.
PhosphoSiteiP63269.

Proteomic databases

PaxDbiP63269.
PRIDEiP63269.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000042699; ENSRNOP00000050322; ENSRNOG00000029401.
GeneIDi25365.
KEGGirno:25365.
UCSCiRGD:2027. rat.

Organism-specific databases

CTDi72.
RGDi2027. Actg2.

Phylogenomic databases

eggNOGiKOG0676. Eukaryota.
COG5277. LUCA.
GeneTreeiENSGT00760000118957.
HOGENOMiHOG000233340.
HOVERGENiHBG003771.
InParanoidiP63269.
KOiK12315.
OMAiKCDESIC.
OrthoDBiEOG72RMZ1.
PhylomeDBiP63269.

Enzyme and pathway databases

ReactomeiR-RNO-445355. Smooth Muscle Contraction.

Miscellaneous databases

PROiP63269.

Gene expression databases

GenevisibleiP63269. RN.

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...

Publicationsi

« Hide 'large scale' publications
  1. "The development expression of the rat alpha-vascular and gamma-enteric smooth muscle isoactins: isolation and characterization of a rat gamma-enteric actin cDNA."
    McHugh K.M., Lessard J.L.
    Mol. Cell. Biol. 8:5224-5231(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Ovary.

Entry informationi

Entry nameiACTH_RAT
AccessioniPrimary (citable) accession number: P63269
Secondary accession number(s): P12718
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: June 8, 2016
This is version 91 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

Complete proteome, Reference proteome

Documents

  1. 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.