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Protein

Actin, gamma-enteric smooth muscle

Gene

Actg2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -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.

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.

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionMuscle protein
LigandATP-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
Cleaved into the following chain:
Gene namesi
Name:Actg2
Synonyms:Acta3, Actsg
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 4

Organism-specific databases

RGDi2027 Actg2

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00004429532 – 376Actin, gamma-enteric smooth muscle, intermediate formBy similarityAdd BLAST375
ChainiPRO_00004429543 – 376Actin, gamma-enteric smooth muscleBy similarityAdd BLAST374

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylcysteine; in intermediate formBy 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 promotes actin repolymerization.By similarity
Monomethylation at Lys-85 (K85me1) 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

Keywords - PTMi

Acetylation, Oxidation

Proteomic databases

PaxDbiP63269
PRIDEiP63269

PTM databases

iPTMnetiP63269
PhosphoSitePlusiP63269

Expressioni

Gene expression databases

BgeeiENSRNOG00000029401
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 interactor
IntActiP63269, 1 interactor
STRINGi10116.ENSRNOP00000050322

Structurei

3D structure databases

ProteinModelPortaliP63269
SMRiP63269
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the actin family.Curated

Phylogenomic databases

eggNOGiKOG0676 Eukaryota
COG5277 LUCA
GeneTreeiENSGT00760000118957
HOGENOMiHOG000233340
HOVERGENiHBG003771
InParanoidiP63269
KOiK12315
OMAiATLAMCE
OrthoDBiEOG091G08LD
PhylomeDBiP63269

Family and domain databases

InterProiView protein in InterPro
IPR004000 Actin
IPR020902 Actin/actin-like_CS
IPR004001 Actin_CS
PANTHERiPTHR11937 PTHR11937, 1 hit
PfamiView protein in Pfam
PF00022 Actin, 1 hit
PRINTSiPR00190 ACTIN
SMARTiView protein in SMART
SM00268 ACTIN, 1 hit
PROSITEiView protein in PROSITE
PS00406 ACTINS_1, 1 hit
PS00432 ACTINS_2, 1 hit
PS01132 ACTINS_ACT_LIKE, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiACTH_RAT
AccessioniPrimary (citable) accession number: P63269
Secondary accession number(s): P12718
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: March 28, 2018
This is version 103 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
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Main funding by: National Institutes of Health