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Protein

Actin, alpha skeletal muscle 3

Gene

act3

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Actins are highly conserved proteins that are involved in various types of cell motility.

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Muscle protein

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Actin, alpha skeletal muscle 3
Alternative name(s):
Actin alpha 3
Femoral (alpha 3) actin
Gene namesi
Name:act3
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-6253091. act3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000008681 – 2Removed in mature form2
ChainiPRO_00000008693 – 377Actin, alpha skeletal muscle 3Add BLAST375

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei3N-acetylaspartateBy similarity1
Modified residuei46Methionine (R)-sulfoxideBy similarity1
Modified residuei49Methionine (R)-sulfoxideBy similarity1
Modified residuei75Tele-methylhistidineBy similarity1

Post-translational modificationi

Oxidation of Met-46 and Met-49 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, Methylation, Oxidation

Proteomic databases

PRIDEiP04752.

Expressioni

Tissue specificityi

Shows overlapping but distinct expression patterns with other actins. In tailbud embryos, expressed in embryonic muscle (myotomes). In adults, expressed exclusively in skeletal muscle.1 Publication

Developmental stagei

First expressed after neurulation (stage 18), and expressed throughout development.1 Publication

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.

Structurei

3D structure databases

ProteinModelPortaliP04752.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the actin family.Curated

Phylogenomic databases

HOVERGENiHBG003771.
KOiK10354.

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.

P04752-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCDDDETTAL VCDNGSGLVK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG
60 70 80 90 100
QKDSYVGDEA QSKRGILTLK YPIEHGIITN WDDMEKIWHH TFYNELRVAP
110 120 130 140 150
EEHPTLLTEA PLNPKANREK MTQIMFETFN VPAMYVAIQA VLSLYASGRT
160 170 180 190 200
TGIVLDSGDG VTHNVPIYEG YALPHAIQRL DLAGRDLTDY LMKILTERGY
210 220 230 240 250
SFVTTAEREI VRDIKEKLAY VALDFENEMA TAASSSSLEK SYELPDGQVI
260 270 280 290 300
TIGNERFRCP ETLFQPSFIG MESAGIHETT YNSIMKCDID IRKDLYANNV
310 320 330 340 350
LSGGTTMYPG IADRMQKEIT ALAPSTMKIK IIAPPERKYS VWIGGSILAS
360 370
LSTFQQMWIT KQEYDEAGPS IVHRKCF
Length:377
Mass (Da):41,984
Last modified:January 1, 1990 - v2
Checksum:i7FBE432AA278F915
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03470 mRNA. Translation: CAA27187.1.
X12525 Genomic DNA. Translation: CAA31041.1.
BC041199 mRNA. Translation: AAH41199.1.
BC170065 mRNA. Translation: AAI70065.1.
PIRiB24848.
RefSeqiNP_001082366.1. NM_001088897.2.
NP_001090199.1. NM_001096730.1.
UniGeneiXl.24656.
Xl.57512.
Xl.83409.

Genome annotation databases

GeneIDi398426.
779096.
KEGGixla:398426.
xla:779096.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03470 mRNA. Translation: CAA27187.1.
X12525 Genomic DNA. Translation: CAA31041.1.
BC041199 mRNA. Translation: AAH41199.1.
BC170065 mRNA. Translation: AAI70065.1.
PIRiB24848.
RefSeqiNP_001082366.1. NM_001088897.2.
NP_001090199.1. NM_001096730.1.
UniGeneiXl.24656.
Xl.57512.
Xl.83409.

3D structure databases

ProteinModelPortaliP04752.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP04752.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi398426.
779096.
KEGGixla:398426.
xla:779096.

Organism-specific databases

CTDi104113.
XenbaseiXB-GENE-6253091. act3.

Phylogenomic databases

HOVERGENiHBG003771.
KOiK10354.

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...

Entry informationi

Entry nameiACT3_XENLA
AccessioniPrimary (citable) accession number: P04752
Secondary accession number(s): B7ZR72, Q5D0D1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 1, 1990
Last modified: November 30, 2016
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Xenopus contains at least three sarcomeric alpha actin genes that are preferentially expressed in either heart or skeletal muscle. Due to the tetraploid nature of Xenopus laevis, each of these three alpha actin genes is present in at least two copies.
PubMed:3172214 suggest that the sequences isolated in PubMed:3009830 (alpha3-II) and PubMed:3172214 (alpha3-I) may represent paralogous genes in tetraploid Xenopus laevis.
The cardiac versus skeletal expression patterns of actins are probably sequence-dependent; Xenopus cardiac actins contain a Glu at position 3 of the mature peptide, whereas skeletal actins contain an Asp at this position.

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.