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Protein

Actin, cytoplasmic 1

Gene

actb

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 and are ubiquitously expressed in all eukaryotic cells.

GO - Molecular functioni

Complete GO annotation...

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Actin, cytoplasmic 1
Alternative name(s):
Beta-actin
Cytoplasmic beta-actin
Cleaved into the following chain:
Gene namesi
Name:actb
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-866011. actb.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL5170.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 375375Actin, cytoplasmic 1PRO_0000367097Add
BLAST
Initiator methionineiRemoved; alternateBy similarity
Chaini2 – 375374Actin, cytoplasmic 1, N-terminally processedPRO_0000000793Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine; in Actin, cytoplasmic 1; alternateBy similarity
Modified residuei2 – 21N-acetylglutamate; in Actin, cytoplasmic 1, N-terminally processedBy similarity
Modified residuei44 – 441Methionine (R)-sulfoxideBy similarity
Modified residuei47 – 471Methionine (R)-sulfoxideBy similarity
Modified residuei73 – 731Tele-methylhistidineBy similarity

Post-translational modificationi

Oxidation of Met-44 and Met-47 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

PRIDEiO93400.

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

BioGridi99791. 4 interactions.

Chemistry

BindingDBiO93400.

Structurei

3D structure databases

ProteinModelPortaliO93400.
SMRiO93400. Positions 2-375.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the actin family.Curated

Phylogenomic databases

HOVERGENiHBG003771.
KOiK05692.

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.

O93400-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEDDIAALVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK
60 70 80 90 100
DSYVGDEAQS KRGILTLKYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE
110 120 130 140 150
HPVLLTEAPL NPKANREKMT QIMFETFNTP AMYVAIQAVL SLYASGRTTG
160 170 180 190 200
IVMDSGDGVT HTVPIYEGYA LPHAILRLDL AGRDLTDYLM KILTERGYSF
210 220 230 240 250
TTTAEREIVR DIKEKLCYVA LDFEQEMATA ASSSSLEKSY ELPDGQVITI
260 270 280 290 300
GNERFRCPEA LFQPSFLGME SCGIHETTYN SIMKCDVDIR KDLYANTVLS
310 320 330 340 350
GGTTMYPGIA DRMQKEITAL APSTMKIKII APPERKYSVW IGGSILASLS
360 370
TFQQMWISKQ EYDESGPSIV HRKCF
Length:375
Mass (Da):41,767
Last modified:November 1, 1998 - v1
Checksum:i8956C3725A60F96E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF079161 mRNA. Translation: AAC27796.1.
BC041203 mRNA. Translation: AAH41203.1.
BC084121 mRNA. Translation: AAH84121.1.
RefSeqiNP_001082422.1. NM_001088953.1.
UniGeneiXl.4138.

Genome annotation databases

GeneIDi398459.
KEGGixla:398459.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF079161 mRNA. Translation: AAC27796.1.
BC041203 mRNA. Translation: AAH41203.1.
BC084121 mRNA. Translation: AAH84121.1.
RefSeqiNP_001082422.1. NM_001088953.1.
UniGeneiXl.4138.

3D structure databases

ProteinModelPortaliO93400.
SMRiO93400. Positions 2-375.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi99791. 4 interactions.

Chemistry

BindingDBiO93400.
ChEMBLiCHEMBL5170.

Proteomic databases

PRIDEiO93400.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi398459.
KEGGixla:398459.

Organism-specific databases

CTDi60.
XenbaseiXB-GENE-866011. actb.

Phylogenomic databases

HOVERGENiHBG003771.
KOiK05692.

Miscellaneous databases

PROiO93400.

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

« Hide 'large scale' publications
  1. "Xenopus laevis cytoplasmic beta actin."
    Ko C.M., Bae S.W., Lee N.S., Son Y.H., Jung H.M.
    Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. NIH - Xenopus Gene Collection (XGC) project
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Embryo.

Entry informationi

Entry nameiACTB_XENLA
AccessioniPrimary (citable) accession number: O93400
Secondary accession number(s): Q5XHD7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: November 1, 1998
Last modified: June 8, 2016
This is version 88 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.

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.