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Protein

Actin, cytoplasmic 1

Gene

actb

Organism
Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
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.By similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-XTR-190873. Gap junction degradation.
R-XTR-196025. Formation of annular gap junctions.
R-XTR-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-XTR-3928662. EPHB-mediated forward signaling.
R-XTR-3928665. EPH-ephrin mediated repulsion of cells.
R-XTR-437239. Recycling pathway of L1.
R-XTR-4420097. VEGFA-VEGFR2 Pathway.
R-XTR-445095. Interaction between L1 and Ankyrins.
R-XTR-446353. Cell-extracellular matrix interactions.
R-XTR-5626467. RHO GTPases activate IQGAPs.
R-XTR-5663213. RHO GTPases Activate WASPs and WAVEs.
R-XTR-5663220. RHO GTPases Activate Formins.
R-XTR-5696394. DNA Damage Recognition in GG-NER.

Names & Taxonomyi

Protein namesi
Recommended name:
Actin, cytoplasmic 1
Alternative name(s):
Beta-actin
Cleaved into the following chain:
Gene namesi
Name:actb
ORF Names:TNeu072n05.1
OrganismiXenopus tropicalis (Western clawed frog) (Silurana tropicalis)
Taxonomic identifieri8364 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusSilurana
Proteomesi
  • UP000008143 Componenti: Unassembled WGS sequence

Organism-specific databases

XenbaseiXB-GENE-490883. actb.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 375375Actin, cytoplasmic 1PRO_0000367098Add
BLAST
Initiator methionineiRemoved; alternateBy similarity
Chaini2 – 375374Actin, cytoplasmic 1, N-terminally processedPRO_0000292338Add
BLAST

Amino acid modifications

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

PaxDbiQ6NVA9.
PRIDEiQ6NVA9.

Expressioni

Gene expression databases

BgeeiENSXETG00000025116.

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 (By similarity).By similarity

Protein-protein interaction databases

STRINGi8364.ENSXETP00000003955.

Structurei

3D structure databases

ProteinModelPortaliQ6NVA9.
SMRiQ6NVA9. Positions 2-375.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the actin family.Curated

Phylogenomic databases

eggNOGiKOG0676. Eukaryota.
COG5277. LUCA.
GeneTreeiENSGT00760000118957.
HOGENOMiHOG000233340.
HOVERGENiHBG003771.
InParanoidiQ6NVA9.
KOiK05692.
OMAiLFQPNVL.
OrthoDBiEOG091G08LD.
TreeFamiTF354237.

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.

Q6NVA9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDDDIAALVV 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):41,753
Last modified:July 5, 2004 - v1
Checksum:i79568672AF60CB72
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR855434 mRNA. Translation: CAJ82356.1.
BC068217 mRNA. Translation: AAH68217.1.
BC082343 mRNA. Translation: AAH82343.1.
RefSeqiNP_998884.1. NM_213719.1.
UniGeneiStr.47413.

Genome annotation databases

EnsembliENSXETT00000003955; ENSXETP00000003955; ENSXETG00000025116.
GeneIDi407952.
KEGGixtr:407952.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR855434 mRNA. Translation: CAJ82356.1.
BC068217 mRNA. Translation: AAH68217.1.
BC082343 mRNA. Translation: AAH82343.1.
RefSeqiNP_998884.1. NM_213719.1.
UniGeneiStr.47413.

3D structure databases

ProteinModelPortaliQ6NVA9.
SMRiQ6NVA9. Positions 2-375.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi8364.ENSXETP00000003955.

Proteomic databases

PaxDbiQ6NVA9.
PRIDEiQ6NVA9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSXETT00000003955; ENSXETP00000003955; ENSXETG00000025116.
GeneIDi407952.
KEGGixtr:407952.

Organism-specific databases

CTDi60.
XenbaseiXB-GENE-490883. actb.

Phylogenomic databases

eggNOGiKOG0676. Eukaryota.
COG5277. LUCA.
GeneTreeiENSGT00760000118957.
HOGENOMiHOG000233340.
HOVERGENiHBG003771.
InParanoidiQ6NVA9.
KOiK05692.
OMAiLFQPNVL.
OrthoDBiEOG091G08LD.
TreeFamiTF354237.

Enzyme and pathway databases

ReactomeiR-XTR-190873. Gap junction degradation.
R-XTR-196025. Formation of annular gap junctions.
R-XTR-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-XTR-3928662. EPHB-mediated forward signaling.
R-XTR-3928665. EPH-ephrin mediated repulsion of cells.
R-XTR-437239. Recycling pathway of L1.
R-XTR-4420097. VEGFA-VEGFR2 Pathway.
R-XTR-445095. Interaction between L1 and Ankyrins.
R-XTR-446353. Cell-extracellular matrix interactions.
R-XTR-5626467. RHO GTPases activate IQGAPs.
R-XTR-5663213. RHO GTPases Activate WASPs and WAVEs.
R-XTR-5663220. RHO GTPases Activate Formins.
R-XTR-5696394. DNA Damage Recognition in GG-NER.

Gene expression databases

BgeeiENSXETG00000025116.

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 nameiACTB_XENTR
AccessioniPrimary (citable) accession number: Q6NVA9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: July 5, 2004
Last modified: September 7, 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 (By similarity).By similarity

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.