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Protein

Actin, cytoplasmic 1

Gene

actba

Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
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

Complete GO annotation...

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-DRE-190873. Gap junction degradation.
R-DRE-196025. Formation of annular gap junctions.
R-DRE-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-DRE-3928662. EPHB-mediated forward signaling.
R-DRE-3928665. EPH-ephrin mediated repulsion of cells.
R-DRE-437239. Recycling pathway of L1.
R-DRE-4420097. VEGFA-VEGFR2 Pathway.
R-DRE-445095. Interaction between L1 and Ankyrins.
R-DRE-446353. Cell-extracellular matrix interactions.
R-DRE-5250924. B-WICH complex positively regulates rRNA expression.
R-DRE-5626467. RHO GTPases activate IQGAPs.
R-DRE-5663213. RHO GTPases Activate WASPs and WAVEs.
R-DRE-5663220. RHO GTPases Activate Formins.
R-DRE-5689603. UCH proteinases.
R-DRE-5696394. DNA Damage Recognition in GG-NER.
R-DRE-8856828. Clathrin-mediated endocytosis.

Names & Taxonomyi

Protein namesi
Recommended name:
Actin, cytoplasmic 1
Alternative name(s):
Beta-actin-1
Cleaved into the following chain:
Gene namesi
Name:actba
Synonyms:bact, bactin1, bactzf
OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
Taxonomic identifieri7955 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
Proteomesi
  • UP000000437 Componenti: Chromosome 1

Organism-specific databases

ZFINiZDB-GENE-000329-1. actb1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003670871 – 375Actin, cytoplasmic 1Add BLAST375
Initiator methionineiRemoved; alternateBy similarity
ChainiPRO_00000007952 – 375Actin, cytoplasmic 1, N-terminally processedAdd BLAST374

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionine; in Actin, cytoplasmic 1; alternateBy similarity1
Modified residuei2N-acetylaspartate; in Actin, cytoplasmic 1, N-terminally processedBy similarity1
Modified residuei44Methionine (R)-sulfoxideBy similarity1
Modified residuei47Methionine (R)-sulfoxideBy similarity1
Modified residuei73Tele-methylhistidineBy similarity1

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

PaxDbiQ7ZVI7.
PRIDEiQ7ZVI7.

Expressioni

Tissue specificityi

Skeletal muscle, heart, gill, digestive tissue and brain. Widespread expression throughout the brain, with highest levels in regions where neuronal proliferation is greatest.1 Publication

Gene expression databases

BgeeiENSDARG00000037746.
ExpressionAtlasiQ7ZVI7. differential.

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

IntActiQ7ZVI7. 1 interactor.
MINTiMINT-8283530.
STRINGi7955.ENSDARP00000054986.

Structurei

3D structure databases

ProteinModelPortaliQ7ZVI7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the actin family.Curated

Phylogenomic databases

eggNOGiKOG0676. Eukaryota.
COG5277. LUCA.
GeneTreeiENSGT00760000118957.
HOGENOMiHOG000233340.
HOVERGENiHBG003771.
InParanoidiQ7ZVI7.
KOiK05692.
OMAiTFQQART.
OrthoDBiEOG091G08LD.
PhylomeDBiQ7ZVI7.
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.

Q7ZVI7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDEEIAALVV 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 LDFEQEMGTA ASSSSLEKSY ELPDGQVITI
260 270 280 290 300
GNERFRCPEA LFQPSFLGME SCGIHETTFN SIMKCDVDIR KDLYANTVLS
310 320 330 340 350
GGTTMYPGIA DRMQKEITSL APSTMKIKII APPERKYSVW IGGSILASLS
360 370
TFQQMWISKQ EYDESGPSIV HRKCF
Length:375
Mass (Da):41,767
Last modified:March 29, 2005 - v2
Checksum:iCDAC90490F8F11AF
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti66T → S in AAH45846 (Ref. 2) Curated1
Sequence conflicti104L → V in AAC13314 (PubMed:9987040).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF057040 mRNA. Translation: AAC13314.1.
BC045846 mRNA. Translation: AAH45846.1.
BC063950 mRNA. Translation: AAH63950.1.
RefSeqiNP_571106.1. NM_131031.1.
UniGeneiDr.35143.

Genome annotation databases

EnsembliENSDART00000054987; ENSDARP00000054986; ENSDARG00000037746.
GeneIDi57934.
KEGGidre:57934.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF057040 mRNA. Translation: AAC13314.1.
BC045846 mRNA. Translation: AAH45846.1.
BC063950 mRNA. Translation: AAH63950.1.
RefSeqiNP_571106.1. NM_131031.1.
UniGeneiDr.35143.

3D structure databases

ProteinModelPortaliQ7ZVI7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ7ZVI7. 1 interactor.
MINTiMINT-8283530.
STRINGi7955.ENSDARP00000054986.

Proteomic databases

PaxDbiQ7ZVI7.
PRIDEiQ7ZVI7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSDART00000054987; ENSDARP00000054986; ENSDARG00000037746.
GeneIDi57934.
KEGGidre:57934.

Organism-specific databases

CTDi57934.
ZFINiZDB-GENE-000329-1. actb1.

Phylogenomic databases

eggNOGiKOG0676. Eukaryota.
COG5277. LUCA.
GeneTreeiENSGT00760000118957.
HOGENOMiHOG000233340.
HOVERGENiHBG003771.
InParanoidiQ7ZVI7.
KOiK05692.
OMAiTFQQART.
OrthoDBiEOG091G08LD.
PhylomeDBiQ7ZVI7.
TreeFamiTF354237.

Enzyme and pathway databases

ReactomeiR-DRE-190873. Gap junction degradation.
R-DRE-196025. Formation of annular gap junctions.
R-DRE-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-DRE-3928662. EPHB-mediated forward signaling.
R-DRE-3928665. EPH-ephrin mediated repulsion of cells.
R-DRE-437239. Recycling pathway of L1.
R-DRE-4420097. VEGFA-VEGFR2 Pathway.
R-DRE-445095. Interaction between L1 and Ankyrins.
R-DRE-446353. Cell-extracellular matrix interactions.
R-DRE-5250924. B-WICH complex positively regulates rRNA expression.
R-DRE-5626467. RHO GTPases activate IQGAPs.
R-DRE-5663213. RHO GTPases Activate WASPs and WAVEs.
R-DRE-5663220. RHO GTPases Activate Formins.
R-DRE-5689603. UCH proteinases.
R-DRE-5696394. DNA Damage Recognition in GG-NER.
R-DRE-8856828. Clathrin-mediated endocytosis.

Miscellaneous databases

PROiQ7ZVI7.

Gene expression databases

BgeeiENSDARG00000037746.
ExpressionAtlasiQ7ZVI7. differential.

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 nameiACTB1_DANRE
AccessioniPrimary (citable) accession number: Q7ZVI7
Secondary accession number(s): O73815, P12714, Q6P3K9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 16, 2004
Last sequence update: March 29, 2005
Last modified: November 30, 2016
This is version 110 of the entry and version 2 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.