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Protein

Actin, cytoplasmic 1

Gene

actb

Organism
Oryzias latipes (Japanese rice fish) (Japanese killifish)
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
OlCA1
Cleaved into the following chain:
Gene namesi
Name:actb
OrganismiOryzias latipes (Japanese rice fish) (Japanese killifish)
Taxonomic identifieri8090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiNeoteleosteiAcanthomorphataOvalentariaAtherinomorphaeBeloniformesAdrianichthyidaeOryziinaeOryzias
Proteomesi
  • UP000001038 Componenti: Chromosome 8

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_0000367092Add
BLAST
Initiator methionineiRemoved; alternateBy similarity
Chaini2 – 375374Actin, cytoplasmic 1, N-terminally processedPRO_0000000805Add
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
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

PRIDEiP79818.

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

STRINGi8090.ENSORLP00000017151.

Structurei

3D structure databases

ProteinModelPortaliP79818.
SMRiP79818. Positions 2-375.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the actin family.Curated

Phylogenomic databases

eggNOGiKOG0676. Eukaryota.
COG5277. LUCA.
GeneTreeiENSGT00760000118957.
HOGENOMiHOG000233340.
HOVERGENiHBG003771.
InParanoidiP79818.
KOiK05692.
OMAiMCKAGCA.
OrthoDBiEOG72RMZ1.
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.

P79818-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDDDIAALVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK
60 70 80 90 100
DSYVGDEAQS KRGILTLKYP IEHGIVTNWD DMEKIWHHTF YNELRIAPEE
110 120 130 140 150
HPVLLTEAPL NPKANREKMT QIMFETFNSP 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 SCGIHETTYN SIMKCDVDIR KDLYANTVLS
310 320 330 340 350
GGTTMYPGIA DRMQKEITAL APSTMKIKII APPERKYSVW IGGSILASLS
360 370
TFQQMWISKQ EYDESGPSIV HRKCF
Length:375
Mass (Da):41,739
Last modified:November 1, 1998 - v2
Checksum:iA01D760B5DF68112
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D89627 mRNA. Translation: BAA31750.1.
S74868 Genomic DNA. Translation: AAD14159.2.
RefSeqiNP_001098278.1. NM_001104808.1.
UniGeneiOla.4471.

Genome annotation databases

EnsembliENSORLT00000017152; ENSORLP00000017151; ENSORLG00000013676.
GeneIDi100049433.
KEGGiola:100049433.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D89627 mRNA. Translation: BAA31750.1.
S74868 Genomic DNA. Translation: AAD14159.2.
RefSeqiNP_001098278.1. NM_001104808.1.
UniGeneiOla.4471.

3D structure databases

ProteinModelPortaliP79818.
SMRiP79818. Positions 2-375.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi8090.ENSORLP00000017151.

Proteomic databases

PRIDEiP79818.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSORLT00000017152; ENSORLP00000017151; ENSORLG00000013676.
GeneIDi100049433.
KEGGiola:100049433.

Organism-specific databases

CTDi60.

Phylogenomic databases

eggNOGiKOG0676. Eukaryota.
COG5277. LUCA.
GeneTreeiENSGT00760000118957.
HOGENOMiHOG000233340.
HOVERGENiHBG003771.
InParanoidiP79818.
KOiK05692.
OMAiMCKAGCA.
OrthoDBiEOG72RMZ1.
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]
ProtoNetiSearch...

Publicationsi

  1. "Medaka actin genes."
    Kusakabe R., Kusakabe T., Suzuki N.
    Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "An efficient expression vector for transgenic medaka construction."
    Takagi S., Sasado T., Tamiya G., Ozato K., Wakamatsu Y., Takeshita A., Kimura M.
    Mol. Mar. Biol. Biotechnol. 3:192-199(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiACTB_ORYLA
AccessioniPrimary (citable) accession number: P79818
Secondary accession number(s): Q91393
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: November 1, 1998
Last modified: November 11, 2015
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

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.