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Protein

Actin, alpha cardiac muscle 1

Gene

Actc1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Muscle protein

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-RNO-390522. Striated Muscle Contraction.

Names & Taxonomyi

Protein namesi
Recommended name:
Actin, alpha cardiac muscle 1
Alternative name(s):
Alpha-cardiac actin
Gene namesi
Name:Actc1
Synonyms:Actc
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 3

Organism-specific databases

RGDi2026. Actc1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000008161 – 2Removed in mature formBy similarity2
ChainiPRO_00000008173 – 377Actin, alpha cardiac muscle 1Add BLAST375

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei3N-acetylaspartateBy similarity1
Modified residuei46Methionine (R)-sulfoxideBy similarity1
Modified residuei49Methionine (R)-sulfoxideBy similarity1
Modified residuei86N6-methyllysineBy 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
Monomethylation at Lys-86 (K84me1) regulates actin-myosin interaction and actomyosin-dependent processes. Demethylation by ALKBH4 is required for maintaining actomyosin dynamics supporting normal cleavage furrow ingression during cytokinesis and cell migration (By similarity).By similarity

Keywords - PTMi

Acetylation, Methylation, Oxidation

Proteomic databases

PaxDbiP68035.
PRIDEiP68035.

PTM databases

iPTMnetiP68035.
PhosphoSitePlusiP68035.

Expressioni

Gene expression databases

BgeeiENSRNOG00000008536.
GenevisibleiP68035. RN.

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

BioGridi247946. 4 interactors.
MINTiMINT-1868886.
STRINGi10116.ENSRNOP00000011773.

Structurei

3D structure databases

ProteinModelPortaliP68035.
SMRiP68035.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the actin family.Curated

Phylogenomic databases

eggNOGiKOG0676. Eukaryota.
COG5277. LUCA.
GeneTreeiENSGT00760000118957.
HOVERGENiHBG003771.
InParanoidiP68035.
KOiK12314.
OMAiSCHAGCG.
OrthoDBiEOG091G08LD.
PhylomeDBiP68035.
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.

P68035-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCDDEETTAL 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 YALPHAIMRL DLAGRDLTDY LMKILTERGY
210 220 230 240 250
SFVTTAEREI VRDIKEKLCY 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
LSTFQQMWIS KQEYDEAGPS IVHRKCF
Length:377
Mass (Da):42,019
Last modified:March 20, 1987 - v1
Checksum:iE5C10FA19730CAD2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X80130 mRNA. Translation: CAA56429.1.
BC127451 mRNA. Translation: AAI27452.1.
RefSeqiNP_062056.1. NM_019183.1.
UniGeneiRn.3114.

Genome annotation databases

EnsembliENSRNOT00000011773; ENSRNOP00000011773; ENSRNOG00000008536.
GeneIDi29275.
KEGGirno:29275.
UCSCiRGD:2026. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X80130 mRNA. Translation: CAA56429.1.
BC127451 mRNA. Translation: AAI27452.1.
RefSeqiNP_062056.1. NM_019183.1.
UniGeneiRn.3114.

3D structure databases

ProteinModelPortaliP68035.
SMRiP68035.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247946. 4 interactors.
MINTiMINT-1868886.
STRINGi10116.ENSRNOP00000011773.

PTM databases

iPTMnetiP68035.
PhosphoSitePlusiP68035.

Proteomic databases

PaxDbiP68035.
PRIDEiP68035.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000011773; ENSRNOP00000011773; ENSRNOG00000008536.
GeneIDi29275.
KEGGirno:29275.
UCSCiRGD:2026. rat.

Organism-specific databases

CTDi70.
RGDi2026. Actc1.

Phylogenomic databases

eggNOGiKOG0676. Eukaryota.
COG5277. LUCA.
GeneTreeiENSGT00760000118957.
HOVERGENiHBG003771.
InParanoidiP68035.
KOiK12314.
OMAiSCHAGCG.
OrthoDBiEOG091G08LD.
PhylomeDBiP68035.
TreeFamiTF354237.

Enzyme and pathway databases

ReactomeiR-RNO-390522. Striated Muscle Contraction.

Miscellaneous databases

PROiP68035.

Gene expression databases

BgeeiENSRNOG00000008536.
GenevisibleiP68035. RN.

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 nameiACTC_RAT
AccessioniPrimary (citable) accession number: P68035
Secondary accession number(s): A0JPJ4, P04270
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: March 20, 1987
Last modified: November 2, 2016
This is version 99 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.

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.