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Protein

Actin, alpha cardiac muscle 1

Gene

actc1

Organism
Xenopus laevis (African clawed frog)
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.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Muscle protein

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Actin, alpha cardiac muscle 1
Alternative name(s):
Actin alpha 1
Alpha-cardiac actin
Gene namesi
Name:actc1
Synonyms:acta1, actc
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-865367. actc1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 22Removed in mature formBy similarityPRO_0000000820
Chaini3 – 377375Actin, alpha cardiac muscle 1PRO_0000000821Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei3 – 31N-acetylaspartateBy similarity
Modified residuei46 – 461Methionine (R)-sulfoxideBy similarity
Modified residuei49 – 491Methionine (R)-sulfoxideBy similarity
Modified residuei75 – 751Tele-methylhistidineBy similarity

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

Keywords - PTMi

Acetylation, Methylation, Oxidation

Expressioni

Tissue specificityi

Shows overlapping but distinct expression patterns with other actins. In tailbud embryos, expressed in embryonic muscle (myotomes). In adults, expressed only in heart muscle.2 Publications

Developmental stagei

Expressed from the end of gastrulation.1 Publication

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.

Structurei

3D structure databases

ProteinModelPortaliP04751.
SMRiP04751. Positions 6-377.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the actin family.Curated

Phylogenomic databases

HOVERGENiHBG003771.
KOiK12314.

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.

P04751-1 [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 YALPHAIQRL 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):42,016
Last modified:August 13, 1987 - v1
Checksum:iC3E276EFA11CD1B5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04669 Genomic DNA. Translation: CAA28375.1.
X03469 mRNA. Translation: CAA27186.1.
BC041197 mRNA. Translation: AAH41197.1.
BC077221 mRNA. Translation: AAH77221.1.
BC099316 mRNA. Translation: AAH99316.1.
PIRiA25705. A24848.
RefSeqiNP_001080060.1. NM_001086591.1.
UniGeneiXl.1115.

Genome annotation databases

GeneIDi379752.
KEGGixla:379752.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04669 Genomic DNA. Translation: CAA28375.1.
X03469 mRNA. Translation: CAA27186.1.
BC041197 mRNA. Translation: AAH41197.1.
BC077221 mRNA. Translation: AAH77221.1.
BC099316 mRNA. Translation: AAH99316.1.
PIRiA25705. A24848.
RefSeqiNP_001080060.1. NM_001086591.1.
UniGeneiXl.1115.

3D structure databases

ProteinModelPortaliP04751.
SMRiP04751. Positions 6-377.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi379752.
KEGGixla:379752.

Organism-specific databases

CTDi70.
XenbaseiXB-GENE-865367. actc1.

Phylogenomic databases

HOVERGENiHBG003771.
KOiK12314.

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. "Upstream sequences required for tissue-specific activation of the cardiac actin gene in Xenopus laevis embryos."
    Mohun T.J., Garrett N., Gurdon J.B.
    EMBO J. 5:3185-3193(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Isolation and characterization of sarcomeric actin genes expressed in Xenopus laevis embryos."
    Stutz F., Spohr G.
    J. Mol. Biol. 187:349-361(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-43.
  3. NIH - Xenopus Gene Collection (XGC) project
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Embryo and Heart.
  4. "Cell type-specific activation of actin genes in the early amphibian embryo."
    Mohun T.J., Brennan S., Dathan N., Fairman S., Gurdon J.B.
    Nature 311:716-721(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  5. "A third striated muscle actin gene is expressed during early development in the amphibian Xenopus laevis."
    Mohun T.J., Garrett N., Stutz F., Spohr G.
    J. Mol. Biol. 202:67-76(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.

Entry informationi

Entry nameiACTC_XENLA
AccessioniPrimary (citable) accession number: P04751
Secondary accession number(s): Q6AZU8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: November 11, 2015
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Xenopus contains at least three sarcomeric alpha actin genes that are preferentially expressed in either heart or skeletal muscle. Due to the tetraploid nature of Xenopus laevis, each of these three alpha actin genes is present in at least two copies.
The cardiac versus skeletal expression patterns of actins are probably sequence-dependent. For example, cardiac actins contain a Glu at position 3 of the mature peptide, whereas skeletal actins contain an Asp at this position.

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.