ACTC_XENTR
ID ACTC_XENTR Reviewed; 377 AA.
AC Q6P640;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Actin, alpha cardiac muscle 1 {ECO:0000250|UniProtKB:P04751, ECO:0000312|EMBL:AAH62494.1};
DE AltName: Full=Actin alpha 1 {ECO:0000250|UniProtKB:P04751};
DE AltName: Full=Alpha-cardiac actin {ECO:0000250|UniProtKB:P04751};
DE Contains:
DE RecName: Full=Actin, alpha cardiac muscle 1, intermediate form;
DE Flags: Precursor;
GN Name=actc1 {ECO:0000312|EMBL:AAH62494.1,
GN ECO:0000312|Xenbase:XB-GENE-480347};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1] {ECO:0000312|EMBL:AAH62494.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tadpole {ECO:0000312|EMBL:AAH62494.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=3172214; DOI=10.1016/0022-2836(88)90519-0;
RA Mohun T.J., Garrett N., Stutz F., Spohr G.;
RT "A third striated muscle actin gene is expressed during early development
RT in the amphibian Xenopus laevis.";
RL J. Mol. Biol. 202:67-76(1988).
CC -!- FUNCTION: Actins are highly conserved proteins that are involved in
CC various types of cell motility. {ECO:0000305}.
CC -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a
CC structural filament (F-actin) in the form of a two-stranded helix. Each
CC actin can bind to 4 others. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: In tailbud embryos, expressed in embryonic muscle
CC (myotomes). In adults, expressed in adult limb muscle.
CC {ECO:0000269|PubMed:3172214}.
CC -!- DEVELOPMENTAL STAGE: Expressed in developing embryos and adults.
CC {ECO:0000269|PubMed:3172214}.
CC -!- PTM: Oxidation of Met-46 and Met-49 by MICALs (MICAL1, MICAL2 or
CC MICAL3) to form methionine sulfoxide promotes actin filament
CC depolymerization. MICAL1 and MICAL2 produce the (R)-S-oxide form. The
CC (R)-S-oxide form is reverted by MSRB1 and MSRB2, which promotes actin
CC repolymerization. {ECO:0000250|UniProtKB:P68033}.
CC -!- PTM: Monomethylation at Lys-86 (K86me1) regulates actin-myosin
CC interaction and actomyosin-dependent processes. Demethylation by ALKBH4
CC is required for maintaining actomyosin dynamics supporting normal
CC cleavage furrow ingression during cytokinesis and cell migration.
CC {ECO:0000250|UniProtKB:P68032}.
CC -!- PTM: Methylated at His-75 by SETD3. {ECO:0000250|UniProtKB:P68032}.
CC -!- MISCELLANEOUS: Xenopus contains at least three sarcomeric alpha actin
CC genes that are preferentially expressed in either heart or skeletal
CC muscle. {ECO:0000305}.
CC -!- MISCELLANEOUS: The cardiac versus skeletal expression patterns of
CC actins are probably sequence-dependent; Xenopus cardiac actins contain
CC a Glu at position 3 of the mature peptide, whereas skeletal actins
CC contain an Asp at this position. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the actin family. {ECO:0000255}.
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DR EMBL; BC062494; AAH62494.1; -; mRNA.
DR RefSeq; NP_989094.1; NM_203763.1.
DR AlphaFoldDB; Q6P640; -.
DR SMR; Q6P640; -.
DR DNASU; 394698; -.
DR Ensembl; ENSXETT00000028240; ENSXETP00000028240; ENSXETG00000012911.
DR GeneID; 394698; -.
DR KEGG; xtr:394698; -.
DR CTD; 70; -.
DR Xenbase; XB-GENE-480347; actc1.
DR InParanoid; Q6P640; -.
DR OrthoDB; 649708at2759; -.
DR PhylomeDB; Q6P640; -.
DR Reactome; R-XTR-390522; Striated Muscle Contraction.
DR Reactome; R-XTR-9013026; RHOB GTPase cycle.
DR Proteomes; UP000008143; Chromosome 8.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000012911; Expressed in thoracic segment of trunk and 14 other tissues.
DR GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR GO; GO:0044297; C:cell body; ISS:AgBase.
DR GO; GO:0005737; C:cytoplasm; ISS:AgBase.
DR GO; GO:0005869; C:dynactin complex; IBA:GO_Central.
DR GO; GO:0030175; C:filopodium; ISS:AgBase.
DR GO; GO:0030027; C:lamellipodium; ISS:AgBase.
DR GO; GO:0030017; C:sarcomere; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0017022; F:myosin binding; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0033275; P:actin-myosin filament sliding; IBA:GO_Central.
DR GO; GO:0060047; P:heart contraction; IBA:GO_Central.
DR GO; GO:0090131; P:mesenchyme migration; ISS:AgBase.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:AgBase.
DR InterPro; IPR004000; Actin.
DR InterPro; IPR020902; Actin/actin-like_CS.
DR InterPro; IPR004001; Actin_CS.
DR InterPro; IPR043129; ATPase_NBD.
DR PANTHER; PTHR11937; PTHR11937; 1.
DR Pfam; PF00022; Actin; 1.
DR PRINTS; PR00190; ACTIN.
DR SMART; SM00268; ACTIN; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS00406; ACTINS_1; 1.
DR PROSITE; PS00432; ACTINS_2; 1.
DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Cytoplasm; Cytoskeleton; Methylation;
KW Muscle protein; Nucleotide-binding; Oxidation; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..377
FT /note="Actin, alpha cardiac muscle 1, intermediate form"
FT /evidence="ECO:0000250|UniProtKB:P62737"
FT /id="PRO_0000443003"
FT CHAIN 3..377
FT /note="Actin, alpha cardiac muscle 1"
FT /evidence="ECO:0000250|UniProtKB:P68135"
FT /id="PRO_0000399464"
FT MOD_RES 2
FT /note="N-acetylcysteine; in intermediate form"
FT /evidence="ECO:0000250|UniProtKB:P62737"
FT MOD_RES 3
FT /note="N-acetylaspartate; in Actin, alpha cardiac muscle 1"
FT /evidence="ECO:0000250|UniProtKB:P68135"
FT MOD_RES 46
FT /note="Methionine (R)-sulfoxide"
FT /evidence="ECO:0000250|UniProtKB:P68033"
FT MOD_RES 49
FT /note="Methionine (R)-sulfoxide"
FT /evidence="ECO:0000250|UniProtKB:P68033"
FT MOD_RES 75
FT /note="Tele-methylhistidine"
FT /evidence="ECO:0000250|UniProtKB:P62739"
FT MOD_RES 86
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P68032"
SQ SEQUENCE 377 AA; 42019 MW; E5C10FA19730CAD2 CRC64;
MCDDEETTAL VCDNGSGLVK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG QKDSYVGDEA
QSKRGILTLK YPIEHGIITN WDDMEKIWHH TFYNELRVAP EEHPTLLTEA PLNPKANREK
MTQIMFETFN VPAMYVAIQA VLSLYASGRT TGIVLDSGDG VTHNVPIYEG YALPHAIMRL
DLAGRDLTDY LMKILTERGY SFVTTAEREI VRDIKEKLCY VALDFENEMA TAASSSSLEK
SYELPDGQVI TIGNERFRCP ETLFQPSFIG MESAGIHETT YNSIMKCDID IRKDLYANNV
LSGGTTMYPG IADRMQKEIT ALAPSTMKIK IIAPPERKYS VWIGGSILAS LSTFQQMWIS
KQEYDEAGPS IVHRKCF
