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Database: UniProt
Entry: A0A2K5KDY2_COLAP
LinkDB: A0A2K5KDY2_COLAP
Original site: A0A2K5KDY2_COLAP 
ID   A0A2K5KDY2_COLAP        Unreviewed;       127 AA.
AC   A0A2K5KDY2;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Actin, gamma-enteric smooth muscle {ECO:0000256|ARBA:ARBA00039913};
DE   AltName: Full=Gamma-2-actin {ECO:0000256|ARBA:ARBA00041480};
DE   AltName: Full=Smooth muscle gamma-actin {ECO:0000256|ARBA:ARBA00042341};
OS   Colobus angolensis palliatus (Peters' Angolan colobus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Colobinae; Colobus.
OX   NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000039305.1, ECO:0000313|Proteomes:UP000233080};
RN   [1] {ECO:0000313|Ensembl:ENSCANP00000039305.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: Actins are highly conserved proteins that are involved in
CC       various types of cell motility and are ubiquitously expressed in all
CC       eukaryotic cells. {ECO:0000256|ARBA:ARBA00003520}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000256|ARBA:ARBA00001836};
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:0000256|ARBA:ARBA00038582}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000256|ARBA:ARBA00004245}.
CC   -!- SIMILARITY: Belongs to the actin family.
CC       {ECO:0000256|ARBA:ARBA00006752}.
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DR   AlphaFoldDB; A0A2K5KDY2; -.
DR   Ensembl; ENSCANT00000062564.1; ENSCANP00000039305.1; ENSCANG00000043310.1.
DR   Proteomes; UP000233080; Unplaced.
DR   Gene3D; 3.30.420.40; -; 1.
DR   InterPro; IPR004000; Actin.
DR   InterPro; IPR004001; Actin_CS.
DR   InterPro; IPR043129; ATPase_NBD.
DR   PANTHER; PTHR11937; ACTIN; 1.
DR   PANTHER; PTHR11937:SF201; ACTIN, GAMMA-ENTERIC SMOOTH MUSCLE; 1.
DR   Pfam; PF00022; Actin; 1.
DR   PRINTS; PR00190; ACTIN.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 1.
DR   PROSITE; PS00406; ACTINS_1; 1.
PE   3: Inferred from homology;
KW   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233080}.
SQ   SEQUENCE   127 AA;  13890 MW;  B155AF30DE9CCAE2 CRC64;
     MCEEETTALV CDNGSGLCKA GFAGDDAPRA VFPSIVGRPR HQGVMVGMGQ KDSYVGDEAQ
     SKRGILTLKY PIEHGIITNW DDMEKPHNHF SNLGCQHLSL DYCNDFLADF LVSCPHSPNS
     FSTLLQS
//
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