ID L5L4R2_PTEAL Unreviewed; 404 AA.
AC L5L4R2;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 26.
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};
GN ORFNames=PAL_GLEAN10008520 {ECO:0000313|EMBL:ELK18390.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK18390.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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, ECO:0000256|RuleBase:RU000487}.
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DR EMBL; KB030330; ELK18390.1; -; Genomic_DNA.
DR AlphaFoldDB; L5L4R2; -.
DR STRING; 9402.L5L4R2; -.
DR eggNOG; KOG0676; Eukaryota.
DR InParanoid; L5L4R2; -.
DR Proteomes; UP000010552; Unassembled WGS sequence.
DR GO; GO:0044297; C:cell body; ISS:AgBase.
DR GO; GO:0005737; C:cytoplasm; ISS:AgBase.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0030175; C:filopodium; ISS:AgBase.
DR GO; GO:0030027; C:lamellipodium; ISS:AgBase.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0090131; P:mesenchyme migration; ISS:AgBase.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:AgBase.
DR CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR InterPro; IPR004000; Actin.
DR InterPro; IPR020902; Actin/actin-like_CS.
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 SMART; SM00268; ACTIN; 1.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR PROSITE; PS00406; ACTINS_1; 1.
DR PROSITE; PS00432; ACTINS_2; 1.
DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000010552};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..404
FT /note="Actin, gamma-enteric smooth muscle"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003969907"
SQ SEQUENCE 404 AA; 44801 MW; D5AD0ECCEBECC8AA CRC64;
MTGNGFKASV LVLACEVLQL LVHLATLTMC EEETTALVCD NGSGLCKAGF AGDDAPRAVF
PSIVGRPRHQ GVMVGMGQKD SYVGDEAQSK RGILTLKYPI EHGIITNWDD MEKIWHHSFY
NELRVAPEEH PTLLTEAPLN PKANREKMTQ IMFETFNVPA MYVAIQAVLS LYASGRTTGI
VLDSGDGVTH NVPIYEGYAL PHAIMRLDLA GRDLTDYLMK ILTERGYSFV TTAEREIVRD
IKEKLCYVAL DFENEMATAA SSSSLEKSYE LPDGQVITIG NERFRCPETL FQPSFIGMES
AGIHETTYNS IMKCDIDIRK DLYANNVLSG GTTMYPGIAD RMQKEITALA PSTMKIKIIA
PPERKYSVWI GGSILASLST FQQMWISKPE YDEAGPSIVH RKCF
//
