ACTG_CHICK
ID ACTG_CHICK Reviewed; 375 AA.
AC Q5ZMQ2;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Actin, cytoplasmic 2;
DE AltName: Full=Gamma-actin;
DE Contains:
DE RecName: Full=Actin, cytoplasmic 2, N-terminally processed;
GN Name=ACTG1; ORFNames=RCJMB04_1h13;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
RN [2]
RP PROTEIN SEQUENCE OF 2-37; 85-113; 178-191; 197-206; 239-254; 291-326 AND
RP 360-372, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT GLU-2, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V., Black E.J., Gillespie D.A.;
RL Submitted (JAN-2007) 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:0000250|UniProtKB:P63261}.
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.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P63261}.
CC -!- PTM: Oxidation of Met-44 and Met-47 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 promote actin
CC repolymerization. {ECO:0000250|UniProtKB:P63260}.
CC -!- PTM: Methylated at His-73 by SETD3. {ECO:0000250|UniProtKB:P63261}.
CC -!- MISCELLANEOUS: In vertebrates 3 main groups of actin isoforms, alpha,
CC beta and gamma have been identified. The alpha actins are found in
CC muscle tissues and are a major constituent of the contractile
CC apparatus. The beta and gamma actins coexist in most cell types as
CC components of the cytoskeleton and as mediators of internal cell
CC motility.
CC -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
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DR EMBL; AJ719332; CAG30991.1; -; mRNA.
DR RefSeq; NP_001295542.1; NM_001308613.1.
DR RefSeq; XP_015135388.1; XM_015279902.1.
DR AlphaFoldDB; Q5ZMQ2; -.
DR SMR; Q5ZMQ2; -.
DR IntAct; Q5ZMQ2; 1.
DR STRING; 9031.ENSGALP00000042680; -.
DR PRIDE; Q5ZMQ2; -.
DR Ensembl; ENSGALT00000061419; ENSGALP00000047898; ENSGALG00000028749.
DR GeneID; 776816; -.
DR KEGG; gga:776816; -.
DR CTD; 776816; -.
DR VEuPathDB; HostDB:LOC776816; -.
DR eggNOG; KOG0676; Eukaryota.
DR GeneTree; ENSGT00950000182960; -.
DR HOGENOM; CLU_027965_0_2_1; -.
DR InParanoid; Q5ZMQ2; -.
DR OMA; WICKSEY; -.
DR OrthoDB; 649708at2759; -.
DR Reactome; R-GGA-114608; Platelet degranulation.
DR Reactome; R-GGA-190873; Gap junction degradation.
DR Reactome; R-GGA-196025; Formation of annular gap junctions.
DR Reactome; R-GGA-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-GGA-3928662; EPHB-mediated forward signaling.
DR Reactome; R-GGA-3928665; EPH-ephrin mediated repulsion of cells.
DR Reactome; R-GGA-437239; Recycling pathway of L1.
DR Reactome; R-GGA-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-GGA-5626467; RHO GTPases activate IQGAPs.
DR Reactome; R-GGA-5663213; RHO GTPases Activate WASPs and WAVEs.
DR Reactome; R-GGA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-GGA-5674135; MAP2K and MAPK activation.
DR Reactome; R-GGA-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-GGA-9013418; RHOBTB2 GTPase cycle.
DR PRO; PR:Q5ZMQ2; -.
DR Proteomes; UP000000539; Chromosome 18.
DR Bgee; ENSGALG00000028749; Expressed in cerebellum and 12 other tissues.
DR ExpressionAtlas; Q5ZMQ2; baseline and differential.
DR GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; ISS:AgBase.
DR GO; GO:0097433; C:dense body; ISS:AgBase.
DR GO; GO:0005925; C:focal adhesion; ISS:AgBase.
DR GO; GO:0005886; C:plasma membrane; ISS:AgBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0098973; F:structural constituent of postsynaptic actin cytoskeleton; IBA:GO_Central.
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 1: Evidence at protein level;
KW Acetylation; ATP-binding; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Methylation; Nucleotide-binding; Oxidation;
KW Reference proteome.
FT CHAIN 1..375
FT /note="Actin, cytoplasmic 2"
FT /id="PRO_0000367105"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000269|Ref.2"
FT CHAIN 2..375
FT /note="Actin, cytoplasmic 2, N-terminally processed"
FT /id="PRO_0000280766"
FT MOD_RES 1
FT /note="N-acetylmethionine; in Actin, cytoplasmic 2;
FT alternate"
FT /evidence="ECO:0000250|UniProtKB:P63261"
FT MOD_RES 2
FT /note="N-acetylglutamate; in Actin, cytoplasmic 2, N-
FT terminally processed"
FT /evidence="ECO:0000269|Ref.2"
FT MOD_RES 44
FT /note="Methionine (R)-sulfoxide"
FT /evidence="ECO:0000250|UniProtKB:P63260"
FT MOD_RES 47
FT /note="Methionine (R)-sulfoxide"
FT /evidence="ECO:0000250|UniProtKB:P63260"
FT MOD_RES 73
FT /note="Tele-methylhistidine"
FT /evidence="ECO:0000250|UniProtKB:P63260"
SQ SEQUENCE 375 AA; 41793 MW; 54D08F986964EFD5 CRC64;
MEEEIAALVI DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS
KRGILTLKYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE HPVLLTEAPL NPKANREKMT
QIMFETFNTP AMYVAIQAVL SLYASGRTTG IVMDSGDGVT HTVPIYEGYA LPHAILRLDL
AGRDLTDYLM KILTERGYSF TTTAEREIVR DIKEKLCYVA LDFEQEMATA ASSSSLEKSY
ELPDGQVITI GNERFRCPEA LFQPSFLGME SCGIHETTFN SIMKCDVDIR KDLYANTVLS
GGTTMYPGIA DRMQKEITAL APSTMKIKII APPERKYSVW IGGSILASLS TFQQMWISKQ
EYDESGPSIV HRKCF
