ID ACTB_PANTR Reviewed; 375 AA.
AC Q5R1X3;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 01-MAY-2013, entry version 74.
DE RecName: Full=Actin, cytoplasmic 1;
DE AltName: Full=Beta-actin;
DE Contains:
DE RecName: Full=Actin, cytoplasmic 1, N-terminally processed;
GN Name=ACTB;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Cerebellum;
RA Hirai M., Sakate R., Hida M., Sugano S., Hayasaka I., Suto Y.,
RA Osada N., Hashimoto K.;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Actins are highly conserved proteins that are involved
CC in various types of cell motility and are ubiquitously expressed
CC in all eukaryotic cells.
CC -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a
CC structural filament (F-actin) in the form of a two-stranded helix.
CC Each actin can bind to 4 others. Identified in a mRNP granule
CC complex, at least composed of ACTB, ACTN4, DHX9, ERG, HNRNPA1,
CC HNRNPA2B1, HNRNPAB, HNRNPD, HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8,
CC IGF2BP1, ILF2, ILF3, NCBP1, NCL, PABPC1, PABPC4, PABPN1, RPLP0,
CC RPS3, RPS3A, RPS4X, RPS8, RPS9, SYNCRIP, TROVE2, YBX1 and
CC untranslated mRNAs. Component of the BAF complex, which includes
CC at least actin (ACTB), ARID1A, ARID1B/BAF250, SMARCA2,
CC SMARCA4/BRG1, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57,
CC SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more
CC of SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C. In muscle
CC cells, the BAF complex also contains DPF3. Found in a complex with
CC XPO6, Ran, ACTB and PFN1. Component of the MLL5-L complex, at
CC least composed of MLL5, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB
CC and OGT. Interacts with XPO6 and EMD. Interacts with ERBB2 (By
CC similarity). Interacts with GCSAM (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Note=Localized in
CC cytoplasmic mRNP granules containing untranslated mRNAs (By
CC similarity).
CC -!- PTM: ISGylated (By similarity).
CC -!- PTM: Oxidation of Met-44 by MICALs (MICAL1, MICAL2 or MICAL3) to
CC form methionine sulfoxide promotes actin filament
CC depolymerization. Methionine sulfoxide is produced
CC stereospecifically, but it is not known whether the (S)-S-oxide or
CC the (R)-S-oxide is produced (By similarity).
CC -!- MISCELLANEOUS: In vertebrates 3 main groups of actin isoforms,
CC alpha, beta and gamma have been identified. The alpha actins are
CC found in muscle tissues and are a major constituent of the
CC contractile apparatus. The beta and gamma actins coexist in most
CC cell types as components of the cytoskeleton and as mediators of
CC internal cell motility.
CC -!- SIMILARITY: Belongs to the actin family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AB188274; BAD74025.1; -; mRNA.
DR RefSeq; NP_001009945.1; NM_001009945.1.
DR UniGene; Ptr.177; -.
DR ProteinModelPortal; Q5R1X3; -.
DR STRING; 9598.ENSPTRP00000039339; -.
DR PRIDE; Q5R1X3; -.
DR Ensembl; ENSPTRT00000042865; ENSPTRP00000039339; ENSPTRG00000018890.
DR GeneID; 450133; -.
DR KEGG; ptr:450133; -.
DR CTD; 60; -.
DR eggNOG; COG0666; -.
DR GeneTree; ENSGT00690000101979; -.
DR HOGENOM; HOG000233340; -.
DR HOVERGEN; HBG003771; -.
DR InParanoid; Q5R1X3; -.
DR KO; K05692; -.
DR OrthoDB; EOG41JZC9; -.
DR NextBio; 20833096; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR InterPro; IPR004000; Actin-related.
DR InterPro; IPR020902; Actin/actin-like_CS.
DR InterPro; IPR004001; Actin_CS.
DR PANTHER; PTHR11937; PTHR11937; 1.
DR Pfam; PF00022; Actin; 1.
DR PRINTS; PR00190; ACTIN.
DR SMART; SM00268; ACTIN; 1.
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; Complete proteome; Cytoplasm; Cytoskeleton;
KW Methylation; Nucleotide-binding; Oxidation; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1 375 Actin, cytoplasmic 1.
FT /FTId=PRO_0000367077.
FT INIT_MET 1 1 Removed; alternate (By similarity).
FT CHAIN 2 375 Actin, cytoplasmic 1, N-terminally
FT processed.
FT /FTId=PRO_0000000777.
FT MOD_RES 1 1 N-acetylmethionine (By similarity).
FT MOD_RES 2 2 N-acetylaspartate; in Actin, cytoplasmic
FT 1, N-terminally processed (By
FT similarity).
FT MOD_RES 44 44 Methionine sulfoxide (By similarity).
FT MOD_RES 73 73 Tele-methylhistidine (By similarity).
SQ SEQUENCE 375 AA; 41737 MW; 6AFD05CA94E360E2 CRC64;
MDDDIAALVV 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
//
