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ARP3_TAKRU
ID   ARP3_TAKRU              Reviewed;         418 AA.
AC   O73723;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Actin-related protein 3;
DE   AltName: Full=Actin-like protein 3;
GN   Name=actr3; Synonyms=arp3;
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9573354; DOI=10.1016/s0378-1119(98)00096-1;
RA   Venkatesh B., Brenner S.;
RT   "Genomic structure and sequence of the pufferfish (Fugu rubripes) gene
RT   encoding an actin-related protein.";
RL   Gene 211:169-175(1998).
CC   -!- FUNCTION: ATP-binding component of the Arp2/3 complex, a multiprotein
CC       complex that mediates actin polymerization upon stimulation by
CC       nucleation-promoting factor (NPF). The Arp2/3 complex mediates the
CC       formation of branched actin networks in the cytoplasm, providing the
CC       force for cell motility (By similarity). Seems to contact the pointed
CC       end of the daughter actin filament (By similarity). In addition to its
CC       role in the cytoplasmic cytoskeleton, the Arp2/3 complex also promotes
CC       actin polymerization in the nucleus, thereby regulating gene
CC       transcription and repair of damaged DNA (By similarity). The Arp2/3
CC       complex promotes homologous recombination (HR) repair in response to
CC       DNA damage by promoting nuclear actin polymerization, leading to drive
CC       motility of double-strand breaks (DSBs) (By similarity).
CC       {ECO:0000250|UniProtKB:P61158, ECO:0000250|UniProtKB:Q801P7}.
CC   -!- SUBUNIT: Component of the Arp2/3 complex composed of actr2/arp2,
CC       actr3/arp3, arpc1b, arpc2, arpc3, arpc4 and arpc5.
CC       {ECO:0000250|UniProtKB:Q801P7}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:Q801P7}. Cell projection
CC       {ECO:0000250|UniProtKB:Q801P7}. Nucleus {ECO:0000250|UniProtKB:P61158}.
CC   -!- SIMILARITY: Belongs to the actin family. ARP3 subfamily. {ECO:0000305}.
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DR   EMBL; AF034581; AAC18521.1; -; Genomic_DNA.
DR   PIR; JC6567; JC6567.
DR   AlphaFoldDB; O73723; -.
DR   SMR; O73723; -.
DR   STRING; 31033.ENSTRUP00000026810; -.
DR   PRIDE; O73723; -.
DR   eggNOG; KOG0678; Eukaryota.
DR   InParanoid; O73723; -.
DR   Proteomes; UP000005226; Unplaced.
DR   GO; GO:0005885; C:Arp2/3 protein complex; ISS:UniProtKB.
DR   GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; ISS:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   InterPro; IPR004000; Actin.
DR   InterPro; IPR020902; Actin/actin-like_CS.
DR   InterPro; IPR015623; Arp3.
DR   InterPro; IPR043129; ATPase_NBD.
DR   PANTHER; PTHR11937; PTHR11937; 1.
DR   PANTHER; PTHR11937:SF175; PTHR11937:SF175; 1.
DR   Pfam; PF00022; Actin; 1.
DR   SMART; SM00268; ACTIN; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
DR   PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE   3: Inferred from homology;
KW   Actin-binding; ATP-binding; Cell projection; Cytoplasm; Cytoskeleton;
KW   Nucleotide-binding; Nucleus; Reference proteome.
FT   CHAIN           1..418
FT                   /note="Actin-related protein 3"
FT                   /id="PRO_0000089082"
SQ   SEQUENCE   418 AA;  47465 MW;  0B8C53B2C9F569C9 CRC64;
     MAGRLPACVV DCGTGYTKLG YAGNTEPQFI MPSCIAIKES SKVGDQAQRR MMRGVDDLDF
     FIGDEAIDKP PYATKWPIRH GIVEDWDLME RFMEQIIFKY LRAEPEDHYF LLTEPPLNTP
     ENREYTAEIM FESFNVPGLY IAVQAVLALA ASWTSRQVGE RTLTGTVIDS GDGVTHVIPV
     AEGYVIGSCI KHIPIAGRDI TYFTQQLLRE REVGIPPEQS LETAKAVKER FSYVCPDLVK
     EFNKYDTDGS KWIKQYTGIN AITKKEFTID VGYERFLGPE IFFHPEFANP DFTQPISEVV
     DEVIQNCPID VRRPLYKNIV LSGGSTMFRD FGRRLQRDLK RTVDARLKMS EELSGGKLKP
     KPIDVQVITH HMQRYAVWFG GSMLASTPEF YQVCHTKKDY EEIGPSICRH NPVFGVMS
 
 
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