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ARP3_PONAB
ID   ARP3_PONAB              Reviewed;         418 AA.
AC   Q5R8R1;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Actin-related protein 3;
DE   AltName: Full=Actin-like protein 3;
GN   Name=ACTR3; Synonyms=ARP3;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex, and Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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. Seems to contact the pointed end of the
CC       daughter actin filament. In podocytes, required for the formation of
CC       lamellipodia downstream of AVIL and PLCE1 regulation. In addition to
CC       its role in the cytoplasmic cytoskeleton, the Arp2/3 complex also
CC       promotes actin polymerization in the nucleus, thereby regulating gene
CC       transcription and repair of damaged DNA. The Arp2/3 complex promotes
CC       homologous recombination (HR) repair in response to DNA damage by
CC       promoting nuclear actin polymerization, leading to drive motility of
CC       double-strand breaks (DSBs). Plays a role in ciliogenesis.
CC       {ECO:0000250|UniProtKB:P61158}.
CC   -!- SUBUNIT: Component of the Arp2/3 complex composed of ACTR2/ARP2,
CC       ACTR3/ARP3, ARPC1B/p41-ARC, ARPC2/p34-ARC, ARPC3/p21-ARC, ARPC4/p20-ARC
CC       and ARPC5/p16-ARC. Interacts with WHDC1. Interacts weakly with MEFV.
CC       Interacts with AVIL. {ECO:0000250|UniProtKB:P61158}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:P61158}. Cell projection
CC       {ECO:0000250|UniProtKB:P61158}. Nucleus {ECO:0000250|UniProtKB:P61158}.
CC       Note=In pre-apoptotic cells, colocalizes with MEFV in large specks
CC       (pyroptosomes). {ECO:0000250|UniProtKB:P61158}.
CC   -!- SIMILARITY: Belongs to the actin family. ARP3 subfamily. {ECO:0000305}.
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DR   EMBL; CR859690; CAH91849.1; -; mRNA.
DR   EMBL; CR925987; CAI29632.1; -; mRNA.
DR   RefSeq; NP_001126071.1; NM_001132599.1.
DR   AlphaFoldDB; Q5R8R1; -.
DR   SMR; Q5R8R1; -.
DR   STRING; 9601.ENSPPYP00000014282; -.
DR   PRIDE; Q5R8R1; -.
DR   Ensembl; ENSPPYT00000062233; ENSPPYP00000039515; ENSPPYG00000036644.
DR   GeneID; 100173023; -.
DR   KEGG; pon:100173023; -.
DR   CTD; 10096; -.
DR   eggNOG; KOG0678; Eukaryota.
DR   GeneTree; ENSGT00940000155065; -.
DR   HOGENOM; CLU_027965_3_0_1; -.
DR   InParanoid; Q5R8R1; -.
DR   OMA; TAEFKSY; -.
DR   OrthoDB; 649708at2759; -.
DR   TreeFam; TF300644; -.
DR   Proteomes; UP000001595; Chromosome 2B.
DR   GO; GO:0005885; C:Arp2/3 protein complex; ISS:UniProtKB.
DR   GO; GO:0005903; C:brush border; IEA:Ensembl.
DR   GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB.
DR   GO; GO:0051015; F:actin filament binding; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:Ensembl.
DR   GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; ISS:UniProtKB.
DR   GO; GO:0008356; P:asymmetric cell division; IEA:Ensembl.
DR   GO; GO:0071346; P:cellular response to interferon-gamma; IEA:Ensembl.
DR   GO; GO:0060271; P:cilium assembly; IEA:Ensembl.
DR   GO; GO:0007163; P:establishment or maintenance of cell polarity; IEA:Ensembl.
DR   GO; GO:0016344; P:meiotic chromosome movement towards spindle pole; IEA:Ensembl.
DR   GO; GO:0033206; P:meiotic cytokinesis; IEA:Ensembl.
DR   GO; GO:0010592; P:positive regulation of lamellipodium assembly; ISS:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0051653; P:spindle localization; IEA:Ensembl.
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   2: Evidence at transcript level;
KW   Acetylation; Actin-binding; ATP-binding; Cell projection; Cytoplasm;
KW   Cytoskeleton; Nucleotide-binding; Nucleus; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P61158"
FT   CHAIN           2..418
FT                   /note="Actin-related protein 3"
FT                   /id="PRO_0000089081"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P61158"
FT   MOD_RES         240
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P61158"
FT   MOD_RES         244
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P61158"
FT   MOD_RES         251
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P61158"
FT   MOD_RES         254
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P61158"
SQ   SEQUENCE   418 AA;  47371 MW;  23E5564198B81C63 CRC64;
     MAGRLPACVV DCGTGYTKLG YAGNTEPQFI IPSCIAIKES AKVGDQAQRR VMKGVDDLDF
     FIGDEAIEKP TYATKWPIRH GIVEDWDLME RFMEQVIFKY LRAEPEDHYF LLTEPPLNTP
     ENREYTAEIM FESFNVPGLY IAVQAVLALA ASWTSRQVGE RTLTGTVIDS GDGVTHVIPV
     AEGYVIGSCI KHIPIAGRDI TYFIQQLLRD REVGIPPEQS LETAKAVKER YSYVCPDLVK
     EFNKYDTDGS KWIKQYTGIN AISKKEFSID VGYERFLGPE IFFHPEFANP DFTQPISEVV
     DEVIQNCPID VRRPLYKNIV LSGGSTMFRD FGRRLQRDLK RTVDARLKLS EELSGGRLKP
     KPIDVQVITH HMQRYAVWFG GSMLASTPEF YQVCHTKKDY EEIGPSICRH NPVFGVMS
 
 
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