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Actin-related protein 3 (Actin-like protein 3)

 ARP3_RAT                Reviewed;         418 AA.
Q4V7C7; A9CM89; A9CM90;
01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
05-JUL-2005, sequence version 1.
22-NOV-2017, entry version 99.
RecName: Full=Actin-related protein 3;
AltName: Full=Actin-like protein 3;
Name=Actr3; Synonyms=Arp3;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], VARIANT PHE-111, AND TISSUE SPECIFICITY.
STRAIN=Buffalo/Mna, and Wistar Kyoto/Ncrj; TISSUE=Kidney;
PubMed=18064521; DOI=10.1007/s00335-007-9078-5;
Akiyama K., Morita H., Suetsugu S., Kuraba S., Numata Y., Yamamoto Y.,
Inui K., Ideura T., Wakisaka N., Nakano K., Oniki H., Takenawa T.,
Matsuyama M., Yoshimura A.;
"Actin-related protein 3 (Arp3) is mutated in proteinuric BUF/Mna
rats.";
Mamm. Genome 19:41-50(2008).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Brown Norway; TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
PubMed=19343716; DOI=10.1002/pmic.200800664;
Maurya D.K., Sundaram C.S., Bhargava P.;
"Proteome profile of the mature rat olfactory bulb.";
Proteomics 9:2593-2599(2009).
-!- FUNCTION: Functions as ATP-binding component of the Arp2/3 complex
which is involved in regulation of actin polymerization and
together with an activating nucleation-promoting factor (NPF)
mediates the formation of branched actin networks. Seems to
contact the pointed end of the daughter actin filament. Plays a
role in ciliogenesis (By similarity). {ECO:0000250}.
-!- SUBUNIT: Component of the Arp2/3 complex composed of ARP2, ARP3,
ARPC1B/p41-ARC, ARPC2/p34-ARC, ARPC3/p21-ARC, ARPC4/p20-ARC and
ARPC5/p16-ARC. Interacts with WHDC1. Interacts weakly with MEFV
(By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
{ECO:0000250|UniProtKB:P61158}. Cell projection
{ECO:0000250|UniProtKB:P61158}. Note=In pre-apoptotic cells,
colocalizes with MEFV in large specks (pyroptosomes).
{ECO:0000250|UniProtKB:P61158}.
-!- TISSUE SPECIFICITY: Detected in brain and kidney glomeruli (at
protein level). Detected in kidney, lung and spleen.
{ECO:0000269|PubMed:18064521}.
-!- SIMILARITY: Belongs to the actin family. ARP3 subfamily.
{ECO:0000305}.
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EMBL; AB292042; BAF94208.1; -; mRNA.
EMBL; AB292043; BAF94209.1; -; mRNA.
EMBL; AB294577; BAF94221.1; -; Genomic_DNA.
EMBL; AB294578; BAF94241.1; -; Genomic_DNA.
EMBL; BC098014; AAH98014.1; -; mRNA.
RefSeq; NP_112330.1; NM_031068.1.
UniGene; Rn.103326; -.
ProteinModelPortal; Q4V7C7; -.
SMR; Q4V7C7; -.
BioGrid; 249604; 1.
IntAct; Q4V7C7; 2.
MINT; MINT-3376858; -.
STRING; 10116.ENSRNOP00000004520; -.
iPTMnet; Q4V7C7; -.
PhosphoSitePlus; Q4V7C7; -.
World-2DPAGE; 0004:Q4V7C7; -.
PaxDb; Q4V7C7; -.
PRIDE; Q4V7C7; -.
Ensembl; ENSRNOT00000004520; ENSRNOP00000004520; ENSRNOG00000003206.
GeneID; 81732; -.
KEGG; rno:81732; -.
UCSC; RGD:71024; rat.
CTD; 10096; -.
RGD; 71024; Actr3.
eggNOG; KOG0678; Eukaryota.
eggNOG; COG5277; LUCA.
GeneTree; ENSGT00550000074695; -.
HOGENOM; HOG000233339; -.
HOVERGEN; HBG003771; -.
InParanoid; Q4V7C7; -.
KO; K18584; -.
PhylomeDB; Q4V7C7; -.
Reactome; R-RNO-2029482; Regulation of actin dynamics for phagocytic cup formation.
Reactome; R-RNO-3928662; EPHB-mediated forward signaling.
Reactome; R-RNO-5663213; RHO GTPases Activate WASPs and WAVEs.
Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
PRO; PR:Q4V7C7; -.
Proteomes; UP000002494; Chromosome 13.
Bgee; ENSRNOG00000003206; -.
ExpressionAtlas; Q4V7C7; baseline and differential.
Genevisible; Q4V7C7; RN.
GO; GO:0061831; C:apical ectoplasmic specialization; IDA:RGD.
GO; GO:0061828; C:apical tubulobulbar complex; IDA:RGD.
GO; GO:0005885; C:Arp2/3 protein complex; ISO:RGD.
GO; GO:0061832; C:basal ectoplasmic specialization; IDA:RGD.
GO; GO:0005903; C:brush border; ISO:RGD.
GO; GO:0031252; C:cell leading edge; IDA:RGD.
GO; GO:0005911; C:cell-cell junction; IDA:RGD.
GO; GO:0061830; C:concave side of sperm head; IDA:RGD.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0060076; C:excitatory synapse; IDA:RGD.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0005925; C:focal adhesion; ISO:RGD.
GO; GO:0000139; C:Golgi membrane; IDA:RGD.
GO; GO:0030056; C:hemidesmosome; IDA:RGD.
GO; GO:0030027; C:lamellipodium; IDA:RGD.
GO; GO:0061851; C:leading edge of lamellipodium; IDA:RGD.
GO; GO:0016020; C:membrane; ISO:RGD.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
GO; GO:0002102; C:podosome; IDA:RGD.
GO; GO:0061825; C:podosome core; IDA:RGD.
GO; GO:0001726; C:ruffle; IDA:RGD.
GO; GO:0003779; F:actin binding; IDA:RGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0051117; F:ATPase binding; IPI:RGD.
GO; GO:0005200; F:structural constituent of cytoskeleton; ISO:RGD.
GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; ISO:RGD.
GO; GO:0048708; P:astrocyte differentiation; IMP:RGD.
GO; GO:0008356; P:asymmetric cell division; ISO:RGD.
GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IEP:RGD.
GO; GO:0071347; P:cellular response to interleukin-1; IEP:RGD.
GO; GO:1905835; P:cellular response to pyrimidine ribonucleotide; IEP:RGD.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IDA:RGD.
GO; GO:0035984; P:cellular response to trichostatin A; IEP:RGD.
GO; GO:1905837; P:cellular response to triterpenoid; IEP:RGD.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IDA:RGD.
GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
GO; GO:0007163; P:establishment or maintenance of cell polarity; ISO:RGD.
GO; GO:0051321; P:meiotic cell cycle; ISO:RGD.
GO; GO:0016344; P:meiotic chromosome movement towards spindle pole; ISO:RGD.
GO; GO:0033206; P:meiotic cytokinesis; ISO:RGD.
GO; GO:0030517; P:negative regulation of axon extension; IMP:RGD.
GO; GO:1904171; P:negative regulation of bleb assembly; IMP:RGD.
GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; IMP:RGD.
GO; GO:0030838; P:positive regulation of actin filament polymerization; IMP:RGD.
GO; GO:0048711; P:positive regulation of astrocyte differentiation; IMP:RGD.
GO; GO:0050775; P:positive regulation of dendrite morphogenesis; IMP:RGD.
GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; IMP:RGD.
GO; GO:0010763; P:positive regulation of fibroblast migration; IMP:RGD.
GO; GO:0051491; P:positive regulation of filopodium assembly; IMP:RGD.
GO; GO:0010592; P:positive regulation of lamellipodium assembly; IMP:RGD.
GO; GO:0045666; P:positive regulation of neuron differentiation; IMP:RGD.
GO; GO:0032092; P:positive regulation of protein binding; IMP:RGD.
GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IMP:RGD.
GO; GO:0090314; P:positive regulation of protein targeting to membrane; IMP:RGD.
GO; GO:0051965; P:positive regulation of synapse assembly; IMP:RGD.
GO; GO:0043519; P:regulation of myosin II filament organization; IMP:RGD.
GO; GO:0032355; P:response to estradiol; IEP:RGD.
GO; GO:0071503; P:response to heparin; IEP:RGD.
GO; GO:0061843; P:Sertoli cell barrier remodeling; IEP:RGD.
GO; GO:0007283; P:spermatogenesis; IEP:RGD.
GO; GO:0051653; P:spindle localization; ISO:RGD.
InterPro; IPR004000; Actin.
InterPro; IPR020902; Actin/actin-like_CS.
InterPro; IPR015623; Arp3.
PANTHER; PTHR11937; PTHR11937; 1.
PANTHER; PTHR11937:SF175; PTHR11937:SF175; 1.
Pfam; PF00022; Actin; 1.
SMART; SM00268; ACTIN; 1.
PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
1: Evidence at protein level;
Acetylation; Actin-binding; ATP-binding; Cell projection;
Cilium biogenesis/degradation; Complete proteome; Cytoplasm;
Cytoskeleton; Nucleotide-binding; Polymorphism; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P61158}.
CHAIN 2 418 Actin-related protein 3.
/FTId=PRO_0000342356.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:P61158}.
MOD_RES 240 240 N6-acetyllysine.
{ECO:0000250|UniProtKB:P61158}.
MOD_RES 244 244 N6-acetyllysine.
{ECO:0000250|UniProtKB:P61158}.
MOD_RES 251 251 N6-acetyllysine.
{ECO:0000250|UniProtKB:P61158}.
MOD_RES 254 254 N6-acetyllysine.
{ECO:0000250|UniProtKB:P61158}.
VARIANT 111 111 L -> F. {ECO:0000269|PubMed:18064521}.
SEQUENCE 418 AA; 47357 MW; 806FED7A08ABA455 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 KWIKQYTGVN AISKKEFSID VGYERFLGPE IFFHPEFANP DFTQPISEVV
DEVIQNCPID VRRPLYKNIV LSGGSTMFRD FGRRLQRDLK RTVDARLKLS EELSGGRLKP
KPIDVQVITH HMQRYAVWFG GSMLASTPEF YQVCHTKKDY EEIGPSICRH NPVFGVMS


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