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Protein

Actin-related protein 3

Gene

Actr3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Molecular functioni

GO - Biological processi

  • Arp2/3 complex-mediated actin nucleation Source: MGI
  • asymmetric cell division Source: MGI
  • cilium morphogenesis Source: UniProtKB
  • establishment or maintenance of cell polarity Source: MGI
  • meiotic cell cycle Source: MGI
  • meiotic chromosome movement towards spindle pole Source: MGI
  • meiotic cytokinesis Source: MGI
  • spindle localization Source: MGI
Complete GO annotation...

Keywords - Biological processi

Cilium biogenesis/degradation

Keywords - Ligandi

Actin-binding, ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-MMU-3928662. EPHB-mediated forward signaling.
R-MMU-5663213. RHO GTPases Activate WASPs and WAVEs.

Names & Taxonomyi

Protein namesi
Recommended name:
Actin-related protein 3
Alternative name(s):
Actin-like protein 3
Gene namesi
Name:Actr3
Synonyms:Arp3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1921367. Actr3.

Subcellular locationi

  • Cytoplasmcytoskeleton By similarity
  • Cell projection By similarity

  • Note: In pre-apoptotic cells, colocalizes with MEFV in large specks (pyroptosomes).By similarity

GO - Cellular componenti

  • Arp2/3 protein complex Source: MGI
  • brush border Source: UniProtKB
  • cell-cell junction Source: MGI
  • cytoplasm Source: UniProtKB-KW
  • extracellular exosome Source: MGI
  • focal adhesion Source: MGI
  • lamellipodium Source: MGI
  • membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 418417Actin-related protein 3PRO_0000089080Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei240 – 2401N6-acetyllysineBy similarity
Modified residuei244 – 2441N6-acetyllysineCombined sources
Modified residuei251 – 2511N6-acetyllysineBy similarity
Modified residuei254 – 2541N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ99JY9.
MaxQBiQ99JY9.
PaxDbiQ99JY9.
PRIDEiQ99JY9.

PTM databases

iPTMnetiQ99JY9.
SwissPalmiQ99JY9.

Expressioni

Gene expression databases

BgeeiQ99JY9.
CleanExiMM_ACTR3.
ExpressionAtlasiQ99JY9. baseline and differential.
GenevisibleiQ99JY9. MM.

Interactioni

Subunit structurei

Component of the Arp2/3 complex composed of ARP2, ARP3, ARPC1B, 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).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
CttnQ605985EBI-773994,EBI-397955

Protein-protein interaction databases

BioGridi216504. 5 interactions.
IntActiQ99JY9. 14 interactions.
MINTiMINT-1863083.
STRINGi10090.ENSMUSP00000027579.

Structurei

3D structure databases

ProteinModelPortaliQ99JY9.
SMRiQ99JY9. Positions 3-417.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the actin family. ARP3 subfamily.Curated

Phylogenomic databases

eggNOGiKOG0678. Eukaryota.
COG5277. LUCA.
GeneTreeiENSGT00550000074695.
HOGENOMiHOG000233339.
HOVERGENiHBG003771.
InParanoidiQ99JY9.
KOiK18584.
OMAiKMQRYAV.
OrthoDBiEOG7TMZRM.
PhylomeDBiQ99JY9.
TreeFamiTF300644.

Family and domain databases

InterProiIPR004000. Actin.
IPR020902. Actin/actin-like_CS.
IPR015623. Arp3_met.
[Graphical view]
PANTHERiPTHR11937. PTHR11937. 1 hit.
PTHR11937:SF253. PTHR11937:SF253. 1 hit.
PfamiPF00022. Actin. 1 hit.
[Graphical view]
SMARTiSM00268. ACTIN. 1 hit.
[Graphical view]
PROSITEiPS01132. ACTINS_ACT_LIKE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q99JY9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGRLPACVV DCGTGYTKLG YAGNTEPQFI IPSCIAIKES AKVGDQAQRR
60 70 80 90 100
VMKGVDDLDF FIGDEAIEKP TYATKWPIRH GIVEDWDLME RFMEQVIFKY
110 120 130 140 150
LRAEPEDHYF LLTEPPLNTP ENREYTAEIM FESFNVPGLY IAVQAVLALA
160 170 180 190 200
ASWTSRQVGE RTLTGTVIDS GDGVTHVIPV AEGYVIGSCI KHIPIAGRDI
210 220 230 240 250
TYFIQQLLRD REVGIPPEQS LETAKAVKER YSYVCPDLVK EFNKYDTDGS
260 270 280 290 300
KWIKQYTGVN AISKKEFSID VGYERFLGPE IFFHPEFANP DFTQPISEVV
310 320 330 340 350
DEVIQNCPID VRRPLYKNIV LSGGSTMFRD FGRRLQRDLK RTVDARLKLS
360 370 380 390 400
EELSGGRLKP KPIDVQVITH HMQRYAVWFG GSMLASTPEF YQVCHTKKDY
410
EEIGPSICRH NPVFGVMS
Length:418
Mass (Da):47,357
Last modified:January 23, 2007 - v3
Checksum:i806FED7A08ABA455
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti176 – 1761H → P in BAB23368 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004554 mRNA. Translation: BAB23368.1.
AK083343 mRNA. Translation: BAC38876.1.
BC005557 mRNA. Translation: AAH05557.1.
BC080806 mRNA. Translation: AAH80806.1.
CCDSiCCDS15242.1.
RefSeqiNP_001192314.1. NM_001205385.1.
NP_001192315.1. NM_001205386.1.
NP_076224.1. NM_023735.2.
UniGeneiMm.183102.
Mm.471990.

Genome annotation databases

EnsembliENSMUST00000027579; ENSMUSP00000027579; ENSMUSG00000026341.
ENSMUST00000178474; ENSMUSP00000137503; ENSMUSG00000026341.
GeneIDi74117.
KEGGimmu:74117.
UCSCiuc007cke.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004554 mRNA. Translation: BAB23368.1.
AK083343 mRNA. Translation: BAC38876.1.
BC005557 mRNA. Translation: AAH05557.1.
BC080806 mRNA. Translation: AAH80806.1.
CCDSiCCDS15242.1.
RefSeqiNP_001192314.1. NM_001205385.1.
NP_001192315.1. NM_001205386.1.
NP_076224.1. NM_023735.2.
UniGeneiMm.183102.
Mm.471990.

3D structure databases

ProteinModelPortaliQ99JY9.
SMRiQ99JY9. Positions 3-417.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi216504. 5 interactions.
IntActiQ99JY9. 14 interactions.
MINTiMINT-1863083.
STRINGi10090.ENSMUSP00000027579.

PTM databases

iPTMnetiQ99JY9.
SwissPalmiQ99JY9.

Proteomic databases

EPDiQ99JY9.
MaxQBiQ99JY9.
PaxDbiQ99JY9.
PRIDEiQ99JY9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000027579; ENSMUSP00000027579; ENSMUSG00000026341.
ENSMUST00000178474; ENSMUSP00000137503; ENSMUSG00000026341.
GeneIDi74117.
KEGGimmu:74117.
UCSCiuc007cke.2. mouse.

Organism-specific databases

CTDi10096.
MGIiMGI:1921367. Actr3.

Phylogenomic databases

eggNOGiKOG0678. Eukaryota.
COG5277. LUCA.
GeneTreeiENSGT00550000074695.
HOGENOMiHOG000233339.
HOVERGENiHBG003771.
InParanoidiQ99JY9.
KOiK18584.
OMAiKMQRYAV.
OrthoDBiEOG7TMZRM.
PhylomeDBiQ99JY9.
TreeFamiTF300644.

Enzyme and pathway databases

ReactomeiR-MMU-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-MMU-3928662. EPHB-mediated forward signaling.
R-MMU-5663213. RHO GTPases Activate WASPs and WAVEs.

Miscellaneous databases

ChiTaRSiActr3. mouse.
NextBioi339820.
PROiQ99JY9.
SOURCEiSearch...

Gene expression databases

BgeeiQ99JY9.
CleanExiMM_ACTR3.
ExpressionAtlasiQ99JY9. baseline and differential.
GenevisibleiQ99JY9. MM.

Family and domain databases

InterProiIPR004000. Actin.
IPR020902. Actin/actin-like_CS.
IPR015623. Arp3_met.
[Graphical view]
PANTHERiPTHR11937. PTHR11937. 1 hit.
PTHR11937:SF253. PTHR11937:SF253. 1 hit.
PfamiPF00022. Actin. 1 hit.
[Graphical view]
SMARTiSM00268. ACTIN. 1 hit.
[Graphical view]
PROSITEiPS01132. ACTINS_ACT_LIKE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Lung and Thymus.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Mammary gland.
  3. Lubec G., Klug S.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 103-123 AND 199-219, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Hippocampus.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-244, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiARP3_MOUSE
AccessioniPrimary (citable) accession number: Q99JY9
Secondary accession number(s): Q9DC56
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: January 23, 2007
Last modified: March 16, 2016
This is version 132 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.