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Protein

Actin-related protein 3

Gene

ACTR3

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 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

  1. ATP binding Source: UniProtKB-KW
  2. structural constituent of cytoskeleton Source: Ensembl

GO - Biological processi

  1. Arp2/3 complex-mediated actin nucleation Source: Ensembl
  2. asymmetric cell division Source: Ensembl
  3. cilium morphogenesis Source: UniProtKB
  4. establishment or maintenance of cell polarity Source: Ensembl
  5. meiotic chromosome movement towards spindle pole Source: Ensembl
  6. meiotic cytokinesis Source: Ensembl
  7. spindle localization Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Cilium biogenesis/degradation

Keywords - Ligandi

Actin-binding, ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_211475. Regulation of actin dynamics for phagocytic cup formation.
REACT_259381. EPHB-mediated forward signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Actin-related protein 3
Alternative name(s):
Actin-2
Actin-like protein 3
Gene namesi
Name:ACTR3
Synonyms:ARP3
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Unplaced

Subcellular locationi

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

GO - Cellular componenti

  1. Arp2/3 protein complex Source: Ensembl
  2. cell-cell junction Source: Ensembl
  3. cytosol Source: Reactome
  4. extracellular vesicular exosome Source: Ensembl
  5. focal adhesion Source: Ensembl
  6. lamellipodium Source: Ensembl
  7. membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 418417Actin-related protein 3PRO_0000089078Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP61157.
PRIDEiP61157.

Expressioni

Gene expression databases

ExpressionAtlasiP61157. baseline.

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
CttnQ605984EBI-351419,EBI-397955From a different organism.
PTK2Q009445EBI-351419,EBI-2896409From a different organism.
WASLO004013EBI-351419,EBI-957615From a different organism.

Protein-protein interaction databases

DIPiDIP-29790N.
IntActiP61157. 5 interactions.
STRINGi9913.ENSBTAP00000004410.

Structurei

Secondary structure

1
418
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 125Combined sources
Beta strandi14 – 218Combined sources
Beta strandi28 – 336Combined sources
Beta strandi35 – 373Combined sources
Helixi56 – 583Combined sources
Beta strandi60 – 623Combined sources
Helixi63 – 664Combined sources
Beta strandi72 – 754Combined sources
Turni77 – 804Combined sources
Beta strandi82 – 843Combined sources
Helixi86 – 9813Combined sources
Turni99 – 1013Combined sources
Helixi105 – 1073Combined sources
Beta strandi110 – 1145Combined sources
Helixi120 – 13213Combined sources
Beta strandi137 – 1437Combined sources
Helixi144 – 1518Combined sources
Helixi152 – 1543Combined sources
Beta strandi155 – 1573Combined sources
Beta strandi165 – 1739Combined sources
Beta strandi175 – 1817Combined sources
Helixi187 – 1893Combined sources
Beta strandi191 – 1944Combined sources
Helixi197 – 20913Combined sources
Helixi217 – 2193Combined sources
Helixi220 – 23112Combined sources
Helixi238 – 24710Combined sources
Helixi249 – 2513Combined sources
Beta strandi254 – 2596Combined sources
Turni261 – 2633Combined sources
Beta strandi266 – 2716Combined sources
Helixi274 – 2807Combined sources
Turni281 – 2833Combined sources
Helixi285 – 2873Combined sources
Helixi296 – 30611Combined sources
Helixi309 – 3113Combined sources
Helixi314 – 3174Combined sources
Beta strandi319 – 3235Combined sources
Helixi324 – 3263Combined sources
Helixi331 – 35323Combined sources
Turni372 – 3754Combined sources
Helixi376 – 3849Combined sources
Helixi388 – 3936Combined sources
Beta strandi394 – 3963Combined sources
Helixi397 – 4037Combined sources
Helixi405 – 4095Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K8KX-ray2.00A1-418[»]
1TYQX-ray2.55A1-418[»]
1U2VX-ray2.55A1-418[»]
2P9IX-ray2.46A1-418[»]
2P9KX-ray2.59A1-418[»]
2P9LX-ray2.65A1-418[»]
2P9NX-ray2.85A1-418[»]
2P9PX-ray2.90A1-418[»]
2P9SX-ray2.68A1-418[»]
2P9UX-ray2.75A1-418[»]
3DXKX-ray2.70A1-418[»]
3DXMX-ray2.85A1-418[»]
3RSEX-ray2.65A1-418[»]
3UKRX-ray2.48A1-418[»]
3UKUX-ray2.75A1-418[»]
3ULEX-ray2.50A1-418[»]
4JD2X-ray3.08A1-418[»]
ProteinModelPortaliP61157.
SMRiP61157. Positions 3-417.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP61157.

Family & Domainsi

Sequence similaritiesi

Belongs to the actin family. ARP3 subfamily.Curated

Phylogenomic databases

eggNOGiCOG5277.
HOGENOMiHOG000233339.
HOVERGENiHBG003771.
InParanoidiP61157.
KOiK18584.

Family and domain databases

InterProiIPR004000. Actin.
IPR020902. Actin/actin-like_CS.
IPR015623. Arp3.
[Graphical view]
PANTHERiPTHR11937. PTHR11937. 1 hit.
PTHR11937:SF175. PTHR11937:SF175. 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.

P61157-1 [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
KWIKQYTGIN 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):47,371
Last modified:January 23, 2007 - v3
Checksum:i23E5564198B81C63
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti344 – 3441D → G in AAI23583 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D12816 mRNA. Translation: BAA02249.1.
BC123582 mRNA. Translation: AAI23583.1.
BC142009 mRNA. Translation: AAI42010.1.
PIRiJQ1616.
RefSeqiNP_776651.1. NM_174226.2.
UniGeneiBt.4292.

Genome annotation databases

GeneIDi281597.
KEGGibta:281597.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D12816 mRNA. Translation: BAA02249.1.
BC123582 mRNA. Translation: AAI23583.1.
BC142009 mRNA. Translation: AAI42010.1.
PIRiJQ1616.
RefSeqiNP_776651.1. NM_174226.2.
UniGeneiBt.4292.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K8KX-ray2.00A1-418[»]
1TYQX-ray2.55A1-418[»]
1U2VX-ray2.55A1-418[»]
2P9IX-ray2.46A1-418[»]
2P9KX-ray2.59A1-418[»]
2P9LX-ray2.65A1-418[»]
2P9NX-ray2.85A1-418[»]
2P9PX-ray2.90A1-418[»]
2P9SX-ray2.68A1-418[»]
2P9UX-ray2.75A1-418[»]
3DXKX-ray2.70A1-418[»]
3DXMX-ray2.85A1-418[»]
3RSEX-ray2.65A1-418[»]
3UKRX-ray2.48A1-418[»]
3UKUX-ray2.75A1-418[»]
3ULEX-ray2.50A1-418[»]
4JD2X-ray3.08A1-418[»]
ProteinModelPortaliP61157.
SMRiP61157. Positions 3-417.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29790N.
IntActiP61157. 5 interactions.
STRINGi9913.ENSBTAP00000004410.

Proteomic databases

PaxDbiP61157.
PRIDEiP61157.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi281597.
KEGGibta:281597.

Organism-specific databases

CTDi10096.

Phylogenomic databases

eggNOGiCOG5277.
HOGENOMiHOG000233339.
HOVERGENiHBG003771.
InParanoidiP61157.
KOiK18584.

Enzyme and pathway databases

ReactomeiREACT_211475. Regulation of actin dynamics for phagocytic cup formation.
REACT_259381. EPHB-mediated forward signaling.

Miscellaneous databases

EvolutionaryTraceiP61157.
NextBioi20805540.

Gene expression databases

ExpressionAtlasiP61157. baseline.

Family and domain databases

InterProiIPR004000. Actin.
IPR020902. Actin/actin-like_CS.
IPR015623. Arp3.
[Graphical view]
PANTHERiPTHR11937. PTHR11937. 1 hit.
PTHR11937:SF175. PTHR11937:SF175. 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. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Thymus.
  2. NIH - Mammalian Gene Collection (MGC) project
    Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Thymus.
  3. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF ARP2/3 COMPLEX.
  4. "Crystal structures of actin-related protein 2/3 complex with bound ATP or ADP."
    Nolen B.J., Littlefield R.S., Pollard T.D.
    Proc. Natl. Acad. Sci. U.S.A. 101:15627-15632(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF ARP2/3 COMPLEX WITH BOUND ATP.

Entry informationi

Entry nameiARP3_BOVIN
AccessioniPrimary (citable) accession number: P61157
Secondary accession number(s): A5PJ90, P32391, Q08DS8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: January 23, 2007
Last modified: March 4, 2015
This is version 100 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.