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Protein

Actin-related protein 2/3 complex subunit 1B

Gene

ARPC1B

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Functions as 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.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Actin-related protein 2/3 complex subunit 1B
Alternative name(s):
Arp2/3 complex 41 kDa subunit
p41-ARC
Gene namesi
Name:ARPC1B
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 25

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002397012 – 372Actin-related protein 2/3 complex subunit 1BAdd BLAST371

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei82N6-acetyllysineBy similarity1
Modified residuei310PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ58CQ2.
PeptideAtlasiQ58CQ2.
PRIDEiQ58CQ2.

Expressioni

Gene expression databases

BgeeiENSBTAG00000046248.

Interactioni

Subunit structurei

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.

GO - Molecular functioni

Protein-protein interaction databases

DIPiDIP-29791N.
STRINGi9913.ENSBTAP00000056302.

Structurei

Secondary structure

1372
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 6Combined sources4
Beta strandi14 – 16Combined sources3
Beta strandi20 – 25Combined sources6
Beta strandi28 – 38Combined sources11
Beta strandi41 – 49Combined sources9
Beta strandi55 – 61Combined sources7
Turni62 – 65Combined sources4
Beta strandi66 – 71Combined sources6
Beta strandi72 – 74Combined sources3
Beta strandi76 – 82Combined sources7
Beta strandi85 – 91Combined sources7
Beta strandi99 – 104Combined sources6
Beta strandi108 – 115Combined sources8
Beta strandi118 – 126Combined sources9
Turni127 – 130Combined sources4
Beta strandi131 – 137Combined sources7
Beta strandi145 – 150Combined sources6
Beta strandi154 – 161Combined sources8
Beta strandi166 – 170Combined sources5
Turni174 – 176Combined sources3
Beta strandi194 – 197Combined sources4
Beta strandi201 – 203Combined sources3
Beta strandi205 – 210Combined sources6
Beta strandi212 – 221Combined sources10
Turni222 – 224Combined sources3
Beta strandi225 – 230Combined sources6
Helixi231 – 233Combined sources3
Beta strandi237 – 241Combined sources5
Beta strandi243 – 245Combined sources3
Beta strandi247 – 254Combined sources8
Beta strandi257 – 262Combined sources6
Beta strandi268 – 273Combined sources6
Turni274 – 277Combined sources4
Beta strandi278 – 281Combined sources4
Helixi298 – 304Combined sources7
Beta strandi322 – 327Combined sources6
Beta strandi329 – 337Combined sources9
Turni338 – 340Combined sources3
Beta strandi343 – 349Combined sources7
Beta strandi352 – 358Combined sources7
Helixi359 – 365Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K8KX-ray2.00C1-372[»]
1TYQX-ray2.55C1-372[»]
1U2VX-ray2.55C1-372[»]
2P9IX-ray2.46C1-372[»]
2P9KX-ray2.59C1-372[»]
2P9LX-ray2.65C1-372[»]
2P9NX-ray2.85C1-372[»]
2P9PX-ray2.90C1-372[»]
2P9SX-ray2.68C1-372[»]
2P9UX-ray2.75C1-372[»]
3DXKX-ray2.70C1-372[»]
3DXMX-ray2.85C1-372[»]
3RSEX-ray2.65C1-372[»]
3UKRX-ray2.48C1-372[»]
3UKUX-ray2.75C1-372[»]
3ULEX-ray2.50C1-372[»]
4JD2X-ray3.08C1-372[»]
4XEIX-ray3.87C1-372[»]
4XF2X-ray5.00C/V1-372[»]
ProteinModelPortaliQ58CQ2.
SMRiQ58CQ2.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ58CQ2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati6 – 45WD 1Add BLAST40
Repeati50 – 89WD 2Add BLAST40
Repeati94 – 135WD 3Add BLAST42
Repeati140 – 179WD 4Add BLAST40
Repeati242 – 280WD 5Add BLAST39
Repeati324 – 367WD 6Add BLAST44

Sequence similaritiesi

Belongs to the WD repeat ARPC1 family.Curated
Contains 6 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiKOG1523. Eukaryota.
ENOG410XNWX. LUCA.
GeneTreeiENSGT00390000008339.
HOGENOMiHOG000181752.
HOVERGENiHBG050560.
InParanoidiQ58CQ2.
KOiK05757.
OMAiVLFTYDS.
OrthoDBiEOG091G096H.
TreeFamiTF315041.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR030141. ARC1B.
IPR017383. ARPC1.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
PANTHERiPTHR10709. PTHR10709. 1 hit.
PTHR10709:SF10. PTHR10709:SF10. 1 hit.
PfamiPF00400. WD40. 2 hits.
[Graphical view]
PIRSFiPIRSF038093. ARP2/3_su1. 1 hit.
SMARTiSM00320. WD40. 5 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS50082. WD_REPEATS_2. 1 hit.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q58CQ2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAYHSFLVEP ISCHAWNKDR TQIAICPNNH EVHIYEKSGN KWVQVHELKE
60 70 80 90 100
HNGQVTGIDW APDSNRIVTC GTDRNAYVWT LKGRTWKPTL VILRINRAAR
110 120 130 140 150
CVRWAPNEKK FAVGSGSRVI SICYFEQEND WWVCKHIKKP IRSTVLSLDW
160 170 180 190 200
HPNSVLLAAG SCDFKCRIFS AYIKEVEERP APTPWGSKMP FGELMFESSS
210 220 230 240 250
SCGWVHGVCF SANGSRVAWV SHDSTVCLAD ADKKMAVATL ASETLPLLAV
260 270 280 290 300
TFITESSLVA AGHDCFPVLF TYDSAAGKLS FGGRLDVPKQ SSQRGLTARE
310 320 330 340 350
RFQNLDKKAS SEGSAAAGAG LDSLHKNSVS QISVLSGGKA KCSQFCTTGM
360 370
DGGMSIWDVR SLESALKDLK IV
Length:372
Mass (Da):40,976
Last modified:January 23, 2007 - v4
Checksum:iB412F9C50DC93748
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti66R → H in AAX46742 (PubMed:16305752).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT021526 mRNA. Translation: AAX46373.1.
BT021895 mRNA. Translation: AAX46742.1.
BT026160 mRNA. Translation: ABG66999.1.
BC102942 mRNA. Translation: AAI02943.1.
RefSeqiNP_001014844.1. NM_001014844.3.
UniGeneiBt.23192.

Genome annotation databases

EnsembliENSBTAT00000064158; ENSBTAP00000056302; ENSBTAG00000046248.
GeneIDi326600.
KEGGibta:326600.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT021526 mRNA. Translation: AAX46373.1.
BT021895 mRNA. Translation: AAX46742.1.
BT026160 mRNA. Translation: ABG66999.1.
BC102942 mRNA. Translation: AAI02943.1.
RefSeqiNP_001014844.1. NM_001014844.3.
UniGeneiBt.23192.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K8KX-ray2.00C1-372[»]
1TYQX-ray2.55C1-372[»]
1U2VX-ray2.55C1-372[»]
2P9IX-ray2.46C1-372[»]
2P9KX-ray2.59C1-372[»]
2P9LX-ray2.65C1-372[»]
2P9NX-ray2.85C1-372[»]
2P9PX-ray2.90C1-372[»]
2P9SX-ray2.68C1-372[»]
2P9UX-ray2.75C1-372[»]
3DXKX-ray2.70C1-372[»]
3DXMX-ray2.85C1-372[»]
3RSEX-ray2.65C1-372[»]
3UKRX-ray2.48C1-372[»]
3UKUX-ray2.75C1-372[»]
3ULEX-ray2.50C1-372[»]
4JD2X-ray3.08C1-372[»]
4XEIX-ray3.87C1-372[»]
4XF2X-ray5.00C/V1-372[»]
ProteinModelPortaliQ58CQ2.
SMRiQ58CQ2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29791N.
STRINGi9913.ENSBTAP00000056302.

Proteomic databases

PaxDbiQ58CQ2.
PeptideAtlasiQ58CQ2.
PRIDEiQ58CQ2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000064158; ENSBTAP00000056302; ENSBTAG00000046248.
GeneIDi326600.
KEGGibta:326600.

Organism-specific databases

CTDi10095.

Phylogenomic databases

eggNOGiKOG1523. Eukaryota.
ENOG410XNWX. LUCA.
GeneTreeiENSGT00390000008339.
HOGENOMiHOG000181752.
HOVERGENiHBG050560.
InParanoidiQ58CQ2.
KOiK05757.
OMAiVLFTYDS.
OrthoDBiEOG091G096H.
TreeFamiTF315041.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiQ58CQ2.

Gene expression databases

BgeeiENSBTAG00000046248.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR030141. ARC1B.
IPR017383. ARPC1.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
PANTHERiPTHR10709. PTHR10709. 1 hit.
PTHR10709:SF10. PTHR10709:SF10. 1 hit.
PfamiPF00400. WD40. 2 hits.
[Graphical view]
PIRSFiPIRSF038093. ARP2/3_su1. 1 hit.
SMARTiSM00320. WD40. 5 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS50082. WD_REPEATS_2. 1 hit.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiARC1B_BOVIN
AccessioniPrimary (citable) accession number: Q58CQ2
Secondary accession number(s): Q0V8Q8, Q58DS1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 102 of the entry and version 4 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

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.