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Protein

Profilin-1A

Gene
N/A
Organism
Acanthamoeba castellanii (Amoeba)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei116 – 1161Actin

GO - Molecular functioni

  • actin monomer binding Source: UniProtKB

GO - Biological processi

  • actin cytoskeleton organization Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Profilin-1A
Alternative name(s):
Acidic profilin IA
Profilin IA
OrganismiAcanthamoeba castellanii (Amoeba)
Taxonomic identifieri5755 [NCBI]
Taxonomic lineageiEukaryotaAmoebozoaDiscoseaLongamoebiaCentramoebidaAcanthamoebidaeAcanthamoeba

Subcellular locationi

GO - Cellular componenti

  • actin cytoskeleton Source: UniProtKB
  • cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 126125Profilin-1APRO_0000199583Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei104 – 1041N6,N6,N6-trimethyllysine1 Publication

Keywords - PTMi

Methylation

Interactioni

Subunit structurei

Occurs in many kinds of cells as a complex with monomeric actin in a 1:1 ratio.

GO - Molecular functioni

  • actin monomer binding Source: UniProtKB

Structurei

Secondary structure

1
126
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 86Combined sources
Turni9 – 113Combined sources
Helixi12 – 143Combined sources
Beta strandi18 – 247Combined sources
Beta strandi29 – 324Combined sources
Helixi40 – 4910Combined sources
Helixi54 – 574Combined sources
Beta strandi61 – 633Combined sources
Beta strandi66 – 738Combined sources
Beta strandi75 – 828Combined sources
Beta strandi85 – 917Combined sources
Beta strandi93 – 1019Combined sources
Helixi107 – 12317Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PRQX-ray2.50A2-126[»]
2PRFNMR-A2-126[»]
ProteinModelPortaliP68696.
SMRiP68696. Positions 2-126.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP68696.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 3635Actin-bindingSequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the profilin family.Curated

Family and domain databases

InterProiIPR005455. PFN.
IPR027310. Profilin_CS.
[Graphical view]
PANTHERiPTHR11604. PTHR11604. 1 hit.
PfamiPF00235. Profilin. 1 hit.
[Graphical view]
PRINTSiPR00392. PROFILIN.
PR01640. PROFILINPLNT.
SMARTiSM00392. PROF. 1 hit.
[Graphical view]
SUPFAMiSSF55770. SSF55770. 1 hit.
PROSITEiPS00414. PROFILIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P68696-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSWQTYVDTN LVGTGAVTQA AILGLDGNTW ATSAGFAVTP AQGQTLASAF
60 70 80 90 100
NNADPIRASG FDLAGVHYVT LRADDRSIYG KKGSAGVITV KTSKSILVGV
110 120
YNEKIQPGTA ANVVEKLADY LIGQGF
Length:126
Mass (Da):13,084
Last modified:January 23, 2007 - v2
Checksum:i69EA51991FE3D58B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21S → T AA sequence (PubMed:3881427).Curated
Sequence conflicti5 – 51T → S AA sequence (PubMed:3881427).Curated
Sequence conflicti32 – 332TS → SF AA sequence (PubMed:3881427).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L27485 mRNA. Translation: AAA27710.1.
PIRiB48405.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L27485 mRNA. Translation: AAA27710.1.
PIRiB48405.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PRQX-ray2.50A2-126[»]
2PRFNMR-A2-126[»]
ProteinModelPortaliP68696.
SMRiP68696. Positions 2-126.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP68696.

Family and domain databases

InterProiIPR005455. PFN.
IPR027310. Profilin_CS.
[Graphical view]
PANTHERiPTHR11604. PTHR11604. 1 hit.
PfamiPF00235. Profilin. 1 hit.
[Graphical view]
PRINTSiPR00392. PROFILIN.
PR01640. PROFILINPLNT.
SMARTiSM00392. PROF. 1 hit.
[Graphical view]
SUPFAMiSSF55770. SSF55770. 1 hit.
PROSITEiPS00414. PROFILIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPRO1A_ACACA
AccessioniPrimary (citable) accession number: P68696
Secondary accession number(s): P07763
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: December 9, 2015
This is version 59 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

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.