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Protein

Profilin-2

Gene

Pfn2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 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 (By similarity).By similarity

GO - Molecular functioni

  • actin binding Source: RGD

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiR-RNO-376176. Signaling by Robo receptor.
R-RNO-5663220. RHO GTPases Activate Formins.

Names & Taxonomyi

Protein namesi
Recommended name:
Profilin-2
Alternative name(s):
Profilin II
Gene namesi
Name:Pfn2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 2

Organism-specific databases

RGDi621826. Pfn2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 140139Profilin-2PRO_0000199578Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ9EPC6.
PRIDEiQ9EPC6.

PTM databases

iPTMnetiQ9EPC6.
PhosphoSiteiQ9EPC6.

Expressioni

Gene expression databases

ExpressionAtlasiQ9EPC6. baseline and differential.
GenevisibleiQ9EPC6. RN.

Interactioni

Subunit structurei

Occurs in many kinds of cells as a complex with monomeric actin in a 1:1 ratio (By similarity). Interacts with PFN2 (By similarity).By similarity

GO - Molecular functioni

  • actin binding Source: RGD

Protein-protein interaction databases

BioGridi249528. 1 interaction.
IntActiQ9EPC6. 2 interactions.
MINTiMINT-142801.
STRINGi10116.ENSRNOP00000062782.

Structurei

Secondary structure

1
140
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 98Combined sources
Helixi11 – 144Combined sources
Beta strandi15 – 2410Combined sources
Beta strandi26 – 283Combined sources
Beta strandi30 – 345Combined sources
Helixi40 – 423Combined sources
Helixi45 – 528Combined sources
Helixi58 – 625Combined sources
Beta strandi64 – 663Combined sources
Beta strandi69 – 768Combined sources
Turni81 – 833Combined sources
Beta strandi85 – 906Combined sources
Beta strandi93 – 964Combined sources
Beta strandi100 – 1056Combined sources
Beta strandi107 – 1159Combined sources
Helixi121 – 13717Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VK3X-ray1.70A1-140[»]
ProteinModelPortaliQ9EPC6.
SMRiQ9EPC6. Positions 2-140.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9EPC6.

Family & Domainsi

Sequence similaritiesi

Belongs to the profilin family.Curated

Phylogenomic databases

eggNOGiKOG1755. Eukaryota.
ENOG41126PD. LUCA.
GeneTreeiENSGT00390000010143.
HOGENOMiHOG000171592.
HOVERGENiHBG053683.
InParanoidiQ9EPC6.
KOiK05759.
OrthoDBiEOG7JMGGT.

Family and domain databases

InterProiIPR005455. PFN.
IPR029891. PFN2.
IPR005454. Profilin1/2/3_vertebrate.
IPR027310. Profilin_CS.
[Graphical view]
PANTHERiPTHR13936:SF15. PTHR13936:SF15. 1 hit.
PfamiPF00235. Profilin. 1 hit.
[Graphical view]
PRINTSiPR00392. PROFILIN.
PR01639. PROFILINMAML.
SMARTiSM00392. PROF. 1 hit.
[Graphical view]
SUPFAMiSSF55770. SSF55770. 1 hit.
PROSITEiPS00414. PROFILIN. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform IIa (identifier: Q9EPC6-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAGWQSYVDN LMCDGCCQEA AIVGYCDAKY VWAATAGGVF QSITPAEIDV
60 70 80 90 100
IIGKDREGFF TNGLTLGGKK CSVIRDSLYV DSDCTMDIRT KSQGGEPTYN
110 120 130 140
VAVGRAGRVL VFVMGKEGVH GGGLNKKAYS MAKYLRDSGF
Length:140
Mass (Da):15,002
Last modified:January 23, 2007 - v3
Checksum:i0146DF257BD9C20B
GO
Isoform IIb (identifier: Q9EPC6-2)

Sequence is not available
Length:
Mass (Da):

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti139 – 1402GF → WVLAARQTVKY (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF228736 mRNA. Translation: AAG24947.1.
AF228737 mRNA. Translation: AAG24948.1.
AY004289 mRNA. Translation: AAF86616.1.
RefSeqiNP_110500.1. NM_030873.1.
XP_003749330.1. XM_003749282.2. [Q9EPC6-1]
XP_006232452.1. XM_006232390.2. [Q9EPC6-1]
UniGeneiRn.203100.

Genome annotation databases

EnsembliENSRNOT00000023469; ENSRNOP00000023469; ENSRNOG00000017427. [Q9EPC6-1]
GeneIDi100909840.
81531.
KEGGirno:100909840.
rno:81531.
UCSCiRGD:621826. rat. [Q9EPC6-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF228736 mRNA. Translation: AAG24947.1.
AF228737 mRNA. Translation: AAG24948.1.
AY004289 mRNA. Translation: AAF86616.1.
RefSeqiNP_110500.1. NM_030873.1.
XP_003749330.1. XM_003749282.2. [Q9EPC6-1]
XP_006232452.1. XM_006232390.2. [Q9EPC6-1]
UniGeneiRn.203100.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VK3X-ray1.70A1-140[»]
ProteinModelPortaliQ9EPC6.
SMRiQ9EPC6. Positions 2-140.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249528. 1 interaction.
IntActiQ9EPC6. 2 interactions.
MINTiMINT-142801.
STRINGi10116.ENSRNOP00000062782.

PTM databases

iPTMnetiQ9EPC6.
PhosphoSiteiQ9EPC6.

Proteomic databases

PaxDbiQ9EPC6.
PRIDEiQ9EPC6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000023469; ENSRNOP00000023469; ENSRNOG00000017427. [Q9EPC6-1]
GeneIDi100909840.
81531.
KEGGirno:100909840.
rno:81531.
UCSCiRGD:621826. rat. [Q9EPC6-1]

Organism-specific databases

CTDi5217.
RGDi621826. Pfn2.

Phylogenomic databases

eggNOGiKOG1755. Eukaryota.
ENOG41126PD. LUCA.
GeneTreeiENSGT00390000010143.
HOGENOMiHOG000171592.
HOVERGENiHBG053683.
InParanoidiQ9EPC6.
KOiK05759.
OrthoDBiEOG7JMGGT.

Enzyme and pathway databases

ReactomeiR-RNO-376176. Signaling by Robo receptor.
R-RNO-5663220. RHO GTPases Activate Formins.

Miscellaneous databases

EvolutionaryTraceiQ9EPC6.
PROiQ9EPC6.

Gene expression databases

ExpressionAtlasiQ9EPC6. baseline and differential.
GenevisibleiQ9EPC6. RN.

Family and domain databases

InterProiIPR005455. PFN.
IPR029891. PFN2.
IPR005454. Profilin1/2/3_vertebrate.
IPR027310. Profilin_CS.
[Graphical view]
PANTHERiPTHR13936:SF15. PTHR13936:SF15. 1 hit.
PfamiPF00235. Profilin. 1 hit.
[Graphical view]
PRINTSiPR00392. PROFILIN.
PR01639. PROFILINMAML.
SMARTiSM00392. PROF. 1 hit.
[Graphical view]
SUPFAMiSSF55770. SSF55770. 1 hit.
PROSITEiPS00414. PROFILIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Profilin II is alternatively spliced, resulting in profilin isoforms that are differentially expressed and have distinct biochemical properties."
    Lambrechts A., Braun A., Jonckheere V., Aszodi A., Lanier L.M., Robbens J., Van Colen I., Vandekerckhove J., Faessler R., Ampe C.
    Mol. Cell. Biol. 20:8209-8219(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "Novel genes expression in rat brain."
    Xiao H., Huang Q., Zhang F., Yang Z., Chen Z., Han Z., Zhang X.
    Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  3. Lubec G., Afjehi-Sadat L., Chen W.-Q.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 55-69; 92-105 AND 109-116, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Hippocampus and Spinal cord.

Entry informationi

Entry nameiPROF2_RAT
AccessioniPrimary (citable) accession number: Q9EPC6
Secondary accession number(s): Q9JHU7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2002
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 108 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, Direct protein sequencing, 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.