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Protein

Profilin-2

Gene

Pfn2

Organism
Mus musculus (Mouse)
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.

GO - Molecular functioni

GO - Biological processi

  • actin cytoskeleton organization Source: InterPro
  • negative regulation of actin filament polymerization Source: MGI
  • negative regulation of epithelial cell migration Source: UniProtKB
  • negative regulation of ruffle assembly Source: UniProtKB
  • positive regulation of actin filament bundle assembly Source: MGI
  • positive regulation of actin filament polymerization Source: MGI
  • positive regulation of ATPase activity Source: MGI
  • positive regulation of peptidyl-serine phosphorylation Source: UniProtKB
  • positive regulation of stress fiber assembly Source: UniProtKB
  • protein stabilization Source: MGI
  • regulation of synaptic vesicle exocytosis Source: MGI
Complete GO annotation...

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Profilin-2
Alternative name(s):
Profilin II
Gene namesi
Name:Pfn2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:97550. Pfn2.

Subcellular locationi

GO - Cellular componenti

  • cytoskeleton Source: UniProtKB-SubCell
  • cytosol Source: Reactome
  • extracellular exosome Source: MGI
  • terminal bouton Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 140139Profilin-2PRO_0000199576Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9JJV2.
MaxQBiQ9JJV2.
PaxDbiQ9JJV2.
PRIDEiQ9JJV2.

2D gel databases

REPRODUCTION-2DPAGEQ9JJV2.
UCD-2DPAGEQ9JJV2.

PTM databases

iPTMnetiQ9JJV2.
PhosphoSiteiQ9JJV2.

Expressioni

Tissue specificityi

Isoform IIa is the main isoform and is abundant in brain. Isoform IIb is a minor isoform.

Gene expression databases

BgeeiQ9JJV2.
CleanExiMM_PFN2.
ExpressionAtlasiQ9JJV2. baseline and differential.
GenevisibleiQ9JJV2. MM.

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 (PubMed:19403918).By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Dnm1P390532EBI-990256,EBI-397785

GO - Molecular functioni

Protein-protein interaction databases

BioGridi202127. 11 interactions.
IntActiQ9JJV2. 5 interactions.
MINTiMINT-1531870.
STRINGi10090.ENSMUSP00000068890.

Structurei

Secondary structure

1
140
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 128Combined sources
Beta strandi17 – 248Combined 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 strandi94 – 963Combined 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
2V8CX-ray1.98A1-140[»]
2V8FX-ray1.10A/B1-140[»]
ProteinModelPortaliQ9JJV2.
SMRiQ9JJV2. Positions 2-140.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9JJV2.

Family & Domainsi

Sequence similaritiesi

Belongs to the profilin family.Curated

Phylogenomic databases

eggNOGiKOG1755. Eukaryota.
ENOG41126PD. LUCA.
GeneTreeiENSGT00390000010143.
HOGENOMiHOG000171592.
HOVERGENiHBG053683.
InParanoidiQ9JJV2.
KOiK05759.
OMAiFFHMCSV.
OrthoDBiEOG7JMGGT.
PhylomeDBiQ9JJV2.
TreeFamiTF331744.

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 (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9JJV2-1) [UniParc]FASTAAdd to basket

Also known as: IIa

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 QSITPVEIDM
60 70 80 90 100
IVGKDREGFF TNGLTLGAKK CSVIRDSLYV DGDCTMDIRT KSQGGEPTYN
110 120 130 140
VAVGRAGRVL VFVMGKEGVH GGGLNKKAYS MAKYLRDSGF
Length:140
Mass (Da):15,032
Last modified:January 23, 2007 - v3
Checksum:iE780BF62E9EC8476
GO
Isoform 2 (identifier: Q9JJV2-2) [UniParc]FASTAAdd to basket

Also known as: IIb

The sequence of this isoform differs from the canonical sequence as follows:
     109-140: VLVFVMGKEGVHGGGLNKKAYSMAKYLRDSGF → ALVIVMGKEGVHAGTINKKTYELALYLKRSVTNLYLAS

Show »
Length:146
Mass (Da):15,738
Checksum:i415EBAD1E92842BC
GO
Isoform 3 (identifier: Q9JJV2-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-49: Missing.

Note: No experimental confirmation available.
Show »
Length:91
Mass (Da):9,798
Checksum:i3E34B08C5626DB2E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti36 – 361A → G in AAG09753 (PubMed:11027290).Curated
Sequence conflicti36 – 361A → G in AAG09756 (PubMed:11027290).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4949Missing in isoform 3. 1 PublicationVSP_024736Add
BLAST
Alternative sequencei109 – 14032VLVFV…RDSGF → ALVIVMGKEGVHAGTINKKT YELALYLKRSVTNLYLAS in isoform 2. 1 PublicationVSP_005218Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ272203 mRNA. Translation: CAB87382.1.
AF237680 Genomic DNA. Translation: AAG09753.1.
AF237680 Genomic DNA. Translation: AAG09755.1.
AF237680 Genomic DNA. Translation: AAG09756.1.
AK132651 mRNA. Translation: BAE21281.1.
AK164145 mRNA. Translation: BAE37648.1.
BC024363 mRNA. Translation: AAH24363.1.
CCDSiCCDS17364.1. [Q9JJV2-1]
RefSeqiNP_062283.1. NM_019410.3. [Q9JJV2-1]
UniGeneiMm.271744.

Genome annotation databases

EnsembliENSMUST00000066882; ENSMUSP00000068890; ENSMUSG00000027805. [Q9JJV2-1]
ENSMUST00000119344; ENSMUSP00000112391; ENSMUSG00000027805. [Q9JJV2-3]
ENSMUST00000122210; ENSMUSP00000113526; ENSMUSG00000027805. [Q9JJV2-3]
GeneIDi18645.
KEGGimmu:18645.
UCSCiuc008phm.1. mouse. [Q9JJV2-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ272203 mRNA. Translation: CAB87382.1.
AF237680 Genomic DNA. Translation: AAG09753.1.
AF237680 Genomic DNA. Translation: AAG09755.1.
AF237680 Genomic DNA. Translation: AAG09756.1.
AK132651 mRNA. Translation: BAE21281.1.
AK164145 mRNA. Translation: BAE37648.1.
BC024363 mRNA. Translation: AAH24363.1.
CCDSiCCDS17364.1. [Q9JJV2-1]
RefSeqiNP_062283.1. NM_019410.3. [Q9JJV2-1]
UniGeneiMm.271744.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2V8CX-ray1.98A1-140[»]
2V8FX-ray1.10A/B1-140[»]
ProteinModelPortaliQ9JJV2.
SMRiQ9JJV2. Positions 2-140.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202127. 11 interactions.
IntActiQ9JJV2. 5 interactions.
MINTiMINT-1531870.
STRINGi10090.ENSMUSP00000068890.

PTM databases

iPTMnetiQ9JJV2.
PhosphoSiteiQ9JJV2.

2D gel databases

REPRODUCTION-2DPAGEQ9JJV2.
UCD-2DPAGEQ9JJV2.

Proteomic databases

EPDiQ9JJV2.
MaxQBiQ9JJV2.
PaxDbiQ9JJV2.
PRIDEiQ9JJV2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000066882; ENSMUSP00000068890; ENSMUSG00000027805. [Q9JJV2-1]
ENSMUST00000119344; ENSMUSP00000112391; ENSMUSG00000027805. [Q9JJV2-3]
ENSMUST00000122210; ENSMUSP00000113526; ENSMUSG00000027805. [Q9JJV2-3]
GeneIDi18645.
KEGGimmu:18645.
UCSCiuc008phm.1. mouse. [Q9JJV2-1]

Organism-specific databases

CTDi5217.
MGIiMGI:97550. Pfn2.

Phylogenomic databases

eggNOGiKOG1755. Eukaryota.
ENOG41126PD. LUCA.
GeneTreeiENSGT00390000010143.
HOGENOMiHOG000171592.
HOVERGENiHBG053683.
InParanoidiQ9JJV2.
KOiK05759.
OMAiFFHMCSV.
OrthoDBiEOG7JMGGT.
PhylomeDBiQ9JJV2.
TreeFamiTF331744.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiPfn2. mouse.
EvolutionaryTraceiQ9JJV2.
NextBioi294640.
PROiQ9JJV2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JJV2.
CleanExiMM_PFN2.
ExpressionAtlasiQ9JJV2. baseline and differential.
GenevisibleiQ9JJV2. MM.

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

« Hide 'large scale' publications
  1. "Alternative splicing of the mouse profilin II gene generates functionally different profilin isoforms."
    Di Nardo A., Gareus R., Kwiatkowski D., Witke W.
    J. Cell Sci. 113:3795-3803(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
  2. "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 [GENOMIC DNA].
  3. "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] (ISOFORMS 1 AND 3).
    Strain: C57BL/6J.
    Tissue: Hippocampus and Testis.
  4. "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] (ISOFORM 1).
  5. Lubec G., Klug S.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 55-69; 76-89 AND 92-105, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Hippocampus.
  6. "The interaction of proline-rich ligands with profilin probed with an enzyme-linked immunosorbent assay."
    Veniere S., Ampe C., Vandekerckhove J., Lambrechts A.
    J. Biomol. Screen. 14:350-359(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PFN2.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Kidney, Liver and Testis.

Entry informationi

Entry nameiPROF2_MOUSE
AccessioniPrimary (citable) accession number: Q9JJV2
Secondary accession number(s): Q3TPT7
, Q3V171, Q9ES48, Q9ES49, Q9ES50
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 131 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.