Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9WVE8 (PACN2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein kinase C and casein kinase substrate in neurons protein 2
Alternative name(s):
Syndapin-2
Syndapin-II
Gene names
Name:Pacsin2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length486 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Lipid-binding protein that is able to promote the tubulation of the phosphatidic acid-containing membranes it preferentially binds. Plays a role in intracellular vesicle-mediated transport. Involved in the endocytosis of cell-surface receptors like the EGF receptor, contributing to its internalization in the absence of EGF stimulus. May also play a role in the formation of caveolae at the cell membrane. Recruits DNM2 to caveolae, and thereby plays a role in caveola-mediated endocytosis. Ref.3 Ref.4 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10

Subunit structure

Homodimer. May form heterooligomers with other PACSINs. Interacts (via NPF motifs) with EHD1 (via EH domain). Interacts with EHD3. Interacts (via the SH3 domain) with MICALL1. Interacts with RAC1. Interacts (via SH3 domain) with DNM1, SYN1, SYNJ1 and WASL. Interacts with CAV1. Interacts with TRPV4. Ref.3 Ref.4 Ref.5 Ref.7 Ref.8 Ref.12

Subcellular location

Cytoplasm. Cytoplasmcytoskeleton. Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Cell projectionruffle membrane; Peripheral membrane protein; Cytoplasmic side. Early endosome. Recycling endosome membrane By similarity. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection. Membranecaveola. Note: Detected at the neck of flask-shaped caveolae. Localization to tubular recycling endosomes probably requires interaction with MICALL1 and EHD1. Ref.1 Ref.3 Ref.4 Ref.6 Ref.7 Ref.8 Ref.10

Tissue specificity

Widely expressed (at protein level). Ref.1 Ref.3

Domain

The F-BAR domain forms a coiled coil and mediates membrane-binding and membrane tubulation. In the autoinhibited conformation, interaction with the SH3 domain inhibits membrane tubulation mediated by the F-BAR domain. Ref.6 Ref.12

Post-translational modification

Phosphorylated by casein kinase 2 (CK2) and protein kinase C (PKC) By similarity.

Sequence similarities

Belongs to the PACSIN family.

Contains 1 FCH domain.

Contains 1 SH3 domain.

Ontologies

Keywords
   Biological processEndocytosis
   Cellular componentCell membrane
Cell projection
Cytoplasm
Cytoplasmic vesicle
Cytoskeleton
Endosome
Membrane
   DomainCoiled coil
SH3 domain
   LigandLipid-binding
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin cytoskeleton organization

Inferred from electronic annotation. Source: InterPro

caveola assembly

Inferred from sequence or structural similarity. Source: UniProtKB

caveolin-mediated endocytosis

Inferred from sequence or structural similarity. Source: UniProtKB

cell projection morphogenesis

Inferred from mutant phenotype Ref.6. Source: UniProtKB

membrane tubulation

Inferred from mutant phenotype Ref.6. Source: UniProtKB

negative regulation of endocytosis

Inferred from direct assay Ref.3. Source: MGI

signal transduction

Traceable author statement Ref.1. Source: MGI

   Cellular_componentcaveola

Inferred from direct assay Ref.7. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.3. Source: MGI

cytoplasmic vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Inferred from direct assay Ref.1. Source: MGI

early endosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

extrinsic component of membrane

Inferred from direct assay Ref.6. Source: UniProtKB

recycling endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

ruffle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncytoskeletal protein binding

Inferred from direct assay Ref.3. Source: MGI

lipid binding

Inferred from direct assay Ref.6. Source: UniProtKB

phosphatidic acid binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 486486Protein kinase C and casein kinase substrate in neurons protein 2
PRO_0000161796

Regions

Domain11 – 7565FCH
Domain426 – 48661SH3
Region1 – 306306F-BAR domain
Coiled coil25 – 274250
Motif362 – 3643NPF1
Motif405 – 4073NPF2
Motif417 – 4193NPF3

Amino acid modifications

Modified residue531N6-acetyllysine Ref.11

Experimental info

Mutagenesis401D → K: Slight increase in affinity for membranes. Increases membrane tubulation activity. Ref.6
Mutagenesis501R → D: Slight decrease in affinity for membranes. Nearly abolishes membrane tubulation activity. Ref.6
Mutagenesis124 – 1252MM → TT: Nearly abolishes membrane tubulation activity.
Mutagenesis1891K → E: Decreases affinity for membranes. Ref.6
Mutagenesis4781P → L: Loss of DNM1-, SYNJ1- and WASL-binding. Ref.3

Secondary structure

........................ 486
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9WVE8 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 66C17ECCC767E0E7

FASTA48655,833
        10         20         30         40         50         60 
MSVTYDDSVG VEVSSDSFWE VGNYKRTVKR IDDGHRLCGD LMNCLHERAR IEKAYAQQLT 

        70         80         90        100        110        120 
EWARRWRQLV EKGPQYGTVE KAWIAVMSEA ERVSELHLEV KASLMNEDFE KIKNWQKEAF 

       130        140        150        160        170        180 
HKQMMGGFKE TKEAEDGFRK AQKPWAKKLK EVEAAKKAHH TACKEEKLAI SREANSKADP 

       190        200        210        220        230        240 
SLNPEQLKKL QDKIEKCKQD VLKTKDKYEK SLKELDQTTP QYMENMEQVF EQCQQFEEKR 

       250        260        270        280        290        300 
LRFFREVLLE VQKHLDLSNV ASYKTIYREL EQSIKAADAV EDLRWFRANH GPGMAMNWPQ 

       310        320        330        340        350        360 
FEEWSADLNR TLSRREKKKA VDGVTLTGIN QTGDQSGQNK PGSNLSVPSN PAQSTQLQSS 

       370        380        390        400        410        420 
YNPFEDEDDT GSSISEKEDI KAKNVSSYEK TQTYPTDWSD DESNNPFSST DANGDSNPFD 

       430        440        450        460        470        480 
EDTTSGTEVR VRALYDYEGQ EHDELSFKAG DELTKIEDED EQGWCKGRLD SGQVGLYPAN 


YVEAIQ 

« Hide

References

« Hide 'large scale' references
[1]"PACSIN 2, a novel member of the PACSIN family of cytoplasmic adapter proteins."
Ritter B., Modregger J., Paulsson M., Plomann M.
FEBS Lett. 454:356-362(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Strain: C57BL/6 X DBA.
[2]"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].
Tissue: Mammary gland.
[3]"All three PACSIN isoforms bind to endocytic proteins and inhibit endocytosis."
Modregger J., Ritter B., Witter B., Paulsson M., Plomann M.
J. Cell Sci. 113:4511-4521(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH DNM1; SYNJ1 AND WASL, HOMOOLIGOMERIZATION, HETEROOLIGOMERIZATION WITH PACSIN1 AND PACSIN3, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF PRO-478.
[4]"EHD proteins associate with syndapin I and II and such interactions play a crucial role in endosomal recycling."
Braun A., Pinyol R., Dahlhaus R., Koch D., Fonarev P., Grant B.D., Kessels M.M., Qualmann B.
Mol. Biol. Cell 16:3642-3658(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH EHD1 AND EHD3, SUBCELLULAR LOCATION.
[5]"PACSINs bind to the TRPV4 cation channel. PACSIN 3 modulates the subcellular localization of TRPV4."
Cuajungco M.P., Grimm C., Oshima K., D'hoedt D., Nilius B., Mensenkamp A.R., Bindels R.J., Plomann M., Heller S.
J. Biol. Chem. 281:18753-18762(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TRPV4.
[6]"Mapping of the basic amino-acid residues responsible for tubulation and cellular protrusion by the EFC/F-BAR domain of pacsin2/Syndapin II."
Shimada A., Takano K., Shirouzu M., Hanawa-Suetsugu K., Terada T., Toyooka K., Umehara T., Yamamoto M., Yokoyama S., Suetsugu S.
FEBS Lett. 584:1111-1118(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DOMAIN, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-40; ARG-50; 124-MET-MET-125 AND LYS-189.
[7]"Essential role of PACSIN2/syndapin-II in caveolae membrane sculpting."
Senju Y., Itoh Y., Takano K., Hamada S., Suetsugu S.
J. Cell Sci. 124:2032-2040(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CAV1, SUBCELLULAR LOCATION.
[8]"The F-BAR domain protein PACSIN2 associates with Rac1 and regulates cell spreading and migration."
de Kreuk B.J., Nethe M., Fernandez-Borja M., Anthony E.C., Hensbergen P.J., Deelder A.M., Plomann M., Hordijk P.L.
J. Cell Sci. 124:2375-2388(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RAC1.
[9]"Pacsin 2 is recruited to caveolae and functions in caveolar biogenesis."
Hansen C.G., Howard G., Nichols B.J.
J. Cell Sci. 124:2777-2785(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"The F-BAR protein PACSIN2 regulates epidermal growth factor receptor internalization."
de Kreuk B.J., Anthony E.C., Geerts D., Hordijk P.L.
J. Biol. Chem. 287:43438-43453(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[11]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-53, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[12]"A hinge in the distal end of the PACSIN 2 F-BAR domain may contribute to membrane-curvature sensing."
Plomann M., Wittmann J.G., Rudolph M.G.
J. Mol. Biol. 400:129-136(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 16-302, SUBUNIT, DOMAIN.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF128535 mRNA. Translation: AAD41780.1.
BC023502 mRNA. Translation: AAH23502.1.
RefSeqNP_001152981.1. NM_001159509.1.
NP_001152982.1. NM_001159510.1.
NP_035992.1. NM_011862.3.
UniGeneMm.23978.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3LLLX-ray3.30A/B16-302[»]
ProteinModelPortalQ9WVE8.
SMRQ9WVE8. Positions 16-302, 429-484.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9WVE8. 3 interactions.
MINTMINT-1697712.

Chemistry

ChEMBLCHEMBL2176817.

PTM databases

PhosphoSiteQ9WVE8.

Proteomic databases

PaxDbQ9WVE8.
PRIDEQ9WVE8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000056177; ENSMUSP00000058320; ENSMUSG00000016664.
ENSMUST00000165095; ENSMUSP00000130098; ENSMUSG00000016664.
ENSMUST00000171436; ENSMUSP00000131504; ENSMUSG00000016664.
GeneID23970.
KEGGmmu:23970.
UCSCuc007xba.2. mouse.

Organism-specific databases

CTD11252.
MGIMGI:1345153. Pacsin2.

Phylogenomic databases

eggNOGNOG283356.
GeneTreeENSGT00510000046376.
HOGENOMHOG000007245.
HOVERGENHBG053486.
InParanoidQ9WVE8.
OMACKQDVLK.
OrthoDBEOG75TMBJ.
PhylomeDBQ9WVE8.
TreeFamTF313677.

Gene expression databases

ArrayExpressQ9WVE8.
BgeeQ9WVE8.
GenevestigatorQ9WVE8.

Family and domain databases

InterProIPR001060. FCH_dom.
IPR028521. PACSIN2.
IPR001452. SH3_domain.
[Graphical view]
PANTHERPTHR10959:SF2. PTHR10959:SF2. 1 hit.
PfamPF00611. FCH. 1 hit.
[Graphical view]
PRINTSPR00452. SH3DOMAIN.
SMARTSM00055. FCH. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
PROSITEPS50133. FCH. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPACSIN2. mouse.
EvolutionaryTraceQ9WVE8.
NextBio303853.
PROQ9WVE8.
SOURCESearch...

Entry information

Entry namePACN2_MOUSE
AccessionPrimary (citable) accession number: Q9WVE8
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 2002
Last sequence update: November 1, 1999
Last modified: April 16, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot