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Q9WVE8

- PACN2_MOUSE

UniProt

Q9WVE8 - PACN2_MOUSE

Protein

Protein kinase C and casein kinase substrate in neurons protein 2

Gene

Pacsin2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
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    Functioni

    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.7 Publications

    GO - Molecular functioni

    1. cytoskeletal protein binding Source: MGI
    2. lipid binding Source: UniProtKB
    3. phosphatidic acid binding Source: UniProtKB
    4. protein binding Source: MGI

    GO - Biological processi

    1. actin cytoskeleton organization Source: InterPro
    2. caveola assembly Source: UniProtKB
    3. caveolin-mediated endocytosis Source: UniProtKB
    4. cell projection morphogenesis Source: UniProtKB
    5. membrane tubulation Source: UniProtKB
    6. negative regulation of endocytosis Source: MGI
    7. protein localization to endosome Source: Ensembl
    8. signal transduction Source: MGI

    Keywords - Biological processi

    Endocytosis

    Keywords - Ligandi

    Lipid-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein kinase C and casein kinase substrate in neurons protein 2
    Alternative name(s):
    Syndapin-2
    Syndapin-II
    Gene namesi
    Name:Pacsin2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 15

    Organism-specific databases

    MGIiMGI:1345153. Pacsin2.

    Subcellular locationi

    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.

    GO - Cellular componenti

    1. caveola Source: UniProtKB
    2. cell-cell junction Source: MGI
    3. cytoplasm Source: MGI
    4. cytoplasmic vesicle membrane Source: UniProtKB-SubCell
    5. cytoskeleton Source: UniProtKB-SubCell
    6. cytosol Source: MGI
    7. early endosome Source: UniProtKB-SubCell
    8. extrinsic component of membrane Source: UniProtKB
    9. recycling endosome membrane Source: UniProtKB-SubCell
    10. ruffle membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Endosome, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi40 – 401D → K: Slight increase in affinity for membranes. Increases membrane tubulation activity. 1 Publication
    Mutagenesisi50 – 501R → D: Slight decrease in affinity for membranes. Nearly abolishes membrane tubulation activity. 1 Publication
    Mutagenesisi124 – 1252MM → TT: Nearly abolishes membrane tubulation activity.
    Mutagenesisi189 – 1891K → E: Decreases affinity for membranes. 1 Publication
    Mutagenesisi478 – 4781P → L: Loss of DNM1-, SYNJ1- and WASL-binding. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 486486Protein kinase C and casein kinase substrate in neurons protein 2PRO_0000161796Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei53 – 531N6-acetyllysine1 Publication

    Post-translational modificationi

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

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9WVE8.
    PaxDbiQ9WVE8.
    PRIDEiQ9WVE8.

    PTM databases

    PhosphoSiteiQ9WVE8.

    Expressioni

    Tissue specificityi

    Widely expressed (at protein level).2 Publications

    Gene expression databases

    ArrayExpressiQ9WVE8.
    BgeeiQ9WVE8.
    GenevestigatoriQ9WVE8.

    Interactioni

    Subunit structurei

    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 TRPV4.6 Publications

    Protein-protein interaction databases

    IntActiQ9WVE8. 3 interactions.
    MINTiMINT-1697712.

    Structurei

    Secondary structure

    1
    486
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni21 – 244
    Helixi25 – 7147
    Helixi77 – 10630
    Helixi108 – 11710
    Beta strandi124 – 1285
    Helixi131 – 17444
    Helixi184 – 1929
    Turni193 – 1986
    Helixi199 – 2024
    Helixi204 – 21613
    Helixi220 – 25536
    Helixi261 – 27515
    Helixi279 – 28911

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3LLLX-ray3.30A/B16-302[»]
    ProteinModelPortaliQ9WVE8.
    SMRiQ9WVE8. Positions 16-302, 429-484.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9WVE8.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini11 – 7565FCHPROSITE-ProRule annotationAdd
    BLAST
    Domaini426 – 48661SH3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 306306F-BAR domainAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili25 – 274250Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi362 – 3643NPF1
    Motifi405 – 4073NPF2
    Motifi417 – 4193NPF3

    Domaini

    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.2 Publications

    Sequence similaritiesi

    Belongs to the PACSIN family.Curated
    Contains 1 FCH domain.PROSITE-ProRule annotation
    Contains 1 SH3 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, SH3 domain

    Phylogenomic databases

    eggNOGiNOG283356.
    GeneTreeiENSGT00510000046376.
    HOGENOMiHOG000007245.
    HOVERGENiHBG053486.
    InParanoidiQ9WVE8.
    OMAiCKQDVLK.
    OrthoDBiEOG75TMBJ.
    PhylomeDBiQ9WVE8.
    TreeFamiTF313677.

    Family and domain databases

    InterProiIPR001060. FCH_dom.
    IPR028521. PACSIN2.
    IPR001452. SH3_domain.
    [Graphical view]
    PANTHERiPTHR10959:SF2. PTHR10959:SF2. 1 hit.
    PfamiPF00611. FCH. 1 hit.
    PF14604. SH3_9. 1 hit.
    [Graphical view]
    PRINTSiPR00452. SH3DOMAIN.
    SMARTiSM00055. FCH. 1 hit.
    SM00326. SH3. 1 hit.
    [Graphical view]
    SUPFAMiSSF50044. SSF50044. 1 hit.
    PROSITEiPS50133. FCH. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9WVE8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSVTYDDSVG VEVSSDSFWE VGNYKRTVKR IDDGHRLCGD LMNCLHERAR    50
    IEKAYAQQLT EWARRWRQLV EKGPQYGTVE KAWIAVMSEA ERVSELHLEV 100
    KASLMNEDFE KIKNWQKEAF HKQMMGGFKE TKEAEDGFRK AQKPWAKKLK 150
    EVEAAKKAHH TACKEEKLAI SREANSKADP SLNPEQLKKL QDKIEKCKQD 200
    VLKTKDKYEK SLKELDQTTP QYMENMEQVF EQCQQFEEKR LRFFREVLLE 250
    VQKHLDLSNV ASYKTIYREL EQSIKAADAV EDLRWFRANH GPGMAMNWPQ 300
    FEEWSADLNR TLSRREKKKA VDGVTLTGIN QTGDQSGQNK PGSNLSVPSN 350
    PAQSTQLQSS YNPFEDEDDT GSSISEKEDI KAKNVSSYEK TQTYPTDWSD 400
    DESNNPFSST DANGDSNPFD EDTTSGTEVR VRALYDYEGQ EHDELSFKAG 450
    DELTKIEDED EQGWCKGRLD SGQVGLYPAN YVEAIQ 486
    Length:486
    Mass (Da):55,833
    Last modified:November 1, 1999 - v1
    Checksum:i66C17ECCC767E0E7
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF128535 mRNA. Translation: AAD41780.1.
    BC023502 mRNA. Translation: AAH23502.1.
    CCDSiCCDS27701.1.
    RefSeqiNP_001152981.1. NM_001159509.1.
    NP_001152982.1. NM_001159510.1.
    NP_035992.1. NM_011862.3.
    UniGeneiMm.23978.

    Genome annotation databases

    EnsembliENSMUST00000056177; ENSMUSP00000058320; ENSMUSG00000016664.
    ENSMUST00000165095; ENSMUSP00000130098; ENSMUSG00000016664.
    ENSMUST00000171436; ENSMUSP00000131504; ENSMUSG00000016664.
    GeneIDi23970.
    KEGGimmu:23970.
    UCSCiuc007xba.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF128535 mRNA. Translation: AAD41780.1 .
    BC023502 mRNA. Translation: AAH23502.1 .
    CCDSi CCDS27701.1.
    RefSeqi NP_001152981.1. NM_001159509.1.
    NP_001152982.1. NM_001159510.1.
    NP_035992.1. NM_011862.3.
    UniGenei Mm.23978.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3LLL X-ray 3.30 A/B 16-302 [» ]
    ProteinModelPortali Q9WVE8.
    SMRi Q9WVE8. Positions 16-302, 429-484.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9WVE8. 3 interactions.
    MINTi MINT-1697712.

    Chemistry

    ChEMBLi CHEMBL2176817.

    PTM databases

    PhosphoSitei Q9WVE8.

    Proteomic databases

    MaxQBi Q9WVE8.
    PaxDbi Q9WVE8.
    PRIDEi Q9WVE8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000056177 ; ENSMUSP00000058320 ; ENSMUSG00000016664 .
    ENSMUST00000165095 ; ENSMUSP00000130098 ; ENSMUSG00000016664 .
    ENSMUST00000171436 ; ENSMUSP00000131504 ; ENSMUSG00000016664 .
    GeneIDi 23970.
    KEGGi mmu:23970.
    UCSCi uc007xba.2. mouse.

    Organism-specific databases

    CTDi 11252.
    MGIi MGI:1345153. Pacsin2.

    Phylogenomic databases

    eggNOGi NOG283356.
    GeneTreei ENSGT00510000046376.
    HOGENOMi HOG000007245.
    HOVERGENi HBG053486.
    InParanoidi Q9WVE8.
    OMAi CKQDVLK.
    OrthoDBi EOG75TMBJ.
    PhylomeDBi Q9WVE8.
    TreeFami TF313677.

    Miscellaneous databases

    ChiTaRSi PACSIN2. mouse.
    EvolutionaryTracei Q9WVE8.
    NextBioi 303853.
    PROi Q9WVE8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9WVE8.
    Bgeei Q9WVE8.
    Genevestigatori Q9WVE8.

    Family and domain databases

    InterProi IPR001060. FCH_dom.
    IPR028521. PACSIN2.
    IPR001452. SH3_domain.
    [Graphical view ]
    PANTHERi PTHR10959:SF2. PTHR10959:SF2. 1 hit.
    Pfami PF00611. FCH. 1 hit.
    PF14604. SH3_9. 1 hit.
    [Graphical view ]
    PRINTSi PR00452. SH3DOMAIN.
    SMARTi SM00055. FCH. 1 hit.
    SM00326. SH3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 1 hit.
    PROSITEi PS50133. FCH. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiPACN2_MOUSE
    AccessioniPrimary (citable) accession number: Q9WVE8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 2002
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 108 of the entry and version 1 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. 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

    External Data

    Dasty 3