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Q61644

- PACN1_MOUSE

UniProt

Q61644 - PACN1_MOUSE

Protein

Protein kinase C and casein kinase substrate in neurons protein 1

Gene

Pacsin1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Binds to membranes via its F-BAR domain and mediates membrane tubulation. Plays a role in the reorganization of the microtubule cytoskeleton via its interaction with MAPT; this decreases microtubule stability and inhibits MAPT-induced microtubule polymerization. Plays a role in cellular transport processes by recruiting DNM1, DNM2 and DNM3 to membranes. Plays a role in the reorganization of the actin cytoskeleton and in neuron morphogenesis via its interaction with COBL and WASL, and by recruiting COBL to the cell cortex. Plays a role in the regulation of neurite formation, neurite branching and the regulation of neurite length. Required for normal synaptic vesicle endocytosis; this process retrieves previously released neurotransmitters to accommodate multiple cycles of neurotransmission. Required for normal excitatory and inhibitory synaptic transmission.4 Publications

    GO - Molecular functioni

    1. cytoskeletal protein binding Source: MGI
    2. phospholipid binding Source: UniProtKB
    3. protein binding Source: IntAct

    GO - Biological processi

    1. actin filament organization Source: InterPro
    2. membrane tubulation Source: UniProtKB
    3. negative regulation of endocytosis Source: MGI
    4. neuron projection morphogenesis Source: UniProtKB
    5. protein localization to membrane Source: UniProtKB
    6. signal transduction Source: MGI
    7. synaptic vesicle endocytosis Source: UniProtKB

    Keywords - Biological processi

    Endocytosis

    Keywords - Ligandi

    Lipid-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein kinase C and casein kinase substrate in neurons protein 1
    Alternative name(s):
    Syndapin-1
    Gene namesi
    Name:Pacsin1
    Synonyms:Pacsin
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 17

    Organism-specific databases

    MGIiMGI:1345181. Pacsin1.

    Subcellular locationi

    Cytoplasm. Cell projection By similarity. Cell junctionsynapsesynaptosome By similarity. Cell projectionruffle membrane. Membrane; Peripheral membrane protein. Cytoplasmic vesicle membrane; Peripheral membrane protein. Cell junctionsynapse. Cytoplasmcytosol. Cell membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
    Note: In primary neuronal cultures, present at a high level in presynaptic nerve terminals and in the cell body. Colocalizes with DNM1 at vesicular structures in the cell body and neurites By similarity. Colocalizes with MAPT in axons.By similarity

    GO - Cellular componenti

    1. axon terminus Source: UniProtKB
    2. cell junction Source: UniProtKB-KW
    3. COPI-coated vesicle Source: MGI
    4. cytoplasm Source: UniProtKB
    5. cytoplasmic vesicle membrane Source: UniProtKB-SubCell
    6. cytosol Source: UniProtKB-SubCell
    7. ruffle membrane Source: UniProtKB
    8. synapse Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoplasmic vesicle, Membrane, Synapse, Synaptosome

    Pathology & Biotechi

    Disruption phenotypei

    Mice are born at the expected Mendelian rate, but display a slightly reduced body weight and reduced fertility. Mice display increased synaptic vesicle diameter and impaired compensatory synaptic vesicle endocytosis after high synapse activity. Rod photoreceptor ribbon synapses display an abnormally high number of endosome-like structures and tubular elements after light exposure. Mice display defects in excitatory and inhibitory synaptic transmission in the hippocampus, and display a tendency to seizures when confronted with novelty.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi122 – 1232IM → FF: Increases membrane tubulation.
    Mutagenesisi122 – 1232IM → QQ: Abolishes membrane tubulation. No effect on phospholipid binding.
    Mutagenesisi127 – 1271K → E: Abolishes membrane tubulation; when associated with E-130. 1 Publication
    Mutagenesisi130 – 1301K → E: Abolishes membrane tubulation; when associated with E-127. 1 Publication
    Mutagenesisi145 – 1484KKMK → EEME: Abolishes membrane tubulation.
    Mutagenesisi400 – 4001E → R: Impairs interaction with DNM1.
    Mutagenesisi434 – 4341P → L: Abolishes interaction with DNM1, MAPT, SYNJ1 and WASL. 3 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 441441Protein kinase C and casein kinase substrate in neurons protein 1PRO_0000161793Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei76 – 761PhosphoserineBy similarity
    Modified residuei181 – 1811PhosphothreonineBy similarity
    Modified residuei391 – 3911Phosphotyrosine1 Publication

    Post-translational modificationi

    Phosphorylated by casein kinase 2 (CK2) and protein kinase C (PKC).1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ61644.
    PaxDbiQ61644.
    PRIDEiQ61644.

    2D gel databases

    UCD-2DPAGEQ61644.

    PTM databases

    PhosphoSiteiQ61644.

    Expressioni

    Tissue specificityi

    Highly expressed in brain. Detected in hippocampus and dorsal root ganglion neurons. Detected in rod photoreceptor terminals in the outer plexiform layer of the retina (at protein level). In CNS neurons, high levels in the pyramidal cells of the hippocampus, Purkinje cells of the cerebellum and large neurons of the cortex and brain stem.4 Publications

    Developmental stagei

    Expression is seen at embryonic day 17 and is up-regulated developmentally with a correlation to neuronal differentiation.

    Gene expression databases

    ArrayExpressiQ61644.
    BgeeiQ61644.
    GenevestigatoriQ61644.

    Interactioni

    Subunit structurei

    Homodimer. May form heterooligomers with other PACSINs. Interacts with both COBL and DBNL. Identified in a complex composed of COBL, PACSIN1 and WASL. Interacts with EHD3 By similarity. Interacts (via SH3 domain) with SYNJ1 and WASL. Interacts (via SH3 domain) with DNM1; the interaction is reduced by DNM1 phosphorylation. Interacts with DNM2 and DNM3. Interacts with MAPT. Interacts with EHD1. Interacts with TRPV4.By similarity6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MaptP106375EBI-2255561,EBI-774043
    MaptP19332-56EBI-2255561,EBI-8758676From a different organism.

    Protein-protein interaction databases

    DIPiDIP-53108N.
    IntActiQ61644. 8 interactions.
    MINTiMINT-4106465.
    STRINGi10090.ENSMUSP00000110522.

    Structurei

    Secondary structure

    1
    441
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni19 – 224
    Helixi23 – 7048
    Helixi75 – 10430
    Helixi106 – 11712
    Beta strandi124 – 1263
    Helixi127 – 17549
    Beta strandi176 – 1783
    Helixi182 – 25372
    Helixi255 – 2573
    Helixi260 – 27415
    Helixi277 – 28812
    Beta strandi386 – 3894
    Beta strandi396 – 4005
    Beta strandi408 – 4114
    Beta strandi417 – 4248
    Beta strandi430 – 4345
    Helixi435 – 4373

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2X3VX-ray2.45A/B/C1-337[»]
    2X3WX-ray2.64A/B/C1-337[»]
    D382-441[»]
    2X3XX-ray3.35A/B/C1-337[»]
    D/E382-441[»]
    ProteinModelPortaliQ61644.
    SMRiQ61644. Positions 13-304, 385-440.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ61644.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini10 – 7364FCHPROSITE-ProRule annotationAdd
    BLAST
    Domaini382 – 44160SH3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 304304F-BAR domainAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili23 – 272250Add
    BLAST

    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. DNM1 binding abolishes autoinhibition.1 Publication

    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.
    InParanoidiQ61644.
    OMAiAMTREAN.
    OrthoDBiEOG75TMBJ.
    PhylomeDBiQ61644.
    TreeFamiTF313677.

    Family and domain databases

    InterProiIPR001060. FCH_dom.
    IPR028518. PACSIN1.
    IPR001452. SH3_domain.
    [Graphical view]
    PANTHERiPTHR10959:SF7. PTHR10959:SF7. 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.

    Q61644-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSGSYDEASE EITDSFWEVG NYKRTVKRID DGHRLCNDLM SCVQERAKIE    50
    KAYAQQLTDW AKRWRQLIEK GPQYGSLERA WGAMMTEADK VSELHQEVKN 100
    SLLNEDLEKV KNWQKDAYHK QIMGGFKETK EAEDGFRKAQ KPWAKKMKEL 150
    EAAKKAYHLA CKEERLAMTR EMNSKTEQSV TPEQQKKLVD KVDKCRQDVQ 200
    KTQEKYEKVL EDVGKTTPQY MEGMEQVFEQ CQQFEEKRLV FLKEVLLDIK 250
    RHLNLAENSS YMHVYRELEQ AIRGADAQED LRWFRSTSGP GMPMNWPQFE 300
    EWNPDLPHTT AKKEKQPKKA EGATLSNATG AVESTSQAGD RGSVSSYDRG 350
    QTYATEWSDD ESGNPFGGNE ANGGANPFED DAKGVRVRAL YDYDGQEQDE 400
    LSFKAGDELT KLGEEDEQGW CRGRLDSGQL GLYPANYVEA I 441
    Length:441
    Mass (Da):50,575
    Last modified:November 1, 1996 - v1
    Checksum:i21BEB339A14A41F9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X85124 mRNA. Translation: CAA59437.1.
    BC014698 mRNA. Translation: AAH14698.1.
    CCDSiCCDS28567.1.
    RefSeqiNP_001273672.1. NM_001286743.1.
    NP_001273673.1. NM_001286744.1.
    NP_035991.1. NM_011861.3.
    NP_848142.1. NM_178365.4.
    XP_006524289.1. XM_006524226.1.
    XP_006536813.1. XM_006536750.1.
    UniGeneiMm.4926.

    Genome annotation databases

    EnsembliENSMUST00000045896; ENSMUSP00000044168; ENSMUSG00000040276.
    ENSMUST00000097360; ENSMUSP00000094973; ENSMUSG00000040276.
    ENSMUST00000114872; ENSMUSP00000110522; ENSMUSG00000040276.
    ENSMUST00000114873; ENSMUSP00000110523; ENSMUSG00000040276.
    GeneIDi23969.
    KEGGimmu:23969.
    UCSCiuc008bpj.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X85124 mRNA. Translation: CAA59437.1 .
    BC014698 mRNA. Translation: AAH14698.1 .
    CCDSi CCDS28567.1.
    RefSeqi NP_001273672.1. NM_001286743.1.
    NP_001273673.1. NM_001286744.1.
    NP_035991.1. NM_011861.3.
    NP_848142.1. NM_178365.4.
    XP_006524289.1. XM_006524226.1.
    XP_006536813.1. XM_006536750.1.
    UniGenei Mm.4926.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2X3V X-ray 2.45 A/B/C 1-337 [» ]
    2X3W X-ray 2.64 A/B/C 1-337 [» ]
    D 382-441 [» ]
    2X3X X-ray 3.35 A/B/C 1-337 [» ]
    D/E 382-441 [» ]
    ProteinModelPortali Q61644.
    SMRi Q61644. Positions 13-304, 385-440.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-53108N.
    IntActi Q61644. 8 interactions.
    MINTi MINT-4106465.
    STRINGi 10090.ENSMUSP00000110522.

    PTM databases

    PhosphoSitei Q61644.

    2D gel databases

    UCD-2DPAGE Q61644.

    Proteomic databases

    MaxQBi Q61644.
    PaxDbi Q61644.
    PRIDEi Q61644.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000045896 ; ENSMUSP00000044168 ; ENSMUSG00000040276 .
    ENSMUST00000097360 ; ENSMUSP00000094973 ; ENSMUSG00000040276 .
    ENSMUST00000114872 ; ENSMUSP00000110522 ; ENSMUSG00000040276 .
    ENSMUST00000114873 ; ENSMUSP00000110523 ; ENSMUSG00000040276 .
    GeneIDi 23969.
    KEGGi mmu:23969.
    UCSCi uc008bpj.1. mouse.

    Organism-specific databases

    CTDi 29993.
    MGIi MGI:1345181. Pacsin1.

    Phylogenomic databases

    eggNOGi NOG283356.
    GeneTreei ENSGT00510000046376.
    HOGENOMi HOG000007245.
    HOVERGENi HBG053486.
    InParanoidi Q61644.
    OMAi AMTREAN.
    OrthoDBi EOG75TMBJ.
    PhylomeDBi Q61644.
    TreeFami TF313677.

    Miscellaneous databases

    EvolutionaryTracei Q61644.
    NextBioi 303847.
    PROi Q61644.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q61644.
    Bgeei Q61644.
    Genevestigatori Q61644.

    Family and domain databases

    InterProi IPR001060. FCH_dom.
    IPR028518. PACSIN1.
    IPR001452. SH3_domain.
    [Graphical view ]
    PANTHERi PTHR10959:SF7. PTHR10959:SF7. 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, a brain protein that is upregulated upon differentiation into neuronal cells."
      Plomann M., Lange R., Vopper G., Cremer H., Heinlein U.A.O., Scheff S., Baldwin S.A., Leitges M., Cramer M., Paulsson M., Barthels D.
      Eur. J. Biochem. 256:201-211(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
      Strain: C57BL/6J.
      Tissue: Cerebellum.
    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: Eye.
    3. Lubec G., Kang S.U.
      Submitted (APR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 52-62; 71-79; 319-341 AND 425-441, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6.
      Tissue: Brain.
    4. "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 PACSIN2 AND PACSIN3, TISSUE SPECIFICITY, MUTAGENESIS OF PRO-434.
    5. "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: INTERACTION WITH EHD1.
    6. "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.
    7. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
      Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
      J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-391, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    8. Cited for: FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH DNM1; DNM2 AND DNM3, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    9. "PACSIN1, a Tau-interacting protein, regulates axonal elongation and branching by facilitating microtubule instability."
      Liu Y., Lv K., Li Z., Yu A.C., Chen J., Teng J.
      J. Biol. Chem. 287:39911-39924(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MAPT, MUTAGENESIS OF PRO-434, TISSUE SPECIFICITY.
    10. Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 1-337, SUBCELLULAR LOCATION, FUNCTION, SUBUNIT, INTERACTION WITH DNM1, MUTAGENESIS OF 122-ILE-MET-123; LYS-127; LYS-130; 145-LYS--LYS-148 AND PRO-434, DOMAIN, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiPACN1_MOUSE
    AccessioniPrimary (citable) accession number: Q61644
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 2002
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 114 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, 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

    External Data

    Dasty 3