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Protein

Protein kinase C and casein kinase substrate in neurons protein 1

Gene

Pacsin1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

  • cytoskeletal protein binding Source: MGI
  • phospholipid binding Source: UniProtKB

GO - Biological processi

  • actin filament organization Source: InterPro
  • cytoskeleton organization Source: GO_Central
  • membrane tubulation Source: UniProtKB
  • negative regulation of endocytosis Source: MGI
  • neuron projection morphogenesis Source: UniProtKB
  • protein localization to membrane Source: UniProtKB
  • signal transduction Source: MGI
  • synaptic vesicle endocytosis Source: UniProtKB
Complete GO annotation...

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 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:1345181. Pacsin1.

Subcellular locationi

GO - Cellular componenti

  • axon terminus Source: UniProtKB
  • cell junction Source: UniProtKB-KW
  • COPI-coated vesicle Source: MGI
  • cytoplasm Source: UniProtKB
  • cytoplasmic vesicle membrane Source: UniProtKB-SubCell
  • cytosol Source: UniProtKB-SubCell
  • endosome Source: GO_Central
  • membrane Source: GO_Central
  • myelin sheath Source: UniProtKB
  • ruffle membrane Source: UniProtKB
  • synapse Source: UniProtKB-SubCell
Complete GO annotation...

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. 1 Publication
Mutagenesisi122 – 1232IM → QQ: Abolishes membrane tubulation. No effect on phospholipid binding. 1 Publication
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. 1 Publication
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).

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

BgeeiQ61644.
ExpressionAtlasiQ61644. baseline and differential.
GenevisibleiQ61644. MM.

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.ENSMUSP00000044168.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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 – 280271F-BARPROSITE-ProRule annotationAdd
BLAST
Domaini382 – 44160SH3PROSITE-ProRule annotationAdd
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 F-BAR domain.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, SH3 domain

Phylogenomic databases

eggNOGiNOG283356.
GeneTreeiENSGT00510000046376.
HOGENOMiHOG000007245.
HOVERGENiHBG053486.
InParanoidiQ61644.
OMAiQSNTPEQ.
OrthoDBiEOG75TMBJ.
PhylomeDBiQ61644.
TreeFamiTF313677.

Family and domain databases

InterProiIPR031160. F_BAR.
IPR001060. 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.
PROSITEiPS51741. F_BAR. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q61644-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGSYDEASE EITDSFWEVG NYKRTVKRID DGHRLCNDLM SCVQERAKIE
60 70 80 90 100
KAYAQQLTDW AKRWRQLIEK GPQYGSLERA WGAMMTEADK VSELHQEVKN
110 120 130 140 150
SLLNEDLEKV KNWQKDAYHK QIMGGFKETK EAEDGFRKAQ KPWAKKMKEL
160 170 180 190 200
EAAKKAYHLA CKEERLAMTR EMNSKTEQSV TPEQQKKLVD KVDKCRQDVQ
210 220 230 240 250
KTQEKYEKVL EDVGKTTPQY MEGMEQVFEQ CQQFEEKRLV FLKEVLLDIK
260 270 280 290 300
RHLNLAENSS YMHVYRELEQ AIRGADAQED LRWFRSTSGP GMPMNWPQFE
310 320 330 340 350
EWNPDLPHTT AKKEKQPKKA EGATLSNATG AVESTSQAGD RGSVSSYDRG
360 370 380 390 400
QTYATEWSDD ESGNPFGGNE ANGGANPFED DAKGVRVRAL YDYDGQEQDE
410 420 430 440
LSFKAGDELT KLGEEDEQGW CRGRLDSGQL GLYPANYVEA I
Length:441
Mass (Da):50,575
Last modified:November 1, 1996 - v1
Checksum:i21BEB339A14A41F9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_006524226.2.
XP_006536813.1. XM_006536750.2.
XP_011243607.1. XM_011245305.1.
XP_011244733.1. XM_011246431.1.
UniGeneiMm.4926.

Genome annotation databases

EnsembliENSMUST00000045896; ENSMUSP00000044168; ENSMUSG00000040276.
ENSMUST00000097360; ENSMUSP00000094973; ENSMUSG00000040276.
ENSMUST00000114872; ENSMUSP00000110522; ENSMUSG00000040276.
ENSMUST00000114873; ENSMUSP00000110523; ENSMUSG00000040276.
GeneIDi23969.
KEGGimmu:23969.
UCSCiuc008bpj.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_006524226.2.
XP_006536813.1. XM_006536750.2.
XP_011243607.1. XM_011245305.1.
XP_011244733.1. XM_011246431.1.
UniGeneiMm.4926.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

DIPiDIP-53108N.
IntActiQ61644. 8 interactions.
MINTiMINT-4106465.
STRINGi10090.ENSMUSP00000044168.

PTM databases

PhosphoSiteiQ61644.

2D gel databases

UCD-2DPAGEQ61644.

Proteomic databases

MaxQBiQ61644.
PaxDbiQ61644.
PRIDEiQ61644.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000045896; ENSMUSP00000044168; ENSMUSG00000040276.
ENSMUST00000097360; ENSMUSP00000094973; ENSMUSG00000040276.
ENSMUST00000114872; ENSMUSP00000110522; ENSMUSG00000040276.
ENSMUST00000114873; ENSMUSP00000110523; ENSMUSG00000040276.
GeneIDi23969.
KEGGimmu:23969.
UCSCiuc008bpj.2. mouse.

Organism-specific databases

CTDi29993.
MGIiMGI:1345181. Pacsin1.

Phylogenomic databases

eggNOGiNOG283356.
GeneTreeiENSGT00510000046376.
HOGENOMiHOG000007245.
HOVERGENiHBG053486.
InParanoidiQ61644.
OMAiQSNTPEQ.
OrthoDBiEOG75TMBJ.
PhylomeDBiQ61644.
TreeFamiTF313677.

Miscellaneous databases

EvolutionaryTraceiQ61644.
NextBioi303847.
PROiQ61644.
SOURCEiSearch...

Gene expression databases

BgeeiQ61644.
ExpressionAtlasiQ61644. baseline and differential.
GenevisibleiQ61644. MM.

Family and domain databases

InterProiIPR031160. F_BAR.
IPR001060. 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.
PROSITEiPS51741. F_BAR. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: July 22, 2015
This is version 122 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

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 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.