Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Protein kinase C and casein kinase substrate in neurons protein 1

Gene

Pacsin1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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
  • identical protein binding Source: IntAct
  • phospholipid binding Source: UniProtKB

GO - Biological processi

Keywordsi

Biological processEndocytosis
LigandLipid-binding

Enzyme and pathway databases

ReactomeiR-MMU-8856828 Clathrin-mediated endocytosis

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:1345181 Pacsin1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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)DescriptionActionsGraphical viewLength
Mutagenesisi122 – 123IM → FF: Increases membrane tubulation. 1 Publication2
Mutagenesisi122 – 123IM → QQ: Abolishes membrane tubulation. No effect on phospholipid binding. 1 Publication2
Mutagenesisi127K → E: Abolishes membrane tubulation; when associated with E-130. 1 Publication1
Mutagenesisi130K → E: Abolishes membrane tubulation; when associated with E-127. 1 Publication1
Mutagenesisi145 – 148KKMK → EEME: Abolishes membrane tubulation. 1 Publication4
Mutagenesisi400E → R: Impairs interaction with DNM1. 1
Mutagenesisi434P → L: Abolishes interaction with DNM1, MAPT, SYNJ1 and WASL. 3 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001617931 – 441Protein kinase C and casein kinase substrate in neurons protein 1Add BLAST441

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2PhosphoserineBy similarity1
Modified residuei76PhosphoserineBy similarity1
Modified residuei181PhosphothreonineBy similarity1
Modified residuei343PhosphoserineCombined sources1
Modified residuei345PhosphoserineCombined sources1
Modified residuei346PhosphoserineBy similarity1
Modified residuei358PhosphoserineCombined sources1
Modified residuei362PhosphoserineBy similarity1
Modified residuei391PhosphotyrosineCombined sources1
Modified residuei402PhosphoserineCombined sources1
Modified residuei427PhosphoserineCombined sources1

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-2DPAGEiQ61644

PTM databases

iPTMnetiQ61644
PhosphoSitePlusiQ61644

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

BgeeiENSMUSG00000040276 Expressed in 157 organ(s), highest expression level in olfactory bulb
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

GO - Molecular functioni

Protein-protein interaction databases

DIPiDIP-53108N
IntActiQ61644, 11 interactors
MINTiQ61644
STRINGi10090.ENSMUSP00000044168

Structurei

Secondary structure

1441
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ61644
SMRiQ61644
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ61644

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini10 – 280F-BARPROSITE-ProRule annotationAdd BLAST271
Domaini382 – 441SH3PROSITE-ProRule annotationAdd BLAST60

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili23 – 272Add BLAST250

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

Keywords - Domaini

Coiled coil, SH3 domain

Phylogenomic databases

eggNOGiKOG2856 Eukaryota
ENOG410XRX2 LUCA
GeneTreeiENSGT00510000046376
HOGENOMiHOG000007245
HOVERGENiHBG053486
InParanoidiQ61644
KOiK20123
OMAiHQEVKNS
OrthoDBiEOG091G0AS9
PhylomeDBiQ61644
TreeFamiTF313677

Family and domain databases

CDDicd07680 F-BAR_PACSIN1, 1 hit
cd11998 SH3_PACSIN1-2, 1 hit
Gene3Di