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Q61644

- PACN1_MOUSE

UniProt

Q61644 - PACN1_MOUSE

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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: 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

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

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
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: 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. ruffle membrane Source: UniProtKB
  6. synapse Source: UniProtKB-KW
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).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

BgeeiQ61644.
ExpressionAtlasiQ61644. baseline and differential.
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 – 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 – 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

        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_006524226.1.
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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

Bgeei Q61644.
ExpressionAtlasi Q61644. baseline and differential.
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

« 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: November 26, 2014
This is version 116 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