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Protein

Protein kinase C and casein kinase substrate in neurons protein 1

Gene

Pacsin1

Organism
Rattus norvegicus (Rat)
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.5 Publications

GO - Molecular functioni

  • phospholipid binding Source: UniProtKB

GO - Biological processi

  • actin filament organization Source: InterPro
  • cytoskeleton organization Source: RGD
  • establishment of protein localization to plasma membrane Source: BHF-UCL
  • membrane tubulation Source: UniProtKB
  • neuron projection morphogenesis Source: UniProtKB
  • positive regulation of dendrite development Source: BHF-UCL
  • protein localization to membrane Source: UniProtKB
  • regulation of endocytosis Source: GO_Central
  • 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):
Dynamin proline-rich domain-interacting protein
Short name:
Dynamin PRD-interacting protein
Synaptic, dynamin-associated protein I
Syndapin-1
Syndapin-I
Short name:
SdpI
Gene namesi
Name:Pacsin1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3247. Pacsin1.

Subcellular locationi

GO - Cellular componenti

  • axon terminus Source: UniProtKB
  • cell junction Source: UniProtKB-KW
  • cytoplasm Source: UniProtKB
  • cytoplasmic vesicle membrane Source: UniProtKB-SubCell
  • cytosol Source: UniProtKB-SubCell
  • endosome Source: GO_Central
  • perinuclear region of cytoplasm Source: BHF-UCL
  • plasma membrane Source: BHF-UCL
  • ruffle membrane Source: UniProtKB
  • synapse Source: BHF-UCL
  • terminal bouton Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi62 – 632KR → QQ: Reduces membrane-binding. Abolishes membrane tubulation. 1 Publication
Mutagenesisi76 – 761S → A: No effect on membrane-binding. Reduces membrane tubulation. 1 Publication
Mutagenesisi127 – 1271K → Q: Reduces membrane-binding; when associated with Q-130. Abolishes membrane tubulation. 1 Publication
Mutagenesisi130 – 1301K → Q: Reduces membrane-binding. Abolishes membrane tubulation; when associated with Q-127. 1 Publication
Mutagenesisi154 – 1552KK → QQ: Reduces membrane-binding. Abolishes membrane tubulation. 1 Publication
Mutagenesisi181 – 1811T → A: No effect on membrane-binding. 1 Publication
Mutagenesisi181 – 1811T → E: Reduces membrane-binding. Abolishes membrane tubulation. 1 Publication
Mutagenesisi276 – 2761D → A: Reduces membrane tubulation; when associated with A-280. 1 Publication
Mutagenesisi280 – 2801D → A: Reduces membrane tubulation; when associated with A-276. 1 Publication
Mutagenesisi434 – 4341P → L: Abolishes interaction with DNM1, SYNJ1 and WASL. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 441441Protein kinase C and casein kinase substrate in neurons protein 1PRO_0000161794Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21PhosphoserineCombined sources
Modified residuei76 – 761Phosphoserine1 Publication
Modified residuei181 – 1811Phosphothreonine1 Publication
Modified residuei343 – 3431PhosphoserineBy similarity
Modified residuei345 – 3451PhosphoserineBy similarity
Modified residuei346 – 3461PhosphoserineCombined sources
Modified residuei358 – 3581PhosphoserineCombined sources
Modified residuei362 – 3621PhosphoserineCombined sources
Modified residuei391 – 3911PhosphotyrosineBy similarity
Modified residuei402 – 4021PhosphoserineBy similarity
Modified residuei427 – 4271PhosphoserineCombined sources

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9Z0W5.
PRIDEiQ9Z0W5.

PTM databases

iPTMnetiQ9Z0W5.
PhosphoSiteiQ9Z0W5.

Expressioni

Tissue specificityi

Highly expressed in brain (at protein level).4 Publications

Interactioni

Subunit structurei

Homodimer. May form heterooligomers with other PACSINs. Interacts with MAPT. Interacts with TRPV4 (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 both COBL and DBNL. Identified in a complex composed of COBL, PACSIN1 and WASL. Interacts with EHD1 and EHD3.By similarity8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CoblD3ZUI55EBI-1550185,EBI-7003590
CoblQ5NBX114EBI-1550185,EBI-1550138From a different organism.
Dnm1P215754EBI-1550185,EBI-80070
NCKIPSDQ9NZQ36EBI-1550185,EBI-745080From a different organism.

Protein-protein interaction databases

BioGridi248321. 2 interactions.
DIPiDIP-39836N.
IntActiQ9Z0W5. 6 interactions.
MINTiMINT-196270.
STRINGi10116.ENSRNOP00000036285.

Structurei

3D structure databases

ProteinModelPortaliQ9Z0W5.
ModBaseiSearch...
MobiDBiSearch...

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 – 272250By similarityAdd
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 (By similarity).By similarity

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

eggNOGiKOG2856. Eukaryota.
ENOG410XRX2. LUCA.
HOGENOMiHOG000007245.
HOVERGENiHBG053486.
InParanoidiQ9Z0W5.
KOiK20123.
PhylomeDBiQ9Z0W5.

Family and domain databases

InterProiIPR031160. F_BAR.
IPR001060. FCH_dom.
IPR028518. PACSIN1.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR23065:SF16. PTHR23065:SF16. 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.

Q9Z0W5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGPYDEASE 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 CKEEKLAMTR EMNSKTEQSV TPEQQKKLVD KVDKCRQDVQ
210 220 230 240 250
KTQEKYEKVL EDVGKTTPQY MEGMEQVFEQ CQQFEEKRLV FLKEVLLDIK
260 270 280 290 300
RHLNLAENSS YIHVYRELEQ AIRGADAQED LRWFRSTSGP GMPMNWPQFE
310 320 330 340 350
EWNPDLPHTA AKKEKQPKKA EGAALSNATG AVESTSQAGD RGSVSSYDRG
360 370 380 390 400
QAYATEWSDD ESGNPFGGNE ANGGANPFED DAKGVRVRAL YDYDGQEQDE
410 420 430 440
LSFKAGDELT KLGEEDEQGW CRGRLDSGQL GLYPANYVEA I
Length:441
Mass (Da):50,449
Last modified:May 1, 1999 - v1
Checksum:i585B328850572DF8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF104402 mRNA. Translation: AAD16887.1.
RefSeqiNP_058990.1. NM_017294.1.
UniGeneiRn.161729.

Genome annotation databases

GeneIDi29704.
KEGGirno:29704.
UCSCiRGD:3247. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF104402 mRNA. Translation: AAD16887.1.
RefSeqiNP_058990.1. NM_017294.1.
UniGeneiRn.161729.

3D structure databases

ProteinModelPortaliQ9Z0W5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248321. 2 interactions.
DIPiDIP-39836N.
IntActiQ9Z0W5. 6 interactions.
MINTiMINT-196270.
STRINGi10116.ENSRNOP00000036285.

PTM databases

iPTMnetiQ9Z0W5.
PhosphoSiteiQ9Z0W5.

Proteomic databases

PaxDbiQ9Z0W5.
PRIDEiQ9Z0W5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi29704.
KEGGirno:29704.
UCSCiRGD:3247. rat.

Organism-specific databases

CTDi29993.
RGDi3247. Pacsin1.

Phylogenomic databases

eggNOGiKOG2856. Eukaryota.
ENOG410XRX2. LUCA.
HOGENOMiHOG000007245.
HOVERGENiHBG053486.
InParanoidiQ9Z0W5.
KOiK20123.
PhylomeDBiQ9Z0W5.

Miscellaneous databases

PROiQ9Z0W5.

Family and domain databases

InterProiIPR031160. F_BAR.
IPR001060. FCH_dom.
IPR028518. PACSIN1.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR23065:SF16. PTHR23065:SF16. 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. "Syndapin I, a synaptic dynamin-binding protein that associates with the neural Wiskott-Aldrich syndrome protein."
    Qualmann B., Roos J., DiGregorio P.J., Kelly R.B.
    Mol. Biol. Cell 10:501-513(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 71-90 AND 412-429, INTERACTION WITH DNM1; SYNJ1 AND WASL, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF PRO-434.
    Strain: Sprague-Dawley.
    Tissue: Brain.
  2. Lubec G., Diao W., Kang S.U., Lubec S.
    Submitted (SEP-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 71-79; 197-215; 252-266; 274-282 AND 389-404, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain and Hippocampus.
  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: SUBCELLULAR LOCATION.
  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: INTERACTION WITH EHD1 AND EHD3, TISSUE SPECIFICITY.
  5. "Syndapin I is the phosphorylation-regulated dynamin I partner in synaptic vesicle endocytosis."
    Anggono V., Smillie K.J., Graham M.E., Valova V.A., Cousin M.A., Robinson P.J.
    Nat. Neurosci. 9:752-760(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH DNM1, PARTIAL PROTEIN SEQUENCE, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
  6. "Cordon-bleu is an actin nucleation factor and controls neuronal morphology."
    Ahuja R., Pinyol R., Reichenbach N., Custer L., Klingensmith J., Kessels M.M., Qualmann B.
    Cell 131:337-350(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH COBL AND DBNL.
  7. "Syndapin I and endophilin I bind overlapping proline-rich regions of dynamin I: role in synaptic vesicle endocytosis."
    Anggono V., Robinson P.J.
    J. Neurochem. 102:931-943(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH DNM1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  8. "F-BAR proteins of the syndapin family shape the plasma membrane and are crucial for neuromorphogenesis."
    Dharmalingam E., Haeckel A., Pinyol R., Schwintzer L., Koch D., Kessels M.M., Qualmann B.
    J. Neurosci. 29:13315-13327(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DOMAIN, SUBCELLULAR LOCATION, INTERACTION WITH WASL.
  9. "The functions of the actin nucleator Cobl in cellular morphogenesis critically depend on syndapin I."
    Schwintzer L., Koch N., Ahuja R., Grimm J., Kessels M.M., Qualmann B.
    EMBO J. 30:3147-3159(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH COBL, IDENTIFICATION IN A COMPLEX WITH COBL AND WASL.
  10. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-346; SER-358; SER-362 AND SER-427, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Phosphorylation of syndapin I F-BAR domain at two helix-capping motifs regulates membrane tubulation."
    Quan A., Xue J., Wielens J., Smillie K.J., Anggono V., Parker M.W., Cousin M.A., Graham M.E., Robinson P.J.
    Proc. Natl. Acad. Sci. U.S.A. 109:3760-3765(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT SER-76 AND THR-181, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH DNM1 AND WASL, DOMAIN, MUTAGENESIS OF 62-LYS-LYS-63; SER-76; LYS-127; LYS-130; 154-LYS-LYS-155; THR-181; ASP-276 AND ASP-280, TISSUE SPECIFICITY.

Entry informationi

Entry nameiPACN1_RAT
AccessioniPrimary (citable) accession number: Q9Z0W5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 2002
Last sequence update: May 1, 1999
Last modified: July 6, 2016
This is version 115 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.