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Protein kinase C and casein kinase substrate in neurons protein 1 (Dynamin proline-rich domain-interacting protein) (Dynamin PRD-interacting protein) (Synaptic, dynamin-associated protein I) (Syndapin-1) (Syndapin-I) (SdpI)

 PACN1_RAT               Reviewed;         441 AA.
Q9Z0W5;
13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
23-MAY-2018, entry version 128.
RecName: Full=Protein kinase C and casein kinase substrate in neurons protein 1;
AltName: Full=Dynamin proline-rich domain-interacting protein;
Short=Dynamin PRD-interacting protein;
AltName: Full=Synaptic, dynamin-associated protein I;
AltName: Full=Syndapin-1;
AltName: Full=Syndapin-I;
Short=SdpI;
Name=Pacsin1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 71-90 AND 412-429,
INTERACTION WITH DNM1; SYNJ1 AND WASL, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND MUTAGENESIS OF PRO-434.
STRAIN=Sprague-Dawley; TISSUE=Brain;
PubMed=9950691; DOI=10.1091/mbc.10.2.501;
Qualmann B., Roos J., DiGregorio P.J., Kelly R.B.;
"Syndapin I, a synaptic dynamin-binding protein that associates with
the neural Wiskott-Aldrich syndrome protein.";
Mol. Biol. Cell 10:501-513(1999).
[2]
PROTEIN SEQUENCE OF 71-79; 197-215; 252-266; 274-282 AND 389-404, AND
IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Brain, and Hippocampus;
Lubec G., Diao W., Kang S.U., Lubec S.;
Submitted (SEP-2007) to UniProtKB.
[3]
SUBCELLULAR LOCATION.
PubMed=11082044;
Modregger J., Ritter B., Witter B., Paulsson M., Plomann M.;
"All three PACSIN isoforms bind to endocytic proteins and inhibit
endocytosis.";
J. Cell Sci. 113:4511-4521(2000).
[4]
INTERACTION WITH EHD1 AND EHD3, AND TISSUE SPECIFICITY.
PubMed=15930129; DOI=10.1091/mbc.E05-01-0076;
Braun A., Pinyol R., Dahlhaus R., Koch D., Fonarev P., Grant B.D.,
Kessels M.M., Qualmann B.;
"EHD proteins associate with syndapin I and II and such interactions
play a crucial role in endosomal recycling.";
Mol. Biol. Cell 16:3642-3658(2005).
[5]
FUNCTION, INTERACTION WITH DNM1, PARTIAL PROTEIN SEQUENCE, SUBCELLULAR
LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=16648848; DOI=10.1038/nn1695;
Anggono V., Smillie K.J., Graham M.E., Valova V.A., Cousin M.A.,
Robinson P.J.;
"Syndapin I is the phosphorylation-regulated dynamin I partner in
synaptic vesicle endocytosis.";
Nat. Neurosci. 9:752-760(2006).
[6]
INTERACTION WITH COBL AND DBNL.
PubMed=17956734; DOI=10.1016/j.cell.2007.08.030;
Ahuja R., Pinyol R., Reichenbach N., Custer L., Klingensmith J.,
Kessels M.M., Qualmann B.;
"Cordon-bleu is an actin nucleation factor and controls neuronal
morphology.";
Cell 131:337-350(2007).
[7]
FUNCTION, INTERACTION WITH DNM1, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=17437541; DOI=10.1111/j.1471-4159.2007.04574.x;
Anggono V., Robinson P.J.;
"Syndapin I and endophilin I bind overlapping proline-rich regions of
dynamin I: role in synaptic vesicle endocytosis.";
J. Neurochem. 102:931-943(2007).
[8]
FUNCTION, DOMAIN, SUBCELLULAR LOCATION, AND INTERACTION WITH WASL.
PubMed=19846719; DOI=10.1523/JNEUROSCI.3973-09.2009;
Dharmalingam E., Haeckel A., Pinyol R., Schwintzer L., Koch D.,
Kessels M.M., Qualmann B.;
"F-BAR proteins of the syndapin family shape the plasma membrane and
are crucial for neuromorphogenesis.";
J. Neurosci. 29:13315-13327(2009).
[9]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH COBL, AND
IDENTIFICATION IN A COMPLEX WITH COBL AND WASL.
PubMed=21725280; DOI=10.1038/emboj.2011.207;
Schwintzer L., Koch N., Ahuja R., Grimm J., Kessels M.M., Qualmann B.;
"The functions of the actin nucleator Cobl in cellular morphogenesis
critically depend on syndapin I.";
EMBO J. 30:3147-3159(2011).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-346; SER-358;
SER-362 AND SER-427, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[11]
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, AND TISSUE
SPECIFICITY.
PubMed=22355135; DOI=10.1073/pnas.1108294109;
Quan A., Xue J., Wielens J., Smillie K.J., Anggono V., Parker M.W.,
Cousin M.A., Graham M.E., Robinson P.J.;
"Phosphorylation of syndapin I F-BAR domain at two helix-capping
motifs regulates membrane tubulation.";
Proc. Natl. Acad. Sci. U.S.A. 109:3760-3765(2012).
-!- FUNCTION: 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.
{ECO:0000269|PubMed:16648848, ECO:0000269|PubMed:17437541,
ECO:0000269|PubMed:19846719, ECO:0000269|PubMed:21725280,
ECO:0000269|PubMed:22355135}.
-!- SUBUNIT: 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. {ECO:0000250,
ECO:0000269|PubMed:15930129, ECO:0000269|PubMed:16648848,
ECO:0000269|PubMed:17437541, ECO:0000269|PubMed:17956734,
ECO:0000269|PubMed:19846719, ECO:0000269|PubMed:21725280,
ECO:0000269|PubMed:22355135, ECO:0000269|PubMed:9950691}.
-!- INTERACTION:
D3ZUI5:Cobl; NbExp=6; IntAct=EBI-1550185, EBI-7003590;
Q5NBX1:Cobl (xeno); NbExp=14; IntAct=EBI-1550185, EBI-1550138;
Q5NBX1-1:Cobl (xeno); NbExp=2; IntAct=EBI-1550185, EBI-16174243;
P21575:Dnm1; NbExp=4; IntAct=EBI-1550185, EBI-80070;
Q9NZQ3:NCKIPSD (xeno); NbExp=6; IntAct=EBI-1550185, EBI-745080;
-!- SUBCELLULAR LOCATION: Cytoplasm. Cell projection. Cell junction,
synapse, synaptosome. Cell projection, ruffle membrane
{ECO:0000250}. Membrane; Peripheral membrane protein. Cytoplasmic
vesicle membrane {ECO:0000250}; Peripheral membrane protein
{ECO:0000250}. Cell junction, synapse {ECO:0000250}. Cytoplasm,
cytosol {ECO:0000250}. Cell membrane; Peripheral membrane protein;
Cytoplasmic side. Note=Colocalizes with MAPT in axons (By
similarity). 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.
{ECO:0000250}.
-!- TISSUE SPECIFICITY: Highly expressed in brain (at protein level).
{ECO:0000269|PubMed:15930129, ECO:0000269|PubMed:17437541,
ECO:0000269|PubMed:22355135, ECO:0000269|PubMed:9950691}.
-!- DOMAIN: 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). {ECO:0000250}.
-!- PTM: Phosphorylated by casein kinase 2 (CK2) and protein kinase C
(PKC). {ECO:0000305|PubMed:22355135}.
-!- SIMILARITY: Belongs to the PACSIN family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF104402; AAD16887.1; -; mRNA.
RefSeq; NP_058990.1; NM_017294.1.
UniGene; Rn.161729; -.
ProteinModelPortal; Q9Z0W5; -.
SMR; Q9Z0W5; -.
BioGrid; 248321; 2.
DIP; DIP-39836N; -.
ELM; Q9Z0W5; -.
IntAct; Q9Z0W5; 6.
MINT; Q9Z0W5; -.
STRING; 10116.ENSRNOP00000036285; -.
iPTMnet; Q9Z0W5; -.
PhosphoSitePlus; Q9Z0W5; -.
SwissPalm; Q9Z0W5; -.
PaxDb; Q9Z0W5; -.
PRIDE; Q9Z0W5; -.
GeneID; 29704; -.
KEGG; rno:29704; -.
UCSC; RGD:3247; rat.
CTD; 29993; -.
RGD; 3247; Pacsin1.
eggNOG; KOG2856; Eukaryota.
eggNOG; ENOG410XRX2; LUCA.
HOGENOM; HOG000007245; -.
HOVERGEN; HBG053486; -.
InParanoid; Q9Z0W5; -.
KO; K20123; -.
PhylomeDB; Q9Z0W5; -.
PRO; PR:Q9Z0W5; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0043679; C:axon terminus; IDA:UniProtKB.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0005768; C:endosome; IBA:GO_Central.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
GO; GO:0032587; C:ruffle membrane; ISS:UniProtKB.
GO; GO:0045202; C:synapse; IDA:BHF-UCL.
GO; GO:0043195; C:terminal bouton; HDA:ParkinsonsUK-UCL.
GO; GO:0005543; F:phospholipid binding; IDA:UniProtKB.
GO; GO:0007015; P:actin filament organization; IEA:InterPro.
GO; GO:0007010; P:cytoskeleton organization; IDA:RGD.
GO; GO:0048812; P:neuron projection morphogenesis; IMP:UniProtKB.
GO; GO:0097320; P:plasma membrane tubulation; IMP:UniProtKB.
GO; GO:1900006; P:positive regulation of dendrite development; IDA:BHF-UCL.
GO; GO:0072657; P:protein localization to membrane; ISS:UniProtKB.
GO; GO:0072659; P:protein localization to plasma membrane; IDA:BHF-UCL.
GO; GO:0030100; P:regulation of endocytosis; IBA:GO_Central.
GO; GO:0048488; P:synaptic vesicle endocytosis; ISS:UniProtKB.
CDD; cd07680; F-BAR_PACSIN1; 1.
CDD; cd11998; SH3_PACSIN1-2; 1.
Gene3D; 1.20.1270.60; -; 1.
InterPro; IPR027267; AH/BAR_dom_sf.
InterPro; IPR031160; F_BAR.
InterPro; IPR001060; FCH_dom.
InterPro; IPR028518; PACSIN1.
InterPro; IPR035743; PACSIN1/PACSIN2_SH3.
InterPro; IPR037454; PACSIN1_F-BAR.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
PANTHER; PTHR23065:SF16; PTHR23065:SF16; 1.
Pfam; PF00611; FCH; 1.
Pfam; PF14604; SH3_9; 1.
PRINTS; PR00452; SH3DOMAIN.
SMART; SM00055; FCH; 1.
SMART; SM00326; SH3; 1.
SUPFAM; SSF103657; SSF103657; 1.
SUPFAM; SSF50044; SSF50044; 1.
PROSITE; PS51741; F_BAR; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
Cell junction; Cell membrane; Cell projection; Coiled coil;
Complete proteome; Cytoplasm; Cytoplasmic vesicle;
Direct protein sequencing; Endocytosis; Lipid-binding; Membrane;
Phosphoprotein; Reference proteome; SH3 domain; Synapse; Synaptosome.
CHAIN 1 441 Protein kinase C and casein kinase
substrate in neurons protein 1.
/FTId=PRO_0000161794.
DOMAIN 10 280 F-BAR. {ECO:0000255|PROSITE-
ProRule:PRU01077}.
DOMAIN 382 441 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
COILED 23 272 {ECO:0000250}.
MOD_RES 2 2 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 76 76 Phosphoserine.
{ECO:0000269|PubMed:22355135}.
MOD_RES 181 181 Phosphothreonine.
{ECO:0000269|PubMed:22355135}.
MOD_RES 343 343 Phosphoserine.
{ECO:0000250|UniProtKB:Q61644}.
MOD_RES 345 345 Phosphoserine.
{ECO:0000250|UniProtKB:Q61644}.
MOD_RES 346 346 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 358 358 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 362 362 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 391 391 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q61644}.
MOD_RES 402 402 Phosphoserine.
{ECO:0000250|UniProtKB:Q61644}.
MOD_RES 427 427 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MUTAGEN 62 63 KR->QQ: Reduces membrane-binding.
Abolishes membrane tubulation.
{ECO:0000269|PubMed:22355135}.
MUTAGEN 76 76 S->A: No effect on membrane-binding.
Reduces membrane tubulation.
{ECO:0000269|PubMed:22355135}.
MUTAGEN 127 127 K->Q: Reduces membrane-binding; when
associated with Q-130. Abolishes membrane
tubulation.
{ECO:0000269|PubMed:22355135}.
MUTAGEN 130 130 K->Q: Reduces membrane-binding. Abolishes
membrane tubulation; when associated with
Q-127. {ECO:0000269|PubMed:22355135}.
MUTAGEN 154 155 KK->QQ: Reduces membrane-binding.
Abolishes membrane tubulation.
{ECO:0000269|PubMed:22355135}.
MUTAGEN 181 181 T->A: No effect on membrane-binding.
{ECO:0000269|PubMed:22355135}.
MUTAGEN 181 181 T->E: Reduces membrane-binding. Abolishes
membrane tubulation.
{ECO:0000269|PubMed:22355135}.
MUTAGEN 276 276 D->A: Reduces membrane tubulation; when
associated with A-280.
{ECO:0000269|PubMed:22355135}.
MUTAGEN 280 280 D->A: Reduces membrane tubulation; when
associated with A-276.
{ECO:0000269|PubMed:22355135}.
MUTAGEN 434 434 P->L: Abolishes interaction with DNM1,
SYNJ1 and WASL.
{ECO:0000269|PubMed:9950691}.
SEQUENCE 441 AA; 50449 MW; 585B328850572DF8 CRC64;
MSGPYDEASE EITDSFWEVG NYKRTVKRID DGHRLCNDLM SCVQERAKIE KAYAQQLTDW
AKRWRQLIEK GPQYGSLERA WGAMMTEADK VSELHQEVKN SLLNEDLEKV KNWQKDAYHK
QIMGGFKETK EAEDGFRKAQ KPWAKKMKEL EAAKKAYHLA CKEEKLAMTR EMNSKTEQSV
TPEQQKKLVD KVDKCRQDVQ KTQEKYEKVL EDVGKTTPQY MEGMEQVFEQ CQQFEEKRLV
FLKEVLLDIK RHLNLAENSS YIHVYRELEQ AIRGADAQED LRWFRSTSGP GMPMNWPQFE
EWNPDLPHTA AKKEKQPKKA EGAALSNATG AVESTSQAGD RGSVSSYDRG QAYATEWSDD
ESGNPFGGNE ANGGANPFED DAKGVRVRAL YDYDGQEQDE LSFKAGDELT KLGEEDEQGW
CRGRLDSGQL GLYPANYVEA I


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