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Protein kinase C and casein kinase substrate in neurons 2 protein (Synaptic dynamin-associated protein II) (Syndapin-2) (Syndapin-II) (SdpII)

 PACN2_RAT               Reviewed;         488 AA.
Q9QY17; Q9QY18; Q9QY19; Q9QY20;
13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
13-AUG-2002, sequence version 2.
22-NOV-2017, entry version 126.
RecName: Full=Protein kinase C and casein kinase substrate in neurons 2 protein;
AltName: Full=Synaptic dynamin-associated protein II;
AltName: Full=Syndapin-2;
AltName: Full=Syndapin-II;
Short=SdpII;
Name=Pacsin2;
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] (ISOFORMS 1; 2; 3 AND 4), FUNCTION,
INTERACTION WITH DNM1; SYN1; SYNJ1 AND WASL, SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
STRAIN=Sprague-Dawley; TISSUE=Brain;
PubMed=10704453; DOI=10.1083/jcb.148.5.1047;
Qualmann B., Kelly R.B.;
"Syndapin isoforms participate in receptor-mediated endocytosis and
actin organization.";
J. Cell Biol. 148:1047-1062(2000).
[2]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-401, 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).
-!- FUNCTION: Lipid-binding protein that is able to promote the
tubulation of the phosphatidic acid-containing membranes it
preferentially binds. Plays a role in intracellular vesicle-
mediated transport. Involved in the endocytosis of cell-surface
receptors like the EGF receptor, contributing to its
internalization in the absence of EGF stimulus. May also play a
role in the formation of caveolae at the cell membrane. Recruits
DNM2 to caveolae, and thereby plays a role in caveola-mediated
endocytosis. {ECO:0000269|PubMed:10704453}.
-!- SUBUNIT: Homodimer. May form heterooligomers with other PACSINs.
Interacts (via NPF motifs) with EHD1 (via EH domain). Interacts
with EHD3. Interacts (via the SH3 domain) with MICALL1. Interacts
with RAC1. Interacts (via SH3 domain) with DNM1, SYN1, SYNJ1 and
WASL. Interacts with CAV1. Interacts with TRPV4.
{ECO:0000269|PubMed:10704453}.
-!- INTERACTION:
Q5NBX1:Cobl (xeno); NbExp=4; IntAct=EBI-491201, EBI-1550138;
Q641Z6:Ehd1; NbExp=2; IntAct=EBI-491201, EBI-492911;
Q9EQP2:Ehd4 (xeno); NbExp=4; IntAct=EBI-491201, EBI-491022;
Q9NZQ3:NCKIPSD (xeno); NbExp=2; IntAct=EBI-491201, EBI-745080;
P18545:PDE6G (xeno); NbExp=4; IntAct=EBI-491201, EBI-2622029;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10704453}.
Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasmic vesicle
membrane {ECO:0000269|PubMed:10704453}; Peripheral membrane
protein {ECO:0000269|PubMed:10704453}; Cytoplasmic side
{ECO:0000269|PubMed:10704453}. Cell projection, ruffle membrane
{ECO:0000250}; Peripheral membrane protein {ECO:0000250};
Cytoplasmic side {ECO:0000250}. Early endosome {ECO:0000250}.
Recycling endosome membrane {ECO:0000250}. Cell membrane
{ECO:0000250}; Peripheral membrane protein {ECO:0000250};
Cytoplasmic side {ECO:0000250}. Cell projection {ECO:0000250}.
Membrane, caveola {ECO:0000250}. Note=Detected at the neck of
flask-shaped caveolae. Localization to tubular recycling endosomes
probably requires interaction with MICALL1 and EHD1.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=Aa, SdpII-l;
IsoId=Q9QY17-1; Sequence=Displayed;
Name=2; Synonyms=Ab;
IsoId=Q9QY17-2; Sequence=VSP_004519;
Name=3; Synonyms=Ba;
IsoId=Q9QY17-3; Sequence=VSP_004518;
Name=4; Synonyms=Bb, SdpII-s;
IsoId=Q9QY17-4; Sequence=VSP_004518, VSP_004519;
-!- TISSUE SPECIFICITY: Widely expressed (at protein level). Isoforms
1/3 are predominantly expressed in heart and in PC-12 cells, a
pheochromocytoma cell line (at protein level). Isoforms 2/4 are
widely expressed with highest levels in muscle, testis and brain
(at protein level). {ECO:0000269|PubMed:10704453}.
-!- 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 (By similarity). Endocytic
vesicle-like distribution. {ECO:0000250}.
-!- PTM: Phosphorylated by casein kinase 2 (CK2) and protein kinase C
(PKC). {ECO:0000250}.
-!- SIMILARITY: Belongs to the PACSIN family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF139492; AAF22211.1; -; mRNA.
EMBL; AF139493; AAF22212.1; -; mRNA.
EMBL; AF139494; AAF22213.1; -; mRNA.
EMBL; AF139495; AAF22214.1; -; mRNA.
RefSeq; NP_570096.2; NM_130740.2. [Q9QY17-3]
RefSeq; XP_006242112.1; XM_006242050.3. [Q9QY17-1]
RefSeq; XP_006242113.1; XM_006242051.2. [Q9QY17-1]
RefSeq; XP_006242114.1; XM_006242052.3. [Q9QY17-1]
RefSeq; XP_006242115.1; XM_006242053.2. [Q9QY17-1]
RefSeq; XP_006242117.1; XM_006242055.2. [Q9QY17-3]
RefSeq; XP_006242120.1; XM_006242058.2. [Q9QY17-2]
RefSeq; XP_006242122.1; XM_006242060.2. [Q9QY17-4]
RefSeq; XP_017450116.1; XM_017594627.1. [Q9QY17-1]
UniGene; Rn.17106; -.
ProteinModelPortal; Q9QY17; -.
SMR; Q9QY17; -.
ELM; Q9QY17; -.
IntAct; Q9QY17; 5.
MINT; MINT-4567486; -.
STRING; 10116.ENSRNOP00000060074; -.
iPTMnet; Q9QY17; -.
PhosphoSitePlus; Q9QY17; -.
PaxDb; Q9QY17; -.
PRIDE; Q9QY17; -.
Ensembl; ENSRNOT00000013398; ENSRNOP00000013398; ENSRNOG00000009756. [Q9QY17-3]
Ensembl; ENSRNOT00000067913; ENSRNOP00000060074; ENSRNOG00000009756. [Q9QY17-1]
Ensembl; ENSRNOT00000088125; ENSRNOP00000072822; ENSRNOG00000009756. [Q9QY17-3]
GeneID; 124461; -.
KEGG; rno:124461; -.
CTD; 11252; -.
RGD; 69411; Pacsin2.
eggNOG; KOG2856; Eukaryota.
eggNOG; ENOG410XRX2; LUCA.
GeneTree; ENSGT00510000046376; -.
HOGENOM; HOG000007245; -.
HOVERGEN; HBG053486; -.
InParanoid; Q9QY17; -.
KO; K20123; -.
OMA; CKGRMNG; -.
PhylomeDB; Q9QY17; -.
Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
PRO; PR:Q9QY17; -.
Proteomes; UP000002494; Chromosome 7.
Bgee; ENSRNOG00000009756; -.
ExpressionAtlas; Q9QY17; baseline and differential.
Genevisible; Q9QY17; RN.
GO; GO:0005901; C:caveola; ISO:RGD.
GO; GO:0005911; C:cell-cell junction; ISO:RGD.
GO; GO:0005737; C:cytoplasm; ISO:RGD.
GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; ISO:RGD.
GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
GO; GO:0005768; C:endosome; IBA:GO_Central.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0019898; C:extrinsic component of membrane; ISS:UniProtKB.
GO; GO:0005925; C:focal adhesion; ISO:RGD.
GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
GO; GO:0055038; C:recycling endosome membrane; ISO:RGD.
GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
GO; GO:0045296; F:cadherin binding; ISO:RGD.
GO; GO:0008092; F:cytoskeletal protein binding; ISO:RGD.
GO; GO:0042802; F:identical protein binding; ISO:RGD.
GO; GO:0008289; F:lipid binding; ISO:RGD.
GO; GO:0070300; F:phosphatidic acid binding; ISS:UniProtKB.
GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
GO; GO:0070836; P:caveola assembly; ISS:UniProtKB.
GO; GO:0072584; P:caveolin-mediated endocytosis; ISS:UniProtKB.
GO; GO:0048858; P:cell projection morphogenesis; ISS:UniProtKB.
GO; GO:0045806; P:negative regulation of endocytosis; ISO:RGD.
GO; GO:0097320; P:plasma membrane tubulation; ISS:UniProtKB.
GO; GO:0036010; P:protein localization to endosome; ISO:RGD.
GO; GO:0030100; P:regulation of endocytosis; IBA:GO_Central.
CDD; cd11998; SH3_PACSIN1-2; 1.
InterPro; IPR027267; AH/BAR_dom_sf.
InterPro; IPR031160; F_BAR.
InterPro; IPR001060; FCH_dom.
InterPro; IPR035743; PACSIN1/PACSIN2_SH3.
InterPro; IPR028521; PACSIN2.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
PANTHER; PTHR23065:SF14; PTHR23065:SF14; 1.
Pfam; PF00611; FCH; 1.
Pfam; PF00018; SH3_1; 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;
Acetylation; Alternative splicing; Cell membrane; Cell projection;
Coiled coil; Complete proteome; Cytoplasm; Cytoplasmic vesicle;
Cytoskeleton; Endocytosis; Endosome; Lipid-binding; Membrane;
Phosphoprotein; Reference proteome; SH3 domain.
CHAIN 1 488 Protein kinase C and casein kinase
substrate in neurons 2 protein.
/FTId=PRO_0000161797.
DOMAIN 11 282 F-BAR. {ECO:0000255|PROSITE-
ProRule:PRU01077}.
DOMAIN 428 488 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
COILED 25 274 {ECO:0000250}.
MOTIF 364 366 NPF1.
MOTIF 407 409 NPF2.
MOTIF 419 421 NPF3.
MOD_RES 53 53 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9WVE8}.
MOD_RES 273 273 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UNF0}.
MOD_RES 401 401 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 448 448 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UNF0}.
VAR_SEQ 302 303 Missing (in isoform 3 and isoform 4).
{ECO:0000303|PubMed:10704453}.
/FTId=VSP_004518.
VAR_SEQ 346 386 Missing (in isoform 2 and isoform 4).
{ECO:0000303|PubMed:10704453}.
/FTId=VSP_004519.
SEQUENCE 488 AA; 55978 MW; B2975012EF0FDF56 CRC64;
MSVTYDDSVG VEVSSDSFWE VGNYKRTVKR IDDGHRLCGD LMNCLHERAR IEKAYAQQLT
EWARRWRQLV EKGPQYGTVE KAWMAVMSEA ERVSELHLEV KASLMNEDFE KIKNWQKEAF
HKQMMGGFKE TKEAEDGFRK AQKPWAKKLK EVDAAKKAHH TACKEEKLAV SREANSKADP
SLNPEQLKKL QDKIEKCKQD VLKTKDKYEK ALKELDQTTP QYMENMEQVF EQCQQFEEKR
LRFFREVLLE VQKHLDLSNV ASYKGIYREL EQSIKAADAV EDLRWFRANH GPGMAMNWPQ
FEDEEWSADL NRTLSRREKK KAADGVTLTG INQTGDQSGQ NKPSSNLSVP SNPAQSTQLQ
SSYNPFEDED DTGSSVSEKE DIKAKNVSSY EKTQNYPADW SDDESNNPFS STDANGDSNP
FDEDTTSGTE VRVRALYDYE GQEHDELSFK AGDELTKIED EDEQGWCKGR LDSGQVGLYP
ANYVEAIQ


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