PACN2_RAT
ID PACN2_RAT Reviewed; 488 AA.
AC Q9QY17; Q9QY18; Q9QY19; Q9QY20;
DT 13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-2002, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Protein kinase C and casein kinase substrate in neurons 2 protein;
DE AltName: Full=Synaptic dynamin-associated protein II;
DE AltName: Full=Syndapin-2;
DE AltName: Full=Syndapin-II;
DE Short=SdpII;
GN Name=Pacsin2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), FUNCTION, INTERACTION
RP WITH DNM1; SYN1; SYNJ1 AND WASL, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=10704453; DOI=10.1083/jcb.148.5.1047;
RA Qualmann B., Kelly R.B.;
RT "Syndapin isoforms participate in receptor-mediated endocytosis and actin
RT organization.";
RL J. Cell Biol. 148:1047-1062(2000).
RN [2]
RP SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=22718246; DOI=10.1007/s00418-012-0945-0;
RA Koch D., Westermann M., Kessels M.M., Qualmann B.;
RT "Ultrastructural freeze-fracture immunolabeling identifies plasma membrane-
RT localized syndapin II as a crucial factor in shaping caveolae.";
RL Histochem. Cell Biol. 138:215-230(2012).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-401, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Regulates the morphogenesis and endocytosis of caveolae
CC (PubMed:22718246). Lipid-binding protein that is able to promote the
CC tubulation of the phosphatidic acid-containing membranes it
CC preferentially binds. Plays a role in intracellular vesicle-mediated
CC transport. Involved in the endocytosis of cell-surface receptors like
CC the EGF receptor, contributing to its internalization in the absence of
CC EGF stimulus. {ECO:0000269|PubMed:10704453,
CC ECO:0000269|PubMed:22718246}.
CC -!- SUBUNIT: Homodimer (By similarity). May form heterooligomers with other
CC PACSINs (By similarity). Interacts (via NPF motifs) with EHD1 (via EH
CC domain) (By similarity). Interacts with EHD3 (By similarity). Interacts
CC (via the SH3 domain) with MICALL1 (By similarity). Interacts with RAC1
CC (By similarity). Interacts (via SH3 domain) with DNM1, SYN1, SYNJ1 and
CC WASL (PubMed:10704453). Interacts with CAV1 (By similarity). Interacts
CC with TRPV4 (By similarity). {ECO:0000250|UniProtKB:Q9UNF0,
CC ECO:0000250|UniProtKB:Q9WVE8, ECO:0000269|PubMed:10704453}.
CC -!- INTERACTION:
CC Q9QY17; Q641Z6: Ehd1; NbExp=2; IntAct=EBI-491201, EBI-492911;
CC Q9QY17; Q5NBX1: Cobl; Xeno; NbExp=4; IntAct=EBI-491201, EBI-1550138;
CC Q9QY17; Q9EQP2: Ehd4; Xeno; NbExp=4; IntAct=EBI-491201, EBI-491022;
CC Q9QY17; Q9NZQ3: NCKIPSD; Xeno; NbExp=2; IntAct=EBI-491201, EBI-745080;
CC Q9QY17; P18545: PDE6G; Xeno; NbExp=4; IntAct=EBI-491201, EBI-2622029;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10704453}.
CC Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:10704453}; Peripheral membrane protein
CC {ECO:0000269|PubMed:10704453}; Cytoplasmic side
CC {ECO:0000269|PubMed:10704453}. Cell projection, ruffle membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}. Early endosome {ECO:0000250}. Recycling endosome
CC membrane {ECO:0000250}. Cell membrane {ECO:0000269|PubMed:22718246};
CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}. Cell projection {ECO:0000250}. Membrane, caveola
CC {ECO:0000269|PubMed:22718246}. Note=Detected at the neck of flask-
CC shaped caveolae. Localization to tubular recycling endosomes probably
CC requires interaction with MICALL1 and EHD1.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=Aa, SdpII-l;
CC IsoId=Q9QY17-1; Sequence=Displayed;
CC Name=2; Synonyms=Ab;
CC IsoId=Q9QY17-2; Sequence=VSP_004519;
CC Name=3; Synonyms=Ba;
CC IsoId=Q9QY17-3; Sequence=VSP_004518;
CC Name=4; Synonyms=Bb, SdpII-s;
CC IsoId=Q9QY17-4; Sequence=VSP_004518, VSP_004519;
CC -!- TISSUE SPECIFICITY: Widely expressed (at protein level). Isoforms 1/3
CC are predominantly expressed in heart and in PC-12 cells, a
CC pheochromocytoma cell line (at protein level). Isoforms 2/4 are widely
CC expressed with highest levels in muscle, testis and brain (at protein
CC level). {ECO:0000269|PubMed:10704453}.
CC -!- DOMAIN: The F-BAR domain forms a coiled coil and mediates membrane-
CC binding and membrane tubulation. In the autoinhibited conformation,
CC interaction with the SH3 domain inhibits membrane tubulation mediated
CC by the F-BAR domain (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated by casein kinase 2 (CK2) and protein kinase C
CC (PKC). Phosphorylation by PKC probably decreases the membrane binding
CC and tubulation capacities of PACSIN2, thereby modulating the lifetime
CC of caveolae (By similarity). {ECO:0000250|UniProtKB:Q9WVE8}.
CC -!- DISRUPTION PHENOTYPE: Reduces the density of caveolae.
CC {ECO:0000269|PubMed:22718246}.
CC -!- SIMILARITY: Belongs to the PACSIN family. {ECO:0000305}.
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DR EMBL; AF139492; AAF22211.1; -; mRNA.
DR EMBL; AF139493; AAF22212.1; -; mRNA.
DR EMBL; AF139494; AAF22213.1; -; mRNA.
DR EMBL; AF139495; AAF22214.1; -; mRNA.
DR RefSeq; NP_570096.2; NM_130740.2. [Q9QY17-3]
DR RefSeq; XP_006242112.1; XM_006242050.3. [Q9QY17-1]
DR RefSeq; XP_006242113.1; XM_006242051.2. [Q9QY17-1]
DR RefSeq; XP_006242114.1; XM_006242052.3. [Q9QY17-1]
DR RefSeq; XP_006242115.1; XM_006242053.2. [Q9QY17-1]
DR RefSeq; XP_006242117.1; XM_006242055.2. [Q9QY17-3]
DR RefSeq; XP_006242120.1; XM_006242058.2. [Q9QY17-2]
DR RefSeq; XP_006242122.1; XM_006242060.2. [Q9QY17-4]
DR RefSeq; XP_017450116.1; XM_017594627.1. [Q9QY17-1]
DR AlphaFoldDB; Q9QY17; -.
DR SMR; Q9QY17; -.
DR BioGRID; 250783; 1.
DR ELM; Q9QY17; -.
DR IntAct; Q9QY17; 6.
DR MINT; Q9QY17; -.
DR STRING; 10116.ENSRNOP00000060074; -.
DR iPTMnet; Q9QY17; -.
DR PhosphoSitePlus; Q9QY17; -.
DR jPOST; Q9QY17; -.
DR PaxDb; Q9QY17; -.
DR PRIDE; Q9QY17; -.
DR Ensembl; ENSRNOT00000013398; ENSRNOP00000013398; ENSRNOG00000009756. [Q9QY17-4]
DR Ensembl; ENSRNOT00000088125; ENSRNOP00000072822; ENSRNOG00000009756. [Q9QY17-3]
DR GeneID; 124461; -.
DR KEGG; rno:124461; -.
DR CTD; 11252; -.
DR RGD; 69411; Pacsin2.
DR VEuPathDB; HostDB:ENSRNOG00000009756; -.
DR eggNOG; KOG2856; Eukaryota.
DR GeneTree; ENSGT00950000182973; -.
DR InParanoid; Q9QY17; -.
DR OMA; MEAMAHV; -.
DR OrthoDB; 727724at2759; -.
DR PhylomeDB; Q9QY17; -.
DR Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
DR PRO; PR:Q9QY17; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000009756; Expressed in stomach and 19 other tissues.
DR ExpressionAtlas; Q9QY17; baseline and differential.
DR Genevisible; Q9QY17; RN.
DR GO; GO:0005901; C:caveola; ISO:RGD.
DR GO; GO:0005911; C:cell-cell junction; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0019898; C:extrinsic component of membrane; ISS:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0055038; C:recycling endosome membrane; ISO:RGD.
DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008092; F:cytoskeletal protein binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0008289; F:lipid binding; ISO:RGD.
DR GO; GO:0070300; F:phosphatidic acid binding; ISS:UniProtKB.
DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR GO; GO:0070836; P:caveola assembly; ISS:UniProtKB.
DR GO; GO:0072584; P:caveolin-mediated endocytosis; ISS:UniProtKB.
DR GO; GO:0048858; P:cell projection morphogenesis; ISS:UniProtKB.
DR GO; GO:0007010; P:cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:RGD.
DR GO; GO:0045806; P:negative regulation of endocytosis; ISO:RGD.
DR GO; GO:0097320; P:plasma membrane tubulation; ISS:UniProtKB.
DR GO; GO:0036010; P:protein localization to endosome; ISO:RGD.
DR GO; GO:0030100; P:regulation of endocytosis; IBA:GO_Central.
DR CDD; cd07679; F-BAR_PACSIN2; 1.
DR CDD; cd11998; SH3_PACSIN1-2; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR035743; PACSIN1/PACSIN2_SH3.
DR InterPro; IPR028521; PACSIN2.
DR InterPro; IPR037453; PACSIN2_F-BAR.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR23065:SF14; PTHR23065:SF14; 1.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell membrane; Cell projection;
KW Coiled coil; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Endocytosis;
KW Endosome; Lipid-binding; Membrane; Phosphoprotein; Reference proteome;
KW SH3 domain.
FT CHAIN 1..488
FT /note="Protein kinase C and casein kinase substrate in
FT neurons 2 protein"
FT /id="PRO_0000161797"
FT DOMAIN 11..282
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 428..488
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 163..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 25..274
FT /evidence="ECO:0000250"
FT MOTIF 364..366
FT /note="NPF1"
FT MOTIF 407..409
FT /note="NPF2"
FT MOTIF 419..421
FT /note="NPF3"
FT COMPBIAS 327..370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 53
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9WVE8"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UNF0"
FT MOD_RES 315
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:Q9WVE8"
FT MOD_RES 375
FT /note="Phosphoserine; by IKKB"
FT /evidence="ECO:0000250|UniProtKB:Q9WVE8"
FT MOD_RES 401
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 448
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UNF0"
FT VAR_SEQ 302..303
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:10704453"
FT /id="VSP_004518"
FT VAR_SEQ 346..386
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:10704453"
FT /id="VSP_004519"
SQ 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
