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Protein kinase C and casein kinase substrate in neurons protein 2 (x-PACSIN2)

 PACN2_XENLA             Reviewed;         477 AA.
Q9DDA9; Q6GR55;
13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
10-MAY-2017, entry version 88.
RecName: Full=Protein kinase C and casein kinase substrate in neurons protein 2;
Short=x-PACSIN2;
Name=pacsin2;
Xenopus laevis (African clawed frog).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
Xenopus.
NCBI_TaxID=8355;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=11076687; DOI=10.1006/dbio.2000.9871;
Cousin H., Gaultier A., Bleux C., Darribere T., Alfandari D.;
"PACSIN2 is a regulator of the metalloprotease/disintegrin ADAM13.";
Dev. Biol. 227:197-210(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Embryo;
NIH - Xenopus Gene Collection (XGC) project;
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
-!- 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 and thereby
may play a role in caveola-mediated endocytosis. May regulate
adam13 activity by influencing either its subcellular localization
or its catalytic activity. {ECO:0000269|PubMed:11076687}.
-!- SUBUNIT: Interacts with adam13 through the SH3 domains.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11076687}.
Cytoplasmic vesicle {ECO:0000269|PubMed:11076687}. Cell
projection, ruffle membrane {ECO:0000269|PubMed:11076687}.
Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}.
Cytoplasmic vesicle membrane {ECO:0000250}; Peripheral membrane
protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Early
endosome {ECO:0000250}. Recycling endosome membrane {ECO:0000250}.
Cell projection, ruffle membrane {ECO:0000250}; Peripheral
membrane protein {ECO:0000250}; Cytoplasmic side {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. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Ubiquitously expressed with higher expression
in the ectoderm, the neuroectoderm, and dorsal mesoderm layers.
{ECO:0000269|PubMed:11076687}.
-!- DEVELOPMENTAL STAGE: Expressed in two-cell stage, early blastula,
early gastrula, early neurula and early and late tail bud stages.
-!- 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).
{ECO:0000250}.
-!- PTM: Phosphorylated. {ECO:0000250}.
-!- SIMILARITY: Belongs to the PACSIN family. {ECO:0000305}.
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EMBL; AJ277159; CAC17814.1; -; mRNA.
EMBL; BC071076; AAH71076.1; -; mRNA.
RefSeq; NP_001081950.1; NM_001088481.1.
UniGene; Xl.52492; -.
ProteinModelPortal; Q9DDA9; -.
SMR; Q9DDA9; -.
GeneID; 398138; -.
KEGG; xla:398138; -.
CTD; 398138; -.
Xenbase; XB-GENE-489582; pacsin2.
HOVERGEN; HBG053486; -.
KO; K20123; -.
GO; GO:0005901; C:caveola; IEA:UniProtKB-SubCell.
GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
GO; GO:0070300; F:phosphatidic acid binding; ISS:UniProtKB.
GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
GO; GO:0070836; P:caveola assembly; IEA:InterPro.
GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
GO; GO:0097320; P:plasma membrane tubulation; IEA:InterPro.
InterPro; IPR027267; AH/BAR-dom.
InterPro; IPR031160; F_BAR.
InterPro; IPR001060; FCH_dom.
InterPro; IPR028521; PACSIN2.
InterPro; IPR001452; SH3_domain.
PANTHER; PTHR23065:SF28; PTHR23065:SF28; 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.
2: Evidence at transcript level;
Cell membrane; Cell projection; Coiled coil; Cytoplasm;
Cytoplasmic vesicle; Cytoskeleton; Endocytosis; Endosome;
Lipid-binding; Membrane; Phosphoprotein; SH3 domain.
CHAIN 1 477 Protein kinase C and casein kinase
substrate in neurons protein 2.
/FTId=PRO_0000161799.
DOMAIN 11 282 F-BAR. {ECO:0000255|PROSITE-
ProRule:PRU01077}.
DOMAIN 417 477 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
COILED 25 274 {ECO:0000250}.
MOTIF 356 358 NPF1.
MOTIF 396 398 NPF2.
MOTIF 408 410 NPF3.
SEQUENCE 477 AA; 55148 MW; FA6D187769EF93B3 CRC64;
MSGTYDDSVG VEVSSDSFWE VGNYKRTVKR IDDGHRLCND LMNCIHERAR IEKVYAQQLT
EWAKRWKQLV ERGPQYGTVE KAWHNLMTEA EKVSELHLEV KNALMNEDFE KIKNWQKEAF
HKQMMGGFKE TKEADDGFRK AQKPWAKKLK EVEAAKKSYH AACKEEKLAT SRETNSKADP
AMNPEQLKKL QDKVEKSKQD SQKTKEKYEK SLKDLDGTTP QYMENMEQVF EQCQQFEDKR
LSFFREVLLE VEKHLDLSNV ESYASIYREL EYAIKSADAM EDLKWFRNNH GPGMSMNWPQ
FEDWSADLNR TLSRREKKKP TDGVTLTGIS QSGEQSSIQN QHSSHLSVQS AQSTNNPFED
EEETVSINET ENKKIENVGS YEKTHPAEWS DDESNNPFNP SDTNGDNNPF DEDALTTLEV
RVRALYDYDG QELDELSFKA GEELTKIEDE DEQGWCKGRL EGGQVGLYPA NYVESVQ


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