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Protein kinase C and casein kinase substrate in neurons protein 2 (Focal adhesion protein of 52 kDa) (FAP52)

 PACN2_CHICK             Reviewed;         448 AA.
O13154;
13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
01-JUL-1997, sequence version 1.
10-MAY-2017, entry version 108.
RecName: Full=Protein kinase C and casein kinase substrate in neurons protein 2;
AltName: Full=Focal adhesion protein of 52 kDa;
Short=FAP52;
Name=PACSIN2;
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031;
[1]
NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, PHOSPHORYLATION, AND
TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=9287337; DOI=10.1074/jbc.272.37.23278;
Merilaeinen J., Lehto V.-P., Wasenius V.-M.;
"FAP52, a novel, SH3 domain-containing focal adhesion protein.";
J. Biol. Chem. 272:23278-23284(1997).
-!- 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 (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell junction, focal adhesion
{ECO:0000269|PubMed:9287337}. 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: Detected in intestine, cardiac muscle, lung
and brain (at protein level). Expressed in all tissues tested,
including, gizzard, liver, cardiac muscle, skeletal muscle and
skin. {ECO:0000269|PubMed:9287337}.
-!- 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 on serine residues.
{ECO:0000269|PubMed:9287337}.
-!- SIMILARITY: Belongs to the PACSIN family. {ECO:0000305}.
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EMBL; Z50798; CAA90678.1; -; mRNA.
RefSeq; NP_001152983.1; NM_001159511.1.
RefSeq; NP_990420.1; NM_205089.1.
UniGene; Gga.3831; -.
PDB; 4BNE; X-ray; 2.57 A; A/B=1-448.
PDBsum; 4BNE; -.
ProteinModelPortal; O13154; -.
SMR; O13154; -.
PRIDE; O13154; -.
GeneID; 395975; -.
KEGG; gga:395975; -.
CTD; 11252; -.
HOGENOM; HOG000007245; -.
HOVERGEN; HBG053486; -.
InParanoid; O13154; -.
KO; K20123; -.
PhylomeDB; O13154; -.
PRO; PR:O13154; -.
Proteomes; UP000000539; Unplaced.
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:0005829; C:cytosol; ISS:AgBase.
GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
GO; GO:0005768; C:endosome; IBA:GO_Central.
GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
GO; GO:0008092; F:cytoskeletal protein binding; ISS:AgBase.
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:0045806; P:negative regulation of endocytosis; ISS:AgBase.
GO; GO:0097320; P:plasma membrane tubulation; IEA:InterPro.
GO; GO:0030100; P:regulation of endocytosis; IBA:GO_Central.
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; 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;
3D-structure; Cell junction; Cell membrane; Cell projection;
Coiled coil; Complete proteome; Cytoplasm; Cytoplasmic vesicle;
Cytoskeleton; Endocytosis; Endosome; Lipid-binding; Membrane;
Phosphoprotein; Reference proteome; SH3 domain.
CHAIN 1 448 Protein kinase C and casein kinase
substrate in neurons protein 2.
/FTId=PRO_0000161798.
DOMAIN 11 282 F-BAR. {ECO:0000255|PROSITE-
ProRule:PRU01077}.
DOMAIN 388 448 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
COILED 25 274 {ECO:0000250}.
MOTIF 367 369 NPF1.
MOTIF 379 381 NPF2.
TURN 21 24 {ECO:0000244|PDB:4BNE}.
HELIX 25 72 {ECO:0000244|PDB:4BNE}.
HELIX 77 106 {ECO:0000244|PDB:4BNE}.
HELIX 108 119 {ECO:0000244|PDB:4BNE}.
STRAND 126 128 {ECO:0000244|PDB:4BNE}.
HELIX 129 174 {ECO:0000244|PDB:4BNE}.
TURN 175 178 {ECO:0000244|PDB:4BNE}.
HELIX 184 255 {ECO:0000244|PDB:4BNE}.
TURN 257 259 {ECO:0000244|PDB:4BNE}.
HELIX 261 275 {ECO:0000244|PDB:4BNE}.
HELIX 279 290 {ECO:0000244|PDB:4BNE}.
SEQUENCE 448 AA; 51971 MW; 344218153F8698EF CRC64;
MSGSYDDSVG VEVSSDSFWE VGNYKRTVKR IDDGHRLCND LMNCIHERAR IEKVYAQQLT
EWAKRWKQLV EKGPQYGTVE RAWCAFMSEA EKVSELHLEV KGSLMNEDFE KIKNWQKEAF
HKQMMGGFKE TKEAEDGFRK AQKPWAKKLK EVEAAKKAYH AACKEEKLAI SRETNSKADP
ALNPEQLKKL QDKVERSKQD VLKTKAKYEK SLKELDNATP QYMENMEQVF EQCQQFEEKR
LRFFREVLLE VQKHLDLSNV ASYKNIYREL EQNIKTADAV EDLRWFRANQ GPGMSMNWPQ
FEDDEWSADL NRTLSRREKK KASDGVTLTG INQTGDQVSQ PNKHSSVSSY EKNQSYPTDW
SDEESNNPFS STDAKGDTNP FDEDTSPVME VRVRALYDYE GQEQDELSFK AGDELTKMEN
EDEQGWCKGR LDNGQVGLYP ANYVEPIQ


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