PACN2_CHICK
ID PACN2_CHICK Reviewed; 448 AA.
AC O13154;
DT 13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Protein kinase C and casein kinase substrate in neurons protein 2;
DE AltName: Full=Focal adhesion protein of 52 kDa;
DE Short=FAP52;
GN Name=PACSIN2;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, PHOSPHORYLATION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=9287337; DOI=10.1074/jbc.272.37.23278;
RA Merilaeinen J., Lehto V.-P., Wasenius V.-M.;
RT "FAP52, a novel, SH3 domain-containing focal adhesion protein.";
RL J. Biol. Chem. 272:23278-23284(1997).
CC -!- FUNCTION: Regulates the morphogenesis and endocytosis of caveolae (By
CC similarity). 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:0000250, ECO:0000250|UniProtKB:Q9WVE8}.
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion
CC {ECO:0000269|PubMed:9287337}. Cytoplasm {ECO:0000250}. Cytoplasm,
CC cytoskeleton {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}. Early endosome {ECO:0000250}. Recycling endosome
CC membrane {ECO:0000250}. Cell projection, ruffle membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein
CC {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cell projection
CC {ECO:0000250}. Membrane, caveola {ECO:0000250}. Note=Detected at the
CC neck of flask-shaped caveolae. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in intestine, cardiac muscle, lung and
CC brain (at protein level). Expressed in all tissues tested, including,
CC gizzard, liver, cardiac muscle, skeletal muscle and skin.
CC {ECO:0000269|PubMed:9287337}.
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 on serine residues. {ECO:0000269|PubMed:9287337}.
CC -!- SIMILARITY: Belongs to the PACSIN family. {ECO:0000305}.
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DR EMBL; Z50798; CAA90678.1; -; mRNA.
DR RefSeq; NP_001152983.1; NM_001159511.1.
DR RefSeq; NP_990420.1; NM_205089.1.
DR PDB; 4BNE; X-ray; 2.57 A; A/B=1-448.
DR PDBsum; 4BNE; -.
DR AlphaFoldDB; O13154; -.
DR SMR; O13154; -.
DR GeneID; 395975; -.
DR KEGG; gga:395975; -.
DR CTD; 11252; -.
DR VEuPathDB; HostDB:geneid_395975; -.
DR eggNOG; KOG2856; Eukaryota.
DR InParanoid; O13154; -.
DR OrthoDB; 727724at2759; -.
DR PhylomeDB; O13154; -.
DR PRO; PR:O13154; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005901; C:caveola; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISS:AgBase.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008092; F:cytoskeletal protein binding; ISS:AgBase.
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; IEA:InterPro.
DR GO; GO:0007010; P:cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0045806; P:negative regulation of endocytosis; ISS:AgBase.
DR GO; GO:0097320; P:plasma membrane tubulation; IBA:GO_Central.
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; 2.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF14604; SH3_9; 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 3D-structure; Cell junction; Cell membrane; Cell projection; Coiled coil;
KW Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Endocytosis; Endosome;
KW Lipid-binding; Membrane; Phosphoprotein; Reference proteome; SH3 domain.
FT CHAIN 1..448
FT /note="Protein kinase C and casein kinase substrate in
FT neurons protein 2"
FT /id="PRO_0000161798"
FT DOMAIN 11..282
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 388..448
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 315..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 25..274
FT /evidence="ECO:0000250"
FT MOTIF 367..369
FT /note="NPF1"
FT MOTIF 379..381
FT /note="NPF2"
FT COMPBIAS 326..376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT TURN 21..24
FT /evidence="ECO:0007829|PDB:4BNE"
FT HELIX 25..72
FT /evidence="ECO:0007829|PDB:4BNE"
FT HELIX 77..106
FT /evidence="ECO:0007829|PDB:4BNE"
FT HELIX 108..119
FT /evidence="ECO:0007829|PDB:4BNE"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:4BNE"
FT HELIX 129..174
FT /evidence="ECO:0007829|PDB:4BNE"
FT TURN 175..178
FT /evidence="ECO:0007829|PDB:4BNE"
FT HELIX 184..255
FT /evidence="ECO:0007829|PDB:4BNE"
FT TURN 257..259
FT /evidence="ECO:0007829|PDB:4BNE"
FT HELIX 261..275
FT /evidence="ECO:0007829|PDB:4BNE"
FT HELIX 279..290
FT /evidence="ECO:0007829|PDB:4BNE"
SQ 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
