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 24-JAN-2024, entry version 132. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 STRING; 9031.ENSGALP00000022861; -. DR GeneID; 395975; -. DR KEGG; gga:395975; -. DR CTD; 11252; -. DR VEuPathDB; HostDB:geneid_395975; -. DR eggNOG; KOG2856; Eukaryota. DR InParanoid; O13154; -. DR PhylomeDB; O13154; -. DR PRO; PR:O13154; -. DR Proteomes; UP000000539; Unassembled WGS sequence. 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; Arfaptin homology (AH) domain/BAR domain; 1. DR Gene3D; 2.30.30.40; SH3 Domains; 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; IPR037453; PACSIN2_F-BAR. DR InterPro; IPR036028; SH3-like_dom_sf. DR InterPro; IPR001452; SH3_domain. DR PANTHER; PTHR23065; PROLINE-SERINE-THREONINE PHOSPHATASE INTERACTING PROTEIN 1; 1. DR PANTHER; PTHR23065:SF14; PROTEIN KINASE C AND CASEIN KINASE SUBSTRATE IN NEURONS PROTEIN 2; 1. 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; BAR/IMD domain-like; 1. DR SUPFAM; SSF50044; SH3-domain; 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 //