PACN2_XENLA
ID PACN2_XENLA Reviewed; 477 AA.
AC Q9DDA9; Q6GR55;
DT 13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Protein kinase C and casein kinase substrate in neurons protein 2;
DE Short=x-PACSIN2;
GN Name=pacsin2;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=11076687; DOI=10.1006/dbio.2000.9871;
RA Cousin H., Gaultier A., Bleux C., Darribere T., Alfandari D.;
RT "PACSIN2 is a regulator of the metalloprotease/disintegrin ADAM13.";
RL Dev. Biol. 227:197-210(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
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|UniProtKB:Q9WVE8,
CC ECO:0000269|PubMed:11076687}.
CC -!- SUBUNIT: Interacts with adam13 through the SH3 domains.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11076687}.
CC Cytoplasmic vesicle {ECO:0000269|PubMed:11076687}. Cell projection,
CC ruffle membrane {ECO:0000269|PubMed:11076687}. Cytoplasm {ECO:0000250}.
CC Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasmic vesicle 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 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|UniProtKB:Q9UNF0}. Membrane, caveola
CC {ECO:0000250|UniProtKB:Q9UNF0}. Note=Detected at the neck of flask-
CC shaped caveolae. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with higher expression in
CC the ectoderm, the neuroectoderm, and dorsal mesoderm layers.
CC {ECO:0000269|PubMed:11076687}.
CC -!- DEVELOPMENTAL STAGE: Expressed in two-cell stage, early blastula, early
CC gastrula, early neurula and early and late tail bud stages.
CC -!- DOMAIN: The F-BAR domain forms a coiled coil and mediates membrane-
CC binding and membrane tubulation (By similarity). Autoinhibition of
CC these functions is mediated by an interaction between the SH3 and F-BAR
CC domains (By similarity). The F-Bar domain also mediates the binding to
CC the cell actin cytoskeleton through the interaction with CAV-1 (By
CC similarity). {ECO:0000250|UniProtKB:Q9UNF0,
CC ECO:0000250|UniProtKB:Q9WVE8}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PACSIN family. {ECO:0000305}.
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DR EMBL; AJ277159; CAC17814.1; -; mRNA.
DR EMBL; BC071076; AAH71076.1; -; mRNA.
DR RefSeq; NP_001081950.1; NM_001088481.1.
DR AlphaFoldDB; Q9DDA9; -.
DR SMR; Q9DDA9; -.
DR GeneID; 398138; -.
DR KEGG; xla:398138; -.
DR CTD; 398138; -.
DR Xenbase; XB-GENE-489582; pacsin2.S.
DR OrthoDB; 727724at2759; -.
DR Proteomes; UP000186698; Chromosome 3S.
DR GO; GO:0005901; C:caveola; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070300; F:phosphatidic acid binding; ISS:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR GO; GO:0070836; P:caveola assembly; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0097320; P:plasma membrane tubulation; IEA:InterPro.
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 2: Evidence at transcript level;
KW Cell membrane; Cell projection; Coiled coil; Cytoplasm;
KW Cytoplasmic vesicle; Cytoskeleton; Endocytosis; Endosome; Lipid-binding;
KW Membrane; Phosphoprotein; Reference proteome; SH3 domain.
FT CHAIN 1..477
FT /note="Protein kinase C and casein kinase substrate in
FT neurons protein 2"
FT /id="PRO_0000161799"
FT DOMAIN 11..282
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 417..477
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 163..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 25..274
FT /evidence="ECO:0000250"
FT MOTIF 356..358
FT /note="NPF1"
FT MOTIF 396..398
FT /note="NPF2"
FT MOTIF 408..410
FT /note="NPF3"
FT COMPBIAS 186..214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..390
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ 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
