ID A0A3B3HKH9_ORYLA Unreviewed; 442 AA.
AC A0A3B3HKH9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 18-JUN-2025, entry version 32.
DE SubName: Full=Protein kinase C and casein kinase substrate in neurons 3 {ECO:0000313|Ensembl:ENSORLP00000032254.1};
GN Name=pacsin3 {ECO:0000313|Ensembl:ENSORLP00000032254.1};
OS Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000032254.1, ECO:0000313|Proteomes:UP000001038};
RN [1] {ECO:0000313|Ensembl:ENSORLP00000032254.1, ECO:0000313|Proteomes:UP000001038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000032254.1,
RC ECO:0000313|Proteomes:UP000001038};
RX PubMed=17554307; DOI=10.1038/nature05846;
RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T.,
RA Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A.,
RA Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S.,
RA Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S.,
RA Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K.,
RA Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.;
RT "The medaka draft genome and insights into vertebrate genome evolution.";
RL Nature 447:714-719(2007).
RN [2] {ECO:0000313|Ensembl:ENSORLP00000032254.1}
RP IDENTIFICATION.
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000032254.1};
RG Ensembl;
RL Submitted (MAR-2025) to UniProtKB.
CC -!- FUNCTION: Plays a role in endocytosis and regulates internalization of
CC plasma membrane proteins. Overexpression impairs internalization of
CC SLC2A1/GLUT1 and TRPV4 and increases the levels of SLC2A1/GLUT1 and
CC TRPV4 at the cell membrane. Inhibits the TRPV4 calcium channel
CC activity. {ECO:0000256|ARBA:ARBA00055545}.
CC -!- SUBUNIT: Homodimer. May form heterooligomers with other PACSINs.
CC Interacts (via SH3 domain) with DNM1, SYNJ1 and WASL. Interacts with
CC TRPV4. {ECO:0000256|ARBA:ARBA00064966}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004413};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413};
CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}. Cytoplasm
CC {ECO:0000256|ARBA:ARBA00004496}.
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DR RefSeq; XP_023807174.1; XM_023951406.1.
DR RefSeq; XP_023807180.1; XM_023951412.1.
DR RefSeq; XP_023807188.1; XM_023951420.1.
DR AlphaFoldDB; A0A3B3HKH9; -.
DR STRING; 8090.ENSORLP00000032254; -.
DR Ensembl; ENSORLT00000030782.1; ENSORLP00000032254.1; ENSORLG00000019702.2.
DR GeneID; 101167672; -.
DR GeneTree; ENSGT00950000182973; -.
DR InParanoid; A0A3B3HKH9; -.
DR OrthoDB; 10255128at2759; -.
DR Proteomes; UP000001038; Chromosome 3.
DR Bgee; ENSORLG00000019702; Expressed in liver and 13 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR GO; GO:0007010; P:cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0060034; P:notochord cell differentiation; IEA:Ensembl.
DR GO; GO:0014028; P:notochord formation; IEA:Ensembl.
DR GO; GO:0097320; P:plasma membrane tubulation; IBA:GO_Central.
DR GO; GO:0030100; P:regulation of endocytosis; IBA:GO_Central.
DR FunFam; 2.30.30.40:FF:000014; Kinase C and casein kinase substrate in neurons protein; 1.
DR FunFam; 1.20.1270.60:FF:000009; Protein kinase C and casein kinase substrate in neurons 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; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR23065; PROLINE-SERINE-THREONINE PHOSPHATASE INTERACTING PROTEIN 1; 1.
DR PANTHER; PTHR23065:SF18; PROTEIN KINASE C AND CASEIN KINASE SUBSTRATE IN NEURONS PROTEIN 3; 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 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|PROSITE-
KW ProRule:PRU01077}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Membrane {ECO:0000256|ARBA:ARBA00022475};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001038};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 10..280
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 381..442
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 158..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 442 AA; 50485 MW; 48AAEA07DBCF68B3 CRC64;
MSSNGDLGSL GSSDSFWEPG NYKRTVKRID DGHRLCSELI SCFQERAKIE KSYSLQLSDW
AKRWRGIVEK GPQYGTLEKA WHAFMQAADS LSELHMELRQ RLAVEDSEKV RSWQKDAFHK
QLMGGLRETK EADDGFRKAQ KPWVRKLKEV ESSKKSYHQA KKEEWTAANR ETHAKADPSK
SQEEVRKFTN RTERCSQEAE KAKERYLKCL EELNRCNPRY MEDMEQVFDL TQEAERKRLR
FFKEALLDIH THLDLSAKES FKGLYRDLGQ TIRAANDSED LRWWRNTHGP GMSMGWPQFE
EWTPEASRSI SRKERGRLSE DNVVTLTNIV SSGGVEAPPS PITVDTGRVK DYSSDWSDDE
SPKKAGAVNG VGEFDPDEGR TEGVPVRALY DYTGQEADEL SFKAGEQLLK LGEEDEQGWC
KGQLSSGQVG LYPANYVQAA SS
//
