ID A0A7I8VX18_9ANNE Unreviewed; 475 AA.
AC A0A7I8VX18;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 18-JUN-2025, entry version 9.
DE SubName: Full=DgyrCDS9340 {ECO:0000313|EMBL:CAD5120780.1};
GN ORFNames=DGYR_LOCUS8820 {ECO:0000313|EMBL:CAD5120780.1};
OS Dimorphilus gyrociliatus.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Polychaeta;
OC Polychaeta incertae sedis; Dinophilidae; Dimorphilus.
OX NCBI_TaxID=2664684 {ECO:0000313|EMBL:CAD5120780.1, ECO:0000313|Proteomes:UP000549394};
RN [1] {ECO:0000313|EMBL:CAD5120780.1, ECO:0000313|Proteomes:UP000549394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hejnol A.;
RL Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
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:ARBA00004236}.
CC Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Endomembrane system
CC {ECO:0000256|ARBA:ARBA00004184}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004184}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CAD5120780.1}.
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DR EMBL; CAJFCJ010000013; CAD5120780.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7I8VX18; -.
DR EnsemblMetazoa; DGYR_LOCUS8820_t1; CAD5120780.1; DGYR_LOCUS8820.
DR OrthoDB; 10255128at2759; -.
DR Proteomes; UP000549394; Unassembled WGS sequence.
DR GO; GO:0005768; C:endosome; IEA:TreeGrafter.
DR GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter.
DR GO; GO:0005543; F:phospholipid binding; IEA:TreeGrafter.
DR GO; GO:0007010; P:cytoskeleton organization; IEA:TreeGrafter.
DR GO; GO:0097320; P:plasma membrane tubulation; IEA:TreeGrafter.
DR GO; GO:0030100; P:regulation of endocytosis; IEA:TreeGrafter.
DR CDD; cd07655; F-BAR_PACSIN; 1.
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:SF11; SYNDAPIN, ISOFORM C; 1.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF00018; SH3_1; 1.
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:UP000549394};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 27..297
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 417..475
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 189..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..220
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..383
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 475 AA; 54551 MW; 2E4477EBAAE25096 CRC64;
MLQVCRCWRR STPRIMSVSE DISNTGASTG DSFWELDRYK RTVKRLEDGH KLCSEMMQML
HERAELEKNY SKSLRTWASK WEDTVRKGPE YGTTEEACVG LFREAESIAE LHTEVKDKLI
SVVQTQIKAW RDEHYKKPLV GQCKQTKGLE DSFRKAQKPW AKFLTKVLKT KKDYHTAYKT
FNSAENSLNN AQADSSLSDD HKRKLSDKVE KSRREVDSNR EKYEAALREL NGYTSRYIED
MTGVFDSAQR EEKERLDFVR RALEETRNCL NLSDNDNYHN TYEMLASTIE AADSEKDLKW
WSQYHGVDMA MNWPQFEEYS PDMHSISRKD KKSVISGSDG ITITSIKPAQ NNTEYQTQTS
IPEQSTPAHT IQNQPPPAPP QQQQPPQQQQ VQPPPTQGTP FDSNEETWSS HNGTSNEKGV
KVRALYDYAA AESDEISFKV NDIFIKLEDQ DDQGWCKGLK DGVSGLYPAG YASEI
//
