ID A0A0L1IM53_ASPNO Unreviewed; 142 AA.
AC A0A0L1IM53;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Sorting nexin-3 {ECO:0000256|ARBA:ARBA00020436};
GN ORFNames=ANOM_011313 {ECO:0000313|EMBL:KNG80355.1};
OS Aspergillus nomiae NRRL 13137.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1509407 {ECO:0000313|EMBL:KNG80355.1, ECO:0000313|Proteomes:UP000037505};
RN [1] {ECO:0000313|EMBL:KNG80355.1, ECO:0000313|Proteomes:UP000037505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 13137 {ECO:0000313|EMBL:KNG80355.1,
RC ECO:0000313|Proteomes:UP000037505};
RA Moore M.G., Shannon B.M., Brian M.M.;
RT "The Genome of the Aflatoxigenic Filamentous Fungus Aspergillus nomius.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for retention of late Golgi membrane proteins.
CC Component of the retrieval machinery that functions by direct
CC interaction with the cytosolic tails of certain TGN membrane proteins
CC during the sorting/budding process at the prevacuolar compartment.
CC Binds phosphatidylinositol 3-phosphate (PtdIns(P3)).
CC {ECO:0000256|ARBA:ARBA00025533}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004287};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004287};
CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004287}. Prevacuolar
CC compartment membrane {ECO:0000256|ARBA:ARBA00004179}; Peripheral
CC membrane protein {ECO:0000256|ARBA:ARBA00004179}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004179}.
CC -!- SIMILARITY: Belongs to the sorting nexin family.
CC {ECO:0000256|ARBA:ARBA00010883}.
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:KNG80355.1}.
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; JNOM01000626; KNG80355.1; -; Genomic_DNA.
DR RefSeq; XP_015401278.1; XM_015556569.1.
DR AlphaFoldDB; A0A0L1IM53; -.
DR SMR; A0A0L1IM53; -.
DR STRING; 1509407.A0A0L1IM53; -.
DR GeneID; 26813117; -.
DR OrthoDB; 5475877at2759; -.
DR Proteomes; UP000037505; Unassembled WGS sequence.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IEA:InterPro.
DR CDD; cd07295; PX_Grd19; 1.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR042138; PX_Grd19_PX.
DR PANTHER; PTHR45963; RE52028P; 1.
DR PANTHER; PTHR45963:SF2; SORTING NEXIN-12; 1.
DR Pfam; PF00787; PX; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR PROSITE; PS50195; PX; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000037505}.
FT DOMAIN 21..138
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
SQ SEQUENCE 142 AA; 16755 MW; 4FD08197D77FD2EC CRC64;
MQAVPESRQQ TFEEIYGPPE NFLEIEVRNP QTHGTSRNMY TSYEIVCRTN IPAFKLKHSV
VRRRYSDFEY FRDILEREST RVTIPPLPGK VFTNRFSDDV IEHRREGLQR FLQIVAGHPL
LQTGSKVLAS FIQDPNWDRN AW
//
