ID F9FAQ9_FUSOF Unreviewed; 170 AA.
AC F9FAQ9;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Sorting nexin-3 {ECO:0000256|ARBA:ARBA00020436};
GN ORFNames=FOXB_03485 {ECO:0000313|EMBL:EGU85976.1};
OS Fusarium oxysporum (strain Fo5176) (Fusarium vascular wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=660025 {ECO:0000313|EMBL:EGU85976.1};
RN [1] {ECO:0000313|EMBL:EGU85976.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fo5176 {ECO:0000313|EMBL:EGU85976.1};
RX PubMed=21942452; DOI=10.1094/mpmi-08-11-0212;
RA Thatcher L.F., Gardiner D.M., Kazan K., Manners J.;
RT "A highly conserved effector in Fusarium oxysporum is required for full
RT virulence on Arabidopsis.";
RL Mol. Plant Microbe Interact. 25:180-190(2012).
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:EGU85976.1}.
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DR EMBL; AFQF01001210; EGU85976.1; -; Genomic_DNA.
DR AlphaFoldDB; F9FAQ9; -.
DR STRING; 660025.F9FAQ9; -.
DR PaxDb; 5507-FOXG_03665P0; -.
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}.
FT DOMAIN 42..159
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 170 AA; 19247 MW; C2B0594FA89D0C2B CRC64;
MASDQDNSGL DAPGSQFHRP ILQSMPDTRQ QSFDEIYGPP ENFLEIEVRN PRTHGMGRHM
YTDYEILCRT NIPAFKLRQS SVRRRYSDFE YFRDILERES ARVTIPPLPG KVFTNRFSDD
VIEGRRAGLE KFLKIVVGHP LLQTGSKVLA AFVQESQTLT GIATLGDASA
//
