ID A0A1V8UAN8_9PEZI Unreviewed; 182 AA.
AC A0A1V8UAN8;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Sorting nexin-3 {ECO:0000256|ARBA:ARBA00020436};
GN ORFNames=B0A51_10028 {ECO:0000313|EMBL:OQO20581.1};
OS Rachicladosporium sp. CCFEE 5018.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX NCBI_TaxID=1974281 {ECO:0000313|EMBL:OQO20581.1, ECO:0000313|Proteomes:UP000192386};
RN [1] {ECO:0000313|Proteomes:UP000192386}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCFEE 5018 {ECO:0000313|Proteomes:UP000192386};
RA Coleine C., Masonjones S., Stajich J.E.;
RT "Genomes of endolithic fungi from Antarctica.";
RL Submitted (MAR-2017) 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:OQO20581.1}.
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DR EMBL; NAEU01000636; OQO20581.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V8UAN8; -.
DR STRING; 1974281.A0A1V8UAN8; -.
DR Proteomes; UP000192386; Unassembled WGS sequence.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
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 Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000192386}.
FT DOMAIN 61..178
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 182 AA; 20570 MW; 51F2B94E50A4F7D9 CRC64;
MQRIEPRPEA QASPSQGYSN GTEGANGRGQ APVPTGFAST GANPHTQSFE EIYGVPENFL
EIEVIDPQTH QPTASPSSRY TTYLIRLSTN IPAFKLRRSE VRRRYSDFEV FRDLLERESA
RVSIPPLPGK VYLNRFDDAV IEERRRGLER FLRIVAGHPL LQTGSRVLGG FVQDPAWDRN
SW
//
