ID E3RK63_PYRTT Unreviewed; 142 AA.
AC E3RK63;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Sorting nexin-3 {ECO:0000256|ARBA:ARBA00020436};
GN ORFNames=PTT_08599 {ECO:0000313|EMBL:EFQ93865.1};
OS Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus)
OS (Drechslera teres f. teres).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=861557 {ECO:0000313|Proteomes:UP000001067};
RN [1] {ECO:0000313|EMBL:EFQ93865.1, ECO:0000313|Proteomes:UP000001067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0-1 {ECO:0000313|EMBL:EFQ93865.1,
RC ECO:0000313|Proteomes:UP000001067};
RX PubMed=21067574; DOI=10.1186/gb-2010-11-11-r109;
RA Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F., Moffat C.S.,
RA Oliver R.P., Friesen T.L.;
RT "A first genome assembly of the barley fungal pathogen Pyrenophora teres f.
RT teres.";
RL Genome Biol. 11:R109.1-R109.14(2010).
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}.
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DR EMBL; GL533599; EFQ93865.1; -; Genomic_DNA.
DR RefSeq; XP_003298018.1; XM_003297970.1.
DR AlphaFoldDB; E3RK63; -.
DR STRING; 861557.E3RK63; -.
DR EnsemblFungi; EFQ93865; EFQ93865; PTT_08599.
DR KEGG; pte:PTT_08599; -.
DR eggNOG; KOG2527; Eukaryota.
DR HOGENOM; CLU_057172_2_1_1; -.
DR OrthoDB; 5475877at2759; -.
DR Proteomes; UP000001067; 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:UP000001067}.
FT DOMAIN 21..138
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
SQ SEQUENCE 142 AA; 16487 MW; 5A601A98BDE5DF86 CRC64;
MQSLPDARSQ SFEELYGPPE NFLEIEVRNP MTHGVGRGMY TTYEIVMRTN IPAFKLKSST
VRRRYSEFEA FRDILERESA RVTIPPLPGK VLTNRFSDDV IEHRREGLQR FLQIVVGHPL
LQTGSKVLAA FVQDPNWDRH AW
//
