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Database: UniProt
Entry: F4RR89_MELLP
LinkDB: F4RR89_MELLP
Original site: F4RR89_MELLP 
ID   F4RR89_MELLP            Unreviewed;       178 AA.
AC   F4RR89;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=Sorting nexin-3 {ECO:0000256|ARBA:ARBA00020436};
GN   ORFNames=MELLADRAFT_36961 {ECO:0000313|EMBL:EGG05194.1};
OS   Melampsora larici-populina (strain 98AG31 / pathotype 3-4-7) (Poplar leaf
OS   rust fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Pucciniomycetes; Pucciniales; Melampsoraceae; Melampsora.
OX   NCBI_TaxID=747676 {ECO:0000313|Proteomes:UP000001072};
RN   [1] {ECO:0000313|Proteomes:UP000001072}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=98AG31 / pathotype 3-4-7 {ECO:0000313|Proteomes:UP000001072};
RX   PubMed=21536894; DOI=10.1073/pnas.1019315108;
RA   Duplessis S., Cuomo C.A., Lin Y.-C., Aerts A., Tisserant E.,
RA   Veneault-Fourrey C., Joly D.L., Hacquard S., Amselem J., Cantarel B.L.,
RA   Chiu R., Coutinho P.M., Feau N., Field M., Frey P., Gelhaye E.,
RA   Goldberg J., Grabherr M.G., Kodira C.D., Kohler A., Kuees U.,
RA   Lindquist E.A., Lucas S.M., Mago R., Mauceli E., Morin E., Murat C.,
RA   Pangilinan J.L., Park R., Pearson M., Quesneville H., Rouhier N.,
RA   Sakthikumar S., Salamov A.A., Schmutz J., Selles B., Shapiro H.,
RA   Tanguay P., Tuskan G.A., Henrissat B., Van de Peer Y., Rouze P.,
RA   Ellis J.G., Dodds P.N., Schein J.E., Zhong S., Hamelin R.C.,
RA   Grigoriev I.V., Szabo L.J., Martin F.;
RT   "Obligate biotrophy features unraveled by the genomic analysis of rust
RT   fungi.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:9166-9171(2011).
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; GL883114; EGG05194.1; -; Genomic_DNA.
DR   RefSeq; XP_007411559.1; XM_007411497.1.
DR   AlphaFoldDB; F4RR89; -.
DR   STRING; 747676.F4RR89; -.
DR   EnsemblFungi; EGG05194; EGG05194; MELLADRAFT_36961.
DR   GeneID; 18927597; -.
DR   KEGG; mlr:MELLADRAFT_36961; -.
DR   VEuPathDB; FungiDB:MELLADRAFT_36961; -.
DR   eggNOG; KOG2527; Eukaryota.
DR   HOGENOM; CLU_057172_2_1_1; -.
DR   InParanoid; F4RR89; -.
DR   OrthoDB; 5475877at2759; -.
DR   Proteomes; UP000001072; 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:UP000001072}.
FT   DOMAIN          57..174
FT                   /note="PX"
FT                   /evidence="ECO:0000259|PROSITE:PS50195"
FT   REGION          17..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..42
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   178 AA;  20392 MW;  429C3196028EBD23 CRC64;
     MFAPSSSSYN YSFLTNPASQ TSSLPQNGHQ SNRQSAHGGN GPRTVQTLDE MYAVPENYLE
     IEVRHPVTHD NVRKPYTDYE ITCRTNIPAF KVKSSSVRRR YSDFEAFRDI LERESTRVNI
     PSLPGKVFTN RFSDEVIETR REGLERFLQI VAGHPLLQTG SKVLCAFLQD PQWNAHNW
//
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