ID   SNX3_CRYNB              Reviewed;         144 AA.
AC   P0CR61; Q55QY4; Q5KF84;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=Sorting nexin-3;
GN   Name=SNX3; OrderedLocusNames=CNBF2050;
OS   Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS   (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=283643;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-3501A;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
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)) (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus membrane
CC       {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic
CC       side {ECO:0000305}. Prevacuolar compartment membrane {ECO:0000305};
CC       Peripheral membrane protein {ECO:0000305}; Cytoplasmic side
CC       {ECO:0000305}.
CC   -!- DOMAIN: The PX domain binds phosphatidylinositol 3-phosphate which is
CC       necessary for peripheral membrane localization. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
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DR   EMBL; AAEY01000030; EAL20395.1; -; Genomic_DNA.
DR   RefSeq; XP_775042.1; XM_769949.1.
DR   AlphaFoldDB; P0CR61; -.
DR   SMR; P0CR61; -.
DR   EnsemblFungi; EAL20395; EAL20395; CNBF2050.
DR   GeneID; 4936757; -.
DR   KEGG; cnb:CNBF2050; -.
DR   VEuPathDB; FungiDB:CNBF2050; -.
DR   HOGENOM; CLU_057172_2_2_1; -.
DR   Proteomes; UP000001435; Chromosome 6.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   CDD; cd07295; PX_Grd19; 1.
DR   Gene3D; 3.30.1520.10; -; 1.
DR   InterPro; IPR001683; PX_dom.
DR   InterPro; IPR036871; PX_dom_sf.
DR   InterPro; IPR042138; PX_Grd19_PX.
DR   Pfam; PF00787; PX; 1.
DR   SMART; SM00312; PX; 1.
DR   SUPFAM; SSF64268; SSF64268; 1.
DR   PROSITE; PS50195; PX; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Golgi apparatus; Lipid-binding; Membrane; Protein transport;
KW   Transport.
FT   CHAIN           1..144
FT                   /note="Sorting nexin-3"
FT                   /id="PRO_0000410292"
FT   DOMAIN          20..139
FT                   /note="PX"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT   BINDING         63
FT                   /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT                   inositol-3-phosphate)"
FT                   /ligand_id="ChEBI:CHEBI:58088"
FT                   /evidence="ECO:0000250"
FT   BINDING         65
FT                   /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT                   inositol-3-phosphate)"
FT                   /ligand_id="ChEBI:CHEBI:58088"
FT                   /evidence="ECO:0000250"
FT   BINDING         89
FT                   /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT                   inositol-3-phosphate)"
FT                   /ligand_id="ChEBI:CHEBI:58088"
FT                   /evidence="ECO:0000250"
FT   BINDING         96
FT                   /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT                   inositol-3-phosphate)"
FT                   /ligand_id="ChEBI:CHEBI:58088"
FT                   /evidence="ECO:0000250"
FT   BINDING         105
FT                   /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT                   inositol-3-phosphate)"
FT                   /ligand_id="ChEBI:CHEBI:58088"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   144 AA;  16894 MW;  631ACB6F8DFCDB0D CRC64;
     MARMAGRPQT FDEMYSVPES FLEIEIRNPM THGIGRKMYT DYEIVCMTNI PAFKLRHSAV
     RRRYSDFEAF RDILERESTR VNIPPLPGKV RVFTNRFSDE VIEQRREGLQ RFLEIVAGHP
     LLQTGSKVLC AFLQDPAWDK SQWI