SNX4_CRYNB
ID SNX4_CRYNB Reviewed; 493 AA.
AC P0CR63; Q55WP9; Q5KJJ8;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Sorting nexin-4;
DE AltName: Full=Autophagy-related protein 24;
GN Name=SNX4; Synonyms=ATG24; OrderedLocusNames=CNBC0900;
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: Sorting nexin, involved in the separation or division of
CC vacuoles throughout the entire life cycle of the cells. Involved in
CC retrieval of late-Golgi SNAREs from post-Golgi endosomes to the trans-
CC Golgi network, for cytoplasm to vacuole transport (Cvt), autophagy,
CC mitophagy, and pexophagy. {ECO:0000250|UniProtKB:P47057}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P47057}. Preautophagosomal structure membrane
CC {ECO:0000250|UniProtKB:P47057}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P47057}. Endosome membrane
CC {ECO:0000250|UniProtKB:P47057}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P47057}. Note=Endosome and other perivacuolar
CC punctate structures. Associates to phosphatidylinositol 3-phosphate,
CC necessary for peripheral membrane localization to the perivacuolar
CC punctate structures. {ECO:0000250|UniProtKB:P47057}.
CC -!- DOMAIN: The PX domain binds phosphatidylinositol 3-phosphate which is
CC necessary for peripheral membrane localization to the perivacuolar
CC punctate structures. {ECO:0000250|UniProtKB:Q96L94}.
CC -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
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DR EMBL; AAEY01000013; EAL21950.1; -; Genomic_DNA.
DR RefSeq; XP_776597.1; XM_771504.1.
DR AlphaFoldDB; P0CR63; -.
DR SMR; P0CR63; -.
DR EnsemblFungi; AAW42581; AAW42581; CNC06300.
DR EnsemblFungi; EAL21950; EAL21950; CNBC0900.
DR GeneID; 4934754; -.
DR KEGG; cnb:CNBC0900; -.
DR VEuPathDB; FungiDB:CNBC0900; -.
DR HOGENOM; CLU_027221_0_0_1; -.
DR Proteomes; UP000001435; Chromosome 3.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1270.60; -; 1.
DR Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
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 Autophagy; Cytoplasm; Endosome; Lipid-binding; Membrane; Protein transport;
KW Transport.
FT CHAIN 1..493
FT /note="Sorting nexin-4"
FT /id="PRO_0000410293"
FT DOMAIN 89..211
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 132
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|UniProtKB:Q3UR97"
FT BINDING 158
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|UniProtKB:Q96L94"
FT BINDING 177
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|UniProtKB:Q6P4T1"
SQ SEQUENCE 493 AA; 56177 MW; F65645914B8DB4E4 CRC64;
MDQDGFHSIA WDDAPSSNPP LSAPSPSQSP FEEGFESISP SSAQPPASDQ YEGYDNSKAG
EAGDVGVTLD RRERLGGHEV DGSVWNGKWM DVQVREPAKE HEGSKDMYVS YAVKTETSLP
TFRKPLTVVR RRFQDFVFLR EHLVKNFPAC VVPPIPDKHR LEYIKGDRFS PEFVERRRLD
LQRFADRIAR HPVLQRSQLV NDFLQSTEWS VAKHHHISHP PPESHASLID SLSDTFINAF
SRVRKPDARF VEMTEELERF EEGLTGVERV VGRGKSRVDD LAADYQDMAA AYQGLGYLES
GITEPLNRFA EKMLDFSTLL KHMNNTTIEP FLSSSHSLLS YSATHRNVIK LRDQKQLDFE
ELSAYLSAIV SERDRLAALS SGHTAAPVGL GTYLRDQMDK LRGTDDIHTR RERMRKMDGK
IKELQDAVTL AHETSNAFSE EVIKEHAYFE LEKKQEMKDA LQAYTDGQVE MLQQAMDDWD
RIIPLLQRIR VDV
