SNX4_MAGO7
ID SNX4_MAGO7 Reviewed; 495 AA.
AC Q522W5; A4QRA1; G4N719;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Sorting nexin-4;
DE AltName: Full=Autophagy-related protein 24;
GN Name=SNX4; Synonyms=ATG24; ORFNames=MGG_03638;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(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; CM001234; EHA49932.1; -; Genomic_DNA.
DR RefSeq; XP_003716251.1; XM_003716203.1.
DR AlphaFoldDB; Q522W5; -.
DR SMR; Q522W5; -.
DR STRING; 318829.MGG_03638T0; -.
DR EnsemblFungi; MGG_03638T0; MGG_03638T0; MGG_03638.
DR GeneID; 2676514; -.
DR KEGG; mgr:MGG_03638; -.
DR VEuPathDB; FungiDB:MGG_03638; -.
DR eggNOG; KOG2273; Eukaryota.
DR HOGENOM; CLU_027221_2_0_1; -.
DR InParanoid; Q522W5; -.
DR OMA; FIWLRQK; -.
DR OrthoDB; 990775at2759; -.
DR PHI-base; PHI:2086; -.
DR Proteomes; UP000009058; Chromosome 4.
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; SSF103657; SSF103657; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50195; PX; 1.
PE 3: Inferred from homology;
KW Autophagy; Coiled coil; Cytoplasm; Endosome; Lipid-binding; Membrane;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..495
FT /note="Sorting nexin-4"
FT /id="PRO_0000213814"
FT DOMAIN 62..184
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT REGION 20..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 406..443
FT /evidence="ECO:0000255"
FT COMPBIAS 20..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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|UniProtKB:Q3UR97"
FT BINDING 107
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 131
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 150
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 495 AA; 55155 MW; 0397210E0DBE02B1 CRC64;
MGGIDQDNFS NISWQSDRLG AGSSAAHQHG GQESEQPTHN QAEPEPNYTS MIVHGMGLGD
EVLECNVSSP LKENDGTKDA FVSYLVTTHT TFADFQKPDA SVRRRFTDFV FLFKTLSREY
PASAVPPLPD KQRMEYVRGD RFGNDFTSRR AYSLRRFLAR CALHPVLRRS AILHTFLESP
DWNATMRSRA SRSVSMSGTS SGESGNAHYG GGSAGGGSTG GGNSLANSVF DNFADTFINA
FTKVHKPDRR FIEVREKSDK LDEDLAHVEK VVARVSRRET DMEADHKDLA EQFQKLIVLE
PGVEGPVRAF AASVEDTAQG LRGLREATEQ DYLGSLRDLA AYSGALKNLL KAREQKQLDF
EQLTEYLNKS SAERDVLASG GYSSGGALAG AGGFIRSKIE DVRGVDHEQS RRERLRKLEL
RIEELTVEVE RAKKTSELFD EEVIREVSDF ERIKRIELKR QFGSLAQSHT DFYDATIDVW
EKYVKEMEKE GAVAA
