ID   SNX4_PICPA              Reviewed;         661 AA.
AC   Q5H7C3;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Sorting nexin-4;
DE   AltName: Full=Autophagy-related protein 24 {ECO:0000303|PubMed:15563611};
DE   AltName: Full=Pexophagy zeocin-resistant mutant protein 16;
GN   Name=SNX4; Synonyms=ATG24 {ECO:0000303|PubMed:15563611}, PAZ16;
OS   Komagataella pastoris (Yeast) (Pichia pastoris).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Komagataella.
OX   NCBI_TaxID=4922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=PPY12;
RX   PubMed=15563611; DOI=10.1091/mbc.e04-09-0842;
RA   Ano Y., Hattori T., Oku M., Mukaiyama H., Baba M., Ohsumi Y., Kato N.,
RA   Sakai Y.;
RT   "A sorting nexin PpAtg24 regulates vacuolar membrane dynamics during
RT   pexophagy via binding to phosphatidylinositol-3-phosphate.";
RL   Mol. Biol. Cell 16:446-457(2005).
CC   -!- FUNCTION: Required for glucose-induced micropexophagy and ethanol-
CC       induced macropexophagy (PubMed:15563611). Involved in the fusion
CC       between the pexophagosome and the vacuole. Also involved in the
CC       separation or division of vacuoles throughout the entire life cycle of
CC       the cells (PubMed:15563611). {ECO:0000269|PubMed:15563611}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15563611}. Membrane
CC       {ECO:0000269|PubMed:15563611}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:15563611}. Vacuole membrane
CC       {ECO:0000269|PubMed:15563611}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:15563611}. Note=Vacuolar and other perivacuolar
CC       punctate structures.
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; AB191168; BAD89147.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5H7C3; -.
DR   SMR; Q5H7C3; -.
DR   GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IEA:UniProt.
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; Cytoplasm; Lipid-binding; Membrane; Protein transport;
KW   Transport; Vacuole.
FT   CHAIN           1..661
FT                   /note="Sorting nexin-4"
FT                   /id="PRO_0000213816"
FT   DOMAIN          77..198
FT                   /note="PX"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT   REGION          1..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          56..75
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          554..661
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..41
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        56..71
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        554..587
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         120
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         122
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         146
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         165
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   661 AA;  76908 MW;  C5F36BB077B1669C CRC64;
     MSDQFTSIQW DRTEPEGDVP GDSNDHSQVQ INSSINLIEE DQGQEQEQDD LVTTNTVVRG
     GNDSDSNPNE QIPPRDVYIR SKVSQPLKES DGQNFYISYL IETETNEPGL AKTKLKVRRR
     FSDSNFLYNC LANDFPTSII PPLPNKQRLE YIKGDRFGEY FTTKRSIALN NFLNRISKHP
     LLKQAKIYHI FLEDSVNWNT FKQNLKISSN PNSTVGGGST TSANANGELD SFSDYIMNAF
     KKPTYESENA KEFQEITDKS NKLQENINKI DKIYQRVVKR QSEISEDFRL FGDEFKKLNQ
     ILTEGSDTQF DKELSQQFTS FSENIYQISY DSFKLTRQVD LHYLTSLKDL DHYISQIKNM
     IKFKDSKLLD YEMLQNYLNK AIAEKNHLMN GNNVSGSDGA MNFISKKIGS LRGKTPGQTY
     SSGNETNDRI NKLNEKIEFL EREVKETFEL FHTFEKNLIT EYQLFDRIKN DEITTNLHEL
     SQYYLDYYNS VVNHWNDVEI PHSEHLTDEL HVLQQSQLRK NLENISIDPK LDVNSKLFEH
     DDVRLNNDHI RSDLRSIKSQ ERKNEQVHKQ DQEQGEEQEH EQDQVQNQEQ EQEPEELSRE
     EAEVLETPVQ AQEQEQQEPE ELHASQTESH TQSEPQNDNQ HNFDDDGSDE GLVDVEGLEQ
     W