ID   SNX41_ASHGO             Reviewed;         603 AA.
AC   Q759T1;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Sorting nexin-41;
GN   Name=SNX41; OrderedLocusNames=ADR192C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: May be required for cytoplasm to vacuole transport (Cvt) and
CC       pexophagy. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250}; Peripheral
CC       membrane protein {ECO:0000250}. Endomembrane system {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}. Note=Endosome and other
CC       perivacuolar punctate structures. {ECO:0000250}.
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}.
CC   -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
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DR   EMBL; AE016817; AAS52112.1; -; Genomic_DNA.
DR   RefSeq; NP_984288.1; NM_209641.1.
DR   AlphaFoldDB; Q759T1; -.
DR   STRING; 33169.AAS52112; -.
DR   EnsemblFungi; AAS52112; AAS52112; AGOS_ADR192C.
DR   GeneID; 4620450; -.
DR   KEGG; ago:AGOS_ADR192C; -.
DR   eggNOG; KOG2273; Eukaryota.
DR   HOGENOM; CLU_014456_3_0_1; -.
DR   InParanoid; Q759T1; -.
DR   OMA; WIKECLK; -.
DR   Proteomes; UP000000591; Chromosome IV.
DR   GO; GO:0010009; C:cytoplasmic side of endosome membrane; IEA:EnsemblFungi.
DR   GO; GO:0005829; C:cytosol; IEA:GOC.
DR   GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IEA:EnsemblFungi.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:EnsemblFungi.
DR   GO; GO:0042147; P:retrograde transport, endosome to Golgi; IEA:EnsemblFungi.
DR   GO; GO:0061912; P:selective autophagy; IEA:EnsemblFungi.
DR   CDD; cd06867; PX_SNX41_42; 1.
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   InterPro; IPR044106; PX_Snx41/Atg20.
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; Endosome; Lipid-binding; Membrane; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..603
FT                   /note="Sorting nexin-41"
FT                   /id="PRO_0000213825"
FT   DOMAIN          121..241
FT                   /note="PX"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         159
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         161
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         185
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         208
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   603 AA;  68638 MW;  FBF6D5F7AF756F38 CRC64;
     MNSFRESDEE DNNPFSGTNH LYASGIGAVP EGDDDFLSAE VDTADETVQE TREQMMSRLF
     GECEGPRESS AGGWTSGSMG SIGAPDGHSD EVTEFGIDTV LVEGEVRTPG RARVPASYPD
     AEGSLGALRI VDAGQYKDTF GNYAIGYTIA YEGRQVTRRY SEFDSLRQAL ARLLPTVIIP
     PIPSKHPLIR YFLNPLNAEN DIRIIEKRRR LLSRFLNNCH DITDIREHTV FQKFLNPEYI
     WSEVLLTPPV SILPTNNLLA PPLNPTKPSP LHLLLPTPPR RTTSYGSPKT NNPEYDIRFT
     ELESLLLRYH KCLQPVLASS RQKKIHFKQL ASSLADLGAY YNAFSLEDNV INLPHQMDQI
     RDLSRAIEKI GQAVDVNYVS SELLVENIMI LLEEPIGEML QFVQEGREVL RFRMQKQQQF
     HIIDTTIKKR RGRIEELRNF QAQLARLEAA LKQNAEESPT IARAVQRLDA QHLHKQRKSP
     SGELQWTGLF KSRSGSVRTH DSLTTRPVTG DVDVDLLSDE ERAREIARLE GDLEKLNECY
     KLIQRDMLQV NESMARSFDW FIMYLHDTWA LVLRNYTRTL LNWLKDCLTA WKNARVTIDT
     IAV