ID SNX41_EREGS Reviewed; 603 AA.
AC Q759T1;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 107.
DE RecName: Full=Sorting nexin-41;
GN Name=SNX41; OrderedLocusNames=ADR192C;
OS Eremothecium gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL
OS Y-1056) (Yeast) (Ashbya 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; 284811.Q759T1; -.
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; DFKDPWG; -.
DR OrthoDB; 5475877at2759; -.
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:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0006886; P:intracellular protein transport; IEA:EnsemblFungi.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IEA:EnsemblFungi.
DR CDD; cd06867; PX_SNX41_42; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 3.30.1520.10; Phox-like domain; 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 PANTHER; PTHR46979; SORTING NEXIN-41; 1.
DR PANTHER; PTHR46979:SF2; SORTING NEXIN-41; 1.
DR Pfam; PF00787; PX; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF64268; PX domain; 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
//
