ID   SNX41_CANAL             Reviewed;         681 AA.
AC   Q5AD73; A0A1D8PGB4;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2017, sequence version 2.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Sorting nexin-41;
GN   Name=SNX41; OrderedLocusNames=CAALFM_C201310WA;
GN   ORFNames=CaO19.1994, CaO19.9546;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(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; CP017624; AOW27177.1; -; Genomic_DNA.
DR   RefSeq; XP_719444.2; XM_714351.2.
DR   AlphaFoldDB; Q5AD73; -.
DR   STRING; 237561.Q5AD73; -.
DR   PRIDE; Q5AD73; -.
DR   GeneID; 3638788; -.
DR   KEGG; cal:CAALFM_C201310WA; -.
DR   CGD; CAL0000183027; orf19.9546.
DR   VEuPathDB; FungiDB:C2_01310W_A; -.
DR   eggNOG; KOG2273; Eukaryota.
DR   HOGENOM; CLU_025790_0_0_1; -.
DR   InParanoid; Q5AD73; -.
DR   OrthoDB; 632390at2759; -.
DR   PRO; PR:Q5AD73; -.
DR   Proteomes; UP000000559; Chromosome 2.
DR   GO; GO:0005829; C:cytosol; IEA:GOC.
DR   GO; GO:0010008; C:endosome 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   GO; GO:0042147; P:retrograde transport, endosome to Golgi; IEA:InterPro.
DR   CDD; cd06867; PX_SNX41_42; 1.
DR   Gene3D; 3.30.1520.10; -; 1.
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..681
FT                   /note="Sorting nexin-41"
FT                   /id="PRO_0000213826"
FT   DOMAIN          113..236
FT                   /note="PX"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT   REGION          1..94
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          475..505
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          558..597
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        54..75
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        475..499
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        558..595
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         151
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         153
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         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"
FT   BINDING         200
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   681 AA;  78368 MW;  A5A60B693146B30E CRC64;
     MSTDNLFEDI EQDNNPSFYG NPSILNDPYR PIQPPPPQQQ QQQHQENESK QSHTKSPKPP
     LQSIHSGTSN AHPQSQPQHK HKHKHNTSLN NGYPNELVNS TIGLSNRILE LLNDSQLQVD
     IINSEKLVNS SVIVYTIELS SPTTKIVVKR RYSEFKSLRD NLLKLFPTLI IPPIPEKHSI
     LSYLLNTINH SHEISIIEMR KRYFKMFLDD LIFQSDYKLK NCPLLHKFFD PNYELCWYNA
     LNEPPVSLIP DNLLLANPIN PADQNGLYSL LPIVNGFDFN SHIDNLSNLK KINEDLYKLN
     DQVKLYELKG FEQDLEFSIP EELIQFEIKF HQTIKILTDL NKLNSKTTKN YKSMVDTLID
     LGGNLNNFSL QVYQQKSGSN NELSEAIEKF GSTMDQSFLN FESFILNQLV PQWQEPVDQL
     ILYLQNSLGL IKFYKYKIVQ FKILYKLKFN KFQQLINLTN IGGVSSSGSG GGGLLASRIS
     TDNDSNNSNN SGNNNNDGDL DTENFDHLKE LNSPTINNAL KNLSTKKISK KSSWYGLFGG
     NNQTKKFNFQ LPIEEPTTAT GSTEQQSQQQ SAPNSPQREQ QQQQSQSQSH HSHQTSIRFK
     LNHIEKELNK LNQLIELCNQ DMHKLTEALV NTFEEFLSKI ERKWLQLMIT YIQNCKNMFE
     ANLTNWKEFK ESLVNETREV N