SNX41_DEBHA
ID SNX41_DEBHA Reviewed; 670 AA.
AC Q6BHN9;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Sorting nexin-41;
GN Name=SNX41; OrderedLocusNames=DEHA2G17094g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR382139; CAG90784.2; -; Genomic_DNA.
DR RefSeq; XP_462282.2; XM_462282.1.
DR AlphaFoldDB; Q6BHN9; -.
DR STRING; 4959.XP_462282.2; -.
DR EnsemblFungi; CAG90784; CAG90784; DEHA2G17094g.
DR GeneID; 2905215; -.
DR KEGG; dha:DEHA2G17094g; -.
DR VEuPathDB; FungiDB:DEHA2G17094g; -.
DR eggNOG; KOG2273; Eukaryota.
DR HOGENOM; CLU_014456_2_0_1; -.
DR InParanoid; Q6BHN9; -.
DR OMA; CRRMKEV; -.
DR OrthoDB; 632390at2759; -.
DR Proteomes; UP000000599; Chromosome G.
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..670
FT /note="Sorting nexin-41"
FT /id="PRO_0000213828"
FT DOMAIN 123..288
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 42..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 536..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 164
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 166
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 190
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 254
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 670 AA; 76203 MW; 5D49D1700CC9F9D6 CRC64;
MSKGKESKVG SSTPSFDDEE DNNPFPHMQG LASLMSEHRI SNGSNIQDKG DKDNNNNNNY
NNNNNNNNNN NNGDDDDDSI LLYNSNNQND SKSGLNKDTF KSIQINYESR VTRLLRPNSN
VRMQITKAGN SNEGMINTSK TYIVYSIQLI NNDDPSDEIQ TRRRYSDFES LRDVLKKIFP
LIIIPPIPPK NYFKFSMLND LVSGNISQSS NTSSNNSTGA NTSTNTTNGL GSNSTNYSYI
NSTHLNKNKL IEHRKRLLSN FLNNCLAIPQ IRNLEFFAKF LDPNANWTDE ITLISSQLPK
SIYFSNPENG LKTDSIYANL PNPVGNHSIN MSFWKPLQEN KKKLTKKTNK ILNNGNTEAS
SQPSTGTTSP VNHSPDFIKN KYIIDNSCLD DINKKIMANF IGLANDYTEL GTIFNSFSLI
LSDSPMIRSA KAKNNHEEDS KLNLIFDKIG QIFDRSYITI STLIADLETK FSEPLGEAVQ
YSTILQFIEK FERRKVRQKR LLEDDVKDKK QELEELLKAE EGSSKIENVM HAQPISKHSG
LNSRGTNSTQ NVNSSIKSTN SKYKYLPNMN SFKKITQYVT DIIDQNPEQT RKQKITSLQE
KIGTLEKCQG IMLQDISYIT DEINKNFKSF HTKQLKIIYE ILLCYNGFLV EWAKKNVDIW
EEIKDEVEKL
