SNX41_KLULA
ID SNX41_KLULA Reviewed; 575 AA.
AC Q6CWX3;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Sorting nexin-41;
GN Name=SNX41; OrderedLocusNames=KLLA0B00803g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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; CR382122; CAH01959.1; -; Genomic_DNA.
DR RefSeq; XP_451566.1; XM_451566.1.
DR AlphaFoldDB; Q6CWX3; -.
DR STRING; 28985.XP_451566.1; -.
DR EnsemblFungi; CAH01959; CAH01959; KLLA0_B00803g.
DR GeneID; 2897029; -.
DR KEGG; kla:KLLA0_B00803g; -.
DR eggNOG; KOG2273; Eukaryota.
DR HOGENOM; CLU_014456_3_0_1; -.
DR InParanoid; Q6CWX3; -.
DR OMA; WIKECLK; -.
DR Proteomes; UP000000598; Chromosome B.
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..575
FT /note="Sorting nexin-41"
FT /id="PRO_0000213830"
FT DOMAIN 101..221
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT REGION 30..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 139
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 141
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 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"
FT BINDING 188
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 575 AA; 65900 MW; C471FC0DC597465A CRC64;
MNVFDGSDEE DNNPFSGTTH LYASGIAAVT DGPDDYDFTE PSINGSSDEN AQSNAVAEPI
EETDEPAEEI DDDTLQTWRF ASAELSRSSA FETSYTNLLG QGKNPEVIRI VDAGQYRDIY
GKYAIGYKIE FGGIVVTRRY SEFDSLRQSL CRLLPTIIIP PIPSKHPIIK YLFNPLHAKK
DIKIIERRQR LLSRFLNNCH KVREIRNHIV FQKFLNPEYF WKEVLNTPPI SILPMNNLLA
PPLNPTKPSP IHLLLPTPTV LTMRKHEQLI GRNDVMEIKF ADYDSDLIRY KAILQPLNKT
VRSIRSNIQT YSAVLSELGA YFNAFSLENS VFQVSALFEQ MNRLSMGIEK TGQAIDVNYV
SAEIFSEAIM ISLEEGSKEM LQFIHEAQRV LHFRNFKQEQ FYTIETTIKK RKDRIRELKE
ADLQAVRLGE ALKLNAEESP TVAQVMDSMT RKSANKNHTD KQIMGLFRSS ASPNNKSGSD
SISSEVEPHL LTKDERVVQV NKLEKELEKL NECFKLIEKD LQQVNESMDN SLNNLEKYFH
EKWFLIFREL AHNITSWLKD CSESWKNAKQ SIDSI
