SNX4_CANGA
ID SNX4_CANGA Reviewed; 430 AA.
AC Q6FPT9;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Sorting nexin-4;
DE AltName: Full=Autophagy-related protein 24;
GN Name=SNX4; Synonyms=ATG24; OrderedLocusNames=CAGL0J01001g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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: Sorting nexin, involved in the separation or division of
CC vacuoles throughout the entire life cycle of the cells. Involved in
CC retrieval of late-Golgi SNAREs from post-Golgi endosomes to the trans-
CC Golgi network, for cytoplasm to vacuole transport (Cvt), autophagy,
CC mitophagy, and pexophagy. {ECO:0000250|UniProtKB:P47057}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P47057}. Preautophagosomal structure membrane
CC {ECO:0000250|UniProtKB:P47057}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P47057}. Endosome membrane
CC {ECO:0000250|UniProtKB:P47057}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P47057}. Note=Endosome and other perivacuolar
CC punctate structures. Associates to phosphatidylinositol 3-phosphate,
CC necessary for peripheral membrane localization to the perivacuolar
CC punctate structures. {ECO:0000250|UniProtKB:P47057}.
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|UniProtKB:Q96L94}.
CC -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
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DR EMBL; CR380956; CAG60702.1; -; Genomic_DNA.
DR RefSeq; XP_447755.1; XM_447755.1.
DR AlphaFoldDB; Q6FPT9; -.
DR SMR; Q6FPT9; -.
DR STRING; 5478.XP_447755.1; -.
DR EnsemblFungi; CAG60702; CAG60702; CAGL0J01001g.
DR GeneID; 2889847; -.
DR KEGG; cgr:CAGL0J01001g; -.
DR CGD; CAL0133242; CAGL0J01001g.
DR VEuPathDB; FungiDB:CAGL0J01001g; -.
DR eggNOG; KOG2273; Eukaryota.
DR HOGENOM; CLU_027221_0_0_1; -.
DR InParanoid; Q6FPT9; -.
DR OMA; FIWLRQK; -.
DR Proteomes; UP000002428; Chromosome J.
DR GO; GO:0010009; C:cytoplasmic side of endosome membrane; IEA:EnsemblFungi.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005769; C:early endosome; IEA:EnsemblFungi.
DR GO; GO:0019898; C:extrinsic component of membrane; IEA:EnsemblFungi.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IEA:EnsemblFungi.
DR GO; GO:0000422; P:autophagy of mitochondrion; IEA:EnsemblFungi.
DR GO; GO:0032258; P:cytoplasm to vacuole transport by the Cvt pathway; IEA:EnsemblFungi.
DR GO; GO:0034498; P:early endosome to Golgi transport; IEA:EnsemblFungi.
DR GO; GO:0032456; P:endocytic recycling; IEA:EnsemblFungi.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IEA:EnsemblFungi.
DR GO; GO:0036010; P:protein localization to endosome; IEA:EnsemblFungi.
DR GO; GO:0061912; P:selective autophagy; IEA:EnsemblFungi.
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 Pfam; PF00787; PX; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50195; PX; 1.
PE 3: Inferred from homology;
KW Autophagy; Coiled coil; Cytoplasm; Endosome; Lipid-binding; Membrane;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..430
FT /note="Sorting nexin-4"
FT /id="PRO_0000213809"
FT DOMAIN 33..162
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 351..414
FT /evidence="ECO:0000255"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 83
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|UniProtKB:Q3UR97"
FT BINDING 109
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|UniProtKB:Q96L94"
FT BINDING 128
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|UniProtKB:Q6P4T1"
SQ SEQUENCE 430 AA; 49222 MW; 7525E131263CAA6C CRC64;
MDSASADASV TGSGNAKGSS AERVNGGGKF YKLEILVSDP QKRAGEAGLG PYVSYQISTR
TDNPSYHGNQ KASFDDIIVV HRRYNDVVLL HDILQNDHPT CIIPPLPDKK VLQYIAGDRF
GRRFTQRRCH SLQNFLRRVS QHPILSTSKV LEIFLVGNEW DTYRKNIAGT LQNAQKEDVT
DAVMNAFKKV HNQNEEFTEI RDRSDKLDNS VNRINKVFHR VVKKNEAIIE DYSKLGLTLQ
ELQELVSSDN DKLADSLKVF IEGVTQFSYG LQDLNMFIDY EYLIDLKDLS HYIGSMKQTM
RLKDQKQIDY EELSDYLTKS IKEKNNLISG YGGGNFLTSK LEELAGYNQE ASRRDKINKL
ESTISSLTTE LETAKKVADT FEQETLKEVK KFEEIKNDEL KISLNNLADE NIKFYERMLE
TWEKVDQSLR
