SNX4_DEBHA
ID SNX4_DEBHA Reviewed; 582 AA.
AC Q6BZE9;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Sorting nexin-4;
DE AltName: Full=Autophagy-related protein 24;
GN Name=SNX4; Synonyms=ATG24; OrderedLocusNames=DEHA2A01892g;
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: 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; CR382133; CAG84372.2; -; Genomic_DNA.
DR RefSeq; XP_456420.2; XM_456420.1.
DR AlphaFoldDB; Q6BZE9; -.
DR STRING; 4959.XP_456420.2; -.
DR PRIDE; Q6BZE9; -.
DR EnsemblFungi; CAG84372; CAG84372; DEHA2A01892g.
DR GeneID; 2899618; -.
DR KEGG; dha:DEHA2A01892g; -.
DR VEuPathDB; FungiDB:DEHA2A01892g; -.
DR eggNOG; KOG2273; Eukaryota.
DR HOGENOM; CLU_027221_1_0_1; -.
DR InParanoid; Q6BZE9; -.
DR OMA; FIWLRQK; -.
DR OrthoDB; 990775at2759; -.
DR Proteomes; UP000000599; Chromosome A.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IEA:UniProt.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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; 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..582
FT /note="Sorting nexin-4"
FT /id="PRO_0000213811"
FT DOMAIN 116..249
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT REGION 1..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 300..329
FT /evidence="ECO:0000255"
FT COILED 494..529
FT /evidence="ECO:0000255"
FT COMPBIAS 9..58
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 171
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 197
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 216
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 582 AA; 66454 MW; 506993ABE8E310A7 CRC64;
MSSDDQFTSI QWDRDELGPN KETKVNKQET ITEDDEHHNN DNEDKDNDTT KSNEPENIQE
DDETKDDNEP TDSLILSKTG DENISNIESQ NEGDHIVGEP DVNQEPSSDS QTEAYEINVV
VTSPLRDLDS SSKPYISYLL TTATNHPSVM KLSTVKKEQG KEVVEITARR RYGDFRFLFD
CLSNDHPEVM MPPLPSKSNF KYLTGDTFST EFVHKRLHSL DRFVRFITCH KVLSQSSIFH
LFVSDSADWS TFQKNLKISK VGVQESDADK GNSSMTSNVV NKVVNEDLLT ETIMNFLTPS
KHKRETNKEI LEISDKLKKL YENLIKLDKI FTKLNKKNHD LSVDYEQFSQ QIMKLSVIQN
SSDETNEPTT PEINEQKQFA TNFKVFASSL SYFSDNWSNL HKYIDESFLV SLKDCAKYII
SLTNLIELQH NKKIDLQVLQ DYLNKAKSEL QGLGGSHNAP PNPIITHNNG GIVNNTTQLI
RDTLSTSATP NIGSSVTESK VTKLQNRITE LENEISVQSQ LVLDLTNKII NEEYPNWDKF
NKIELKESLL GLCNEEISFY KGLVDNWSDI ELKLLKRLDE LK
