SNX4_CANAL
ID SNX4_CANAL Reviewed; 630 AA.
AC Q5AD77; A0A1D8PGB5; Q5ADK6;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 2.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Sorting nexin-4;
DE AltName: Full=Autophagy-related protein 24;
GN Name=SNX4; Synonyms=ATG24; OrderedLocusNames=CAALFM_C201350CA;
GN ORFNames=CaO19.1990, CaO19.9541;
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: 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; CP017624; AOW27181.1; -; Genomic_DNA.
DR RefSeq; XP_719440.2; XM_714347.2.
DR AlphaFoldDB; Q5AD77; -.
DR STRING; 237561.Q5AD77; -.
DR PRIDE; Q5AD77; -.
DR GeneID; 3638843; -.
DR KEGG; cal:CAALFM_C201350CA; -.
DR CGD; CAL0000187768; SNX4.
DR VEuPathDB; FungiDB:C2_01350C_A; -.
DR eggNOG; KOG2273; Eukaryota.
DR HOGENOM; CLU_027221_1_0_1; -.
DR InParanoid; Q5AD77; -.
DR OMA; FIWLRQK; -.
DR OrthoDB; 990775at2759; -.
DR PRO; PR:Q5AD77; -.
DR Proteomes; UP000000559; Chromosome 2.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000407; C:phagophore assembly site; IBA:GO_Central.
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:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR GO; GO:0032456; P:endocytic recycling; IBA:GO_Central.
DR GO; GO:2000786; P:positive regulation of autophagosome assembly; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IBA:GO_Central.
DR GO; GO:0061709; P:reticulophagy; IBA:GO_Central.
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..630
FT /note="Sorting nexin-4"
FT /id="PRO_0000213808"
FT DOMAIN 187..321
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT REGION 1..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 361..413
FT /evidence="ECO:0000255"
FT COILED 550..581
FT /evidence="ECO:0000255"
FT COMPBIAS 1..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 243
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 269
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 288
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 630 AA; 71842 MW; D70DF4BDB6135AD7 CRC64;
MSSEDQFTSI QWDRDDGENT NNTPTDTTIK SKSSKSKKSK KSSSKKKNGN KISPSSTTET
SDADDTMKEV TDQLESTQIN DDNHEVDDGN KEQNVDANQI GNSDEDPTNS LLLPVNPQPK
EPQEEKEDLQ QQLQQPQQQL ASIQQEPAPI QPPFNAVVND ESLSIQQQQQ QQQPTGYVDI
SYYEKYSIKT TVTHPNRDLD TASKPFISYL VTTTTDNPSI LKLTKEKKPK QGEEYLTFSV
RRRYGDFRYL YESLSNDFPT VMIPPLPSKS NFKYLTGDTF SSEFVHKRLH SLDRFIRFIL
QHKILSQSSI FHLFISNSND WATFTTSLKL KDSSSDESGI VGRVVNEDLI TETVMNFLTP
SKHKKETNKD ILEINDKLKK LYENLIKLDK IFTKLKKKNH ELGNDYDQFS NQILKLSSVQ
KGEDSIMTTN FKIFSDSLNY FSKSYNEMYR YIDENFLISL QDLAKFCLRF IQLIKLKNDK
STDLAVLQDF LNKELANNSG GSGSGSGSGG SGLHQPPNPV ISSYQGGIVN NTTQLIKDTL
STSNTTISNT IKSDKIKNLE QEIAKETKIL TDLTNKIINE EYPNWEKFNK IEIKNSMLGL
CDQNIKFYND LLEKFGEVEM KLIKRLDEDM
