ID J7S7F0_KAZNA Unreviewed; 158 AA.
AC J7S7F0;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Sorting nexin-3 {ECO:0000256|ARBA:ARBA00020436};
GN Name=KNAG0E00280 {ECO:0000313|EMBL:CCK70296.1};
GN OrderedLocusNames=KNAG_0E00280 {ECO:0000313|EMBL:CCK70296.1};
OS Kazachstania naganishii (strain ATCC MYA-139 / BCRC 22969 / CBS 8797 / KCTC
OS 17520 / NBRC 10181 / NCYC 3082 / Yp74L-3) (Yeast) (Saccharomyces
OS naganishii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX NCBI_TaxID=1071383 {ECO:0000313|EMBL:CCK70296.1, ECO:0000313|Proteomes:UP000006310};
RN [1] {ECO:0000313|EMBL:CCK70296.1, ECO:0000313|Proteomes:UP000006310}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-139 / BCRC 22969 / CBS 8797 / CCRC 22969 / KCTC 17520
RC / NBRC 10181 / NCYC 3082 {ECO:0000313|Proteomes:UP000006310};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
RN [2] {ECO:0000313|Proteomes:UP000006310}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-139 / BCRC 22969 / CBS 8797 / CCRC 22969 / KCTC 17520
RC / NBRC 10181 / NCYC 3082 {ECO:0000313|Proteomes:UP000006310};
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Genome sequence of Kazachstania naganishii.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for retention of late Golgi membrane proteins.
CC Component of the retrieval machinery that functions by direct
CC interaction with the cytosolic tails of certain TGN membrane proteins
CC during the sorting/budding process at the prevacuolar compartment.
CC Binds phosphatidylinositol 3-phosphate (PtdIns(P3)).
CC {ECO:0000256|ARBA:ARBA00025533}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004287};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004287};
CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004287}. Prevacuolar
CC compartment membrane {ECO:0000256|ARBA:ARBA00004179}; Peripheral
CC membrane protein {ECO:0000256|ARBA:ARBA00004179}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004179}.
CC -!- SIMILARITY: Belongs to the sorting nexin family.
CC {ECO:0000256|ARBA:ARBA00010883}.
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DR EMBL; HE978318; CCK70296.1; -; Genomic_DNA.
DR AlphaFoldDB; J7S7F0; -.
DR STRING; 1071383.J7S7F0; -.
DR eggNOG; KOG2527; Eukaryota.
DR HOGENOM; CLU_057172_2_1_1; -.
DR OMA; VGRQRYT; -.
DR OrthoDB; 5475877at2759; -.
DR Proteomes; UP000006310; Chromosome 5.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR PANTHER; PTHR45963; RE52028P; 1.
DR PANTHER; PTHR45963:SF2; SORTING NEXIN-12; 1.
DR Pfam; PF00787; PX; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR PROSITE; PS50195; PX; 1.
PE 3: Inferred from homology;
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000006310}.
FT DOMAIN 34..157
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 158 AA; 17879 MW; D13C2657191D9CC4 CRC64;
MRPFQSFSTT EHSTFSSPSP TGPDTPAQYG EPESLMEVEV GAPQTHKIGG ETFTDYEVTA
RTNLPGYARG TTVVRRRYSD FEHLRQCLKN EMVVTNRTRV KIPHLPGKIF LSNRFDERVI
EERQRGLDKW LKSVAGHPLL QVGSAVLVRF LQSRVFSG
//
