ID   SNX16_PONAB             Reviewed;         344 AA.
AC   Q5R6Q7;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Sorting nexin-16;
GN   Name=SNX16;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May be involved in several stages of intracellular
CC       trafficking. Plays a role in protein transport from early to late
CC       endosomes. Plays a role in protein transport to the lysosome. Promotes
CC       degradation of EGFR after EGF signaling (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homooligomer. Interacts with EGFR (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000250}; Peripheral
CC       membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Late
CC       endosome membrane {ECO:0000250}; Peripheral membrane protein
CC       {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC       Lysosome {ECO:0000250}.
CC   -!- DOMAIN: The PX domain mediates interaction with membranes enriched in
CC       phosphatidylinositol 3-phosphate. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
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DR   EMBL; CR860428; CAH92553.1; -; mRNA.
DR   RefSeq; NP_001126495.1; NM_001133023.1.
DR   AlphaFoldDB; Q5R6Q7; -.
DR   SMR; Q5R6Q7; -.
DR   STRING; 9601.ENSPPYP00000020980; -.
DR   GeneID; 100173483; -.
DR   KEGG; pon:100173483; -.
DR   CTD; 64089; -.
DR   eggNOG; KOG2101; Eukaryota.
DR   InParanoid; Q5R6Q7; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005829; C:cytosol; IEA:GOC.
DR   GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR   GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031313; C:extrinsic component of endosome membrane; ISS:UniProtKB.
DR   GO; GO:0005770; C:late endosome; ISS:UniProtKB.
DR   GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0035091; F:phosphatidylinositol binding; ISS:UniProtKB.
DR   GO; GO:0045022; P:early endosome to late endosome transport; ISS:UniProtKB.
DR   GO; GO:0008333; P:endosome to lysosome transport; ISS:UniProtKB.
DR   GO; GO:0006622; P:protein targeting to lysosome; ISS:UniProtKB.
DR   CDD; cd07276; PX_SNX16; 1.
DR   Gene3D; 3.30.1520.10; -; 1.
DR   InterPro; IPR001683; PX_dom.
DR   InterPro; IPR036871; PX_dom_sf.
DR   InterPro; IPR037911; SNX16_PX.
DR   Pfam; PF00787; PX; 1.
DR   SMART; SM00312; PX; 1.
DR   SUPFAM; SSF64268; SSF64268; 1.
DR   PROSITE; PS50195; PX; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Cytoplasm; Endosome; Lipid-binding; Lysosome; Membrane;
KW   Phosphoprotein; Protein transport; Reference proteome; Transport.
FT   CHAIN           1..344
FT                   /note="Sorting nexin-16"
FT                   /id="PRO_0000253040"
FT   DOMAIN          105..218
FT                   /note="PX"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT   REGION          1..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          83..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          223..278
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        13..66
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         144
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         146
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         184
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   MOD_RES         222
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8C080"
SQ   SEQUENCE   344 AA;  39259 MW;  85F5C72AB21900C9 CRC64;
     MATPYVPVPM PIGNSASSFT TNRNQRSSSF GSVSTSSNSS KGQLEDSNMG NFKQTSVPDQ
     MDNTSSVCSS PLIRTKFTGA ASSIEYSTRP RETEEQNPET VNWEDRPSTP TILGYEVMEE
     RAKFTVYKIL VKKTPEESWV VFRRYTDFSR LNDKLKEMFP GFRLALPPKR WFKDNYNADF
     LEDRQLGLQA FLQNLVAHKD IANCLAVREF LCLDDPPGPF DSLEESRVFC ETLEETNYRL
     QKELLEKQKE MESLKKQLSE KQLHIDTLEN RIRTLSLEPE ESLDVSETEG EQILKVESSA
     LEVDQDVLDE ESRADNEPCL HFSEPENAIS EIEVAEVAYD AEED