SNX16_RAT
ID SNX16_RAT Reviewed; 344 AA.
AC P57769; Q6P7R2;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Sorting nexin-16;
GN Name=Snx16;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Hanson B.J., Hong W.;
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN PX, MUTAGENESIS OF TYR-145, SUBUNIT,
RP AND INTERACTION WITH EGFR.
RX PubMed=15292396; DOI=10.1242/jcs.01233;
RA Choi J.H., Hong W.P., Kim M.J., Kim J.H., Ryu S.H., Suh P.G.;
RT "Sorting nexin 16 regulates EGF receptor trafficking by
RT phosphatidylinositol-3-phosphate interaction with the Phox domain.";
RL J. Cell Sci. 117:4209-4218(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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. {ECO:0000269|PubMed:15292396}.
CC -!- SUBUNIT: Homooligomer. Interacts with EGFR.
CC {ECO:0000269|PubMed:15292396}.
CC -!- SUBCELLULAR LOCATION: Early endosome membrane
CC {ECO:0000269|PubMed:15292396}; Peripheral membrane protein
CC {ECO:0000269|PubMed:15292396}; Cytoplasmic side
CC {ECO:0000269|PubMed:15292396}. Late endosome membrane
CC {ECO:0000269|PubMed:15292396}; Peripheral membrane protein
CC {ECO:0000269|PubMed:15292396}; Cytoplasmic side
CC {ECO:0000269|PubMed:15292396}. Cytoplasm {ECO:0000269|PubMed:15292396}.
CC Lysosome {ECO:0000269|PubMed:15292396}.
CC -!- DOMAIN: The PX domain mediates interaction with membranes enriched in
CC phosphatidylinositol 3-phosphate. {ECO:0000269|PubMed:15292396}.
CC -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
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DR EMBL; AF305780; AAG25677.1; -; mRNA.
DR EMBL; BC061554; AAH61554.1; -; mRNA.
DR RefSeq; NP_071625.2; NM_022289.3.
DR AlphaFoldDB; P57769; -.
DR SMR; P57769; -.
DR STRING; 10116.ENSRNOP00000041690; -.
DR PaxDb; P57769; -.
DR PRIDE; P57769; -.
DR Ensembl; ENSRNOT00000083909; ENSRNOP00000068566; ENSRNOG00000009953.
DR GeneID; 64088; -.
DR KEGG; rno:64088; -.
DR UCSC; RGD:620295; rat.
DR CTD; 64089; -.
DR RGD; 620295; Snx16.
DR eggNOG; KOG2101; Eukaryota.
DR GeneTree; ENSGT00390000005651; -.
DR HOGENOM; CLU_069154_0_0_1; -.
DR InParanoid; P57769; -.
DR OrthoDB; 1094695at2759; -.
DR PhylomeDB; P57769; -.
DR PRO; PR:P57769; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000009953; Expressed in cerebellum and 20 other tissues.
DR ExpressionAtlas; P57769; baseline and differential.
DR Genevisible; P57769; RN.
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:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0035091; F:phosphatidylinositol binding; ISS:UniProtKB.
DR GO; GO:0045022; P:early endosome to late endosome transport; IDA:RGD.
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 1: Evidence at protein 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_0000213864"
FT DOMAIN 105..218
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 83..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 223..278
FT /evidence="ECO:0000255"
FT COMPBIAS 13..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..102
FT /note="Basic and acidic 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"
FT MUTAGEN 145
FT /note="Y->A: Abolishes binding to phosphatidylinositol 3-
FT phosphate."
FT /evidence="ECO:0000269|PubMed:15292396"
FT CONFLICT 14
FT /note="N -> D (in Ref. 1; AAG25677)"
FT /evidence="ECO:0000305"
FT CONFLICT 53
FT /note="K -> R (in Ref. 1; AAG25677)"
FT /evidence="ECO:0000305"
FT CONFLICT 133
FT /note="K -> E (in Ref. 2; AAH61554)"
FT /evidence="ECO:0000305"
FT CONFLICT 245
FT /note="L -> R (in Ref. 1; AAG25677)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 344 AA; 38848 MW; 1C6AA9F52B4A2C94 CRC64;
MATPYVPVPM PIGNSASSFT NNRNQRSSSF GSVSTSSNSS KGQLEDSSVG TCKHTNVQDQ
MDSASSVCGS PLIRTKFTGT DSSIEYSARP RDTEEQHPDA LNWEDRPSTP TILGYEVMEE
RAKFTVYKIL VKKSPEESWV VFRRYTDFSR LNDKLKEMFP GFRLALPPKR WFKDNYNADF
LEDRQLGLQA FLQNLVAHKD IANCLAVREF LCLDDPPGPF DSLEESRAFC ETLEETNYHL
QRELLEKQKE VESLKKLLGE KQLHIDALET RIRTLSLEPG ASLYVSRAEG GQILRVQSSV
LQVNRDVLDE ESRADHKPHF NSREAGSAIA DIEVAQLAYN AEDD
