ID   SNX15_MOUSE             Reviewed;         337 AA.
AC   Q91WE1;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 146.
DE   RecName: Full=Sorting nexin-15;
GN   Name=Snx15;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
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   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Lung, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [3]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-105, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, and Embryo;
RX   PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA   Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA   Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
CC   -!- FUNCTION: May be involved in several stages of intracellular
CC       trafficking. Overexpression of SNX15 disrupts the normal trafficking of
CC       proteins from the plasma membrane to recycling endosomes or the TGN (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. Interacts with SNX1, SNX2 and SNX4 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC       {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}; Peripheral
CC       membrane protein {ECO:0000250}; Cytoplasmic side {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; BC016091; AAH16091.1; -; mRNA.
DR   CCDS; CCDS29495.1; -.
DR   RefSeq; NP_081188.1; NM_026912.1.
DR   RefSeq; XP_006531894.1; XM_006531831.3.
DR   AlphaFoldDB; Q91WE1; -.
DR   SMR; Q91WE1; -.
DR   STRING; 10090.ENSMUSP00000025702; -.
DR   GlyGen; Q91WE1; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q91WE1; -.
DR   PhosphoSitePlus; Q91WE1; -.
DR   EPD; Q91WE1; -.
DR   jPOST; Q91WE1; -.
DR   MaxQB; Q91WE1; -.
DR   PaxDb; 10090-ENSMUSP00000025702; -.
DR   PeptideAtlas; Q91WE1; -.
DR   ProteomicsDB; 261595; -.
DR   Pumba; Q91WE1; -.
DR   ABCD; Q91WE1; 79 sequenced antibodies.
DR   Antibodypedia; 29586; 251 antibodies from 30 providers.
DR   DNASU; 69024; -.
DR   Ensembl; ENSMUST00000025702.14; ENSMUSP00000025702.8; ENSMUSG00000024787.15.
DR   GeneID; 69024; -.
DR   KEGG; mmu:69024; -.
DR   UCSC; uc008ghm.1; mouse.
DR   AGR; MGI:1916274; -.
DR   CTD; 29907; -.
DR   MGI; MGI:1916274; Snx15.
DR   VEuPathDB; HostDB:ENSMUSG00000024787; -.
DR   eggNOG; KOG0603; Eukaryota.
DR   eggNOG; KOG2101; Eukaryota.
DR   GeneTree; ENSGT00940000160125; -.
DR   InParanoid; Q91WE1; -.
DR   OMA; YRFFTVT; -.
DR   OrthoDB; 5476410at2759; -.
DR   PhylomeDB; Q91WE1; -.
DR   TreeFam; TF323964; -.
DR   BioGRID-ORCS; 69024; 2 hits in 77 CRISPR screens.
DR   ChiTaRS; Snx15; mouse.
DR   PRO; PR:Q91WE1; -.
DR   Proteomes; UP000000589; Chromosome 19.
DR   RNAct; Q91WE1; Protein.
DR   Bgee; ENSMUSG00000024787; Expressed in embryonic brain and 244 other cell types or tissues.
DR   ExpressionAtlas; Q91WE1; baseline and differential.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0005730; C:nucleolus; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   CDD; cd02677; MIT_SNX15; 1.
DR   Gene3D; 1.20.58.80; Phosphotransferase system, lactose/cellobiose-type IIA subunit; 1.
DR   Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR   InterPro; IPR007330; MIT_dom.
DR   InterPro; IPR036181; MIT_dom_sf.
DR   InterPro; IPR001683; PX_dom.
DR   InterPro; IPR036871; PX_dom_sf.
DR   PANTHER; PTHR15508:SF8; LD24550P; 1.
DR   PANTHER; PTHR15508; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR   Pfam; PF04212; MIT; 1.
DR   Pfam; PF00787; PX; 1.
DR   SMART; SM00745; MIT; 1.
DR   SMART; SM00312; PX; 1.
DR   SUPFAM; SSF116846; MIT domain; 1.
DR   SUPFAM; SSF64268; PX domain; 1.
DR   PROSITE; PS50195; PX; 1.
DR   Genevisible; Q91WE1; MM.
PE   1: Evidence at protein level;
KW   Cytoplasm; Cytoplasmic vesicle; Lipid-binding; Membrane; Methylation;
KW   Phosphoprotein; Protein transport; Reference proteome; Transport.
FT   CHAIN           1..337
FT                   /note="Sorting nexin-15"
FT                   /id="PRO_0000236202"
FT   DOMAIN          1..130
FT                   /note="PX"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT   DOMAIN          265..337
FT                   /note="MIT"
FT   REGION          133..156
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          244..270
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        142..156
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         51
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         53
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         87
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         96
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         105
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         201
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NRS6"
FT   MOD_RES         227
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NRS6"
SQ   SEQUENCE   337 AA;  37742 MW;  743923E18ED9EF4B CRC64;
     MSRQAKDDFL RHYTVSDPRT HPKGYTEYKV TAQFISKKDP EDIKEVVVWK RYSDFRKLHG
     DLAYTHRNLF RRLEEFPAFP RAQVFGRFEA SVIEERRKGA EDLLRFTVPI PALNNSPQLK
     EFFRGGEVTR PSEVSRDLRI LPPPLIPTPP PDEARLLQPL PAERRGQEEL EVPVDPLPSS
     PAQEALDLLF SCDSTEEASS SLARGPLSEA ELALFDPYSK EESTGPSPTH TGELAAIEVE
     SKRLDQEPWE PGGQEEEEAE DGEPAPAYLG QATELITQAL RNEKAGAYAA ALQGYQDGVH
     ILLQGVSGDP SPARREGVKK KAAEYLKRAE MLHTHLP
//