SNX15_MOUSE
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 03-AUG-2022, entry version 137.
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 iPTMnet; Q91WE1; -.
DR PhosphoSitePlus; Q91WE1; -.
DR EPD; Q91WE1; -.
DR jPOST; Q91WE1; -.
DR MaxQB; Q91WE1; -.
DR PaxDb; Q91WE1; -.
DR PeptideAtlas; Q91WE1; -.
DR PRIDE; Q91WE1; -.
DR ProteomicsDB; 261595; -.
DR ABCD; Q91WE1; 80 sequenced antibodies.
DR Antibodypedia; 29586; 234 antibodies from 30 providers.
DR DNASU; 69024; -.
DR Ensembl; ENSMUST00000025702; ENSMUSP00000025702; ENSMUSG00000024787.
DR GeneID; 69024; -.
DR KEGG; mmu:69024; -.
DR UCSC; uc008ghm.1; mouse.
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; 255297at2759; -.
DR PhylomeDB; Q91WE1; -.
DR TreeFam; TF323964; -.
DR BioGRID-ORCS; 69024; 2 hits in 72 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 241 other tissues.
DR ExpressionAtlas; Q91WE1; baseline and differential.
DR Genevisible; Q91WE1; MM.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005769; C:early endosome; IBA:GO_Central.
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 Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR007330; MIT_dom.
DR InterPro; IPR036181; MIT_dom_sf.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR Pfam; PF04212; MIT; 1.
DR Pfam; PF00787; PX; 1.
DR SMART; SM00745; MIT; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF116846; SSF116846; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50195; PX; 1.
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