ID   SNX15_RAT               Reviewed;         338 AA.
AC   Q4V896;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Sorting nexin-15;
GN   Name=Snx15;
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 [LARGE SCALE MRNA].
RC   TISSUE=Placenta;
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).
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; BC097481; AAH97481.1; -; mRNA.
DR   RefSeq; NP_001019923.1; NM_001024752.1.
DR   AlphaFoldDB; Q4V896; -.
DR   SMR; Q4V896; -.
DR   STRING; 10116.ENSRNOP00000028511; -.
DR   PhosphoSitePlus; Q4V896; -.
DR   jPOST; Q4V896; -.
DR   PaxDb; Q4V896; -.
DR   PRIDE; Q4V896; -.
DR   GeneID; 293691; -.
DR   KEGG; rno:293691; -.
DR   UCSC; RGD:1305803; rat.
DR   CTD; 29907; -.
DR   RGD; 1305803; Snx15.
DR   VEuPathDB; HostDB:ENSRNOG00000021007; -.
DR   eggNOG; KOG0603; Eukaryota.
DR   eggNOG; KOG2101; Eukaryota.
DR   HOGENOM; CLU_055745_0_0_1; -.
DR   InParanoid; Q4V896; -.
DR   OMA; YRFFTVT; -.
DR   OrthoDB; 255297at2759; -.
DR   PhylomeDB; Q4V896; -.
DR   TreeFam; TF323964; -.
DR   PRO; PR:Q4V896; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000021007; Expressed in jejunum and 20 other tissues.
DR   Genevisible; Q4V896; RN.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005769; C:early endosome; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Cytoplasm; Cytoplasmic vesicle; Lipid-binding; Membrane; Methylation;
KW   Phosphoprotein; Protein transport; Reference proteome; Transport.
FT   CHAIN           1..338
FT                   /note="Sorting nexin-15"
FT                   /id="PRO_0000236203"
FT   DOMAIN          1..131
FT                   /note="PX"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT   DOMAIN          266..338
FT                   /note="MIT"
FT   REGION          134..155
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          240..270
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         52
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         54
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         88
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         97
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         106
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q91WE1"
FT   MOD_RES         202
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NRS6"
FT   MOD_RES         228
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NRS6"
SQ   SEQUENCE   338 AA;  37905 MW;  33EC50776634F83D CRC64;
     MSRRAKKDDF LRHYTVSDPR THPKGYTEYK VTAQFISKKD PEDIKEVVVW KRYSDFRKLH
     GDLAYTHRNL FRRLEEFPAF PRAQVFGRFE ASVIEERRKG AEDLLRFTVP IPALNNSPQL
     KEFFRGGEVT RPSEVSRDLQ ILPPPLIPTP PSDEARLLQP LPAERRGQEE LEVPVDPLPS
     SPAQEALDLL FCCDSTEEAS SSPARGPLSE AELALFDPYS KEESTGPSPT HTSELAAMEV
     QSKRLDQEPW EPGGREEEEA EDGDPAPAYL GQATELITQA LRNEKAGAYA AALQGYQEGV
     HILLQGVSGD PSPTRREGVK KKAAEYLKRA ETLHAHLP