ID   SNX13_MOUSE             Reviewed;         957 AA.
AC   Q6PHS6;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   24-JAN-2024, entry version 124.
DE   RecName: Full=Sorting nexin-13;
GN   Name=Snx13;
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   STRAIN=C57BL/6J; TISSUE=Brain;
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   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=17077144; DOI=10.1073/pnas.0607974103;
RA   Zheng B., Tang T., Tang N., Kudlicka K., Ohtsubo K., Ma P., Marth J.D.,
RA   Farquhar M.G., Lehtonen E.;
RT   "Essential role of RGS-PX1/sorting nexin 13 in mouse development and
RT   regulation of endocytosis dynamics.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:16776-16781(2006).
CC   -!- FUNCTION: May be involved in several stages of intracellular
CC       trafficking. Acts as a GAP for Galphas (By similarity). May play a role
CC       in endosome homeostasis. {ECO:0000250, ECO:0000269|PubMed:17077144}.
CC   -!- SUBCELLULAR LOCATION: Early endosome 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   -!- DISRUPTION PHENOTYPE: Embryonic lethal. After 8.5 dpc, embryos are
CC       smaller, show failure of neural tube closure and abnormal cephalic
CC       vascularization. None survive after 14.5 dpc. Visceral yolk sac
CC       endoderm cells contain large autophagic vacuoles.
CC       {ECO:0000269|PubMed:17077144}.
CC   -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
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DR   EMBL; BC056394; AAH56394.1; -; mRNA.
DR   CCDS; CCDS56837.1; -.
DR   RefSeq; NP_001014973.2; NM_001014973.2.
DR   AlphaFoldDB; Q6PHS6; -.
DR   SMR; Q6PHS6; -.
DR   BioGRID; 229917; 1.
DR   STRING; 10090.ENSMUSP00000038430; -.
DR   iPTMnet; Q6PHS6; -.
DR   PhosphoSitePlus; Q6PHS6; -.
DR   MaxQB; Q6PHS6; -.
DR   PaxDb; 10090-ENSMUSP00000038430; -.
DR   ProteomicsDB; 261539; -.
DR   Pumba; Q6PHS6; -.
DR   DNASU; 217463; -.
DR   Ensembl; ENSMUST00000048519.17; ENSMUSP00000038430.11; ENSMUSG00000020590.17.
DR   GeneID; 217463; -.
DR   KEGG; mmu:217463; -.
DR   UCSC; uc011yli.1; mouse.
DR   AGR; MGI:2661416; -.
DR   CTD; 23161; -.
DR   MGI; MGI:2661416; Snx13.
DR   eggNOG; KOG2101; Eukaryota.
DR   GeneTree; ENSGT00950000182856; -.
DR   InParanoid; Q6PHS6; -.
DR   OMA; EWTPTNV; -.
DR   OrthoDB; 5392990at2759; -.
DR   PhylomeDB; Q6PHS6; -.
DR   BioGRID-ORCS; 217463; 2 hits in 77 CRISPR screens.
DR   ChiTaRS; Snx13; mouse.
DR   PRO; PR:Q6PHS6; -.
DR   Proteomes; UP000000589; Chromosome 12.
DR   RNAct; Q6PHS6; Protein.
DR   GO; GO:0005769; C:early endosome; ISO:MGI.
DR   GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0035091; F:phosphatidylinositol binding; ISO:MGI.
DR   GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; ISO:MGI.
DR   GO; GO:0006886; P:intracellular protein transport; ISO:MGI.
DR   GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR   CDD; cd06873; PX_SNX13; 1.
DR   CDD; cd08719; RGS_SNX13; 1.
DR   Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR   Gene3D; 1.10.167.10; Regulator of G-protein Signalling 4, domain 2; 1.
DR   InterPro; IPR003114; Phox_assoc.
DR   InterPro; IPR001683; PX_dom.
DR   InterPro; IPR036871; PX_dom_sf.
DR   InterPro; IPR016137; RGS.
DR   InterPro; IPR036305; RGS_sf.
DR   InterPro; IPR044926; RGS_subdomain_2.
DR   InterPro; IPR037437; SNX13_PX.
DR   InterPro; IPR037896; SNX13_RGS.
DR   InterPro; IPR013937; Sorting_nexin_C.
DR   PANTHER; PTHR22775; SORTING NEXIN; 1.
DR   PANTHER; PTHR22775:SF3; SORTING NEXIN-13; 1.
DR   Pfam; PF08628; Nexin_C; 1.
DR   Pfam; PF00787; PX; 1.
DR   Pfam; PF02194; PXA; 1.
DR   Pfam; PF00615; RGS; 1.
DR   SMART; SM00312; PX; 1.
DR   SMART; SM00313; PXA; 1.
DR   SMART; SM00315; RGS; 1.
DR   SUPFAM; SSF64268; PX domain; 1.
DR   SUPFAM; SSF48097; Regulator of G-protein signaling, RGS; 1.
DR   PROSITE; PS50195; PX; 1.
DR   PROSITE; PS51207; PXA; 1.
DR   PROSITE; PS50132; RGS; 1.
PE   2: Evidence at transcript level;
KW   Endosome; Lipid-binding; Membrane; Protein transport; Reference proteome;
KW   Signal transduction inhibitor; Transport.
FT   CHAIN           1..957
FT                   /note="Sorting nexin-13"
FT                   /id="PRO_0000236200"
FT   DOMAIN          97..284
FT                   /note="PXA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00147,
FT                   ECO:0000255|PROSITE-ProRule:PRU00553"
FT   DOMAIN          373..511
FT                   /note="RGS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT   DOMAIN          559..680
FT                   /note="PX"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT   BINDING         601
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         603
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         628
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         642
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"
SQ   SEQUENCE   957 AA;  110819 MW;  45621C3D6F9C1DF3 CRC64;
     MLTEASLSIW GWGSLGIVLF LITFGPFVIF YLAFYILCFV GGGLVVTLLY GKTNSEKYLE
     QCEHSFLPPT SSGVPKCLEE MKREARTIKI DRRLTGANII DEPLQQVIQF SLRDYVQYWY
     YTLSDDESFL LEIRQTLQNA LIQFATRSKE IDWQPYFTTR IVDDFGTHLR VFRKAQQRVT
     EKDDQVKGTA EDLVETFFEV EVEMEKDVCR DLVCTSPKDE EGFLRDLCEV LLYLLLPPGD
     FQSKIMRYFV REILARGILL PLINQLSDPD YINQYVIWMI RDSNCNYEAF MNIIKLSDNI
     GELEAVRDKA AEELQYLRSL DTAGDDINTI KNQINSLLFV KKVCDSRIQR LQSGKEINTV
     KLAANFGKLC TVPLDSILVD NVALQFFMDY MQQTGGQAHL FFWMTVEGYR VTAQQQLEVL
     SGRQRDGKQQ TNQTKGLLRA AAVGIYEQYL SEKASPRVTV DDYLVAKLAD TLNHEDPTPE
     IFDDIQRKVY ELMLRDERFY PSFRQNALYV RMLAELDMLK DPSFRGSDDG DGESFNGSPT
     GSINLSLDDL SSVTSDDSVQ LHAYISDTGV CNDHGKTYAL YAITVHRRNL NTEEMWKTYR
     RYSDFHDFHM RITEQFENLS SILKLPGKKT FNNMDRDFLE KRKKDLNAYL QLLLTPEMMK
     ASPALAHCVY DFLENKAYSK GKGDFARKMD TFVNPLRNSM RNVSNAVKSL PDSLAEGVTK
     MSDNVGRMSE RLGQDIKQSF FKVPPLITKT DSDPEHCRVS AQLDDNVDDN IPLRVMLLLM
     DEVFDLKERN QWLRRNIKNL LQQLIRATYG DTINRKIVDH VDWMTSPEQV ADSVKRFRDA
     FWPNGILAET VPCRDKAIRM RTRIAGKTKL FAIMPDELKH IIGAETTRKG ILRVFEMFQH
     NQLNRRMVYV FLEGFLETLF PQYKFRELFN KLHSRSKQMQ KYKQKLQSTQ APSLQKR
//