SNX13_MOUSE
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 03-AUG-2022, entry version 118.
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 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; Q6PHS6; -.
DR PRIDE; Q6PHS6; -.
DR ProteomicsDB; 261539; -.
DR DNASU; 217463; -.
DR GeneID; 217463; -.
DR KEGG; mmu:217463; -.
DR UCSC; uc011yli.1; mouse.
DR CTD; 23161; -.
DR MGI; MGI:2661416; Snx13.
DR eggNOG; KOG2101; Eukaryota.
DR InParanoid; Q6PHS6; -.
DR OMA; EWTPTNV; -.
DR OrthoDB; 187001at2759; -.
DR PhylomeDB; Q6PHS6; -.
DR BioGRID-ORCS; 217463; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Snx13; mouse.
DR PRO; PR:Q6PHS6; -.
DR Proteomes; UP000000589; Unplaced.
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:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
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 GO; GO:0043547; P:positive regulation of GTPase activity; ISO:MGI.
DR CDD; cd06873; PX_SNX13; 1.
DR CDD; cd08719; RGS_SNX13; 1.
DR Gene3D; 1.10.167.10; -; 1.
DR Gene3D; 3.30.1520.10; -; 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 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; SSF48097; SSF48097; 1.
DR SUPFAM; SSF64268; SSF64268; 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
