SNX18_MOUSE
ID SNX18_MOUSE Reviewed; 614 AA.
AC Q91ZR2;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Sorting nexin-18 {ECO:0000303|PubMed:26567222};
DE AltName: Full=Sorting nexin-associated Golgi protein 1 {ECO:0000303|Ref.1};
GN Name=Snx18 {ECO:0000303|PubMed:26567222, ECO:0000312|MGI:MGI:2137642};
GN Synonyms=Snag1 {ECO:0000303|Ref.1};
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 [MRNA].
RC STRAIN=C57BL/6J;
RA Cohn J.B., Bernstein A., Stanford W.L.;
RT "SNAG1, a novel SH3 and PX domain containing protein.";
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Pancreas, 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 INTERACTION WITH FCHSD1.
RX PubMed=26567222; DOI=10.1242/jcs.178699;
RA Ukken F.P., Bruckner J.J., Weir K.L., Hope S.J., Sison S.L.,
RA Birschbach R.M., Hicks L., Taylor K.L., Dent E.W., Gonsalvez G.B.,
RA O'Connor-Giles K.M.;
RT "BAR-SH3 sorting nexins are conserved interacting proteins of Nervous wreck
RT that organize synapses and promote neurotransmission.";
RL J. Cell Sci. 129:166-177(2016).
CC -!- FUNCTION: Involved in endocytosis and intracellular vesicle
CC trafficking, both during interphase and at the end of mitosis. Required
CC for efficient progress through mitosis and cytokinesis. Required for
CC normal formation of the cleavage furrow at the end of mitosis. Plays a
CC role in endocytosis via clathrin-coated pits, but also clathrin-
CC independent, actin-dependent fluid-phase endocytosis. Plays a role in
CC macropinocytosis. Binds to membranes enriched in phosphatidylinositol
CC 4,5-bisphosphate and promotes membrane tubulation. Stimulates the
CC GTPase activity of DNM2. Promotes DNM2 location at the plasma membrane.
CC Together with DNM2, involved in autophagosome assembly by regulating
CC trafficking from recycling endosomes of phospholipid scramblase ATG9A.
CC {ECO:0000250|UniProtKB:Q96RF0}.
CC -!- SUBUNIT: Heterodimer with SNX9. Interacts with ITCH. Interacts with
CC dynamin-2 (DNM2), SYNJ1 and WASL. Interacts with the AP-1 complex (By
CC similarity). Interacts with FCHSD1 (via the F-BAR domain)
CC (PubMed:26567222). {ECO:0000250|UniProtKB:Q96RF0,
CC ECO:0000269|PubMed:26567222}.
CC -!- INTERACTION:
CC Q91ZR2; P48023: FASLG; Xeno; NbExp=4; IntAct=EBI-6879954, EBI-495538;
CC -!- SUBCELLULAR LOCATION: Endomembrane system
CC {ECO:0000250|UniProtKB:Q96RF0}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q96RF0}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q96RF0}. Endosome membrane
CC {ECO:0000250|UniProtKB:Q96RF0}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q96RF0}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q96RF0}. Recycling endosome membrane
CC {ECO:0000250|UniProtKB:Q96RF0}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q96RF0}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q96RF0}. Cell membrane
CC {ECO:0000250|UniProtKB:Q96RF0}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q96RF0}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q96RF0}. Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:Q96RF0}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q96RF0}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q96RF0}. Note=Localized at sites of endocytosis
CC at the cell membrane. Detected on newly formed macropinosomes.
CC Partially colocalized with clathrin and dynamin at the cell membrane.
CC Transiently recruited to clathrin-coated pits at a late stage of
CC clathrin-coated vesicle formation. {ECO:0000250|UniProtKB:Q96RF0}.
CC -!- DOMAIN: The PX domain mediates interaction with membranes enriched in
CC phosphatidylinositol 4,5-bisphosphate. {ECO:0000250|UniProtKB:Q96RF0}.
CC -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
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DR EMBL; AF408408; AAL02105.1; -; mRNA.
DR AlphaFoldDB; Q91ZR2; -.
DR SMR; Q91ZR2; -.
DR IntAct; Q91ZR2; 2.
DR MINT; Q91ZR2; -.
DR STRING; 10090.ENSMUSP00000104864; -.
DR iPTMnet; Q91ZR2; -.
DR PhosphoSitePlus; Q91ZR2; -.
DR EPD; Q91ZR2; -.
DR jPOST; Q91ZR2; -.
DR MaxQB; Q91ZR2; -.
DR PeptideAtlas; Q91ZR2; -.
DR PRIDE; Q91ZR2; -.
DR ProteomicsDB; 261467; -.
DR MGI; MGI:2137642; Snx18.
DR eggNOG; KOG2528; Eukaryota.
DR InParanoid; Q91ZR2; -.
DR PhylomeDB; Q91ZR2; -.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR ChiTaRS; Snx18; mouse.
DR PRO; PR:Q91ZR2; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q91ZR2; protein.
DR GO; GO:0030136; C:clathrin-coated vesicle; ISO:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
DR GO; GO:0070062; C:extracellular exosome; ISO:MGI.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0030426; C:growth cone; IDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0055038; C:recycling endosome membrane; ISS:UniProtKB.
DR GO; GO:0035091; F:phosphatidylinositol binding; IDA:MGI.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISO:MGI.
DR GO; GO:0036089; P:cleavage furrow formation; ISO:MGI.
DR GO; GO:0006897; P:endocytosis; ISS:UniProtKB.
DR GO; GO:0016197; P:endosomal transport; ISO:MGI.
DR GO; GO:0000281; P:mitotic cytokinesis; ISO:MGI.
DR GO; GO:0097320; P:plasma membrane tubulation; IBA:GO_Central.
DR GO; GO:2000786; P:positive regulation of autophagosome assembly; ISS:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; ISS:UniProtKB.
DR CDD; cd07286; PX_SNX18; 1.
DR CDD; cd11897; SH3_SNX18; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR028646; SNX18.
DR InterPro; IPR035703; SNX18_PX.
DR InterPro; IPR035557; SNX18_SH3.
DR InterPro; IPR014536; Snx9_fam.
DR InterPro; IPR019497; Sorting_nexin_WASP-bd-dom.
DR PANTHER; PTHR45827:SF4; PTHR45827:SF4; 1.
DR Pfam; PF10456; BAR_3_WASP_bdg; 1.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF14604; SH3_9; 1.
DR PIRSF; PIRSF027744; Snx9; 1.
DR SMART; SM00312; PX; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50195; PX; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cell membrane; Cytoplasmic vesicle; Endocytosis;
KW Endosome; Lipid-binding; Membrane; Mitosis; Protein transport;
KW Reference proteome; SH3 domain; Transport.
FT CHAIN 1..614
FT /note="Sorting nexin-18"
FT /id="PRO_0000213867"
FT DOMAIN 1..61
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 266..376
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT DOMAIN 411..614
FT /note="BAR"
FT REGION 85..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..101
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 302
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5X1"
FT BINDING 304
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5X1"
FT BINDING 342
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5X1"
SQ SEQUENCE 614 AA; 67904 MW; BACED9D104571098 CRC64;
MALRARALYD FKSENPGEIS LREHEVLSLC SEQDIEGWLE GINSRGDRGL FPASYVQVIR
APEPGPPADG GPGAPARYAN VPPGGFEPLP AAPPAAFPPL LQPQASPGSF QPPGAGFPYG
GGALQPSPQQ LYGGYQASLG SDDDWDDEWD DSSTVADEPG ALGSGAYPDL DGSSSAGGGA
AGRYRLSTRS DLSLGSRGVS APPAPSVWSQ ELGHGEPQPQ SLLHLRQVGR GGLRAGRGVR
LREGWGQAVR GAGSYGPEWQ ENPYPFQCTI DDPTKQTKFK GMKSYISYKL VPTHTQVPVH
RRYKHFDWLY ARLAEKFPVI SVPHLPEKQA TGRFEEDFIS KRRKGLIWWM NHMASHPVLA
QCDVFQHFLT CPSSTDEKAW KQGKRKAEKD EMVGANFFLT LSTPPAAALD LQEVESKIDG
FKCFTKKMDD SALQLNHTAN EFARKQVTGF KKEYQKVGQS FRGLSQAFEL DQQAFSVGLN
QAIAFTGDAY DAIGELFAEQ PRQDLDPVMD LLALYQGHLA NFPDIIHVQK GALTKVKESR
RHVEEGKMEV QKADGIQDRC NTISFATLAE IHHFHQIRVR DFKSQMQHFL QQQIIFFQKV
TQKLEEALHK YDSV
