SNX18_HUMAN
ID SNX18_HUMAN Reviewed; 628 AA.
AC Q96RF0; B4E2B3; H7BXX3; Q05BB3; Q0VG02;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Sorting nexin-18 {ECO:0000303|PubMed:18411244};
DE AltName: Full=SH3 and PX domain-containing protein 3B;
GN Name=SNX18 {ECO:0000303|PubMed:18411244, ECO:0000312|HGNC:HGNC:19245};
GN Synonyms=SH3PXD3B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ASP-571.
RC TISSUE=Cerebellum;
RA Hong W.;
RT "A novel SH3-, Pro-rich-, and PX-domain protein of the sorting nexin
RT family.";
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT ASP-571.
RC TISSUE=Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP THR-593.
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).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH THE AP-1 COMPLEX, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18411244; DOI=10.1242/jcs.028530;
RA Haberg K., Lundmark R., Carlsson S.R.;
RT "SNX18 is an SNX9 paralog that acts as a membrane tubulator in AP-1-
RT positive endosomal trafficking.";
RL J. Cell Sci. 121:1495-1505(2008).
RN [7]
RP INTERACTION WITH ITCH.
RX PubMed=20491914; DOI=10.1111/j.1742-4658.2010.07698.x;
RA Baumann C., Lindholm C.K., Rimoldi D., Levy F.;
RT "The E3 ubiquitin ligase Itch regulates sorting nexin 9 through an
RT unconventional substrate recognition domain.";
RL FEBS J. 277:2803-2814(2010).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH DNM2; WASL AND SYNJ1, AND
RP SUBUNIT.
RX PubMed=20427313; DOI=10.1242/jcs.064170;
RA Park J., Kim Y., Lee S., Park J.J., Park Z.Y., Sun W., Kim H., Chang S.;
RT "SNX18 shares a redundant role with SNX9 and modulates endocytic
RT trafficking at the plasma membrane.";
RL J. Cell Sci. 123:1742-1750(2010).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21048941; DOI=10.1371/journal.pone.0013763;
RA Wang J.T., Kerr M.C., Karunaratne S., Jeanes A., Yap A.S., Teasdale R.D.;
RT "The SNX-PX-BAR family in macropinocytosis: the regulation of macropinosome
RT formation by SNX-PX-BAR proteins.";
RL PLoS ONE 5:E13763-E13763(2010).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22718350; DOI=10.1242/jcs.105981;
RA Ma M.P., Chircop M.;
RT "SNX9, SNX18 and SNX33 are required for progression through and completion
RT of mitosis.";
RL J. Cell Sci. 125:4372-4382(2012).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH DNM2.
RX PubMed=29437695; DOI=10.15252/embr.201744837;
RA Soereng K., Munson M.J., Lamb C.A., Bjoerndal G.T., Pankiv S.,
RA Carlsson S.R., Tooze S.A., Simonsen A.;
RT "SNX18 regulates ATG9A trafficking from recycling endosomes by recruiting
RT Dynamin-2.";
RL EMBO Rep. 19:0-0(2018).
CC -!- FUNCTION: Involved in endocytosis and intracellular vesicle
CC trafficking, both during interphase and at the end of mitosis
CC (PubMed:20427313, PubMed:18411244, PubMed:21048941, PubMed:22718350).
CC Required for efficient progress through mitosis and cytokinesis
CC (PubMed:22718350). Required for normal formation of the cleavage furrow
CC at the end of mitosis (PubMed:22718350). Plays a role in endocytosis
CC via clathrin-coated pits, but also clathrin-independent, actin-
CC dependent fluid-phase endocytosis (PubMed:20427313). Plays a role in
CC macropinocytosis (PubMed:21048941). Binds to membranes enriched in
CC phosphatidylinositol 4,5-bisphosphate and promotes membrane tubulation
CC (PubMed:18411244). Stimulates the GTPase activity of DNM2
CC (PubMed:20427313). Promotes DNM2 location at the plasma membrane
CC (PubMed:20427313). Together with DNM2, involved in autophagosome
CC assembly by regulating trafficking from recycling endosomes of
CC phospholipid scramblase ATG9A (PubMed:29437695).
CC {ECO:0000269|PubMed:18411244, ECO:0000269|PubMed:20427313,
CC ECO:0000269|PubMed:21048941, ECO:0000269|PubMed:22718350,
CC ECO:0000269|PubMed:29437695}.
CC -!- SUBUNIT: Heterodimer with SNX9 (PubMed:20427313). Interacts with ITCH
CC (PubMed:20491914). Interacts with dynamin-2 (DNM2), SYNJ1 and WASL
CC (PubMed:20427313, PubMed:29437695). Interacts with the AP-1 complex
CC (PubMed:18411244). Interacts with FCHSD1 (via the F-BAR domain) (By
CC similarity). {ECO:0000250|UniProtKB:Q91ZR2,
CC ECO:0000269|PubMed:18411244, ECO:0000269|PubMed:20427313,
CC ECO:0000269|PubMed:20491914, ECO:0000269|PubMed:29437695}.
CC -!- INTERACTION:
CC Q96RF0; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-298169, EBI-11096309;
CC Q96RF0; O14672: ADAM10; NbExp=2; IntAct=EBI-298169, EBI-1536151;
CC Q96RF0; Q13443: ADAM9; NbExp=2; IntAct=EBI-298169, EBI-77903;
CC Q96RF0; Q8N684-3: CPSF7; NbExp=3; IntAct=EBI-298169, EBI-11523759;
CC Q96RF0; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-298169, EBI-3867333;
CC Q96RF0; Q7L190: DPPA4; NbExp=3; IntAct=EBI-298169, EBI-710457;
CC Q96RF0; Q08379: GOLGA2; NbExp=3; IntAct=EBI-298169, EBI-618309;
CC Q96RF0; O75031: HSF2BP; NbExp=3; IntAct=EBI-298169, EBI-7116203;
CC Q96RF0; Q16082: HSPB2; NbExp=3; IntAct=EBI-298169, EBI-739395;
CC Q96RF0; O75525: KHDRBS3; NbExp=3; IntAct=EBI-298169, EBI-722504;
CC Q96RF0; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-298169, EBI-11959885;
CC Q96RF0; Q99750: MDFI; NbExp=3; IntAct=EBI-298169, EBI-724076;
CC Q96RF0; Q4VC12: MSS51; NbExp=3; IntAct=EBI-298169, EBI-11599933;
CC Q96RF0; Q16825: PTPN21; NbExp=3; IntAct=EBI-298169, EBI-2860264;
CC Q96RF0; Q9BXF6: RAB11FIP5; NbExp=3; IntAct=EBI-298169, EBI-1387068;
CC Q96RF0; B2RXF5: ZBTB42; NbExp=3; IntAct=EBI-298169, EBI-12287587;
CC -!- SUBCELLULAR LOCATION: Endomembrane system
CC {ECO:0000269|PubMed:22718350}; Peripheral membrane protein
CC {ECO:0000269|PubMed:18411244}; Cytoplasmic side
CC {ECO:0000269|PubMed:18411244}. Endosome membrane
CC {ECO:0000269|PubMed:29437695}; Peripheral membrane protein
CC {ECO:0000269|PubMed:18411244}; Cytoplasmic side
CC {ECO:0000269|PubMed:18411244}. Recycling endosome membrane
CC {ECO:0000269|PubMed:29437695}; Peripheral membrane protein
CC {ECO:0000269|PubMed:18411244}; Cytoplasmic side
CC {ECO:0000269|PubMed:18411244}. Cell membrane
CC {ECO:0000269|PubMed:20427313}; Peripheral membrane protein
CC {ECO:0000269|PubMed:18411244}; Cytoplasmic side
CC {ECO:0000269|PubMed:18411244}. Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:18411244}; Peripheral membrane protein
CC {ECO:0000269|PubMed:18411244}; Cytoplasmic side
CC {ECO:0000269|PubMed:18411244}. Note=Localized at sites of endocytosis
CC at the cell membrane (PubMed:18411244). Detected on newly formed
CC macropinosomes (PubMed:21048941). Partially colocalized with clathrin
CC and dynamin at the cell membrane (PubMed:20427313). Transiently
CC recruited to clathrin-coated pits at a late stage of clathrin-coated
CC vesicle formation (PubMed:18411244). {ECO:0000269|PubMed:18411244,
CC ECO:0000269|PubMed:20427313, ECO:0000269|PubMed:21048941}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q96RF0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96RF0-2; Sequence=VSP_035839;
CC Name=3;
CC IsoId=Q96RF0-3; Sequence=VSP_045476;
CC -!- DOMAIN: The PX domain mediates interaction with membranes enriched in
CC phosphatidylinositol 4,5-bisphosphate. {ECO:0000269|PubMed:18411244}.
CC -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
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DR EMBL; AF395536; AAK82415.1; -; mRNA.
DR EMBL; AK304195; BAG65075.1; -; mRNA.
DR EMBL; AC091888; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471123; EAW54894.1; -; Genomic_DNA.
DR EMBL; BC060791; AAH60791.1; -; mRNA.
DR EMBL; BC067860; AAH67860.1; -; mRNA.
DR EMBL; BC117218; AAI17219.1; -; mRNA.
DR EMBL; BC117220; AAI17221.1; -; mRNA.
DR CCDS; CCDS3962.1; -. [Q96RF0-1]
DR CCDS; CCDS43317.1; -. [Q96RF0-2]
DR CCDS; CCDS54851.1; -. [Q96RF0-3]
DR RefSeq; NP_001096045.1; NM_001102575.1. [Q96RF0-2]
DR RefSeq; NP_001138899.1; NM_001145427.1. [Q96RF0-3]
DR RefSeq; NP_443102.2; NM_052870.2. [Q96RF0-1]
DR AlphaFoldDB; Q96RF0; -.
DR SMR; Q96RF0; -.
DR BioGRID; 125193; 81.
DR IntAct; Q96RF0; 47.
DR MINT; Q96RF0; -.
DR STRING; 9606.ENSP00000317332; -.
DR iPTMnet; Q96RF0; -.
DR MetOSite; Q96RF0; -.
DR PhosphoSitePlus; Q96RF0; -.
DR BioMuta; SNX18; -.
DR DMDM; 215273942; -.
DR EPD; Q96RF0; -.
DR jPOST; Q96RF0; -.
DR MassIVE; Q96RF0; -.
DR MaxQB; Q96RF0; -.
DR PaxDb; Q96RF0; -.
DR PeptideAtlas; Q96RF0; -.
DR PRIDE; Q96RF0; -.
DR ProteomicsDB; 43428; -.
DR ProteomicsDB; 77957; -. [Q96RF0-1]
DR ProteomicsDB; 77958; -. [Q96RF0-2]
DR Antibodypedia; 23359; 214 antibodies from 32 providers.
DR DNASU; 112574; -.
DR Ensembl; ENST00000326277.5; ENSP00000317332.4; ENSG00000178996.14. [Q96RF0-3]
DR Ensembl; ENST00000343017.11; ENSP00000342276.7; ENSG00000178996.14. [Q96RF0-1]
DR Ensembl; ENST00000381410.5; ENSP00000370817.4; ENSG00000178996.14. [Q96RF0-2]
DR GeneID; 112574; -.
DR KEGG; hsa:112574; -.
DR MANE-Select; ENST00000381410.5; ENSP00000370817.4; NM_001102575.2; NP_001096045.1. [Q96RF0-2]
DR UCSC; uc003jpi.5; human. [Q96RF0-1]
DR CTD; 112574; -.
DR DisGeNET; 112574; -.
DR GeneCards; SNX18; -.
DR HGNC; HGNC:19245; SNX18.
DR HPA; ENSG00000178996; Tissue enhanced (bone).
DR neXtProt; NX_Q96RF0; -.
DR OpenTargets; ENSG00000178996; -.
DR PharmGKB; PA162404304; -.
DR VEuPathDB; HostDB:ENSG00000178996; -.
DR eggNOG; KOG2528; Eukaryota.
DR GeneTree; ENSGT00940000157724; -.
DR HOGENOM; CLU_021494_1_0_1; -.
DR InParanoid; Q96RF0; -.
DR OMA; DGINDRC; -.
DR OrthoDB; 811995at2759; -.
DR PhylomeDB; Q96RF0; -.
DR TreeFam; TF314082; -.
DR PathwayCommons; Q96RF0; -.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR SignaLink; Q96RF0; -.
DR BioGRID-ORCS; 112574; 10 hits in 1080 CRISPR screens.
DR ChiTaRS; SNX18; human.
DR GeneWiki; SNAG1; -.
DR GenomeRNAi; 112574; -.
DR Pharos; Q96RF0; Tbio.
DR PRO; PR:Q96RF0; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q96RF0; protein.
DR Bgee; ENSG00000178996; Expressed in epithelial cell of pancreas and 196 other tissues.
DR Genevisible; Q96RF0; HS.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0055038; C:recycling endosome membrane; IMP:UniProtKB.
DR GO; GO:0035091; F:phosphatidylinositol binding; IBA:GO_Central.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:FlyBase.
DR GO; GO:0036089; P:cleavage furrow formation; IMP:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IDA:UniProtKB.
DR GO; GO:0016197; P:endosomal transport; IMP:UniProtKB.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:UniProtKB.
DR GO; GO:0097320; P:plasma membrane tubulation; IBA:GO_Central.
DR GO; GO:2000786; P:positive regulation of autophagosome assembly; IMP:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA:UniProtKB.
DR GO; GO:0015031; P:protein transport; IMP:UniProtKB.
DR CDD; cd07286; PX_SNX18; 1.
DR CDD; cd11897; SH3_SNX18; 1.
DR DisProt; DP02309; -.
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 Alternative splicing; Cell cycle; Cell division; Cell membrane;
KW Cytoplasmic vesicle; Endocytosis; Endosome; Lipid-binding; Membrane;
KW Mitosis; Protein transport; Reference proteome; SH3 domain; Transport.
FT CHAIN 1..628
FT /note="Sorting nexin-18"
FT /id="PRO_0000213866"
FT DOMAIN 1..61
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 276..386
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT DOMAIN 421..628
FT /note="BAR"
FT REGION 62..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..100
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 312
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 314
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 352
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 VAR_SEQ 542..628
FT /note="KAWPLEQVIWSVLCRLKGATLTAVPLWVSESYSTGEEASRDVDAWVFSLECK
FT LDCSTGSFLLEYLALGNEYSFSKVQRVPLMTVLSF -> ALTKVKESRRHVEEGKMEVQ
FT KADGIQDRCNTISFATLAEIHHFHQIRVRDFKSQMQHFLQQQIIFFQKVTQKLEEALHK
FT YDSV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_035839"
FT VAR_SEQ 592..628
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045476"
FT VARIANT 571
FT /note="E -> D (in dbSNP:rs2548612)"
FT /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.1"
FT /id="VAR_052480"
FT VARIANT 593
FT /note="K -> T (in dbSNP:rs13162502)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_052481"
FT CONFLICT 32
FT /note="E -> G (in Ref. 2; BAG65075)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 628 AA; 68894 MW; BE7B16835BA80F9C CRC64;
MALRARALYD FRSENPGEIS LREHEVLSLC SEQDIEGWLE GVNSRGDRGL FPASYVQVIR
APEPGPAGDG GPGAPARYAN VPPGGFEPLP VAPPASFKPP PDAFQALLQP QQAPPPSTFQ
PPGAGFPYGG GALQPSPQQL YGGYQASQGS DDDWDDEWDD SSTVADEPGA LGSGAYPDLD
GSSSAGVGAA GRYRLSTRSD LSLGSRGGSV PPQHHPSGPK SSATVSRNLN RFSTFVKSGG
EAFVLGEASG FVKDGDKLCV VLGPYGPEWQ 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
GKAWPLEQVI WSVLCRLKGA TLTAVPLWVS ESYSTGEEAS RDVDAWVFSL ECKLDCSTGS
FLLEYLALGN EYSFSKVQRV PLMTVLSF
