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 27-MAR-2024, entry version 183. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 86. DR IntAct; Q96RF0; 48. DR MINT; Q96RF0; -. DR STRING; 9606.ENSP00000342276; -. DR TCDB; 3.A.34.1.1; the sorting nexins of the escrt complexes (sn-escrt). 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; 9606-ENSP00000317332; -. DR PeptideAtlas; Q96RF0; -. DR ProteomicsDB; 43428; -. DR ProteomicsDB; 77957; -. [Q96RF0-1] DR ProteomicsDB; 77958; -. [Q96RF0-2] DR Pumba; Q96RF0; -. DR Antibodypedia; 23359; 225 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 AGR; HGNC:19245; -. 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; MGVNYCL; -. DR OrthoDB; 5401713at2759; -. DR PhylomeDB; Q96RF0; -. DR TreeFam; TF314082; -. DR PathwayCommons; Q96RF0; -. DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis. DR SignaLink; Q96RF0; -. DR BioGRID-ORCS; 112574; 12 hits in 1157 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 198 other cell types or tissues. DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:UniProtKB. DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; 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; Arfaptin homology (AH) domain/BAR domain; 1. DR Gene3D; 3.30.1520.10; Phox-like domain; 1. DR Gene3D; 2.30.30.40; SH3 Domains; 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; IPR035703; SNX18_PX. DR InterPro; IPR035557; SNX18_SH3. DR InterPro; IPR014536; Snx9_fam. DR InterPro; IPR019497; Sorting_nexin_WASP-bd-dom. DR PANTHER; PTHR45827; SORTING NEXIN; 1. DR PANTHER; PTHR45827:SF4; SORTING NEXIN-18; 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; SSF64268; PX domain; 1. DR SUPFAM; SSF50044; SH3-domain; 1. DR PROSITE; PS50195; PX; 1. DR PROSITE; PS50002; SH3; 1. DR Genevisible; Q96RF0; HS. 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 //