{"metadata":{"accession":"cd21670","entry_id":null,"type":"domain","go_terms":null,"source_database":"cdd","member_databases":null,"integrated":null,"hierarchy":null,"name":{"name":"synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain of the extended synaptotagmin (E-Syt) family","short":"SMP_ESyt"},"description":[{"text":"<p>The extended synaptotagmin (E-Syt) family includes a group of Ca2+-regulated intrinsic membrane proteins, such as E-Syt1, E-Syt2 and E-Syt3. They are composed of an N-terminal endoplasmic reticulum (ER)-membrane anchor, a central SMP-domain, and five (E-Syt1) or three C-terminal cytoplasmic C2-domains (E-Syt2 and E-Syt3). The ER-membrane anchor and C2 domains are required for tethering, while the SMP domain is a lipid-binding domain that links the ER with other lipid bilayer-membranes within the cell. This model corresponds to the SMP domain, which has a beta-barrel structure like protein modules in the tubular-lipid-binding (TULIP) superfamily. It dimerizes to form an approximately 90-Angstrom-long cylinder traversed by a channel lined entirely with hydrophobic residues. The following two C2 domains then form arched structures flexibly linked to the SMP domain. [[cite:PUB00075878], [cite:PUB00148191], [cite:PUB00148192], [cite:PUB00148193], [cite:PUB00148197], [cite:PUB00148194], [cite:PUB00145852], [cite:PUB00148195], [cite:PUB00148196], [cite:PUB00093119], [cite:PUB00148190], [cite:PUB00087567], [cite:PUB00146909], [cite:PUB00146903], [cite:PUB00146904], [cite:PUB00146905], [cite:PUB00146906], [cite:PUB00060834], [cite:PUB00111794], [cite:PUB00146907], [cite:PUB00146908], [cite:PUB00092089]]</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00148197":{"PMID":32879390,"ISBN":null,"volume":"10","issue":"1","year":2020,"title":"The short isoform of extended synaptotagmin-2 controls Ca<sup>2+</sup> dynamics in T cells via interaction with STIM1.","URL":null,"raw_pages":"14433","medline_journal":"Sci Rep","ISO_journal":"Sci Rep","authors":["Woo JS","Sun Z","Srikanth S","Gwack Y."],"DOI_URL":null},"PUB00146903":{"PMID":18977228,"ISBN":null,"volume":"582","issue":"28","year":2008,"title":"Structural characterization of soluble E-Syt2.","URL":null,"raw_pages":"3941-7","medline_journal":"FEBS Lett","ISO_journal":"FEBS Lett","authors":["Groer GJ","Haslbeck M","Roessle M","Gessner A."],"DOI_URL":null},"PUB00148195":{"PMID":30589572,"ISBN":null,"volume":"33","issue":"4","year":2019,"title":"Feedback regulation of insulin secretion by extended synaptotagmin-1.","URL":null,"raw_pages":"4716-4728","medline_journal":"FASEB J","ISO_journal":"FASEB J","authors":["Xie B","Nguyen PM","Idevall-Hagren O."],"DOI_URL":null},"PUB00148192":{"PMID":29046455,"ISBN":null,"volume":"92","issue":"1","year":2018,"title":"Extended Synaptotagmin 1 Interacts with Herpes Simplex Virus 1 Glycoprotein M and Negatively Modulates Virus-Induced Membrane Fusion. 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E-Syt2.","URL":null,"raw_pages":"269-80","medline_journal":"Structure","ISO_journal":"Structure","authors":["Xu J","Bacaj T","Zhou A","Tomchick DR","Sudhof TC","Rizo J."],"DOI_URL":null},"PUB00146906":{"PMID":20833364,"ISBN":null,"volume":"19","issue":"3","year":2010,"title":"Extended-synaptotagmin-2 mediates FGF receptor endocytosis and ERK activation in vivo.","URL":null,"raw_pages":"426-39","medline_journal":"Dev Cell","ISO_journal":"Dev Cell","authors":["Jean S","Mikryukov A","Tremblay MG","Baril J","Guillou F","Bellenfant S","Moss T."],"DOI_URL":null},"PUB00146909":{"PMID":17360437,"ISBN":null,"volume":"104","issue":"10","year":2007,"title":"E-Syts, a family of membranous Ca2+-sensor proteins with multiple C2 domains.","URL":null,"raw_pages":"3823-8","medline_journal":"Proc Natl Acad Sci U S A","ISO_journal":"Proc Natl Acad Sci U S A","authors":["Min SW","Chang WP","Sudhof 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