1pd1 is a 2 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
SEC24_YEAST Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. SEC24 specifically recruits cargo proteins like BET1 or SYS1 to the COPII vesicles. The SEC23/24 complex is also involved in internalisation of plasma membrane proteins like the maltose transporter.[1][2][3][4][5][6][7][8][9][10][11][12][13]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
↑Bednarek SY, Ravazzola M, Hosobuchi M, Amherdt M, Perrelet A, Schekman R, Orci L. COPI- and COPII-coated vesicles bud directly from the endoplasmic reticulum in yeast. Cell. 1995 Dec 29;83(7):1183-96. PMID:8548805
↑Campbell JL, Schekman R. Selective packaging of cargo molecules into endoplasmic reticulum-derived COPII vesicles. Proc Natl Acad Sci U S A. 1997 Feb 4;94(3):837-42. PMID:9023343
↑Kuehn MJ, Herrmann JM, Schekman R. COPII-cargo interactions direct protein sorting into ER-derived transport vesicles. Nature. 1998 Jan 8;391(6663):187-90. PMID:9428766 doi:https://dx.doi.org/10.1038/34438
↑Penalver E, Lucero P, Moreno E, Lagunas R. Clathrin and two components of the COPII complex, Sec23p and Sec24p, could be involved in endocytosis of the Saccharomyces cerevisiae maltose transporter. J Bacteriol. 1999 Apr;181(8):2555-63. PMID:10198022
↑Peng R, De Antoni A, Gallwitz D. Evidence for overlapping and distinct functions in protein transport of coat protein Sec24p family members. J Biol Chem. 2000 Apr 14;275(15):11521-8. PMID:10753972
↑Higashio H, Kimata Y, Kiriyama T, Hirata A, Kohno K. Sfb2p, a yeast protein related to Sec24p, can function as a constituent of COPII coats required for vesicle budding from the endoplasmic reticulum. J Biol Chem. 2000 Jun 9;275(23):17900-8. PMID:10749860 doi:https://dx.doi.org/10.1074/jbc.M000751200
↑Shimoni Y, Kurihara T, Ravazzola M, Amherdt M, Orci L, Schekman R. Lst1p and Sec24p cooperate in sorting of the plasma membrane ATPase into COPII vesicles in Saccharomyces cerevisiae. J Cell Biol. 2000 Nov 27;151(5):973-84. PMID:11086000
↑Matsuoka K, Schekman R. The use of liposomes to study COPII- and COPI-coated vesicle formation and membrane protein sorting. Methods. 2000 Apr;20(4):417-28. PMID:10720463 doi:10.1006/meth.2000.0955
↑Kurihara T, Hamamoto S, Gimeno RE, Kaiser CA, Schekman R, Yoshihisa T. Sec24p and Iss1p function interchangeably in transport vesicle formation from the endoplasmic reticulum in Saccharomyces cerevisiae. Mol Biol Cell. 2000 Mar;11(3):983-98. PMID:10712514
↑Miller EA, Beilharz TH, Malkus PN, Lee MC, Hamamoto S, Orci L, Schekman R. Multiple cargo binding sites on the COPII subunit Sec24p ensure capture of diverse membrane proteins into transport vesicles. Cell. 2003 Aug 22;114(4):497-509. PMID:12941277
↑Hamasaki M, Noda T, Ohsumi Y. The early secretory pathway contributes to autophagy in yeast. Cell Struct Funct. 2003 Feb;28(1):49-54. PMID:12655150
↑Sato K, Nakano A. Reconstitution of coat protein complex II (COPII) vesicle formation from cargo-reconstituted proteoliposomes reveals the potential role of GTP hydrolysis by Sar1p in protein sorting. J Biol Chem. 2004 Jan 9;279(2):1330-5. Epub 2003 Nov 19. PMID:14627716 doi:10.1074/jbc.C300457200
↑Schuldiner M, Collins SR, Thompson NJ, Denic V, Bhamidipati A, Punna T, Ihmels J, Andrews B, Boone C, Greenblatt JF, Weissman JS, Krogan NJ. Exploration of the function and organization of the yeast early secretory pathway through an epistatic miniarray profile. Cell. 2005 Nov 4;123(3):507-19. PMID:16269340 doi:S0092-8674(05)00868-8
