SEC24_YEAST
ID SEC24_YEAST Reviewed; 926 AA.
AC P40482; D6VVH8;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Protein transport protein SEC24;
DE AltName: Full=Abnormal nuclear morphology 1;
GN Name=SEC24; Synonyms=ANU1; OrderedLocusNames=YIL109C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP PROTEIN SEQUENCE OF 731-740 AND 774-793, INTERACTION WITH SED5, AND
RP MUTAGENESIS OF CYS-231.
RX PubMed=10097109; DOI=10.1073/pnas.96.7.3751;
RA Peng R., Grabowski R., De Antoni A., Gallwitz D.;
RT "Specific interaction of the yeast cis-Golgi syntaxin Sed5p and the coat
RT protein complex II component Sec24p of endoplasmic reticulum-derived
RT transport vesicles.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:3751-3756(1999).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8548805; DOI=10.1016/0092-8674(95)90144-2;
RA Bednarek S.Y., Ravazzola M., Hosobuchi M., Amherdt M., Perrelet A.,
RA Schekman R.W., Orci L.;
RT "COPI- and COPII-coated vesicles bud directly from the endoplasmic
RT reticulum in yeast.";
RL Cell 83:1183-1196(1995).
RN [6]
RP INTERACTION WITH SEC16.
RX PubMed=8930902; DOI=10.1091/mbc.7.11.1815;
RA Gimeno R.E., Espenshade P.J., Kaiser C.A.;
RT "COPII coat subunit interactions: Sec24p and Sec23p bind to adjacent
RT regions of Sec16p.";
RL Mol. Biol. Cell 7:1815-1823(1996).
RN [7]
RP IDENTIFICATION IN THE COPII COAT, AND INTERACTION WITH SEC16.
RX PubMed=9325247; DOI=10.1074/jbc.272.41.25413;
RA Shaywitz D.A., Espenshade P.J., Gimeno R.E., Kaiser C.A.;
RT "COPII subunit interactions in the assembly of the vesicle coat.";
RL J. Biol. Chem. 272:25413-25416(1997).
RN [8]
RP FUNCTION.
RX PubMed=9023343; DOI=10.1073/pnas.94.3.837;
RA Campbell J.L., Schekman R.W.;
RT "Selective packaging of cargo molecules into endoplasmic reticulum-derived
RT COPII vesicles.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:837-842(1997).
RN [9]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=9568718; DOI=10.1016/s0092-8674(00)81577-9;
RA Matsuoka K., Orci L., Amherdt M., Bednarek S.Y., Hamamoto S.,
RA Schekman R.W., Yeung T.;
RT "COPII-coated vesicle formation reconstituted with purified coat proteins
RT and chemically defined liposomes.";
RL Cell 93:263-275(1998).
RN [10]
RP FUNCTION OF THE SEC23/24 COMPLEX.
RX PubMed=9428766; DOI=10.1038/34438;
RA Kuehn M.J., Herrmann J.M., Schekman R.W.;
RT "COPII-cargo interactions direct protein sorting into ER-derived transport
RT vesicles.";
RL Nature 391:187-190(1998).
RN [11]
RP INTERACTION WITH BET1; BOS1; SAR1 AND SEC23.
RX PubMed=9685263; DOI=10.1126/science.281.5377.698;
RA Springer S., Schekman R.W.;
RT "Nucleation of COPII vesicular coat complex by endoplasmic reticulum to
RT Golgi vesicle SNAREs.";
RL Science 281:698-700(1998).
RN [12]
RP FUNCTION OF THE SEC23/24 COMPLEX.
RX PubMed=10198022; DOI=10.1128/jb.181.8.2555-2563.1999;
RA Penalver E., Lucero P., Moreno E., Lagunas R.;
RT "Clathrin and two components of the COPII complex, Sec23p and Sec24p, could
RT be involved in endocytosis of the Saccharomyces cerevisiae maltose
RT transporter.";
RL J. Bacteriol. 181:2555-2563(1999).
RN [13]
RP INTERACTION WITH SHR3.
RX PubMed=10564255; DOI=10.1091/mbc.10.11.3549;
RA Gilstring C.F., Melin-Larsson M., Ljungdahl P.O.;
RT "Shr3p mediates specific COPII coatomer-cargo interactions required for the
RT packaging of amino acid permeases into ER-derived transport vesicles.";
RL Mol. Biol. Cell 10:3549-3565(1999).
RN [14]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10753972; DOI=10.1074/jbc.275.15.11521;
RA Peng R., De Antoni A., Gallwitz D.;
RT "Evidence for overlapping and distinct functions in protein transport of
RT coat protein Sec24p family members.";
RL J. Biol. Chem. 275:11521-11528(2000).
RN [15]
RP FUNCTION.
RX PubMed=10749860; DOI=10.1074/jbc.m000751200;
RA Higashio H., Kimata Y., Kiriyama T., Hirata A., Kohno K.;
RT "Sfb2p, a yeast protein related to Sec24p, can function as a constituent of
RT COPII coats required for vesicle budding from the endoplasmic reticulum.";
RL J. Biol. Chem. 275:17900-17908(2000).
RN [16]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PMA1.
RX PubMed=11086000; DOI=10.1083/jcb.151.5.973;
RA Shimoni Y., Kurihara T., Ravazzola M., Amherdt M., Orci L., Schekman R.W.;
RT "Lst1p and Sec24p cooperate in sorting of the plasma membrane ATPase into
RT COPII vesicles in Saccharomyces cerevisiae.";
RL J. Cell Biol. 151:973-984(2000).
RN [17]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10720463; DOI=10.1006/meth.2000.0955;
RA Matsuoka K., Schekman R.W.;
RT "The use of liposomes to study COPII- and COPI-coated vesicle formation and
RT membrane protein sorting.";
RL Methods 20:417-428(2000).
RN [18]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10712514; DOI=10.1091/mbc.11.3.983;
RA Kurihara T., Hamamoto S., Gimeno R.E., Kaiser C.A., Schekman R.W.,
RA Yoshihisa T.;
RT "Sec24p and Iss1p function interchangeably in transport vesicle formation
RT from the endoplasmic reticulum in Saccharomyces cerevisiae.";
RL Mol. Biol. Cell 11:983-998(2000).
RN [19]
RP INTERACTION WITH SYS1.
RX PubMed=11726510; DOI=10.1093/emboj/20.23.6742;
RA Votsmeier C., Gallwitz D.;
RT "An acidic sequence of a putative yeast Golgi membrane protein binds COPII
RT and facilitates ER export.";
RL EMBO J. 20:6742-6750(2001).
RN [20]
RP INTERACTION WITH EMP24 AND ERV25.
RX PubMed=11560939; DOI=10.1074/jbc.m108113200;
RA Belden W.J., Barlowe C.;
RT "Distinct roles for the cytoplasmic tail sequences of Emp24p and Erv25p in
RT transport between the endoplasmic reticulum and Golgi complex.";
RL J. Biol. Chem. 276:43040-43048(2001).
RN [21]
RP IDENTIFICATION IN THE COPII COAT.
RX PubMed=11389436; DOI=10.1038/35078500;
RA Antonny B., Madden D.T., Hamamoto S., Orci L., Schekman R.W.;
RT "Dynamics of the COPII coat with GTP and stable analogues.";
RL Nat. Cell Biol. 3:531-537(2001).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [23]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [24]
RP ELECTRON MICROSCOPY OF THE SEC23/24 COMPLEX.
RX PubMed=11535824; DOI=10.1073/pnas.191359398;
RA Lederkremer G.Z., Cheng Y., Petre B.M., Vogan E., Springer S.,
RA Schekman R.W., Walz T., Kirchhausen T.;
RT "Structure of the Sec23p/24p and Sec13p/31p complexes of COPII.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:10704-10709(2001).
RN [25]
RP ELECTRON MICROSCOPY OF THE SEC23/24 COMPLEX.
RX PubMed=11717432; DOI=10.1073/pnas.241522198;
RA Matsuoka K., Schekman R.W., Orci L., Heuser J.E.;
RT "Surface structure of the COPII-coated vesicle.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:13705-13709(2001).
RN [26]
RP SUBCELLULAR LOCATION.
RX PubMed=12235121; DOI=10.1083/jcb.200207053;
RA Supek F., Madden D.T., Hamamoto S., Orci L., Schekman R.W.;
RT "Sec16p potentiates the action of COPII proteins to bud transport
RT vesicles.";
RL J. Cell Biol. 158:1029-1038(2002).
RN [27]
RP STRUCTURE OF THE COPII COMPLEX.
RX PubMed=12671686; DOI=10.1038/sj.embor.embor812;
RA Antonny B., Gounon P., Schekman R.W., Orci L.;
RT "Self-assembly of minimal COPII cages.";
RL EMBO Rep. 4:419-424(2003).
RN [28]
RP FUNCTION, INTERACTION WITH BET1 AND SYS1, AND MUTAGENESIS OF ARG-230;
RP ARG-235; ARG-559; ARG-561 AND LEU-616.
RX PubMed=12941277; DOI=10.1016/s0092-8674(03)00609-3;
RA Miller E.A., Beilharz T.H., Malkus P.N., Lee M.C.S., Hamamoto S., Orci L.,
RA Schekman R.W.;
RT "Multiple cargo binding sites on the COPII subunit Sec24p ensure capture of
RT diverse membrane proteins into transport vesicles.";
RL Cell 114:497-509(2003).
RN [29]
RP FUNCTION.
RX PubMed=12655150; DOI=10.1247/csf.28.49;
RA Hamasaki M., Noda T., Ohsumi Y.;
RT "The early secretory pathway contributes to autophagy in yeast.";
RL Cell Struct. Funct. 28:49-54(2003).
RN [30]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [31]
RP INTERACTION WITH SEC23.
RX PubMed=12778054; DOI=10.1038/ncb1003;
RA Cohen M., Stutz F., Belgareh N., Haguenauer-Tsapis R., Dargemont C.;
RT "Ubp3 requires a cofactor, Bre5, to specifically de-ubiquitinate the COPII
RT protein, Sec23.";
RL Nat. Cell Biol. 5:661-667(2003).
RN [32]
RP COPII COMPLEX ASSEMBLY, AND FUNCTION OF THE COPII COMPLEX.
RX PubMed=14627716; DOI=10.1074/jbc.c300457200;
RA Sato K., Nakano A.;
RT "Reconstitution of coat protein complex II (COPII) vesicle formation from
RT cargo-reconstituted proteoliposomes reveals the potential role of GTP
RT hydrolysis by Sar1p in protein sorting.";
RL J. Biol. Chem. 279:1330-1335(2004).
RN [33]
RP FUNCTION, AND INTERACTION WITH GRH1.
RX PubMed=16269340; DOI=10.1016/j.cell.2005.08.031;
RA Schuldiner M., Collins S.R., Thompson N.J., Denic V., Bhamidipati A.,
RA Punna T., Ihmels J., Andrews B., Boone C., Greenblatt J.F., Weissman J.S.,
RA Krogan N.J.;
RT "Exploration of the function and organization of the yeast early secretory
RT pathway through an epistatic miniarray profile.";
RL Cell 123:507-519(2005).
RN [34]
RP INTERACTION WITH GHR1.
RX PubMed=17261844; DOI=10.1083/jcb.200607151;
RA Behnia R., Barr F.A., Flanagan J.J., Barlowe C., Munro S.;
RT "The yeast orthologue of GRASP65 forms a complex with a coiled-coil protein
RT that contributes to ER to Golgi traffic.";
RL J. Cell Biol. 176:255-261(2007).
RN [35]
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) IN COMPLEX WITH SEC23 AND ZINC.
RX PubMed=12239560; DOI=10.1038/nature01040;
RA Bi X., Corpina R.A., Goldberg J.;
RT "Structure of the Sec23/24-Sar1 pre-budding complex of the COPII vesicle
RT coat.";
RL Nature 419:271-277(2002).
RN [36]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 117-926 IN COMPLEX WITH SED5;
RP SYS1; BET1 AND ZINC, AND INTERACTION WITH SEC22.
RX PubMed=12941276; DOI=10.1016/s0092-8674(03)00608-1;
RA Mossessova E., Bickford L.C., Goldberg J.;
RT "SNARE selectivity of the COPII coat.";
RL Cell 114:483-495(2003).
CC -!- FUNCTION: Component of the coat protein complex II (COPII) which
CC promotes the formation of transport vesicles from the endoplasmic
CC reticulum (ER). The coat has two main functions, the physical
CC deformation of the endoplasmic reticulum membrane into vesicles and the
CC selection of cargo molecules. SEC24 specifically recruits cargo
CC proteins like BET1 or SYS1 to the COPII vesicles. The SEC23/24 complex
CC is also involved in internalization of plasma membrane proteins like
CC the maltose transporter. {ECO:0000269|PubMed:10198022,
CC ECO:0000269|PubMed:10712514, ECO:0000269|PubMed:10720463,
CC ECO:0000269|PubMed:10749860, ECO:0000269|PubMed:10753972,
CC ECO:0000269|PubMed:11086000, ECO:0000269|PubMed:12655150,
CC ECO:0000269|PubMed:12941277, ECO:0000269|PubMed:14627716,
CC ECO:0000269|PubMed:16269340, ECO:0000269|PubMed:8548805,
CC ECO:0000269|PubMed:9023343, ECO:0000269|PubMed:9428766}.
CC -!- SUBUNIT: The COPII coat is composed of at least 7 proteins: the
CC SEC23/24 complex, the SEC13/31 complex, SFB2, SFB3 and the protein
CC SAR1. Interacts with BET1, EMP24, GRH1, SEC22, SED5 and SYS1.
CC {ECO:0000269|PubMed:10097109, ECO:0000269|PubMed:10564255,
CC ECO:0000269|PubMed:11086000, ECO:0000269|PubMed:11389436,
CC ECO:0000269|PubMed:11560939, ECO:0000269|PubMed:11726510,
CC ECO:0000269|PubMed:12239560, ECO:0000269|PubMed:12778054,
CC ECO:0000269|PubMed:12941276, ECO:0000269|PubMed:12941277,
CC ECO:0000269|PubMed:16269340, ECO:0000269|PubMed:17261844,
CC ECO:0000269|PubMed:8930902, ECO:0000269|PubMed:9325247,
CC ECO:0000269|PubMed:9568718, ECO:0000269|PubMed:9685263}.
CC -!- INTERACTION:
CC P40482; Q04410: GRH1; NbExp=4; IntAct=EBI-16592, EBI-32083;
CC P40482; P15303: SEC23; NbExp=5; IntAct=EBI-16592, EBI-16584;
CC P40482; P38968: SEC31; NbExp=4; IntAct=EBI-16592, EBI-20524;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8548805}.
CC Cytoplasmic vesicle, COPII-coated vesicle membrane
CC {ECO:0000269|PubMed:10720463, ECO:0000269|PubMed:10753972,
CC ECO:0000269|PubMed:11086000, ECO:0000269|PubMed:12235121,
CC ECO:0000269|PubMed:8548805, ECO:0000269|PubMed:9568718}; Peripheral
CC membrane protein {ECO:0000269|PubMed:11086000,
CC ECO:0000269|PubMed:8548805}; Cytoplasmic side
CC {ECO:0000269|PubMed:8548805}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:10712514, ECO:0000269|PubMed:8548805}; Peripheral
CC membrane protein; Cytoplasmic side. Golgi apparatus membrane
CC {ECO:0000305|PubMed:8548805}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the SEC23/SEC24 family. SEC24 subfamily.
CC {ECO:0000305}.
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DR EMBL; Z38125; CAA86271.1; -; Genomic_DNA.
DR EMBL; AY692888; AAT92907.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08444.1; -; Genomic_DNA.
DR PIR; S48463; S48463.
DR RefSeq; NP_012157.3; NM_001179457.3.
DR PDB; 1M2V; X-ray; 2.75 A; B=1-926.
DR PDB; 1PCX; X-ray; 2.50 A; A=117-926.
DR PDB; 1PD0; X-ray; 2.60 A; A=117-926.
DR PDB; 1PD1; X-ray; 2.60 A; A=117-926.
DR PDB; 4BZI; EM; 23.00 A; E/F/L/M/N/O=1-926.
DR PDB; 6GNI; EM; 4.90 A; E=133-926.
DR PDB; 6ZGA; EM; 4.60 A; B/F=1-926.
DR PDBsum; 1M2V; -.
DR PDBsum; 1PCX; -.
DR PDBsum; 1PD0; -.
DR PDBsum; 1PD1; -.
DR PDBsum; 4BZI; -.
DR PDBsum; 6GNI; -.
DR PDBsum; 6ZGA; -.
DR AlphaFoldDB; P40482; -.
DR SMR; P40482; -.
DR BioGRID; 34882; 257.
DR ComplexPortal; CPX-2523; COPII vesicle coat complex.
DR DIP; DIP-2233N; -.
DR IntAct; P40482; 23.
DR MINT; P40482; -.
DR STRING; 4932.YIL109C; -.
DR iPTMnet; P40482; -.
DR MaxQB; P40482; -.
DR PaxDb; P40482; -.
DR PRIDE; P40482; -.
DR EnsemblFungi; YIL109C_mRNA; YIL109C; YIL109C.
DR GeneID; 854697; -.
DR KEGG; sce:YIL109C; -.
DR SGD; S000001371; SEC24.
DR VEuPathDB; FungiDB:YIL109C; -.
DR eggNOG; KOG1985; Eukaryota.
DR GeneTree; ENSGT00950000182924; -.
DR HOGENOM; CLU_004589_2_1_1; -.
DR InParanoid; P40482; -.
DR OMA; TFPRDQS; -.
DR BioCyc; YEAST:G3O-31364-MON; -.
DR Reactome; R-SCE-204005; COPII-mediated vesicle transport.
DR Reactome; R-SCE-5694530; Cargo concentration in the ER.
DR Reactome; R-SCE-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
DR EvolutionaryTrace; P40482; -.
DR PRO; PR:P40482; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40482; protein.
DR GO; GO:0030127; C:COPII vesicle coat; IDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:ComplexPortal.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000329; C:fungal-type vacuole membrane; HDA:SGD.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005048; F:signal sequence binding; IMP:SGD.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0090110; P:COPII-coated vesicle cargo loading; IDA:SGD.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0016236; P:macroautophagy; IMP:SGD.
DR GO; GO:1902953; P:positive regulation of ER to Golgi vesicle-mediated transport; IDA:ComplexPortal.
DR GO; GO:0070863; P:positive regulation of protein exit from endoplasmic reticulum; IDA:ComplexPortal.
DR CDD; cd01479; Sec24-like; 1.
DR Gene3D; 3.40.20.10; -; 1.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR InterPro; IPR007123; Gelsolin-like_dom.
DR InterPro; IPR036180; Gelsolin-like_dom_sf.
DR InterPro; IPR006900; Sec23/24_helical_dom.
DR InterPro; IPR036175; Sec23/24_helical_dom_sf.
DR InterPro; IPR006896; Sec23/24_trunk_dom.
DR InterPro; IPR012990; Sec23_24_beta_S.
DR InterPro; IPR041742; Sec24-like_trunk_dom.
DR InterPro; IPR036465; vWFA_dom_sf.
DR InterPro; IPR006895; Znf_Sec23_Sec24.
DR InterPro; IPR036174; Znf_Sec23_Sec24_sf.
DR Pfam; PF00626; Gelsolin; 1.
DR Pfam; PF08033; Sec23_BS; 1.
DR Pfam; PF04815; Sec23_helical; 1.
DR Pfam; PF04811; Sec23_trunk; 1.
DR Pfam; PF04810; zf-Sec23_Sec24; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR SUPFAM; SSF81811; SSF81811; 1.
DR SUPFAM; SSF82754; SSF82754; 1.
DR SUPFAM; SSF82919; SSF82919; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Cytoplasmic vesicle; Direct protein sequencing;
KW Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus; Membrane;
KW Metal-binding; Phosphoprotein; Protein transport; Reference proteome;
KW Transport; Zinc.
FT CHAIN 1..926
FT /note="Protein transport protein SEC24"
FT /id="PRO_0000205150"
FT REGION 24..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..256
FT /note="Zinc finger-like"
FT BINDING 231
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:12239560,
FT ECO:0000269|PubMed:12941276"
FT BINDING 234
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:12239560,
FT ECO:0000269|PubMed:12941276"
FT BINDING 253
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:12239560,
FT ECO:0000269|PubMed:12941276"
FT BINDING 256
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:12239560,
FT ECO:0000269|PubMed:12941276"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MUTAGEN 230
FT /note="R->A: Abolishes binding to and packaging of cargo
FT protein BET1."
FT /evidence="ECO:0000269|PubMed:12941277"
FT MUTAGEN 231
FT /note="C->S: Lethal."
FT /evidence="ECO:0000269|PubMed:10097109"
FT MUTAGEN 235
FT /note="R->A: Abolishes binding to and packaging of cargo
FT protein BET1."
FT /evidence="ECO:0000269|PubMed:12941277"
FT MUTAGEN 559
FT /note="R->M: Abolishes binding to and packaging of cargo
FT protein BET1."
FT /evidence="ECO:0000269|PubMed:12941277"
FT MUTAGEN 561
FT /note="R->M: Abolishes binding to and packaging of cargo
FT protein BET1."
FT /evidence="ECO:0000269|PubMed:12941277"
FT MUTAGEN 616
FT /note="L->W: Abolishes binding to and packaging of cargo
FT protein BET1."
FT /evidence="ECO:0000269|PubMed:12941277"
FT HELIX 64..72
FT /evidence="ECO:0007829|PDB:1M2V"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:1PCX"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:1PCX"
FT HELIX 151..155
FT /evidence="ECO:0007829|PDB:1PCX"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:1PCX"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:1PCX"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:1PCX"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:1PCX"
FT STRAND 182..192
FT /evidence="ECO:0007829|PDB:1PCX"
FT HELIX 193..199
FT /evidence="ECO:0007829|PDB:1PCX"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:1PCX"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:1PCX"
FT TURN 232..234
FT /evidence="ECO:0007829|PDB:1PCX"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:1PCX"
FT TURN 246..249
FT /evidence="ECO:0007829|PDB:1PCX"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:1PCX"
FT TURN 254..256
FT /evidence="ECO:0007829|PDB:1PCX"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:1PCX"
FT HELIX 264..267
FT /evidence="ECO:0007829|PDB:1PCX"
FT HELIX 277..279
FT /evidence="ECO:0007829|PDB:1PCX"
FT HELIX 281..284
FT /evidence="ECO:0007829|PDB:1PCX"
FT STRAND 286..291
FT /evidence="ECO:0007829|PDB:1PCX"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:1PCX"
FT STRAND 305..311
FT /evidence="ECO:0007829|PDB:1PCX"
FT HELIX 314..319
FT /evidence="ECO:0007829|PDB:1PCX"
FT HELIX 321..332
FT /evidence="ECO:0007829|PDB:1PCX"
FT TURN 333..335
FT /evidence="ECO:0007829|PDB:1PCX"
FT STRAND 344..358
FT /evidence="ECO:0007829|PDB:1PCX"
FT HELIX 362..364
FT /evidence="ECO:0007829|PDB:1PCX"
FT STRAND 374..376
FT /evidence="ECO:0007829|PDB:1PCX"
FT TURN 390..392
FT /evidence="ECO:0007829|PDB:1PCX"
FT STRAND 393..395
FT /evidence="ECO:0007829|PDB:1PCX"
FT TURN 396..399
FT /evidence="ECO:0007829|PDB:1PCX"
FT HELIX 400..413
FT /evidence="ECO:0007829|PDB:1PCX"
FT TURN 414..416
FT /evidence="ECO:0007829|PDB:1PCX"
FT HELIX 424..435
FT /evidence="ECO:0007829|PDB:1PCX"
FT TURN 436..438
FT /evidence="ECO:0007829|PDB:1PCX"
FT STRAND 440..448
FT /evidence="ECO:0007829|PDB:1PCX"
FT HELIX 471..475
FT /evidence="ECO:0007829|PDB:1M2V"
FT HELIX 482..492
FT /evidence="ECO:0007829|PDB:1PCX"
FT STRAND 495..505
FT /evidence="ECO:0007829|PDB:1PCX"
FT HELIX 509..517
FT /evidence="ECO:0007829|PDB:1PCX"
FT TURN 518..520
FT /evidence="ECO:0007829|PDB:1PCX"
FT STRAND 523..527
FT /evidence="ECO:0007829|PDB:1PCX"
FT HELIX 534..549
FT /evidence="ECO:0007829|PDB:1PCX"
FT STRAND 554..562
FT /evidence="ECO:0007829|PDB:1PCX"
FT STRAND 566..576
FT /evidence="ECO:0007829|PDB:1PCX"
FT STRAND 578..587
FT /evidence="ECO:0007829|PDB:1PCX"
FT STRAND 594..600
FT /evidence="ECO:0007829|PDB:1PCX"
FT STRAND 606..618
FT /evidence="ECO:0007829|PDB:1PCX"
FT TURN 620..622
FT /evidence="ECO:0007829|PDB:1M2V"
FT STRAND 624..637
FT /evidence="ECO:0007829|PDB:1PCX"
FT HELIX 639..644
FT /evidence="ECO:0007829|PDB:1PCX"
FT HELIX 648..665
FT /evidence="ECO:0007829|PDB:1PCX"
FT HELIX 668..689
FT /evidence="ECO:0007829|PDB:1PCX"
FT STRAND 696..699
FT /evidence="ECO:0007829|PDB:1M2V"
FT STRAND 702..704
FT /evidence="ECO:0007829|PDB:1PCX"
FT HELIX 705..707
FT /evidence="ECO:0007829|PDB:1PCX"
FT HELIX 710..718
FT /evidence="ECO:0007829|PDB:1PCX"
FT TURN 721..723
FT /evidence="ECO:0007829|PDB:1PCX"
FT HELIX 730..742
FT /evidence="ECO:0007829|PDB:1PCX"
FT HELIX 745..752
FT /evidence="ECO:0007829|PDB:1PCX"
FT STRAND 755..758
FT /evidence="ECO:0007829|PDB:1PCX"
FT TURN 759..761
FT /evidence="ECO:0007829|PDB:1M2V"
FT HELIX 791..793
FT /evidence="ECO:0007829|PDB:1PD0"
FT STRAND 799..803
FT /evidence="ECO:0007829|PDB:1PCX"
FT STRAND 805..812
FT /evidence="ECO:0007829|PDB:1PCX"
FT HELIX 818..825
FT /evidence="ECO:0007829|PDB:1PCX"
FT HELIX 830..832
FT /evidence="ECO:0007829|PDB:1PCX"
FT HELIX 847..860
FT /evidence="ECO:0007829|PDB:1PCX"
FT STRAND 870..875
FT /evidence="ECO:0007829|PDB:1PCX"
FT HELIX 885..899
FT /evidence="ECO:0007829|PDB:1PCX"
FT HELIX 913..923
FT /evidence="ECO:0007829|PDB:1PCX"
SQ SEQUENCE 926 AA; 103636 MW; 35E2BDD24CC75899 CRC64;
MSHHKKRVYP QAQLQYGQNA TPLQQPAQFM PPQDPAAAGM SYGQMGMPPQ GAVPSMGQQQ
FLTPAQEQLH QQIDQATTSM NDMHLHNVPL VDPNAYMQPQ VPVQMGTPLQ QQQQPMAAPA
YGQPSAAMGQ NMRPMNQLYP IDLLTELPPP ITDLTLPPPP LVIPPERMLV PSELSNASPD
YIRSTLNAVP KNSSLLKKSK LPFGLVIRPY QHLYDDIDPP PLNEDGLIVR CRRCRSYMNP
FVTFIEQGRR WRCNFCRLAN DVPMQMDQSD PNDPKSRYDR NEIKCAVMEY MAPKEYTLRQ
PPPATYCFLI DVSQSSIKSG LLATTINTLL QNLDSIPNHD ERTRISILCV DNAIHYFKIP
LDSENNEESA DQINMMDIAD LEEPFLPRPN SMVVSLKACR QNIETLLTKI PQIFQSNLIT
NFALGPALKS AYHLIGGVGG KIIVVSGTLP NLGIGKLQRR NESGVVNTSK ETAQLLSCQD
SFYKNFTIDC SKVQITVDLF LASEDYMDVA SLSNLSRFTA GQTHFYPGFS GKNPNDIVKF
STEFAKHISM DFCMETVMRA RGSTGLRMSR FYGHFFNRSS DLCAFSTMPR DQSYLFEVNV
DESIMADYCY VQVAVLLSLN NSQRRIRIIT LAMPTTESLA EVYASADQLA IASFYNSKAV
EKALNSSLDD ARVLINKSVQ DILATYKKEI VVSNTAGGAP LRLCANLRMF PLLMHSLTKH
MAFRSGIVPS DHRASALNNL ESLPLKYLIK NIYPDVYSLH DMADEAGLPV QTEDGEATGT
IVLPQPINAT SSLFERYGLY LIDNGNELFL WMGGDAVPAL VFDVFGTQDI FDIPIGKQEI
PVVENSEFNQ RVRNIINQLR NHDDVITYQS LYIVRGASLS EPVNHASARE VATLRLWASS
TLVEDKILNN ESYREFLQIM KARISK
