SEC13_YEAST
ID SEC13_YEAST Reviewed; 297 AA.
AC Q04491; D6VYK9;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Protein transport protein SEC13;
GN Name=SEC13; Synonyms=ANU3; OrderedLocusNames=YLR208W; ORFNames=L8167.4;
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 [GENOMIC DNA], AND MUTAGENESIS OF SER-224; TRP-262 AND
RP GLY-266.
RX PubMed=8432727; DOI=10.1083/jcb.120.4.865;
RA Pryer N.K., Salama N.R., Schekman R.W., Kaiser C.A.;
RT "Cytosolic Sec13p complex is required for vesicle formation from the
RT endoplasmic reticulum in vitro.";
RL J. Cell Biol. 120:865-875(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [3]
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 [4]
RP PROTEIN SEQUENCE OF 35-39; 79-83; 125-131; 278-282 AND 289-293, AND
RP FUNCTION IN NUCLEAR MRNA EXPORT.
RX PubMed=8565072; DOI=10.1016/s0092-8674(00)80981-2;
RA Siniossoglou S., Wimmer C., Rieger M., Doye V., Tekotte H., Weise C.,
RA Emig S., Segref A., Hurt E.C.;
RT "A novel complex of nucleoporins, which includes Sec13p and a Sec13p
RT homolog, is essential for normal nuclear pores.";
RL Cell 84:265-275(1996).
RN [5]
RP FUNCTION.
RX PubMed=6996832; DOI=10.1016/0092-8674(80)90128-2;
RA Novick P., Field C., Schekman R.W.;
RT "Identification of 23 complementation groups required for post-
RT translational events in the yeast secretory pathway.";
RL Cell 21:205-215(1980).
RN [6]
RP FUNCTION.
RX PubMed=7026045; DOI=10.1016/0092-8674(81)90064-7;
RA Novick P., Ferro S., Schekman R.W.;
RT "Order of events in the yeast secretory pathway.";
RL Cell 25:461-469(1981).
RN [7]
RP FUNCTION.
RX PubMed=2188733; DOI=10.1016/0092-8674(90)90483-u;
RA Kaiser C.A., Schekman R.W.;
RT "Distinct sets of SEC genes govern transport vesicle formation and fusion
RT early in the secretory pathway.";
RL Cell 61:723-733(1990).
RN [8]
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 [9]
RP FUNCTION.
RX PubMed=8909535; DOI=10.1083/jcb.135.3.585;
RA Kuehn M.J., Schekman R.W., Ljungdahl P.O.;
RT "Amino acid permeases require COPII components and the ER resident membrane
RT protein Shr3p for packaging into transport vesicles in vitro.";
RL J. Cell Biol. 135:585-595(1996).
RN [10]
RP FUNCTION.
RX PubMed=9409822; DOI=10.1093/genetics/147.4.1569;
RA Roberg K.J., Bickel S., Rowley N., Kaiser C.A.;
RT "Control of amino acid permease sorting in the late secretory pathway of
RT Saccharomyces cerevisiae by SEC13, LST4, LST7 and LST8.";
RL Genetics 147:1569-1584(1997).
RN [11]
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 [12]
RP FUNCTION.
RX PubMed=9199164; DOI=10.1083/jcb.137.7.1469;
RA Roberg K.J., Rowley N., Kaiser C.A.;
RT "Physiological regulation of membrane protein sorting late in the secretory
RT pathway of Saccharomyces cerevisiae.";
RL J. Cell Biol. 137:1469-1482(1997).
RN [13]
RP FUNCTION.
RX PubMed=9427388; DOI=10.1242/jcs.110.21.2703;
RA Suetterlin C., Doering T.L., Schimmoeller F., Schroeder S., Riezman H.;
RT "Specific requirements for the ER to Golgi transport of GPI-anchored
RT proteins in yeast.";
RL J. Cell Sci. 110:2703-2714(1997).
RN [14]
RP INTERACTION WITH SEC31.
RX PubMed=9190202; DOI=10.1091/mbc.8.2.205;
RA Salama N.R., Chuang J.S., Schekman R.W.;
RT "Sec31 encodes an essential component of the COPII coat required for
RT transport vesicle budding from the endoplasmic reticulum.";
RL Mol. Biol. Cell 8:205-217(1997).
RN [15]
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 [16]
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 [17]
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 [18]
RP FUNCTION, IDENTIFICATION IN THE NUCLEAR PORE COMPLEX, AND SUBCELLULAR
RP LOCATION.
RX PubMed=10684247; DOI=10.1083/jcb.148.4.635;
RA Rout M.P., Aitchison J.D., Suprapto A., Hjertaas K., Zhao Y., Chait B.T.;
RT "The yeast nuclear pore complex: composition, architecture, and transport
RT mechanism.";
RL J. Cell Biol. 148:635-651(2000).
RN [19]
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 [20]
RP FUNCTION, LOCALIZATION AT NPC, AND ROLE IN NPC BIOGENESIS.
RX PubMed=10747086; DOI=10.1083/jcb.149.1.41;
RA Siniossoglou S., Lutzmann M., Santos-Rosa H., Leonard K., Mueller S.,
RA Aebi U., Hurt E.C.;
RT "Structure and assembly of the Nup84p complex.";
RL J. Cell Biol. 149:41-54(2000).
RN [21]
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 [22]
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 [23]
RP FUNCTION, AND HETEROTETRAMERIC COMPLEX WITH SEC31.
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 [24]
RP FUNCTION, AND COPII FORMATION AND STRUCTURE.
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 [25]
RP FUNCTION, ER MEMBRANE AND NUCLEAR ENVELOPE MORPHOLOGY, NPC ASSEMBLY AND
RP DISTRIBUTION, AND MUTAGENESIS OF GLY-176.
RX PubMed=12215173; DOI=10.1186/1471-2156-3-17;
RA Ryan K.J., Wente S.R.;
RT "Isolation and characterization of new Saccharomyces cerevisiae mutants
RT perturbed in nuclear pore complex assembly.";
RL BMC Genet. 3:17-17(2002).
RN [26]
RP FUNCTION, AND NUP84 NPC SUBCOMPLEX ASSEMBLY/STRUCTURE.
RX PubMed=11823431; DOI=10.1093/emboj/21.3.387;
RA Lutzmann M., Kunze R., Buerer A., Aebi U., Hurt E.C.;
RT "Modular self-assembly of a Y-shaped multiprotein complex from seven
RT nucleoporins.";
RL EMBO J. 21:387-397(2002).
RN [27]
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 [28]
RP FUNCTION.
RX PubMed=12475940; DOI=10.1091/mbc.02-05-0082;
RA Fatal N., Suntio T., Makarow M.;
RT "Selective protein exit from yeast endoplasmic reticulum in absence of
RT functional COPII coat component Sec13p.";
RL Mol. Biol. Cell 13:4130-4140(2002).
RN [29]
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 [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 LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [32]
RP REVIEW.
RX PubMed=12757749; DOI=10.1016/s0079-6107(03)00019-1;
RA van Vliet C., Thomas E.C., Merino-Trigo A., Teasdale R.D., Gleeson P.A.;
RT "Intracellular sorting and transport of proteins.";
RL Prog. Biophys. Mol. Biol. 83:1-45(2003).
RN [33]
RP REVIEW.
RX PubMed=12791295; DOI=10.1016/s0962-8924(03)00082-5;
RA Barlowe C.;
RT "Signals for COPII-dependent export from the ER: what's the ticket out?";
RL Trends Cell Biol. 13:295-300(2003).
RN [34]
RP REVIEW.
RX PubMed=12791264; DOI=10.1016/s1534-5807(03)00162-x;
RA Suntharalingam M., Wente S.R.;
RT "Peering through the pore: nuclear pore complex structure, assembly, and
RT function.";
RL Dev. Cell 4:775-789(2003).
RN [35]
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 [36]
RP SUBCELLULAR LOCATION, IDENTIFICATION IN THE SEA COMPLEX, AND FUNCTION.
RX PubMed=21454883; DOI=10.1074/mcp.m110.006478;
RA Dokudovskaya S., Waharte F., Schlessinger A., Pieper U., Devos D.P.,
RA Cristea I.M., Williams R., Salamero J., Chait B.T., Sali A., Field M.C.,
RA Rout M.P., Dargemont C.;
RT "A conserved coatomer-related complex containing Sec13 and Seh1 dynamically
RT associates with the vacuole in Saccharomyces cerevisiae.";
RL Mol. Cell. Proteomics 10:M110.006478.1-M110.006478.17(2011).
RN [37]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Functions as a component of the nuclear pore complex (NPC)
CC and the COPII coat. It is one of 5 proteins constituting the COPII
CC coat, which is involved in anterograde (ER to Golgi) double-membrane
CC transport vesicle formation. First the small GTPase SAR1, activated by
CC and binding to the integral ER membrane protein SEC12, exchanges GDP
CC for GTP and recruits the heterodimer SEC23/24, which in turn recruits
CC the heterotetramer SEC13-SEC31. The polymerization of COPII coat
CC complexes then causes physically the deformation (budding) of the
CC membrane, leading to the creation of a transport vesicle. The COPII
CC complex is dissociated upon SAR1-GTP hydrolysis to SAR1-GDP. SEC23
CC functions as the SAR1 GTPase activating protein, whose activity is
CC stimulated in the presence of SEC13/31. SEC13 is directly or indirectly
CC required for normal ER membrane and nuclear envelope morphology. It
CC also functions as a component of the nuclear pore complex (NPC). NPC
CC components, collectively referred to as nucleoporins (NUPs), can play
CC the role of both NPC structural components and of docking or
CC interaction partners for transiently associated nuclear transport
CC factors. SEC13 is required for efficient mRNA export from the nucleus
CC to the cytoplasm and for correct nuclear pore biogenesis and
CC distribution. Component of the SEA complex which coats the vacuolar
CC membrane and is involved in intracellular trafficking, autophagy,
CC response to nitrogen starvation, and amino acid biogenesis.
CC {ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:10720463,
CC ECO:0000269|PubMed:10747086, ECO:0000269|PubMed:11535824,
CC ECO:0000269|PubMed:11717432, ECO:0000269|PubMed:11823431,
CC ECO:0000269|PubMed:12215173, ECO:0000269|PubMed:12475940,
CC ECO:0000269|PubMed:14627716, ECO:0000269|PubMed:21454883,
CC ECO:0000269|PubMed:2188733, ECO:0000269|PubMed:6996832,
CC ECO:0000269|PubMed:7026045, ECO:0000269|PubMed:8548805,
CC ECO:0000269|PubMed:8565072, ECO:0000269|PubMed:8909535,
CC ECO:0000269|PubMed:9023343, ECO:0000269|PubMed:9199164,
CC ECO:0000269|PubMed:9409822, ECO:0000269|PubMed:9427388}.
CC -!- SUBUNIT: The basic repeat unit of a COPII coated vesicle is composed of
CC 5 proteins: the small GTPase SAR1, the heterodimeric SEC23-SEC24
CC complex, and the heterotetrameric SEC13-SEC31 complex. This repeat unit
CC polymerizes to induce membrane deformation into a transport vesicle.
CC Component of the nuclear pore complex (NPC). NPC constitutes the
CC exclusive means of nucleocytoplasmic transport. NPCs allow the passive
CC diffusion of ions and small molecules and the active, nuclear transport
CC receptor-mediated bidirectional transport of macromolecules such as
CC proteins, RNAs, ribonucleoparticles (RNPs), and ribosomal subunits
CC across the nuclear envelope. Due to its 8-fold rotational symmetry, all
CC subunits are present with 8 copies or multiples thereof. SEC13 is part
CC of the heptameric 0.5 MDa autoassembling NUP84 NPC subcomplex (NUP84,
CC NUP85, NUP120, NUP133, NUP145C, SEC13 and SEH1). Component of the SEA
CC complex composed of at least IML1/SEA1, RTC1/SEA2, MTC5/SEA3, NPR2,
CC NPR3, SEA4, SEC13 and SEH1. {ECO:0000269|PubMed:10684247,
CC ECO:0000269|PubMed:11389436, ECO:0000269|PubMed:21454883,
CC ECO:0000269|PubMed:9325247, ECO:0000269|PubMed:9568718}.
CC -!- INTERACTION:
CC Q04491; Q03897: MTC5; NbExp=5; IntAct=EBI-16529, EBI-32422;
CC Q04491; P49687: NUP145; NbExp=24; IntAct=EBI-16529, EBI-11730;
CC Q04491; P38968: SEC31; NbExp=6; IntAct=EBI-16529, EBI-20524;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle
CC membrane; Peripheral membrane protein; Cytoplasmic side. Endoplasmic
CC reticulum membrane; Peripheral membrane protein; Cytoplasmic side.
CC Nucleus, nuclear pore complex {ECO:0000269|PubMed:10684247}. Vacuole
CC membrane; Peripheral membrane protein.
CC -!- MISCELLANEOUS: Present with 21400 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the WD repeat SEC13 family. {ECO:0000305}.
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DR EMBL; L05929; AAA35028.1; -; Genomic_DNA.
DR EMBL; U14913; AAB67426.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09525.1; -; Genomic_DNA.
DR PIR; A45442; A45442.
DR RefSeq; NP_013309.1; NM_001182095.1.
DR PDB; 2PM6; X-ray; 2.45 A; B/D=1-297.
DR PDB; 2PM7; X-ray; 2.35 A; B/D=1-297.
DR PDB; 2PM9; X-ray; 3.30 A; B=1-297.
DR PDB; 3IKO; X-ray; 3.20 A; A/D/G=1-297.
DR PDB; 3JRO; X-ray; 4.00 A; A=1-297.
DR PDB; 3JRP; X-ray; 2.60 A; A=1-297.
DR PDB; 3MZK; X-ray; 2.69 A; A/D=1-297.
DR PDB; 3MZL; X-ray; 2.80 A; A/C/E/G=1-297.
DR PDB; 4BZJ; EM; 40.00 A; B/F=2-292.
DR PDB; 4BZK; EM; 40.00 A; B/F=1-297.
DR PDB; 4XMM; X-ray; 7.38 A; A=1-297.
DR PDB; 4XMN; X-ray; 7.60 A; A=1-297.
DR PDB; 6ZG5; EM; 40.00 A; B/F=1-297.
DR PDB; 6ZG6; EM; 40.00 A; B/D/F/H=1-297.
DR PDB; 6ZL0; EM; 40.00 A; B/D=1-297.
DR PDB; 7N84; EM; 11.60 A; d/o=1-297.
DR PDB; 7N9F; EM; 37.00 A; d/k=1-297.
DR PDBsum; 2PM6; -.
DR PDBsum; 2PM7; -.
DR PDBsum; 2PM9; -.
DR PDBsum; 3IKO; -.
DR PDBsum; 3JRO; -.
DR PDBsum; 3JRP; -.
DR PDBsum; 3MZK; -.
DR PDBsum; 3MZL; -.
DR PDBsum; 4BZJ; -.
DR PDBsum; 4BZK; -.
DR PDBsum; 4XMM; -.
DR PDBsum; 4XMN; -.
DR PDBsum; 6ZG5; -.
DR PDBsum; 6ZG6; -.
DR PDBsum; 6ZL0; -.
DR PDBsum; 7N84; -.
DR PDBsum; 7N9F; -.
DR AlphaFoldDB; Q04491; -.
DR SMR; Q04491; -.
DR BioGRID; 31476; 301.
DR ComplexPortal; CPX-2523; COPII vesicle coat complex.
DR ComplexPortal; CPX-3231; SEA complex.
DR ComplexPortal; CPX-824; Nuclear pore complex.
DR DIP; DIP-1826N; -.
DR IntAct; Q04491; 30.
DR MINT; Q04491; -.
DR STRING; 4932.YLR208W; -.
DR iPTMnet; Q04491; -.
DR MaxQB; Q04491; -.
DR PaxDb; Q04491; -.
DR PRIDE; Q04491; -.
DR EnsemblFungi; YLR208W_mRNA; YLR208W; YLR208W.
DR GeneID; 850905; -.
DR KEGG; sce:YLR208W; -.
DR SGD; S000004198; SEC13.
DR VEuPathDB; FungiDB:YLR208W; -.
DR eggNOG; KOG1332; Eukaryota.
DR GeneTree; ENSGT00940000153393; -.
DR HOGENOM; CLU_032441_0_1_1; -.
DR InParanoid; Q04491; -.
DR OMA; TVDTGHE; -.
DR BioCyc; YEAST:G3O-32326-MON; -.
DR Reactome; R-SCE-204005; COPII-mediated vesicle transport.
DR Reactome; R-SCE-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-SCE-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-SCE-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-SCE-4570464; SUMOylation of RNA binding proteins.
DR EvolutionaryTrace; Q04491; -.
DR PRO; PR:Q04491; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q04491; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0030127; C:COPII vesicle coat; IDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:ComplexPortal.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005635; C:nuclear envelope; IC:ComplexPortal.
DR GO; GO:0005643; C:nuclear pore; IC:ComplexPortal.
DR GO; GO:0031080; C:nuclear pore outer ring; IDA:SGD.
DR GO; GO:0035859; C:Seh1-associated complex; IDA:SGD.
DR GO; GO:0005774; C:vacuolar membrane; IC:ComplexPortal.
DR GO; GO:0005198; F:structural molecule activity; IDA:SGD.
DR GO; GO:0090114; P:COPII-coated vesicle budding; IMP:SGD.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0051664; P:nuclear pore localization; IMP:SGD.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IC:ComplexPortal.
DR GO; GO:1902953; P:positive regulation of ER to Golgi vesicle-mediated transport; IDA:ComplexPortal.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA:SGD.
DR GO; GO:0070863; P:positive regulation of protein exit from endoplasmic reticulum; IDA:ComplexPortal.
DR GO; GO:0032008; P:positive regulation of TOR signaling; IBA:GO_Central.
DR GO; GO:1904263; P:positive regulation of TORC1 signaling; IMP:SGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:SGD.
DR GO; GO:0032527; P:protein exit from endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central.
DR GO; GO:1903432; P:regulation of TORC1 signaling; IDA:ComplexPortal.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:SGD.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR037596; Sec13.
DR InterPro; IPR037363; Sec13/Seh1_fam.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR11024; PTHR11024; 1.
DR PANTHER; PTHR11024:SF2; PTHR11024:SF2; 1.
DR Pfam; PF00400; WD40; 2.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasmic vesicle; Direct protein sequencing;
KW Endoplasmic reticulum; ER-Golgi transport; Membrane; mRNA transport;
KW Nuclear pore complex; Nucleus; Protein transport; Reference proteome;
KW Repeat; Translocation; Transport; Vacuole; WD repeat.
FT CHAIN 1..297
FT /note="Protein transport protein SEC13"
FT /id="PRO_0000051206"
FT REPEAT 7..46
FT /note="WD 1"
FT REPEAT 51..92
FT /note="WD 2"
FT REPEAT 97..138
FT /note="WD 3"
FT REPEAT 143..195
FT /note="WD 4"
FT REPEAT 202..244
FT /note="WD 5"
FT REPEAT 252..291
FT /note="WD 6"
FT MUTAGEN 176
FT /note="G->R: Leads to mislocalization of NPCs and
FT overproliferation of the nuclear and ER membranes at 34
FT degree Celsius."
FT /evidence="ECO:0000269|PubMed:12215173"
FT MUTAGEN 224
FT /note="S->K: Growth inhibited above 30 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:8432727"
FT MUTAGEN 262
FT /note="W->R: Growth inhibited above 30 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:8432727"
FT MUTAGEN 266
FT /note="G->D: Growth inhibited above 34 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:8432727"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:3MZK"
FT STRAND 5..7
FT /evidence="ECO:0007829|PDB:3JRP"
FT STRAND 12..17
FT /evidence="ECO:0007829|PDB:2PM7"
FT STRAND 21..28
FT /evidence="ECO:0007829|PDB:2PM7"
FT STRAND 33..38
FT /evidence="ECO:0007829|PDB:2PM7"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:2PM7"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:2PM7"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:2PM7"
FT STRAND 68..74
FT /evidence="ECO:0007829|PDB:2PM7"
FT STRAND 79..87
FT /evidence="ECO:0007829|PDB:2PM7"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:2PM7"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:3IKO"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:2PM7"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:2PM7"
FT STRAND 114..120
FT /evidence="ECO:0007829|PDB:2PM7"
FT STRAND 123..130
FT /evidence="ECO:0007829|PDB:2PM7"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:2PM7"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:2PM7"
FT STRAND 148..153
FT /evidence="ECO:0007829|PDB:2PM7"
FT STRAND 157..161
FT /evidence="ECO:0007829|PDB:3MZK"
FT TURN 162..165
FT /evidence="ECO:0007829|PDB:3MZK"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:3MZK"
FT STRAND 172..177
FT /evidence="ECO:0007829|PDB:2PM7"
FT STRAND 182..188
FT /evidence="ECO:0007829|PDB:2PM7"
FT TURN 189..192
FT /evidence="ECO:0007829|PDB:2PM7"
FT STRAND 193..200
FT /evidence="ECO:0007829|PDB:2PM7"
FT STRAND 207..212
FT /evidence="ECO:0007829|PDB:2PM7"
FT STRAND 217..226
FT /evidence="ECO:0007829|PDB:2PM7"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:3IKO"
FT STRAND 231..238
FT /evidence="ECO:0007829|PDB:2PM7"
FT STRAND 244..251
FT /evidence="ECO:0007829|PDB:2PM7"
FT STRAND 257..262
FT /evidence="ECO:0007829|PDB:2PM7"
FT STRAND 264..266
FT /evidence="ECO:0007829|PDB:2PM7"
FT STRAND 269..273
FT /evidence="ECO:0007829|PDB:2PM7"
FT STRAND 274..276
FT /evidence="ECO:0007829|PDB:2PM6"
FT STRAND 278..283
FT /evidence="ECO:0007829|PDB:2PM7"
FT STRAND 285..287
FT /evidence="ECO:0007829|PDB:2PM9"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:2PM7"
SQ SEQUENCE 297 AA; 33043 MW; A94388B4B9CB77FE CRC64;
MVVIANAHNE LIHDAVLDYY GKRLATCSSD KTIKIFEVEG ETHKLIDTLT GHEGPVWRVD
WAHPKFGTIL ASCSYDGKVL IWKEENGRWS QIAVHAVHSA SVNSVQWAPH EYGPLLLVAS
SDGKVSVVEF KENGTTSPII IDAHAIGVNS ASWAPATIEE DGEHNGTKES RKFVTGGADN
LVKIWKYNSD AQTYVLESTL EGHSDWVRDV AWSPTVLLRS YLASVSQDRT CIIWTQDNEQ
GPWKKTLLKE EKFPDVLWRA SWSLSGNVLA LSGGDNKVTL WKENLEGKWE PAGEVHQ
