SEC18_YEAST
ID SEC18_YEAST Reviewed; 758 AA.
AC P18759; D6VQ79; Q07067;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 2.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Vesicular-fusion protein SEC18;
GN Name=SEC18; OrderedLocusNames=YBR080C; ORFNames=YBR0736;
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].
RX PubMed=3054509; DOI=10.1128/mcb.8.10.4098-4109.1988;
RA Eakle K.A., Bernstein M., Emr S.D.;
RT "Characterization of a component of the yeast secretion machinery:
RT identification of the SEC18 gene product.";
RL Mol. Cell. Biol. 8:4098-4109(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7985423; DOI=10.1002/yea.320100711;
RA van der Aart Q.J.M., Barthe C., Doignon F., Aigle M., Crouzet M.,
RA Steensma H.Y.;
RT "Sequence analysis of a 31 kb DNA fragment from the right arm of
RT Saccharomyces cerevisiae chromosome II.";
RL Yeast 10:959-964(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 566-758.
RC STRAIN=ATCC 200060 / W303;
RA Vornlocher H.-P., Hanachi P., Hershey J.W.B.;
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, AND IDENTIFICATION BY
RP 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 [9]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 22-210.
RX PubMed=10611286; DOI=10.1073/pnas.96.26.14759;
RA Babor S.M., Fass D.;
RT "Crystal structure of the Sec18p N-terminal domain.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:14759-14764(1999).
CC -!- FUNCTION: Required for vesicle-mediated transport. Catalyzes the fusion
CC of transport vesicles within the Golgi cisternae. Is also required for
CC transport from the endoplasmic reticulum to the Golgi stack. Seems to
CC function as a fusion protein required for the delivery of cargo
CC proteins to all compartments of the Golgi stack independent of vesicle
CC origin.
CC -!- SUBUNIT: Homohexamer. Binds to SEC17.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MISCELLANEOUS: Present with 5920 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA35031.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M20662; AAA35030.1; -; Genomic_DNA.
DR EMBL; M20662; AAA35031.1; ALT_INIT; Genomic_DNA.
DR EMBL; X76294; CAA53939.1; -; Genomic_DNA.
DR EMBL; Z35949; CAA85025.1; -; Genomic_DNA.
DR EMBL; AF004912; AAB82417.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07199.1; -; Genomic_DNA.
DR PIR; S45477; S45477.
DR RefSeq; NP_009636.3; NM_001178428.3.
DR PDB; 1CR5; X-ray; 2.30 A; A/B/C=22-210.
DR PDBsum; 1CR5; -.
DR AlphaFoldDB; P18759; -.
DR SMR; P18759; -.
DR BioGRID; 32782; 367.
DR DIP; DIP-2497N; -.
DR IntAct; P18759; 17.
DR MINT; P18759; -.
DR STRING; 4932.YBR080C; -.
DR TCDB; 1.F.1.1.2; the synaptosomal vesicle fusion pore (svf-pore) family.
DR iPTMnet; P18759; -.
DR MaxQB; P18759; -.
DR PaxDb; P18759; -.
DR PRIDE; P18759; -.
DR EnsemblFungi; YBR080C_mRNA; YBR080C; YBR080C.
DR GeneID; 852372; -.
DR KEGG; sce:YBR080C; -.
DR SGD; S000000284; SEC18.
DR VEuPathDB; FungiDB:YBR080C; -.
DR eggNOG; KOG0741; Eukaryota.
DR GeneTree; ENSGT00530000064085; -.
DR HOGENOM; CLU_008037_2_0_1; -.
DR InParanoid; P18759; -.
DR OMA; IQHVKGM; -.
DR BioCyc; YEAST:G3O-29048-MON; -.
DR Reactome; R-SCE-204005; COPII-mediated vesicle transport.
DR Reactome; R-SCE-6807878; COPI-mediated anterograde transport.
DR Reactome; R-SCE-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-SCE-6811438; Intra-Golgi traffic.
DR Reactome; R-SCE-6811440; Retrograde transport at the Trans-Golgi-Network.
DR EvolutionaryTrace; P18759; -.
DR PRO; PR:P18759; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P18759; protein.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:SGD.
DR GO; GO:0005795; C:Golgi stack; IBA:GO_Central.
DR GO; GO:0043332; C:mating projection tip; HDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:SGD.
DR GO; GO:0070300; F:phosphatidic acid binding; IDA:SGD.
DR GO; GO:0000149; F:SNARE binding; IDA:SGD.
DR GO; GO:0000045; P:autophagosome assembly; IMP:SGD.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IDA:SGD.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; IMP:SGD.
DR GO; GO:0048219; P:inter-Golgi cisterna vesicle-mediated transport; IMP:SGD.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0016236; P:macroautophagy; IMP:SGD.
DR GO; GO:0035494; P:SNARE complex disassembly; IDA:SGD.
DR GO; GO:0042144; P:vacuole fusion, non-autophagic; IDA:SGD.
DR GO; GO:0048280; P:vesicle fusion with Golgi apparatus; IDA:SGD.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR004201; Cdc48_dom2.
DR InterPro; IPR029067; CDC48_domain_2-like_sf.
DR InterPro; IPR003338; CDC4_N-term_subdom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039812; Vesicle-fus_ATPase.
DR PANTHER; PTHR23078; PTHR23078; 1.
DR Pfam; PF00004; AAA; 2.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF02933; CDC48_2; 1.
DR SMART; SM00382; AAA; 2.
DR SMART; SM01072; CDC48_2; 1.
DR SMART; SM01073; CDC48_N; 1.
DR SUPFAM; SSF50692; SSF50692; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF54585; SSF54585; 1.
DR PROSITE; PS00674; AAA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; ER-Golgi transport;
KW Nucleotide-binding; Phosphoprotein; Protein transport; Reference proteome;
KW Repeat; Transport.
FT CHAIN 1..758
FT /note="Vesicular-fusion protein SEC18"
FT /id="PRO_0000084571"
FT BINDING 281..288
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 564..571
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:18407956"
FT CONFLICT 381
FT /note="Missing (in Ref. 1; AAA35030/AAA35031)"
FT /evidence="ECO:0000305"
FT STRAND 27..33
FT /evidence="ECO:0007829|PDB:1CR5"
FT HELIX 37..40
FT /evidence="ECO:0007829|PDB:1CR5"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:1CR5"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:1CR5"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:1CR5"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:1CR5"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:1CR5"
FT STRAND 64..70
FT /evidence="ECO:0007829|PDB:1CR5"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:1CR5"
FT HELIX 83..89
FT /evidence="ECO:0007829|PDB:1CR5"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:1CR5"
FT HELIX 104..108
FT /evidence="ECO:0007829|PDB:1CR5"
FT STRAND 113..123
FT /evidence="ECO:0007829|PDB:1CR5"
FT HELIX 136..147
FT /evidence="ECO:0007829|PDB:1CR5"
FT STRAND 157..162
FT /evidence="ECO:0007829|PDB:1CR5"
FT STRAND 165..177
FT /evidence="ECO:0007829|PDB:1CR5"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:1CR5"
FT STRAND 203..208
FT /evidence="ECO:0007829|PDB:1CR5"
SQ SEQUENCE 758 AA; 84056 MW; AD6CE77EA3674B3C CRC64;
MFKIPGFGKA AANHTPPDMT NMDTRTRHLK VSNCPNNSYA LANVAAVSPN DFPNNIYIII
DNLFVFTTRH SNDIPPGTIG FNGNQRTWGG WSLNQDVQAK AFDLFKYSGK QSYLGSIDID
ISFRARGKAV STVFDQDELA KQFVRCYESQ IFSPTQYLIM EFQGHFFDLK IRNVQAIDLG
DIEPTSAVAT GIETKGILTK QTQINFFKGR DGLVNLKSSN SLRPRSNAVI RPDFKFEDLG
VGGLDKEFTK IFRRAFASRI FPPSVIEKLG ISHVKGLLLY GPPGTGKTLI ARKIGTMLNA
KEPKIVNGPE ILSKYVGSSE ENIRNLFKDA EAEYRAKGEE SSLHIIIFDE LDSVFKQRGS
RGDGTGVGDN VVNQLLAKMD GVDQLNNILV IGMTNRKDLI DSALLRPGRF EVQVEIHLPD
EKGRLQIFDI QTKKMRENNM MSDDVNLAEL AALTKNFSGA EIEGLVKSAS SFAINKTVNI
GKGATKLNTK DIAKLKVTRE DFLNALNDVT PAFGISEEDL KTCVEGGMML YSERVNSILK
NGARYVRQVR ESDKSRLVSL LIHGPAGSGK TALAAEIALK SGFPFIRLIS PNELSGMSES
AKIAYIDNTF RDAYKSPLNI LVIDSLETLV DWVPIGPRFS NNILQMLKVA LKRKPPQDRR
LLIMTTTSAY SVLQQMDILS CFDNEIAVPN MTNLDELNNV MIESNFLDDA GRVKVINELS
RSCPNFNVGI KKTLTNIETA RHDEDPVNEL VELMTQSA
