SEC18_SCHPO
ID SEC18_SCHPO Reviewed; 792 AA.
AC Q9P7Q4;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Vesicular-fusion protein sec18;
GN Name=sec18; ORFNames=SPAC1834.11c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58 AND THR-252, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR EMBL; CU329670; CAB75779.1; -; Genomic_DNA.
DR PIR; T50122; T50122.
DR RefSeq; NP_594690.1; NM_001020119.2.
DR AlphaFoldDB; Q9P7Q4; -.
DR SMR; Q9P7Q4; -.
DR BioGRID; 278874; 22.
DR IntAct; Q9P7Q4; 2.
DR STRING; 4896.SPAC1834.11c.1; -.
DR iPTMnet; Q9P7Q4; -.
DR MaxQB; Q9P7Q4; -.
DR PaxDb; Q9P7Q4; -.
DR PRIDE; Q9P7Q4; -.
DR EnsemblFungi; SPAC1834.11c.1; SPAC1834.11c.1:pep; SPAC1834.11c.
DR GeneID; 2542410; -.
DR KEGG; spo:SPAC1834.11c; -.
DR PomBase; SPAC1834.11c; sec18.
DR VEuPathDB; FungiDB:SPAC1834.11c; -.
DR eggNOG; KOG0741; Eukaryota.
DR HOGENOM; CLU_008037_2_0_1; -.
DR InParanoid; Q9P7Q4; -.
DR OMA; IQHVKGM; -.
DR PhylomeDB; Q9P7Q4; -.
DR Reactome; R-SPO-204005; COPII-mediated vesicle transport.
DR Reactome; R-SPO-6807878; COPI-mediated anterograde transport.
DR Reactome; R-SPO-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-SPO-6811438; Intra-Golgi traffic.
DR Reactome; R-SPO-6811440; Retrograde transport at the Trans-Golgi-Network.
DR PRO; PR:Q9P7Q4; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005795; C:Golgi stack; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISO:PomBase.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISO:PomBase.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; IBA:GO_Central.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IC:PomBase.
DR GO; GO:0035494; P:SNARE complex disassembly; IEA:InterPro.
DR GO; GO:0042144; P:vacuole fusion, non-autophagic; ISO:PomBase.
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 ATP-binding; Cytoplasm; ER-Golgi transport; Nucleotide-binding;
KW Phosphoprotein; Protein transport; Reference proteome; Repeat; Transport.
FT CHAIN 1..792
FT /note="Vesicular-fusion protein sec18"
FT /id="PRO_0000084570"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 311..318
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 592..599
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 252
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 792 AA; 87554 MW; C983E7ABAC0E80B3 CRC64;
MDSRWKLPFM SNKGTPEQPM RKPLSGSYSH NSAGPTPNMS PFEQKPPLPT HMDVRRPSGP
FRIVKATSTE DALTNCIIVS PMDFKQQYII VDNSRVFSTK PVPGFPQGCL GASQPHREWA
SWSLNQQVHV ADYDPYGPHG APYLHSMTLE VDFQNRNRTT NEPFDGEEMA KLFCSSYQSQ
VFSPGQKIVF DFRSYNIKAT VRTISCVDLL IGENQDAENT ADTSKRGLLT SQTEIQFFKA
AHSALRLKAS MTRPASNAIL QPGFKFEDMG IGGLDSEFSA IFRRAFASRL FPPGMVEKLG
INHVKGILLY GPPGTGKTLI ARQIGKMLNA REPKIVNGPE ILNKYVGQSE ENVRKLFADA
EREYRDRGEE SGLHIIIFDE LDAICKKRGS SGGDTGVGDQ VVNQLLAKMD GVDQLNNILV
IGMTNRKDMI DEALLRPGRL EVHMEISLPD EHGRLQILKI HTSRMASNGI LENDVDMEEL
ASLTKNFSGA EIAGLIKSAS SFAFYRHIKV GTTAAVSGNL ENIKVNRNDF LNALSEVRPA
YGVSEEELES RVQGGIINFG KHIEEIITEG KLFVQQVKNS ERTRLVSVLL SGPIASGKTA
LAATIALGSE FPFVKLVSAE SMVGMNENAR VAHVNRVFED SYKSPLSVIV VDEIERIIDW
VPIGPRFSNT LLQTLMVLFK KQPPKGHRLL ILATTSERTM LSRMDMTQSF DAEIAVPNVS
NVTELDRIIQ SIDSFADSNV RADTLQRLQN FTGTDAVNVG VAKILMIAET AKQDVDVVSC
FVEAMARAIP ME
