SEC17_YEAST
ID SEC17_YEAST Reviewed; 292 AA.
AC P32602; D6VPU9;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Alpha-soluble NSF attachment protein;
DE Short=SNAP-alpha;
DE AltName: Full=N-ethylmaleimide-sensitive factor attachment protein alpha;
DE AltName: Full=Vesicular-fusion protein SEC17;
DE AltName: Full=alpha-SNAP chaperone;
GN Name=SEC17; OrderedLocusNames=YBL050W; ORFNames=YBL0505, YBL0517;
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=1601878; DOI=10.1016/s0021-9258(19)49812-8;
RA Griff I.C., Schekman R., Rothman J.E., Kaiser C.A.;
RT "The yeast SEC17 gene product is functionally equivalent to mammalian
RT alpha-SNAP protein.";
RL J. Biol. Chem. 267:12106-12115(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8154187; DOI=10.1002/yea.320091210;
RA Scherens B., el Bakkoury M., Vierendeels F., Dubois E., Messenguy F.;
RT "Sequencing and functional analysis of a 32,560 bp segment on the left arm
RT of yeast chromosome II. Identification of 26 open reading frames, including
RT the KIP1 and SEC17 genes.";
RL Yeast 9:1355-1371(1993).
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 PROTEIN SEQUENCE OF 2-10; 52-62; 89-110 AND 121-136, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RA Bienvenut W.V., Peters C.;
RL Submitted (MAY-2005) to UniProtKB.
RN [6]
RP FUNCTION.
RX PubMed=8620540; DOI=10.1016/s0092-8674(00)81084-3;
RA Mayer A., Wickner W., Haas A.;
RT "Sec18p (NSF)-driven release of Sec17p (alpha-SNAP) can precede docking and
RT fusion of yeast vacuoles.";
RL Cell 85:83-94(1996).
RN [7]
RP FUNCTION.
RX PubMed=8670830; DOI=10.1002/j.1460-2075.1996.tb00694.x;
RA Haas A., Wickner W.;
RT "Homotypic vacuole fusion requires Sec17p (yeast alpha-SNAP) and Sec18p
RT (yeast NSF).";
RL EMBO J. 15:3296-3305(1996).
RN [8]
RP FUNCTION.
RX PubMed=9144293; DOI=10.1038/387199a0;
RA Nichols B.J., Ungermann C., Pelham H.R.B., Wickner W.T., Haas A.;
RT "Homotypic vacuolar fusion mediated by t- and v-SNAREs.";
RL Nature 387:199-202(1997).
RN [9]
RP FUNCTION, AND INTERACTION WITH CIS-SNARE COMPLEX.
RX PubMed=15889152; DOI=10.1038/sj.emboj.7600658;
RA Collins K.M., Thorngren N.L., Fratti R.A., Wickner W.T.;
RT "Sec17p and HOPS, in distinct SNARE complexes, mediate SNARE complex
RT disruption or assembly for fusion.";
RL EMBO J. 24:1775-1786(2005).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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).
RN [11]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-261, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-292.
RX PubMed=10445030; DOI=10.1016/s1097-2765(00)80190-2;
RA Rice L.M., Brunger A.T.;
RT "Crystal structure of the vesicular transport protein Sec17: implications
RT for SNAP function in SNARE complex disassembly.";
RL Mol. Cell 4:85-95(1999).
CC -!- FUNCTION: SNARE complex protein that binds to cis-SNARE complexes on
CC membranes and is required for vesicular transport between the
CC endoplasmic reticulum and the Golgi apparatus and for homotypic vacuole
CC fusion. During the priming step of membrane fusion, is released from
CC cis-SNARE complexes by SEC18 to establish a pool of unpaired SNAREs,
CC which are required for interactions in trans during docking and fusion
CC steps. Can displace HOPS from SNARE complexes, which may be a
CC prerequisite for trans-SNARE complex disassembly and subsequent rounds
CC of priming, docking and fusion. {ECO:0000269|PubMed:15889152,
CC ECO:0000269|PubMed:8620540, ECO:0000269|PubMed:8670830,
CC ECO:0000269|PubMed:9144293}.
CC -!- SUBUNIT: Binds to vacuolar cis-SNARE complexes composed of the v-SNAREs
CC NYV1, VTI1 and YKT6, and the t-SNAREs VAM3 and VAM7. Interacts with
CC SEC18. {ECO:0000269|PubMed:15889152}.
CC -!- INTERACTION:
CC P32602; Q03322: TLG1; NbExp=3; IntAct=EBI-16558, EBI-38705;
CC P32602; Q08144: TLG2; NbExp=2; IntAct=EBI-16558, EBI-19302;
CC -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein.
CC -!- SIMILARITY: Belongs to the SNAP family. {ECO:0000305}.
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DR EMBL; M93104; AAA35029.1; -; Genomic_DNA.
DR EMBL; Z23261; CAA80796.1; -; Genomic_DNA.
DR EMBL; Z35811; CAA84870.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07069.1; -; Genomic_DNA.
DR PIR; S39837; S39837.
DR RefSeq; NP_009503.1; NM_001178290.1.
DR PDB; 1QQE; X-ray; 2.90 A; A=1-292.
DR PDBsum; 1QQE; -.
DR AlphaFoldDB; P32602; -.
DR SMR; P32602; -.
DR BioGRID; 32648; 409.
DR DIP; DIP-2496N; -.
DR IntAct; P32602; 39.
DR MINT; P32602; -.
DR STRING; 4932.YBL050W; -.
DR TCDB; 1.F.1.1.2; the synaptosomal vesicle fusion pore (svf-pore) family.
DR iPTMnet; P32602; -.
DR MaxQB; P32602; -.
DR PaxDb; P32602; -.
DR PRIDE; P32602; -.
DR EnsemblFungi; YBL050W_mRNA; YBL050W; YBL050W.
DR GeneID; 852230; -.
DR KEGG; sce:YBL050W; -.
DR SGD; S000000146; SEC17.
DR VEuPathDB; FungiDB:YBL050W; -.
DR eggNOG; KOG1586; Eukaryota.
DR GeneTree; ENSGT00390000005826; -.
DR HOGENOM; CLU_046329_0_2_1; -.
DR OMA; WSVKEYL; -.
DR BioCyc; YEAST:G3O-28949-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; P32602; -.
DR PRO; PR:P32602; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P32602; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0019898; C:extrinsic component of membrane; IDA:SGD.
DR GO; GO:0000329; C:fungal-type vacuole membrane; HDA:SGD.
DR GO; GO:0031201; C:SNARE complex; IPI:SGD.
DR GO; GO:0001671; F:ATPase activator activity; IDA:SGD.
DR GO; GO:0005483; F:soluble NSF attachment protein activity; IDA:SGD.
DR GO; GO:0019905; F:syntaxin binding; IBA:GO_Central.
DR GO; GO:0006914; P:autophagy; IMP:SGD.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
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 CDD; cd15832; SNAP; 1.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR000744; NSF_attach.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR13768; PTHR13768; 1.
DR PRINTS; PR00448; NSFATTACHMNT.
DR SUPFAM; SSF48452; SSF48452; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; ER-Golgi transport;
KW Isopeptide bond; Membrane; Protein transport; Reference proteome;
KW Transport; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:22814378"
FT CHAIN 2..292
FT /note="Alpha-soluble NSF attachment protein"
FT /id="PRO_0000219076"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:22814378"
FT CROSSLNK 261
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CONFLICT 103
FT /note="A -> P (in Ref. 1; AAA35029)"
FT /evidence="ECO:0000305"
FT CONFLICT 219
FT /note="Missing (in Ref. 1; AAA35029)"
FT /evidence="ECO:0000305"
FT HELIX 4..14
FT /evidence="ECO:0007829|PDB:1QQE"
FT HELIX 21..25
FT /evidence="ECO:0007829|PDB:1QQE"
FT HELIX 30..49
FT /evidence="ECO:0007829|PDB:1QQE"
FT HELIX 54..69
FT /evidence="ECO:0007829|PDB:1QQE"
FT HELIX 73..89
FT /evidence="ECO:0007829|PDB:1QQE"
FT HELIX 93..109
FT /evidence="ECO:0007829|PDB:1QQE"
FT HELIX 113..129
FT /evidence="ECO:0007829|PDB:1QQE"
FT HELIX 134..150
FT /evidence="ECO:0007829|PDB:1QQE"
FT HELIX 154..170
FT /evidence="ECO:0007829|PDB:1QQE"
FT HELIX 174..186
FT /evidence="ECO:0007829|PDB:1QQE"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:1QQE"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:1QQE"
FT HELIX 198..211
FT /evidence="ECO:0007829|PDB:1QQE"
FT HELIX 215..223
FT /evidence="ECO:0007829|PDB:1QQE"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:1QQE"
FT HELIX 238..249
FT /evidence="ECO:0007829|PDB:1QQE"
FT TURN 253..255
FT /evidence="ECO:0007829|PDB:1QQE"
FT HELIX 256..263
FT /evidence="ECO:0007829|PDB:1QQE"
FT HELIX 271..288
FT /evidence="ECO:0007829|PDB:1QQE"
SQ SEQUENCE 292 AA; 32803 MW; 5002D31F80A65319 CRC64;
MSDPVELLKR AEKKGVPSSG FMKLFSGSDS YKFEEAADLC VQAATIYRLR KELNLAGDSF
LKAADYQKKA GNEDEAGNTY VEAYKCFKSG GNSVNAVDSL ENAIQIFTHR GQFRRGANFK
FELGEILEND LHDYAKAIDC YELAGEWYAQ DQSVALSNKC FIKCADLKAL DGQYIEASDI
YSKLIKSSMG NRLSQWSLKD YFLKKGLCQL AATDAVAAAR TLQEGQSEDP NFADSRESNF
LKSLIDAVNE GDSEQLSEHC KEFDNFMRLD KWKITILNKI KESIQQQEDD LL
