VPS45_YEAST
ID VPS45_YEAST Reviewed; 577 AA.
AC P38932; D6VU50;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Vacuolar protein sorting-associated protein 45;
GN Name=VPS45; Synonyms=STT10, VPL28; OrderedLocusNames=YGL095C;
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=7720726;
RA Piper R.C., Whitters E.A., Stevens T.H.;
RT "Yeast Vps45p is a Sec1p-like protein required for the consumption of
RT vacuole-targeted, post-Golgi transport vesicles.";
RL Eur. J. Cell Biol. 65:305-318(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7628704; DOI=10.1016/0378-1119(95)00214-q;
RA Yoshida S., Ohya Y., Hirose R., Nakano A., Anraku Y.;
RT "STT10, a novel class-D VPS yeast gene required for osmotic integrity
RT related to the PKC1/STT1 protein kinase pathway.";
RL Gene 160:117-122(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7706396; DOI=10.1242/jcs.107.12.3449;
RA Cowles C.R., Emr S.D., Horazdovsky B.F.;
RT "Mutations in the VPS45 gene, a SEC1 homologue, result in vacuolar protein
RT sorting defects and accumulation of membrane vesicles.";
RL J. Cell Sci. 107:3449-3459(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9290212;
RX DOI=10.1002/(sici)1097-0061(19970915)13:11<1077::aid-yea152>3.0.co;2-y;
RA Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.;
RT "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae
RT chromosome VII.";
RL Yeast 13:1077-1090(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [6]
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 [7]
RP INTERACTION WITH TLG2.
RX PubMed=9930650; DOI=10.1016/s0171-9335(98)80084-8;
RA Nichols B.J., Holthuis J.C., Pelham H.R.;
RT "The Sec1p homologue Vps45p binds to the syntaxin Tlg2p.";
RL Eur. J. Cell Biol. 77:263-268(1998).
RN [8]
RP INTERACTION WITH PEP7.
RX PubMed=10359603; DOI=10.1091/mbc.10.6.1873;
RA Tall G.G., Hama H., DeWald D.B., Horazdovsky B.F.;
RT "The phosphatidylinositol 3-phosphate binding protein Vac1p interacts with
RT a Rab GTPase and a Sec1p homologue to facilitate vesicle-mediated vacuolar
RT protein sorting.";
RL Mol. Biol. Cell 10:1873-1889(1999).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=12756236; DOI=10.1083/jcb.200212078;
RA Bryant N.J., James D.E.;
RT "The Sec1p/Munc18 (SM) protein, Vps45p, cycles on and off membranes during
RT vesicle transport.";
RL J. Cell Biol. 161:691-696(2003).
RN [10]
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).
CC -!- FUNCTION: Essential for vacuolar protein sorting. Function in membrane
CC traffic between the Golgi and the vacuole.
CC {ECO:0000269|PubMed:7628704}.
CC -!- SUBUNIT: Interacts with PEP7 and TLG2. {ECO:0000269|PubMed:10359603,
CC ECO:0000269|PubMed:9930650}.
CC -!- INTERACTION:
CC P38932; P32609: PEP7; NbExp=3; IntAct=EBI-20444, EBI-20208;
CC P38932; Q03322: TLG1; NbExp=3; IntAct=EBI-20444, EBI-38705;
CC P38932; Q08144: TLG2; NbExp=4; IntAct=EBI-20444, EBI-19302;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12756236}. Vacuole
CC membrane {ECO:0000269|PubMed:12756236}; Peripheral membrane protein
CC {ECO:0000269|PubMed:12756236}; Cytoplasmic side
CC {ECO:0000269|PubMed:12756236}. Note=Cycles between the cytoplasmic side
CC of the vacuolar membrane and the cytoplasm.
CC -!- MISCELLANEOUS: Present with 5660 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the STXBP/unc-18/SEC1 family. {ECO:0000305}.
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DR EMBL; U07972; AAA79230.1; -; Genomic_DNA.
DR EMBL; D28953; BAA06080.1; -; Genomic_DNA.
DR EMBL; U11049; AAC48980.1; -; Genomic_DNA.
DR EMBL; Z72617; CAA96801.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08011.1; -; Genomic_DNA.
DR PIR; S48542; S48542.
DR RefSeq; NP_011420.3; NM_001180960.3.
DR AlphaFoldDB; P38932; -.
DR SMR; P38932; -.
DR BioGRID; 33156; 165.
DR DIP; DIP-2693N; -.
DR IntAct; P38932; 14.
DR MINT; P38932; -.
DR STRING; 4932.YGL095C; -.
DR iPTMnet; P38932; -.
DR MaxQB; P38932; -.
DR PaxDb; P38932; -.
DR PRIDE; P38932; -.
DR EnsemblFungi; YGL095C_mRNA; YGL095C; YGL095C.
DR GeneID; 852785; -.
DR KEGG; sce:YGL095C; -.
DR SGD; S000003063; VPS45.
DR VEuPathDB; FungiDB:YGL095C; -.
DR eggNOG; KOG1299; Eukaryota.
DR GeneTree; ENSGT00550000075028; -.
DR HOGENOM; CLU_013933_3_1_1; -.
DR InParanoid; P38932; -.
DR OMA; VHQLNNA; -.
DR BioCyc; YEAST:G3O-30595-MON; -.
DR PRO; PR:P38932; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P38932; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0019898; C:extrinsic component of membrane; IDA:SGD.
DR GO; GO:0000139; C:Golgi membrane; IDA:SGD.
DR GO; GO:0031201; C:SNARE complex; IPI:SGD.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000149; F:SNARE binding; IPI:SGD.
DR GO; GO:0051082; F:unfolded protein binding; IMP:SGD.
DR GO; GO:0032258; P:cytoplasm to vacuole transport by the Cvt pathway; IMP:SGD.
DR GO; GO:0006895; P:Golgi to endosome transport; IGI:SGD.
DR GO; GO:0006896; P:Golgi to vacuole transport; IMP:SGD.
DR GO; GO:0048210; P:Golgi vesicle fusion to target membrane; IMP:SGD.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0035543; P:positive regulation of SNARE complex assembly; IMP:SGD.
DR GO; GO:0006623; P:protein targeting to vacuole; IMP:SGD.
DR GO; GO:0007035; P:vacuolar acidification; IMP:SGD.
DR GO; GO:0000011; P:vacuole inheritance; IMP:SGD.
DR GO; GO:0007033; P:vacuole organization; IMP:SGD.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR Gene3D; 3.40.50.1910; -; 1.
DR Gene3D; 3.40.50.2060; -; 1.
DR Gene3D; 3.90.830.10; -; 1.
DR InterPro; IPR043154; Sec-1-like_dom1.
DR InterPro; IPR043127; Sec-1-like_dom3a.
DR InterPro; IPR001619; Sec1-like.
DR InterPro; IPR027482; Sec1-like_dom2.
DR InterPro; IPR036045; Sec1-like_sf.
DR PANTHER; PTHR11679; PTHR11679; 1.
DR Pfam; PF00995; Sec1; 1.
DR PIRSF; PIRSF005715; VPS45_Sec1; 1.
DR SUPFAM; SSF56815; SSF56815; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Membrane; Protein transport; Reference proteome; Transport;
KW Vacuole.
FT CHAIN 1..577
FT /note="Vacuolar protein sorting-associated protein 45"
FT /id="PRO_0000206316"
FT CONFLICT 136
FT /note="F -> S (in Ref. 1; AAA79230)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="P -> T (in Ref. 1; AAA79230)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 577 AA; 67017 MW; 4AA50D568228228F CRC64;
MNLFDVADFY INKIVTSQSK LSVANVNEHQ RIKVLLLDKN TTPTISLCAT QSELLKHEIY
LVERIENEQR EVSRHLRCLV YVKPTEETLQ HLLRELRNPR YGEYQIFFSN IVSKSQLERL
AESDDLEAVT KVEEIFQDFF ILNQDLFSFD LQPREFLSNK LVWSEGGLTK CTNSLVSVLL
SLKIKPDIRY EGASKICERL AKEVSYEIGK NERTFFDFPV MDSTPVLLIL DRNTDPITPL
LQPWTYQSMI NEYIGIKRNI VDLSKVPRID KDLEKVTLSS KQDAFFRDTM YLNFGELGDK
VKQYVTTYKD KTQTNSQINS IEDIKNFIEK YPEFRKLSGN VAKHMAIVGE LDRQLKIKNI
WEISEIEQNL SAHDANEEDF SDLIKLLQNE AVDKYYKLKL ACIYSLNNQT SSDKIRQLVE
ILSQQLPPED VNFFHKFKSL FSRQDKMTQS NHDKDDILTE LARRFNSRMN SKSNTAENVY
MQHIPEISSL LTDLSKNALF RDRFKEIDTQ GHRVIGNQQS KDIPQDVILF VIGGVTYEEA
RLVHDFNGTM NNRMRVVLGG TSILSTKEYM DSIRSAK
