VPS53_YEAST
ID VPS53_YEAST Reviewed; 822 AA.
AC P47061; D6VWF3;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Vacuolar protein sorting-associated protein 53;
GN Name=VPS53; OrderedLocusNames=YJL029C; ORFNames=J1258;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [2]
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 [3]
RP FUNCTION, AND INTERACTION WITH VPS52 AND VPS54.
RX PubMed=10637310; DOI=10.1091/mbc.11.1.305;
RA Conibear E., Stevens T.H.;
RT "Vps52p, Vps53p, and Vps54p form a novel multisubunit complex required for
RT protein sorting at the yeast late Golgi.";
RL Mol. Biol. Cell 11:305-323(2000).
RN [4]
RP FUNCTION, AND INTERACTION WITH TLG1 AND YPT6.
RX PubMed=11689439; DOI=10.1093/emboj/20.21.5991;
RA Siniossoglou S., Pelham H.R.B.;
RT "An effector of Ypt6p binds the SNARE Tlg1p and mediates selective fusion
RT of vesicles with late Golgi membranes.";
RL EMBO J. 20:5991-5998(2001).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12377769; DOI=10.1074/jbc.m209428200;
RA Siniossoglou S., Pelham H.R.B.;
RT "Vps51p links the VFT complex to the SNARE Tlg1p.";
RL J. Biol. Chem. 277:48318-48324(2002).
RN [6]
RP INTERACTION WITH ARL1.
RX PubMed=12620189; DOI=10.1016/s0960-9822(03)00091-5;
RA Panic B., Whyte J.R.C., Munro S.;
RT "The ARF-like GTPases Arl1p and Arl3p act in a pathway that interacts with
RT vesicle-tethering factors at the Golgi apparatus.";
RL Curr. Biol. 13:405-410(2003).
RN [7]
RP FUNCTION, AND INTERACTION WITH VPS51; VPS52 AND VPS54.
RX PubMed=12446664; DOI=10.1074/jbc.m210436200;
RA Reggiori F., Wang C.-W., Stromhaug P.E., Shintani T., Klionsky D.J.;
RT "Vps51 is part of the yeast Vps fifty-three tethering complex essential for
RT retrograde traffic from the early endosome and Cvt vesicle completion.";
RL J. Biol. Chem. 278:5009-5020(2003).
RN [8]
RP FUNCTION, AND INTERACTION WITH VPS51; VPS52; VPS54 AND TLG1.
RX PubMed=12686613; DOI=10.1091/mbc.e02-10-0654;
RA Conibear E., Cleck J.N., Stevens T.H.;
RT "Vps51p mediates the association of the GARP (Vps52/53/54) complex with the
RT late Golgi t-SNARE Tlg1p.";
RL Mol. Biol. Cell 14:1610-1623(2003).
RN [9]
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 [10]
RP IDENTIFICATION BY 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 [11]
RP IDENTIFICATION BY 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).
CC -!- FUNCTION: Involved in retrograde transport from early and late
CC endosomes to late Golgi by linking the vesicle through the t-SNARE TGL1
CC to the Golgi, leading to the membrane fusion between late Golgi and
CC endosomal vesicles. {ECO:0000269|PubMed:10637310,
CC ECO:0000269|PubMed:11689439, ECO:0000269|PubMed:12377769,
CC ECO:0000269|PubMed:12446664, ECO:0000269|PubMed:12686613}.
CC -!- SUBUNIT: Component of the Golgi-associated retrograde protein (GARP)
CC complex, also called VFT (VPS fifty-three) complex, composed of VPS51,
CC VPS52, VPS53 and VPS54. Interacts also with TLG1, YPT6 and ARL1.
CC {ECO:0000269|PubMed:10637310, ECO:0000269|PubMed:11689439,
CC ECO:0000269|PubMed:12446664, ECO:0000269|PubMed:12620189,
CC ECO:0000269|PubMed:12686613}.
CC -!- INTERACTION:
CC P47061; P38116: ARL1; NbExp=3; IntAct=EBI-25828, EBI-2869;
CC P47061; P39904: VPS52; NbExp=7; IntAct=EBI-25828, EBI-16418;
CC P47061; Q12071: VPS54; NbExp=9; IntAct=EBI-25828, EBI-36751;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane;
CC Peripheral membrane protein. Endosome membrane; Peripheral membrane
CC protein.
CC -!- SIMILARITY: Belongs to the VPS53 family. {ECO:0000305}.
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DR EMBL; Z49304; CAA89320.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08769.1; -; Genomic_DNA.
DR PIR; S56801; S56801.
DR RefSeq; NP_012505.1; NM_001181463.1.
DR PDB; 3NS4; X-ray; 2.90 A; A=554-822.
DR PDBsum; 3NS4; -.
DR AlphaFoldDB; P47061; -.
DR SMR; P47061; -.
DR BioGRID; 33730; 710.
DR ComplexPortal; CPX-1718; GARP complex.
DR DIP; DIP-5902N; -.
DR IntAct; P47061; 8.
DR MINT; P47061; -.
DR STRING; 4932.YJL029C; -.
DR iPTMnet; P47061; -.
DR MaxQB; P47061; -.
DR PaxDb; P47061; -.
DR PRIDE; P47061; -.
DR EnsemblFungi; YJL029C_mRNA; YJL029C; YJL029C.
DR GeneID; 853423; -.
DR KEGG; sce:YJL029C; -.
DR SGD; S000003566; VPS53.
DR VEuPathDB; FungiDB:YJL029C; -.
DR eggNOG; KOG2180; Eukaryota.
DR GeneTree; ENSGT00390000015165; -.
DR HOGENOM; CLU_358642_0_0_1; -.
DR InParanoid; P47061; -.
DR OMA; YIDVRFS; -.
DR BioCyc; YEAST:G3O-31498-MON; -.
DR EvolutionaryTrace; P47061; -.
DR PRO; PR:P47061; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47061; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000938; C:GARP complex; IPI:SGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:SGD.
DR GO; GO:0090156; P:cellular sphingolipid homeostasis; IMP:SGD.
DR GO; GO:0006896; P:Golgi to vacuole transport; IMP:SGD.
DR GO; GO:0006623; P:protein targeting to vacuole; IDA:ComplexPortal.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IDA:SGD.
DR Gene3D; 1.10.357.110; -; 1.
DR InterPro; IPR039766; Vps53.
DR InterPro; IPR031745; Vps53_C.
DR InterPro; IPR038260; Vps53_C_sf.
DR InterPro; IPR007234; Vps53_N.
DR PANTHER; PTHR12820; PTHR12820; 2.
DR Pfam; PF16854; VPS53_C; 1.
DR Pfam; PF04100; Vps53_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Endosome; Golgi apparatus; Membrane;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..822
FT /note="Vacuolar protein sorting-associated protein 53"
FT /id="PRO_0000215193"
FT COILED 34..58
FT /evidence="ECO:0000255"
FT COILED 460..484
FT /evidence="ECO:0000255"
FT HELIX 567..569
FT /evidence="ECO:0007829|PDB:3NS4"
FT HELIX 571..598
FT /evidence="ECO:0007829|PDB:3NS4"
FT STRAND 605..608
FT /evidence="ECO:0007829|PDB:3NS4"
FT HELIX 615..638
FT /evidence="ECO:0007829|PDB:3NS4"
FT HELIX 639..643
FT /evidence="ECO:0007829|PDB:3NS4"
FT HELIX 653..676
FT /evidence="ECO:0007829|PDB:3NS4"
FT HELIX 683..693
FT /evidence="ECO:0007829|PDB:3NS4"
FT HELIX 700..710
FT /evidence="ECO:0007829|PDB:3NS4"
FT HELIX 716..729
FT /evidence="ECO:0007829|PDB:3NS4"
FT HELIX 746..750
FT /evidence="ECO:0007829|PDB:3NS4"
FT HELIX 752..763
FT /evidence="ECO:0007829|PDB:3NS4"
FT HELIX 768..776
FT /evidence="ECO:0007829|PDB:3NS4"
SQ SEQUENCE 822 AA; 95449 MW; C75F19FA57157481 CRC64;
MLEGTVDYDP LEDITNILFS KESLNNIDEL ISITRSYKKQ LQEDILKEEN ELKEHPKNSA
EIEASLRKVF QDFKETQDVS ASTELTISNL TEGISYLDIA KKNLTHSLTL FQNLKILTDS
YIQCNELLSQ GSFKKMVSPY KIMCSLAENT FISYKSLDEI NYLLSSISRL KGDTLSKIKQ
NYNALFSGGN ISEHDTALTM ELREGACELL DCDTSTRAQM IDWCLDKLLF EMKEIFRVDD
EAGSLENLSR RYIYFKKILN NFNSKFADYF LKDWEMAVRL TTTFYHITHK DLQTLLKREF
KDKNPSIDLF MTALQSTLDF EKYIDVRFSK KIKEPKLSSC FEPYLTLWVS HQNQMMEKKF
LSYMSEPKYP SNETESLVLP SSADLFRTYR SVLTQTLELI DNNANDSILT SLANFFSRWL
QTYSQKILLP LLLPDNIEVQ DKLEAAKYTV LLINTADYCA TTIDQLEDKL SEFSGNREKL
ANSFTKTKNI YDDLLAKGTS FLLNRVIPLD LNFVWREFIN NDWSNAAIED YSRYMVTLKS
VLKMPALTDA SIKQQQEQPS TLAFILSQFN RDVYKWNFLD KVIDIITTNF VSNTIRLLQP
VPPFSLAGSK RKFETRTVVN IGEQLLLDLE LLKEIFHTLP ESVSNDSDLR ENTSYKRVKR
HADNNIDQLL KFIKLLMAPL DSADDYYETY SKLTNNNPDS AVWSFVLALK GIPWDLALWK
KLWSAYNLET DDTDEGSRPD SNRDLFIFKW DKVLLGQFEN NLARMQDPNW SKFVRQDLKI
SPPVMKRIVS TPQIQQQKEE QKKQSLSVKD FVSHSRFFNR GT
