VPS25_YEAST
ID VPS25_YEAST Reviewed; 202 AA.
AC P47142; D6VWS1;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Vacuolar protein-sorting-associated protein 25;
DE AltName: Full=ESCRT-II complex subunit VPS25;
GN Name=VPS25; Synonyms=VPT25; OrderedLocusNames=YJR102C; ORFNames=J1957;
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, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=12194858; DOI=10.1016/s1534-5807(02)00219-8;
RA Babst M., Katzmann D.J., Snyder W.B., Wendland B., Emr S.D.;
RT "Endosome-associated complex, ESCRT-II, recruits transport machinery for
RT protein sorting at the multivesicular body.";
RL Dev. Cell 3:283-289(2002).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS), AND SUBUNIT.
RX PubMed=15579210; DOI=10.1186/1472-6807-4-10;
RA Wernimont A.K., Weissenhorn W.;
RT "Crystal structure of subunit VPS25 of the endosomal trafficking complex
RT ESCRT-II.";
RL BMC Struct. Biol. 4:10-10(2004).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) IN COMPLEX WITH SNF8 AND VPS36.
RX PubMed=15469844; DOI=10.1016/j.devcel.2004.09.003;
RA Teo H., Perisic O., Gonzalez B., Williams R.L.;
RT "ESCRT-II, an endosome-associated complex required for protein sorting:
RT crystal structure and interactions with ESCRT-III and membranes.";
RL Dev. Cell 7:559-569(2004).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) IN COMPLEX WITH SNF8 AND VPS36.
RX PubMed=15329733; DOI=10.1038/nature02914;
RA Hierro A., Sun J., Rusnak A.S., Kim J., Prag G., Emr S.D., Hurley J.H.;
RT "Structure of the ESCRT-II endosomal trafficking complex.";
RL Nature 431:221-225(2004).
CC -!- FUNCTION: Component of the ESCRT-II complex (endosomal sorting complex
CC required for transport II), which is required for multivesicular body
CC (MVB) formation and sorting of endosomal cargo proteins into MVBs. The
CC MVB pathway mediates delivery of transmembrane proteins into the lumen
CC of the lysosome for degradation. The ESCRT-II complex is probably
CC involved in the recruitment of the ESCRT-III complex.
CC {ECO:0000269|PubMed:12194858}.
CC -!- SUBUNIT: Homodimer. Component of the endosomal sorting complex required
CC for transport II (ESCRT-II), which consists of 2 copies of VPS25, 1
CC copy of SNF8, and 1 copy of VPS36. The ESCRT-II complex interacts
CC directly with the VPS20 subunit of the ESCRT-III complex.
CC {ECO:0000269|PubMed:12194858, ECO:0000269|PubMed:15329733,
CC ECO:0000269|PubMed:15469844, ECO:0000269|PubMed:15579210}.
CC -!- INTERACTION:
CC P47142; Q12483: SNF8; NbExp=6; IntAct=EBI-25595, EBI-30277;
CC P47142; Q04272: VPS20; NbExp=2; IntAct=EBI-25595, EBI-28157;
CC P47142; Q06696: VPS36; NbExp=3; IntAct=EBI-25595, EBI-36540;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12194858}. Endosome
CC membrane {ECO:0000269|PubMed:12194858}; Peripheral membrane protein
CC {ECO:0000269|PubMed:12194858}.
CC -!- SIMILARITY: Belongs to the VPS25 family. {ECO:0000305}.
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DR EMBL; Z49602; CAA89632.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08887.1; -; Genomic_DNA.
DR PIR; S57123; S57123.
DR RefSeq; NP_012636.1; NM_001181760.1.
DR PDB; 1U5T; X-ray; 3.60 A; C/D=1-202.
DR PDB; 1W7P; X-ray; 3.60 A; B/C=1-202.
DR PDB; 1XB4; X-ray; 3.10 A; A/B/C/D=1-202.
DR PDBsum; 1U5T; -.
DR PDBsum; 1W7P; -.
DR PDBsum; 1XB4; -.
DR AlphaFoldDB; P47142; -.
DR SMR; P47142; -.
DR BioGRID; 33858; 115.
DR ComplexPortal; CPX-1623; ESCRT-II complex.
DR DIP; DIP-4446N; -.
DR IntAct; P47142; 8.
DR MINT; P47142; -.
DR STRING; 4932.YJR102C; -.
DR TCDB; 3.A.31.1.1; the endosomal sorting complexes required for transport iii (escrt-iii) family.
DR PaxDb; P47142; -.
DR PRIDE; P47142; -.
DR EnsemblFungi; YJR102C_mRNA; YJR102C; YJR102C.
DR GeneID; 853566; -.
DR KEGG; sce:YJR102C; -.
DR SGD; S000003863; VPS25.
DR VEuPathDB; FungiDB:YJR102C; -.
DR eggNOG; KOG4068; Eukaryota.
DR GeneTree; ENSGT00390000014892; -.
DR HOGENOM; CLU_087657_1_1_1; -.
DR InParanoid; P47142; -.
DR OMA; SQEFHGM; -.
DR BioCyc; YEAST:G3O-31730-MON; -.
DR Reactome; R-SCE-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR EvolutionaryTrace; P47142; -.
DR PRO; PR:P47142; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47142; protein.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0000814; C:ESCRT II complex; IDA:SGD.
DR GO; GO:0042803; F:protein homodimerization activity; IBA:GO_Central.
DR GO; GO:0005198; F:structural molecule activity; IDA:SGD.
DR GO; GO:1904669; P:ATP export; IMP:SGD.
DR GO; GO:0000433; P:carbon catabolite repression of transcription from RNA polymerase II promoter by glucose; IMP:SGD.
DR GO; GO:0006623; P:protein targeting to vacuole; IMP:SGD.
DR GO; GO:0043328; P:protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IBA:GO_Central.
DR GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IDA:ComplexPortal.
DR DisProt; DP01599; -.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.10.10.570; -; 1.
DR InterPro; IPR008570; ESCRT-II_cplx_Vps25-sub.
DR InterPro; IPR014041; ESCRT-II_cplx_Vps25-sub_N.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR13149; PTHR13149; 1.
DR Pfam; PF05871; ESCRT-II; 1.
DR SUPFAM; SSF46785; SSF46785; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Endosome; Membrane; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..202
FT /note="Vacuolar protein-sorting-associated protein 25"
FT /id="PRO_0000215221"
FT HELIX 7..9
FT /evidence="ECO:0007829|PDB:1XB4"
FT HELIX 11..13
FT /evidence="ECO:0007829|PDB:1XB4"
FT HELIX 20..40
FT /evidence="ECO:0007829|PDB:1XB4"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:1XB4"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:1XB4"
FT TURN 79..82
FT /evidence="ECO:0007829|PDB:1XB4"
FT HELIX 87..99
FT /evidence="ECO:0007829|PDB:1XB4"
FT STRAND 102..111
FT /evidence="ECO:0007829|PDB:1XB4"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:1XB4"
FT HELIX 128..140
FT /evidence="ECO:0007829|PDB:1XB4"
FT HELIX 151..154
FT /evidence="ECO:0007829|PDB:1XB4"
FT TURN 164..167
FT /evidence="ECO:0007829|PDB:1XB4"
FT HELIX 170..181
FT /evidence="ECO:0007829|PDB:1XB4"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:1XB4"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:1XB4"
FT STRAND 196..200
FT /evidence="ECO:0007829|PDB:1XB4"
SQ SEQUENCE 202 AA; 23558 MW; 6A4545A8BC772CA2 CRC64;
MSALPPVYSF PPLYTRQPNS LTRRQQISTW IDIISQYCKT KKIWYMSVDG TVINDNELDS
GSTDNDDSKK ISKNLFNNED IQRSVSQVFI DEIWSQMTKE GKCLPIDQSG RRSSNTTTTR
YFILWKSLDS WASLILQWFE DSGKLNQVIT LYELSEGDET VNWEFHRMPE SLLYYCLKPL
CDRNRATMLK DENDKVIAIK VV
