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   08-NOV-2023, entry version 169.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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; 116.
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; 4932-YJR102C; -.
DR   PeptideAtlas; P47142; -.
DR   EnsemblFungi; YJR102C_mRNA; YJR102C; YJR102C.
DR   GeneID; 853566; -.
DR   KEGG; sce:YJR102C; -.
DR   AGR; SGD:S000003863; -.
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; WHTLEEW; -.
DR   OrthoDB; 5489167at2759; -.
DR   BioCyc; YEAST:G3O-31730-MONOMER; -.
DR   Reactome; R-SCE-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR   BioGRID-ORCS; 853566; 0 hits in 10 CRISPR screens.
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; 1.10.10.570; Winged helix' DNA-binding domain. Chain C. Domain 1; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN VPS25; 1.
DR   PANTHER; PTHR13149:SF0; VACUOLAR PROTEIN-SORTING-ASSOCIATED PROTEIN 25; 1.
DR   Pfam; PF05871; ESCRT-II; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 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
//