VPS36_YEAST
ID VPS36_YEAST Reviewed; 566 AA.
AC Q06696; D6VZ53;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Vacuolar protein-sorting-associated protein 36;
DE AltName: Full=ESCRT-II complex subunit VPS36;
GN Name=VPS36; Synonyms=GRD12, VAC3, VPL11; OrderedLocusNames=YLR417W;
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=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
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 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).
RN [5]
RP FUNCTION, SUBUNIT, DOMAIN, AND MUTAGENESIS OF 187-THR-PHE-188.
RX PubMed=15029239; DOI=10.1038/sj.emboj.7600114;
RA Alam S.L., Sun J., Payne M., Welch B.D., Blake B.K., Davis D.R.,
RA Meyer H.H., Emr S.D., Sundquist W.I.;
RT "Ubiquitin interactions of NZF zinc fingers.";
RL EMBO J. 23:1411-1421(2004).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) IN COMPLEX WITH VPS25 AND SNF8, AND
RP FUNCTION.
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 [7]
RP X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) IN COMPLEX WITH VPS25 AND SNF8, AND
RP FUNCTION.
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, which is required for
CC multivesicular body (MVB) formation and sorting of endosomal cargo
CC proteins into MVBs (PubMed:12194858, PubMed:15469844, PubMed:15329733).
CC The MVB pathway mediates delivery of transmembrane proteins into the
CC lumen of the lysosome for degradation (PubMed:12194858). The ESCRT-II
CC complex is probably involved in the recruitment of the ESCRT-III
CC complex (PubMed:12194858). Involved in the trafficking of the plasma
CC membrane ATPase (PubMed:12194858). Its ability to bind ubiquitin plays
CC a central role in endosomal sorting of ubiquitinated cargo proteins by
CC the ESCRT complexes (PubMed:15029239). {ECO:0000269|PubMed:12194858,
CC ECO:0000269|PubMed:15029239, ECO:0000269|PubMed:15329733,
CC ECO:0000269|PubMed:15469844}.
CC -!- SUBUNIT: Component of the endosomal sorting required for transport
CC complex II (ESCRT-II), which consists of 2 copies of VPS25, 1 copy of
CC SNF8, and 1 copy of VPS36 (PubMed:15329733, PubMed:15469844). The
CC ESCRT-II complex interacts directly with the VPS20 subunit of the
CC ESCRT-III complex (PubMed:12194858). Binds ubiquitin (PubMed:15029239).
CC {ECO:0000269|PubMed:12194858, ECO:0000269|PubMed:15029239,
CC ECO:0000269|PubMed:15329733, ECO:0000269|PubMed:15469844}.
CC -!- INTERACTION:
CC Q06696; Q12483: SNF8; NbExp=10; IntAct=EBI-36540, EBI-30277;
CC Q06696; P47142: VPS25; NbExp=3; IntAct=EBI-36540, EBI-25595;
CC Q06696; Q02767: VPS28; NbExp=6; IntAct=EBI-36540, EBI-20387;
CC Q06696; P62991: Ubc; Xeno; NbExp=2; IntAct=EBI-36540, EBI-413074;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12194858}. Endosome
CC membrane {ECO:0000269|PubMed:12194858}; Peripheral membrane protein
CC {ECO:0000269|PubMed:12194858}.
CC -!- DOMAIN: The second RanBP2-type zinc-finger is functional and binds
CC ubiquitin. {ECO:0000269|PubMed:15029239}.
CC -!- MISCELLANEOUS: Present with 2470 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the VPS36 family. {ECO:0000305}.
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DR EMBL; U20162; AAB67493.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09719.1; -; Genomic_DNA.
DR PIR; S59382; S59382.
DR RefSeq; NP_013521.3; NM_001182305.3.
DR PDB; 1U5T; X-ray; 3.60 A; B=396-564.
DR PDB; 1W7P; X-ray; 3.60 A; D=1-566.
DR PDB; 2CAY; X-ray; 1.90 A; A/B=1-98, A=251-289.
DR PDB; 2J9U; X-ray; 2.00 A; B/D=110-171.
DR PDBsum; 1U5T; -.
DR PDBsum; 1W7P; -.
DR PDBsum; 2CAY; -.
DR PDBsum; 2J9U; -.
DR AlphaFoldDB; Q06696; -.
DR SMR; Q06696; -.
DR BioGRID; 31675; 165.
DR ComplexPortal; CPX-1623; ESCRT-II complex.
DR DIP; DIP-1744N; -.
DR IntAct; Q06696; 10.
DR MINT; Q06696; -.
DR STRING; 4932.YLR417W; -.
DR TCDB; 3.A.31.1.1; the endosomal sorting complexes required for transport iii (escrt-iii) family.
DR MaxQB; Q06696; -.
DR PaxDb; Q06696; -.
DR PRIDE; Q06696; -.
DR EnsemblFungi; YLR417W_mRNA; YLR417W; YLR417W.
DR GeneID; 851135; -.
DR KEGG; sce:YLR417W; -.
DR SGD; S000004409; VPS36.
DR VEuPathDB; FungiDB:YLR417W; -.
DR eggNOG; KOG2760; Eukaryota.
DR GeneTree; ENSGT00390000017209; -.
DR HOGENOM; CLU_015433_2_1_1; -.
DR InParanoid; Q06696; -.
DR OMA; YQNGHAY; -.
DR BioCyc; YEAST:G3O-32478-MON; -.
DR Reactome; R-SCE-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR EvolutionaryTrace; Q06696; -.
DR PRO; PR:Q06696; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q06696; protein.
DR GO; GO:0000814; C:ESCRT II complex; IDA:SGD.
DR GO; GO:0031902; C:late endosome membrane; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IEA:InterPro.
DR GO; GO:0043130; F:ubiquitin binding; 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:0032258; P:cytoplasm to vacuole transport by the Cvt pathway; IMP:SGD.
DR GO; GO:0016236; P:macroautophagy; IMP:SGD.
DR GO; GO:0045053; P:protein retention in Golgi apparatus; 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; DP01611; -.
DR Gene3D; 1.10.10.10; -; 2.
DR Gene3D; 2.30.29.30; -; 2.
DR InterPro; IPR021648; GLUE_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR040608; Snf8/Vps36.
DR InterPro; IPR037855; Vps36.
DR InterPro; IPR031558; Vps36-NZF-N.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR PANTHER; PTHR13128; PTHR13128; 1.
DR Pfam; PF04157; EAP30; 1.
DR Pfam; PF16988; Vps36-NZF-N; 1.
DR Pfam; PF11605; Vps36_ESCRT-II; 1.
DR SMART; SM00547; ZnF_RBZ; 2.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF90209; SSF90209; 1.
DR PROSITE; PS51495; GLUE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Endosome; Membrane; Metal-binding;
KW Protein transport; Reference proteome; Repeat; Transport; Zinc;
KW Zinc-finger.
FT CHAIN 1..566
FT /note="Vacuolar protein-sorting-associated protein 36"
FT /id="PRO_0000215227"
FT DOMAIN 7..96
FT /note="GLUE N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00828"
FT DOMAIN 255..288
FT /note="GLUE C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00828"
FT ZN_FING 114..151
FT /note="RanBP2-type 1; degenerate"
FT ZN_FING 177..205
FT /note="RanBP2-type 2"
FT MUTAGEN 187..188
FT /note="TF->GS: Abolishes ubiquitin-binding and vacuole
FT sorting of ubiquitinated proteins."
FT /evidence="ECO:0000269|PubMed:15029239"
FT STRAND 23..34
FT /evidence="ECO:0007829|PDB:2CAY"
FT STRAND 43..60
FT /evidence="ECO:0007829|PDB:2CAY"
FT HELIX 62..65
FT /evidence="ECO:0007829|PDB:2CAY"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:2CAY"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:2CAY"
FT STRAND 74..80
FT /evidence="ECO:0007829|PDB:2CAY"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:2CAY"
FT STRAND 89..96
FT /evidence="ECO:0007829|PDB:2CAY"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:2J9U"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:2J9U"
FT STRAND 126..131
FT /evidence="ECO:0007829|PDB:2J9U"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:2J9U"
FT HELIX 152..155
FT /evidence="ECO:0007829|PDB:2J9U"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:2J9U"
SQ SEQUENCE 566 AA; 64018 MW; 60DDD4EA3A620409 CRC64;
MEYWHYVETT SSGQPLLREG EKDIFIDQSV GLYHGKSKIL QRQRGRIFLT SQRIIYIDDA
KPTQNSLGLE LDDLAYVNYS SGFLTRSPRL ILFFKDPSSK DELGKSAETA SADVVSTWVC
PICMVSNETQ GEFTKDTLPT PICINCGVPA DYELTKSSIN CSNAIDPNAN PQNQFGVNSE
NICPACTFAN HPQIGNCEIC GHRLPNASKV RSKLNRLNFH DSRVHIELEK NSLARNKSSH
SALSSSSSTG SSTEFVQLSF RKSDGVLFSQ ATERALENIL TEKNKHIFNQ NVVSVNGVDM
RKGASSHEYN NEVPFIETKL SRIGISSLEK SRENQLLNND ILFNNALTDL NKLMSLATSI
ERLYKNSNIT MKTKTLNLQD ESTVNEPKTR RPLLILDREK FLNKELFLDE IAREIYEFTL
SEFKDLNSDT NYMIITLVDL YAMYNKSMRI GTGLISPMEM REACERFEHL GLNELKLVKV
NKRILCVTSE KFDVVKEKLV DLIGDNPGSD LLRLTQILSS NNSKSNWTLG ILMEVLQNCV
DEGDLLIDKQ LSGIYYYKNS YWPSHI
