VPS27_YEAST
ID VPS27_YEAST Reviewed; 622 AA.
AC P40343; D6W1I1;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 3.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Vacuolar protein sorting-associated protein 27;
DE AltName: Full=Golgi retention defective protein 11;
GN Name=VPS27; Synonyms=DID7, GRD11, SSV17, VPL23, VPT27;
GN OrderedLocusNames=YNR006W; ORFNames=N2038;
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=7593183; DOI=10.1083/jcb.131.3.603;
RA Piper R.C., Cooper A.A., Yang H., Stevens T.H.;
RT "VPS27 controls vacuolar and endocytic traffic through a prevacuolar
RT compartment in Saccharomyces cerevisiae.";
RL J. Cell Biol. 131:603-617(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=7900425; DOI=10.1002/yea.320101013;
RA Verhasselt P., Aert R., Voet M., Volckaert G.;
RT "Twelve open reading frames revealed in the 23.6 kb segment flanking the
RT centromere on the Saccharomyces cerevisiae chromosome XIV right arm.";
RL Yeast 10:1355-1361(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [4]
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 [5]
RP FUNCTION.
RX PubMed=3062374; DOI=10.1128/mcb.8.11.4936-4948.1988;
RA Robinson J.S., Klionsky D.J., Banta L.M., Emr S.D.;
RT "Protein sorting in Saccharomyces cerevisiae: isolation of mutants
RT defective in the delivery and processing of multiple vacuolar hydrolases.";
RL Mol. Cell. Biol. 8:4936-4948(1988).
RN [6]
RP FUNCTION.
RX PubMed=1493335; DOI=10.1091/mbc.3.12.1389;
RA Raymond C.K., Howald-Stevenson I., Vater C.A., Stevens T.H.;
RT "Morphological classification of the yeast vacuolar protein sorting
RT mutants: evidence for a prevacuolar compartment in class E vps mutants.";
RL Mol. Biol. Cell 3:1389-1402(1992).
RN [7]
RP FUNCTION.
RX PubMed=8649377; DOI=10.1128/mcb.16.6.2700;
RA Nothwehr S.F., Bryant N.J., Stevens T.H.;
RT "The newly identified yeast GRD genes are required for retention of late-
RT Golgi membrane proteins.";
RL Mol. Cell. Biol. 16:2700-2707(1996).
RN [8]
RP FUNCTION.
RX PubMed=9015300; DOI=10.1083/jcb.136.2.287;
RA Bryant N.J., Stevens T.H.;
RT "Two separate signals act independently to localize a yeast late Golgi
RT membrane protein through a combination of retrieval and retention.";
RL J. Cell Biol. 136:287-297(1997).
RN [9]
RP FUNCTION.
RX PubMed=9265642; DOI=10.1083/jcb.138.4.731;
RA Luo W.-J., Chang A.;
RT "Novel genes involved in endosomal traffic in yeast revealed by suppression
RT of a targeting-defective plasma membrane ATPase mutant.";
RL J. Cell Biol. 138:731-746(1997).
RN [10]
RP DOMAIN, AND PHOSPHATIDYLINOSITOL 3-PHOSPHATE BINDING.
RX PubMed=9702203; DOI=10.1016/s1097-2765(00)80125-2;
RA Burd C.G., Emr S.D.;
RT "Phosphatidylinositol(3)-phosphate signaling mediated by specific binding
RT to RING FYVE domains.";
RL Mol. Cell 2:157-162(1998).
RN [11]
RP FUNCTION.
RX PubMed=11208109; DOI=10.1034/j.1600-0854.2000.010308.x;
RA Gerrard S.R., Levi B.P., Stevens T.H.;
RT "Pep12p is a multifunctional yeast syntaxin that controls entry of
RT biosynthetic, endocytic and retrograde traffic into the prevacuolar
RT compartment.";
RL Traffic 1:259-269(2000).
RN [12]
RP FUNCTION.
RX PubMed=11416128; DOI=10.1128/mcb.21.14.4482-4494.2001;
RA Dupre S., Haguenauer-Tsapis R.;
RT "Deubiquitination step in the endocytic pathway of yeast plasma membrane
RT proteins: crucial role of Doa4p ubiquitin isopeptidase.";
RL Mol. Cell. Biol. 21:4482-4494(2001).
RN [13]
RP DOMAIN, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 185-LEU-LEU-186 AND
RP ARG-193.
RX PubMed=12006563; DOI=10.1074/jbc.m201106200;
RA Stahelin R.V., Long F., Diraviyam K., Bruzik K.S., Murray D., Cho W.;
RT "Phosphatidylinositol 3-phosphate induces the membrane penetration of the
RT FYVE domains of Vps27p and Hrs.";
RL J. Biol. Chem. 277:26379-26388(2002).
RN [14]
RP DOMAINS, INTERACTION WITH UBIQUITIN, AND MUTAGENESIS OF SER-270 AND
RP SER-313.
RX PubMed=11988742; DOI=10.1038/ncb790;
RA Shih S.C., Katzmann D.J., Schnell J.D., Sutanto M., Emr S.D., Hicke L.;
RT "Epsins and Vps27p/Hrs contain ubiquitin-binding domains that function in
RT receptor endocytosis.";
RL Nat. Cell Biol. 4:389-393(2002).
RN [15]
RP IDENTIFICATION IN THE ESCRT-0 COMPLEX, AND FUNCTION OF THE ESCRT-0 COMPLEX.
RX PubMed=12055639; DOI=10.1038/ncb815;
RA Bilodeau P.S., Urbanowski J.L., Winistorfer S.C., Piper R.C.;
RT "The Vps27p-Hse1p complex binds ubiquitin and mediates endosomal protein
RT sorting.";
RL Nat. Cell Biol. 4:534-539(2002).
RN [16]
RP FUNCTION.
RX PubMed=11872141; DOI=10.1034/j.1600-0854.2002.30106.x;
RA Prescianotto-Baschong C., Riezman H.;
RT "Ordering of compartments in the yeast endocytic pathway.";
RL Traffic 3:37-49(2002).
RN [17]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH VPS23 AND VPS28.
RX PubMed=12900393; DOI=10.1083/jcb.200302136;
RA Katzmann D.J., Stefan C.J., Babst M., Emr S.D.;
RT "Vps27 recruits ESCRT machinery to endosomes during MVB sorting.";
RL J. Cell Biol. 162:413-423(2003).
RN [18]
RP FUNCTION OF THE ESCRT-0 COMPLEX, AND INTERACTION WITH UBIQUITIN.
RX PubMed=14581452; DOI=10.1083/jcb.200305007;
RA Bilodeau P.S., Winistorfer S.C., Kearney W.R., Robertson A.D., Piper R.C.;
RT "Vps27-Hse1 and ESCRT-I complexes cooperate to increase efficiency of
RT sorting ubiquitinated proteins at the endosome.";
RL J. Cell Biol. 163:237-243(2003).
RN [19]
RP DOMAIN.
RX PubMed=12706728; DOI=10.1016/s0022-2836(03)00325-5;
RA Diraviyam K., Stahelin R.V., Cho W., Murray D.;
RT "Computer modeling of the membrane interaction of FYVE domains.";
RL J. Mol. Biol. 328:721-736(2003).
RN [20]
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 [21]
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 [22]
RP FUNCTION.
RX PubMed=15166140; DOI=10.1534/genetics.167.1.107;
RA Eguez L., Chung Y.-S., Kuchibhatla A., Paidhungat M., Garrett S.;
RT "Yeast Mn2+ transporter, Smf1p, is regulated by ubiquitin-dependent
RT vacuolar protein sorting.";
RL Genetics 167:107-117(2004).
RN [23]
RP FUNCTION, AND INTERACTION WITH ENT3 AND ENT5.
RX PubMed=15107463; DOI=10.1091/mbc.e03-11-0793;
RA Eugster A., Pecheur E.-I., Michel F., Winsor B., Letourneur F., Friant S.;
RT "Ent5p is required with Ent3p and Vps27p for ubiquitin-dependent protein
RT sorting into the multivesicular body.";
RL Mol. Biol. Cell 15:3031-3041(2004).
RN [24]
RP SUBCELLULAR LOCATION.
RX PubMed=15169871; DOI=10.1091/mbc.e04-03-0209;
RA Parrish W.R., Stefan C.J., Emr S.D.;
RT "Essential role for the myotubularin-related phosphatase Ymr1p and the
RT synaptojanin-like phosphatases Sjl2p and Sjl3p in regulation of
RT phosphatidylinositol 3-phosphate in yeast.";
RL Mol. Biol. Cell 15:3567-3579(2004).
RN [25]
RP INTERACTION WITH HSE1 AND VPS23, AND FUNCTION OF THE ESCRT-0 COMPLEX.
RX PubMed=15086794; DOI=10.1111/j.1600-0854.2004.00169.x;
RA Bowers K., Lottridge J., Helliwell S.B., Goldthwaite L.M., Luzio J.P.,
RA Stevens T.H.;
RT "Protein-protein interactions of ESCRT complexes in the yeast Saccharomyces
RT cerevisiae.";
RL Traffic 5:194-210(2004).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157 AND SER-495, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [28]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SEC27; SEC28 AND
RP SEC33.
RX PubMed=17101773; DOI=10.1128/mcb.00577-06;
RA Gabriely G., Kama R., Gerst J.E.;
RT "Involvement of specific COPI subunits in protein sorting from the late
RT endosome to the vacuole in yeast.";
RL Mol. Cell. Biol. 27:526-540(2007).
RN [29]
RP SUBCELLULAR LOCATION.
RX PubMed=17101785; DOI=10.1128/mcb.00699-06;
RA Kama R., Robinson M., Gerst J.E.;
RT "Btn2, a Hook1 ortholog and potential Batten disease-related protein,
RT mediates late endosome-Golgi protein sorting in yeast.";
RL Mol. Cell. Biol. 27:605-621(2007).
RN [30]
RP FUNCTION.
RX PubMed=17135292; DOI=10.1091/mbc.e06-07-0588;
RA Curtiss M., Jones C., Babst M.;
RT "Efficient cargo sorting by ESCRT-I and the subsequent release of ESCRT-I
RT from multivesicular bodies requires the subunit Mvb12.";
RL Mol. Biol. Cell 18:636-645(2007).
RN [31]
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH HSE1 AND DOA1, AND INTERACTION
RP WITH DOA1.
RX PubMed=18508771; DOI=10.1074/jbc.m802982200;
RA Ren J., Pashkova N., Winistorfer S., Piper R.C.;
RT "DOA1/UFD3 plays a role in sorting ubiquitinated membrane proteins into
RT multivesicular bodies.";
RL J. Biol. Chem. 283:21599-21611(2008).
RN [32]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157 AND SER-613, AND
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).
RN [33]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [34]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-294, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [35]
RP X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS) OF 163-230.
RX PubMed=10367894; DOI=10.1016/s0092-8674(00)80776-x;
RA Misra S., Hurley J.H.;
RT "Crystal structure of a phosphatidylinositol 3-phosphate-specific membrane-
RT targeting motif, the FYVE domain of Vps27p.";
RL Cell 97:657-666(1999).
RN [36]
RP STRUCTURE BY NMR OF 250-329.
RX PubMed=12970172; DOI=10.1093/emboj/cdg471;
RA Swanson K.A., Kang R.S., Stamenova S.D., Hicke L., Radhakrishnan I.;
RT "Solution structure of Vps27 UIM-ubiquitin complex important for endosomal
RT sorting and receptor downregulation.";
RL EMBO J. 22:4597-4606(2003).
RN [37]
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 301-320, AND INTERACTION WITH
RP UBIQUITIN.
RX PubMed=12750381; DOI=10.1074/jbc.m302596200;
RA Fisher R.D., Wang B., Alam S.L., Higginson D.S., Robinson H.,
RA Sundquist W.I., Hill C.P.;
RT "Structure and ubiquitin binding of the ubiquitin-interacting motif.";
RL J. Biol. Chem. 278:28976-28984(2003).
CC -!- FUNCTION: Component of the ESCRT-0 complex which is the sorting
CC receptor for ubiquitinated cargo proteins at the multivesicular body
CC (MVB) and recruits ESCRT-I to the MVB outer membrane (PubMed:3062374,
CC PubMed:1493335, PubMed:9265642, PubMed:11416128, PubMed:12055639,
CC PubMed:11872141, PubMed:12900393, PubMed:14581452, PubMed:15166140,
CC PubMed:15107463, PubMed:15086794, PubMed:17135292, PubMed:18508771).
CC Controls exit from the prevacuolar compartment (PVC) in both the
CC forward direction to the vacuole and the return to the Golgi
CC (PubMed:11208109, PubMed:8649377, PubMed:9015300). Allows VPS10 to
CC return to the (trans-Golgi network) TGN from the PVC (PubMed:8649377).
CC Might also function as an alternate adapter in the COPIb clathrin-like
CC coat (PubMed:17101773). {ECO:0000269|PubMed:11208109,
CC ECO:0000269|PubMed:11416128, ECO:0000269|PubMed:11872141,
CC ECO:0000269|PubMed:12055639, ECO:0000269|PubMed:12900393,
CC ECO:0000269|PubMed:14581452, ECO:0000269|PubMed:1493335,
CC ECO:0000269|PubMed:15086794, ECO:0000269|PubMed:15107463,
CC ECO:0000269|PubMed:15166140, ECO:0000269|PubMed:17101773,
CC ECO:0000269|PubMed:17135292, ECO:0000269|PubMed:18508771,
CC ECO:0000269|PubMed:3062374, ECO:0000269|PubMed:8649377,
CC ECO:0000269|PubMed:9015300, ECO:0000269|PubMed:9265642}.
CC -!- SUBUNIT: Component of the ESCRT-0 complex composed of HSE1 and VPS27
CC (PubMed:12055639, PubMed:14581452, PubMed:15086794). Interacts with
CC ENT3 and ENT5, the ESCRT-I subunits VPS23 and VPS28 and with the COPIb
CC subunits SEC27, SEC28 and SEC33 (PubMed:12900393, PubMed:15107463,
CC PubMed:17101773). May form a complex composed of VPS27, HSE1 and DOA1
CC (PubMed:18508771). Interacts with DOA1 (PubMed:18508771). Interacts
CC with ubiquitin (PubMed:11988742, PubMed:12750381, PubMed:14581452).
CC {ECO:0000269|PubMed:11988742, ECO:0000269|PubMed:12055639,
CC ECO:0000269|PubMed:12750381, ECO:0000269|PubMed:12900393,
CC ECO:0000269|PubMed:14581452, ECO:0000269|PubMed:15086794,
CC ECO:0000269|PubMed:15107463, ECO:0000269|PubMed:17101773,
CC ECO:0000269|PubMed:18508771}.
CC -!- INTERACTION:
CC P40343; P38753: HSE1; NbExp=8; IntAct=EBI-20380, EBI-1382;
CC P40343; P40509: SEC28; NbExp=2; IntAct=EBI-20380, EBI-4884;
CC P40343; P25604: STP22; NbExp=7; IntAct=EBI-20380, EBI-411625;
CC P40343; P0CG53: UBB; Xeno; NbExp=6; IntAct=EBI-20380, EBI-5333021;
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:12006563,
CC ECO:0000269|PubMed:12900393, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:15169871, ECO:0000269|PubMed:17101773,
CC ECO:0000269|PubMed:17101785}; Peripheral membrane protein
CC {ECO:0000269|PubMed:12006563, ECO:0000269|PubMed:12900393,
CC ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15169871,
CC ECO:0000269|PubMed:17101773, ECO:0000269|PubMed:17101785}; Cytoplasmic
CC side {ECO:0000269|PubMed:12006563, ECO:0000269|PubMed:12900393,
CC ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15169871,
CC ECO:0000269|PubMed:17101773, ECO:0000269|PubMed:17101785}.
CC -!- DOMAIN: The FYVE domain is involved in the binding to
CC phosphatidylinositol 3-phosphate (PtdIns(3)P) which is required for the
CC association to endosomal membranes.
CC -!- DOMAIN: Both IUM domains are necessary for efficient binding to
CC ubiquitin.
CC -!- MISCELLANEOUS: Present with 172 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the VPS27 family. {ECO:0000305}.
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DR EMBL; U24218; AAA96002.1; -; Genomic_DNA.
DR EMBL; X77395; CAA54574.1; -; Genomic_DNA.
DR EMBL; Z71620; CAA96282.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10547.1; -; Genomic_DNA.
DR PIR; S45129; S45129.
DR RefSeq; NP_014403.3; NM_001183183.3.
DR PDB; 1O06; X-ray; 1.45 A; A=301-320.
DR PDB; 1Q0V; NMR; -; A=249-329.
DR PDB; 1Q0W; NMR; -; A=255-278.
DR PDB; 1VFY; X-ray; 1.15 A; A=163-230.
DR PDB; 2KDI; NMR; -; A=258-277.
DR PDB; 2PJW; X-ray; 3.01 A; V=348-438.
DR PDB; 3R42; X-ray; 1.87 A; B=445-453.
DR PDB; 6NJG; X-ray; 2.35 A; B=256-278.
DR PDBsum; 1O06; -.
DR PDBsum; 1Q0V; -.
DR PDBsum; 1Q0W; -.
DR PDBsum; 1VFY; -.
DR PDBsum; 2KDI; -.
DR PDBsum; 2PJW; -.
DR PDBsum; 3R42; -.
DR PDBsum; 6NJG; -.
DR AlphaFoldDB; P40343; -.
DR SMR; P40343; -.
DR BioGRID; 35831; 762.
DR ComplexPortal; CPX-1622; ESCRT-0 complex.
DR DIP; DIP-1741N; -.
DR IntAct; P40343; 7.
DR MINT; P40343; -.
DR STRING; 4932.YNR006W; -.
DR TCDB; 3.A.31.1.1; the endosomal sorting complexes required for transport iii (escrt-iii) family.
DR iPTMnet; P40343; -.
DR MaxQB; P40343; -.
DR PaxDb; P40343; -.
DR PRIDE; P40343; -.
DR EnsemblFungi; YNR006W_mRNA; YNR006W; YNR006W.
DR GeneID; 855739; -.
DR KEGG; sce:YNR006W; -.
DR SGD; S000005289; VPS27.
DR VEuPathDB; FungiDB:YNR006W; -.
DR eggNOG; KOG1818; Eukaryota.
DR GeneTree; ENSGT00940000170673; -.
DR HOGENOM; CLU_011862_2_0_1; -.
DR InParanoid; P40343; -.
DR OMA; SDMVRSK; -.
DR BioCyc; YEAST:G3O-33324-MON; -.
DR EvolutionaryTrace; P40343; -.
DR PRO; PR:P40343; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P40343; protein.
DR GO; GO:0005768; C:endosome; IDA:SGD.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0033565; C:ESCRT-0 complex; IPI:SGD.
DR GO; GO:0032991; C:protein-containing complex; IMP:CAFA.
DR GO; GO:0005774; C:vacuolar membrane; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:SGD.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0046982; F:protein heterodimerization activity; IMP:CAFA.
DR GO; GO:0043130; F:ubiquitin binding; IDA:SGD.
DR GO; GO:1904669; P:ATP export; IMP:SGD.
DR GO; GO:0045324; P:late endosome to vacuole transport; IMP:SGD.
DR GO; GO:0016237; P:lysosomal microautophagy; IMP:SGD.
DR GO; GO:0140504; P:microlipophagy; IMP:SGD.
DR GO; GO:0071985; P:multivesicular body sorting pathway; IMP:CAFA.
DR GO; GO:1903319; P:positive regulation of protein maturation; IMP:CAFA.
DR GO; GO:0045053; P:protein retention in Golgi apparatus; IMP:SGD.
DR GO; GO:0009306; P:protein secretion; IMP:CAFA.
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 Gene3D; 1.25.40.90; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR017073; HGS/VPS27.
DR InterPro; IPR003903; UIM_dom.
DR InterPro; IPR002014; VHS_dom.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF02809; UIM; 2.
DR Pfam; PF00790; VHS; 1.
DR PIRSF; PIRSF036956; Hrs_Vps27; 1.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00726; UIM; 2.
DR SMART; SM00288; VHS; 1.
DR SUPFAM; SSF48464; SSF48464; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS50330; UIM; 2.
DR PROSITE; PS50179; VHS; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endosome; Isopeptide bond; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..622
FT /note="Vacuolar protein sorting-associated protein 27"
FT /id="PRO_0000065893"
FT DOMAIN 18..149
FT /note="VHS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00218"
FT DOMAIN 258..277
FT /note="UIM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 301..320
FT /note="UIM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT ZN_FING 170..230
FT /note="FYVE-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 236..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..520
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 192
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 200
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 203
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 222
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 225
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956"
FT MOD_RES 495
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 613
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CROSSLNK 294
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT MUTAGEN 185..186
FT /note="LL->AA: Decreases the association to PtdIns(3)P
FT containing membranes."
FT /evidence="ECO:0000269|PubMed:12006563"
FT MUTAGEN 193
FT /note="R->A: Decreases the association to PtdIns(3)P
FT containing membranes."
FT /evidence="ECO:0000269|PubMed:12006563"
FT MUTAGEN 270
FT /note="S->D: Reduces strongly the ubiquitin-binding
FT activity."
FT /evidence="ECO:0000269|PubMed:11988742"
FT MUTAGEN 313
FT /note="S->D: Reduces strongly the ubiquitin-binding
FT activity."
FT /evidence="ECO:0000269|PubMed:11988742"
FT CONFLICT 321..322
FT /note="KL -> NV (in Ref. 1; AAA96002)"
FT /evidence="ECO:0000305"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:1VFY"
FT TURN 193..195
FT /evidence="ECO:0007829|PDB:1VFY"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:1VFY"
FT STRAND 206..210
FT /evidence="ECO:0007829|PDB:1VFY"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:1VFY"
FT STRAND 215..221
FT /evidence="ECO:0007829|PDB:1VFY"
FT HELIX 223..231
FT /evidence="ECO:0007829|PDB:1VFY"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:1Q0V"
FT HELIX 256..269
FT /evidence="ECO:0007829|PDB:6NJG"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:1Q0W"
FT HELIX 304..318
FT /evidence="ECO:0007829|PDB:1O06"
FT HELIX 352..369
FT /evidence="ECO:0007829|PDB:2PJW"
FT TURN 375..379
FT /evidence="ECO:0007829|PDB:2PJW"
FT HELIX 381..436
FT /evidence="ECO:0007829|PDB:2PJW"
SQ SEQUENCE 622 AA; 70974 MW; 76C4501B0EBC9C84 CRC64;
MSVSTPSELD ALIEQATSES IPNGDLDLPI ALEISDVLRS RRVNPKDSMR CIKKRILNTA
DNPNTQLSSW KLTNICVKNG GTPFIKEICS REFMDTMEHV ILREDSNEEL SELVKTILYE
LYVAFKNDSQ LNYVAKVYDK LISRGIKFPE KLTLSNSPTA MFDSKTPADW IDSDACMICS
KKFSLLNRKH HCRSCGGVFC QEHSSNSIPL PDLGIYEPVR VCDSCFEDYD LKRHDDSKKS
KKHRHKRKKD RDYSTPEDEE ELIRKAIELS LKESRNSASS EPIVPVVESK NEVKRQEIEE
EEDPDLKAAI QESLREAEEA KLRSERQKAS RQMQPQQPSP QPQPIHSVDL SDEEKDSIYM
FASLVEKMKS RPLNEILEDS KLQNLAQRVF ASKARLNYAL NDKAQKYNTL IEMNGKISEI
MNIYDRLLEQ QLQSINLSQQ YTLPQVPSDP YNYLTENVQN PAESYQTPPL QQLSSHQYKP
QQDVSRQQSV KANSSPTTNI DHLKTIDVTP HAQQKPQSHV ELAPSDPPYP KEEAEDEGTQ
AVQDEESSTQ ESRERPYPVE TENGETSINK RPQGITRYDF PTVPARKFVQ PESTVPLPAS
SSEIPIKEER PPSPQEELLI EL
