HSE1_YEAST
ID HSE1_YEAST Reviewed; 452 AA.
AC P38753; D3DKR2;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Class E vacuolar protein-sorting machinery protein HSE1;
GN Name=HSE1; OrderedLocusNames=YHL002W;
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=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
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 IDENTIFICATION IN THE ESCRT-0 COMPLEX, FUNCTION OF THE ESCRT-0 COMPLEX, AND
RP SUBCELLULAR LOCATION.
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 [4]
RP FUNCTION OF THE ESCRT-0 COMPLEX.
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 [5]
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 [6]
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 [7]
RP INTERACTION WITH RSP5; VPS23 AND VPS27, AND FUNCTION OF THE ESCRT-0
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162, AND IDENTIFICATION BY
RP 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 [9]
RP FUNCTION, AND INTERACTION WITH RSP5 AND UBP7.
RX PubMed=17079730; DOI=10.1091/mbc.e06-06-0557;
RA Ren J., Kee Y., Huibregtse J.M., Piper R.C.;
RT "Hse1, a component of the yeast Hrs-STAM ubiquitin-sorting complex,
RT associates with ubiquitin peptidases and a ligase to control sorting
RT efficiency into multivesicular bodies.";
RL Mol. Biol. Cell 18:324-335(2007).
RN [10]
RP IDENTIFICATION IN A COMPLEX WITH VPS27 AND DOA1, INTERACTION WITH DOA1, AND
RP MUTAGENESIS OF 254-TRP-TRP-255.
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162, AND IDENTIFICATION BY
RP 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162, AND IDENTIFICATION BY
RP 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 [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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.
CC {ECO:0000269|PubMed:12055639, ECO:0000269|PubMed:14581452,
CC ECO:0000269|PubMed:15086794, ECO:0000269|PubMed:17079730}.
CC -!- SUBUNIT: Component of the ESCRT-0 complex composed of HSE1 and VPS27
CC (PubMed:12055639). Interacts with the ESCRT-I subunit VPS23, the UBP7
CC deubiquitinase and the E3 ligase RSP5 (PubMed:17079730,
CC PubMed:15086794). May form a complex composed of VPS27, HSE1 and DOA1
CC (PubMed:18508771). Interacts (via SH3 domain) with DOA1
CC (PubMed:18508771). {ECO:0000269|PubMed:12055639,
CC ECO:0000269|PubMed:15086794, ECO:0000269|PubMed:17079730,
CC ECO:0000269|PubMed:18508771}.
CC -!- INTERACTION:
CC P38753; Q12168: ACF2; NbExp=2; IntAct=EBI-1382, EBI-32973;
CC P38753; P40563: AIM21; NbExp=4; IntAct=EBI-1382, EBI-25376;
CC P38753; P36037: DOA1; NbExp=3; IntAct=EBI-1382, EBI-6017;
CC P38753; P25604: STP22; NbExp=3; IntAct=EBI-1382, EBI-411625;
CC P38753; P40453: UBP7; NbExp=4; IntAct=EBI-1382, EBI-19857;
CC P38753; P40343: VPS27; NbExp=8; IntAct=EBI-1382, EBI-20380;
CC P38753; P0CG53: UBB; Xeno; NbExp=2; IntAct=EBI-1382, EBI-5333021;
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:12055639,
CC ECO:0000269|PubMed:14562095}; Peripheral membrane protein
CC {ECO:0000269|PubMed:12055639, ECO:0000269|PubMed:14562095}; Cytoplasmic
CC side {ECO:0000269|PubMed:12055639, ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 358 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the STAM family. {ECO:0000305}.
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DR EMBL; U10555; AAB68427.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06685.1; -; Genomic_DNA.
DR PIR; S46798; S46798.
DR RefSeq; NP_011861.1; NM_001179082.1.
DR PDB; 2PJW; X-ray; 3.01 A; H=288-375.
DR PDBsum; 2PJW; -.
DR AlphaFoldDB; P38753; -.
DR SMR; P38753; -.
DR BioGRID; 36423; 344.
DR ComplexPortal; CPX-1622; ESCRT-0 complex.
DR DIP; DIP-1742N; -.
DR IntAct; P38753; 44.
DR MINT; P38753; -.
DR STRING; 4932.YHL002W; -.
DR TCDB; 3.A.31.1.1; the endosomal sorting complexes required for transport iii (escrt-iii) family.
DR iPTMnet; P38753; -.
DR MaxQB; P38753; -.
DR PaxDb; P38753; -.
DR PRIDE; P38753; -.
DR EnsemblFungi; YHL002W_mRNA; YHL002W; YHL002W.
DR GeneID; 856387; -.
DR KEGG; sce:YHL002W; -.
DR SGD; S000000994; HSE1.
DR VEuPathDB; FungiDB:YHL002W; -.
DR eggNOG; KOG2199; Eukaryota.
DR GeneTree; ENSGT00940000168664; -.
DR HOGENOM; CLU_010104_2_0_1; -.
DR InParanoid; P38753; -.
DR OMA; AHALCQN; -.
DR BioCyc; YEAST:G3O-31026-MON; -.
DR Reactome; R-SCE-9013420; RHOU GTPase cycle.
DR EvolutionaryTrace; P38753; -.
DR PRO; PR:P38753; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38753; 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:0035091; F:phosphatidylinositol binding; IEA:InterPro.
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:0071985; P:multivesicular body sorting pathway; IMP:CAFA.
DR GO; GO:1903319; P:positive regulation of protein maturation; IMP:CAFA.
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 InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR003903; UIM_dom.
DR InterPro; IPR002014; VHS_dom.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF00790; VHS; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00726; UIM; 1.
DR SMART; SM00288; VHS; 1.
DR SUPFAM; SSF48464; SSF48464; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS50330; UIM; 1.
DR PROSITE; PS50179; VHS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Endosome; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; SH3 domain; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..452
FT /note="Class E vacuolar protein-sorting machinery protein
FT HSE1"
FT /id="PRO_0000202885"
FT DOMAIN 15..145
FT /note="VHS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00218"
FT DOMAIN 162..181
FT /note="UIM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 217..276
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 144..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..438
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MUTAGEN 254..255
FT /note="WW->AA: Loss of interaction with DOA1."
FT /evidence="ECO:0000269|PubMed:18508771"
FT HELIX 289..294
FT /evidence="ECO:0007829|PDB:2PJW"
FT HELIX 296..310
FT /evidence="ECO:0007829|PDB:2PJW"
FT HELIX 316..319
FT /evidence="ECO:0007829|PDB:2PJW"
FT HELIX 322..331
FT /evidence="ECO:0007829|PDB:2PJW"
FT HELIX 332..334
FT /evidence="ECO:0007829|PDB:2PJW"
FT HELIX 335..371
FT /evidence="ECO:0007829|PDB:2PJW"
FT TURN 372..374
FT /evidence="ECO:0007829|PDB:2PJW"
SQ SEQUENCE 452 AA; 51161 MW; 026267836BBADF69 CRC64;
MSSSAIKIRN ALLKATDPKL RSDNWQYILD VCDLVKEDPE DNGQEVMSLI EKRLEQQDAN
VILRTLSLTV SLAENCGSRL RQEISSKNFT SLLYALIESH SVHITLKKAV TDVVKQLSDS
FKDDPSLRAM GDLYDKIKRK APYLVQPNVP EKHNMSTQAD NSDDEELQKA LKMSLFEYEK
QKKLQEQEKE SAEVLPQQQQ QHQQQNQAPA HKIPAQTVVR RVRALYDLTT NEPDELSFRK
GDVITVLEQV YRDWWKGALR GNMGIFPLNY VTPIVEPSKE EIEKEKNKEA IVFSQKTTID
QLHNSLNAAS KTGNSNEVLQ DPHIGDMYGS VTPLRPQVTR MLGKYAKEKE DMLSLRQVLA
NAERSYNQLM DRAANAHISP PVPGPALYAG MTHANNTPVM PPQRQSYQSN EYSPYPSNLP
IQHPTNSANN TPQYGYDLGY SVVSQPPPGY EQ
