IST1_YEAST
ID IST1_YEAST Reviewed; 298 AA.
AC P53843; D6W0S8;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Vacuolar protein sorting-associated protein IST1;
DE AltName: Full=Increased sodium tolerance protein 1;
GN Name=IST1; OrderedLocusNames=YNL265C; ORFNames=N0809;
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].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8740425;
RX DOI=10.1002/(sici)1097-0061(199604)12:5<505::aid-yea932>3.0.co;2-f;
RA Sen-Gupta M., Lyck R., Fleig U., Niedenthal R.K., Hegemann J.H.;
RT "The sequence of a 24,152 bp segment from the left arm of chromosome XIV
RT from Saccharomyces cerevisiae between the BNI1 and the POL2 genes.";
RL Yeast 12:505-514(1996).
RN [2]
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 [3]
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 [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, INTERACTION WITH VPS4, AND SUBCELLULAR LOCATION.
RX PubMed=18032582; DOI=10.1091/mbc.e07-08-0747;
RA Dimaano C., Jones C.B., Hanono A., Curtiss M., Babst M.;
RT "Ist1 regulates Vps4 localization and assembly.";
RL Mol. Biol. Cell 19:465-474(2008).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH DID2 AND VPS4.
RX PubMed=18032584; DOI=10.1091/mbc.e07-07-0694;
RA Rue S.M., Mattei S., Saksena S., Emr S.D.;
RT "Novel Ist1-Did2 complex functions at a late step in multivesicular body
RT sorting.";
RL Mol. Biol. Cell 19:475-484(2008).
CC -!- FUNCTION: Involved in a late step in sorting of cargo proteins of the
CC multivesicular body (MVB) for incorporation into intralumenal vesicles.
CC The lumenal sequestrated membrane proteins are targeted into the
CC vacuole after fusion of the endosome with the vacuole. Regulates the
CC recruitment of VPS4 to the ESCRT-III complex, probably in conjunction
CC with DID2, and VPS4 catalyzes the disassembly of the ESCRT-III complex.
CC {ECO:0000269|PubMed:18032582, ECO:0000269|PubMed:18032584}.
CC -!- SUBUNIT: Interacts with DID2. Interacts with VPS4 (via MIT domain); the
CC interaction prevents VPS4 oligomerization, competes with the binding of
CC VTA1 to VSP4 and diminishes the ATPase activity of VSP4.
CC {ECO:0000269|PubMed:18032582, ECO:0000269|PubMed:18032584}.
CC -!- INTERACTION:
CC P53843; P69771: DID2; NbExp=3; IntAct=EBI-28245, EBI-2053489;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Endosome. Note=The endosomal location
CC appears to be dependent on DID2.
CC -!- MISCELLANEOUS: Present with 4760 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the IST1 family. {ECO:0000305}.
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DR EMBL; X92494; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z71542; CAA96172.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10294.1; -; Genomic_DNA.
DR PIR; S63238; S63238.
DR RefSeq; NP_014134.1; NM_001183103.1.
DR PDB; 3GGY; X-ray; 1.70 A; A/B=1-193.
DR PDB; 3GGZ; X-ray; 3.80 A; A/B/C/D=1-193.
DR PDBsum; 3GGY; -.
DR PDBsum; 3GGZ; -.
DR AlphaFoldDB; P53843; -.
DR SMR; P53843; -.
DR BioGRID; 35574; 65.
DR DIP; DIP-6713N; -.
DR IntAct; P53843; 29.
DR MINT; P53843; -.
DR STRING; 4932.YNL265C; -.
DR TCDB; 3.A.31.1.1; the endosomal sorting complexes required for transport iii (escrt-iii) family.
DR iPTMnet; P53843; -.
DR MaxQB; P53843; -.
DR PaxDb; P53843; -.
DR PRIDE; P53843; -.
DR EnsemblFungi; YNL265C_mRNA; YNL265C; YNL265C.
DR GeneID; 855456; -.
DR KEGG; sce:YNL265C; -.
DR SGD; S000005209; IST1.
DR VEuPathDB; FungiDB:YNL265C; -.
DR eggNOG; KOG2027; Eukaryota.
DR GeneTree; ENSGT00390000007453; -.
DR HOGENOM; CLU_037652_2_0_1; -.
DR InParanoid; P53843; -.
DR OMA; TLAQDNK; -.
DR BioCyc; YEAST:G3O-33261-MON; -.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR Reactome; R-SCE-9668328; Sealing of the nuclear envelope (NE) by ESCRT-III.
DR EvolutionaryTrace; P53843; -.
DR PRO; PR:P53843; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53843; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005768; C:endosome; IDA:SGD.
DR GO; GO:0032511; P:late endosome to vacuole transport via multivesicular body sorting pathway; IGI:SGD.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1260.60; -; 1.
DR InterPro; IPR005061; Ist1.
DR InterPro; IPR042277; IST1-like.
DR PANTHER; PTHR12161; PTHR12161; 1.
DR Pfam; PF03398; Ist1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Endosome; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..298
FT /note="Vacuolar protein sorting-associated protein IST1"
FT /id="PRO_0000076227"
FT REGION 190..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..298
FT /note="Interaction with VPS4"
FT MOTIF 286..296
FT /note="MIT-interacting motif"
FT COMPBIAS 190..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..283
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 8..46
FT /evidence="ECO:0007829|PDB:3GGY"
FT HELIX 50..82
FT /evidence="ECO:0007829|PDB:3GGY"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:3GGY"
FT HELIX 93..99
FT /evidence="ECO:0007829|PDB:3GGY"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:3GGY"
FT HELIX 105..115
FT /evidence="ECO:0007829|PDB:3GGY"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:3GGY"
FT HELIX 125..135
FT /evidence="ECO:0007829|PDB:3GGY"
FT HELIX 138..147
FT /evidence="ECO:0007829|PDB:3GGY"
FT HELIX 153..159
FT /evidence="ECO:0007829|PDB:3GGY"
FT HELIX 166..179
FT /evidence="ECO:0007829|PDB:3GGY"
FT HELIX 184..188
FT /evidence="ECO:0007829|PDB:3GGY"
SQ SEQUENCE 298 AA; 34496 MW; F16A94BFC7716A1A CRC64;
MAPSMIPFTI KLKTCLKMCI QRLRYAQEKQ QAIAKQSRRQ VAQLLLTNKE QKAHYRVETL
IHDDIHIELL EILELYCELL LARVQVINDI STEEQLVKEH MDDGINEAIR SLIYAILFVD
EVKELSQLKD LMAWKINVEF VNGVIADHID VPEKIIKKCS PSVPKEELVD LYLKEIAKTY
DVPYSKLENS LSSSSSNISS DFSDPSGDIE DNDEEKPILA LDNDDNDNAD AKHPITVKKP
RQNSENIKNE LKIPKDIKKE VIEKKQSEKK TTKRKTKKEQ ENDELDELKK RFDALRRK
