ID YPT35_YEAST Reviewed; 214 AA.
AC P38815; D3DL55;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 27-MAR-2024, entry version 159.
DE RecName: Full=Endosomal/vacuolar adapter protein YPT35 {ECO:0000305};
DE AltName: Full=PX domain-containing protein YPT35 {ECO:0000305};
GN Name=YPT35; OrderedLocusNames=YHR105W;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP DOMAIN.
RX PubMed=11557775; DOI=10.1074/jbc.m108811200;
RA Yu J.W., Lemmon M.A.;
RT "All phox homology (PX) domains from Saccharomyces cerevisiae specifically
RT recognize phosphatidylinositol 3-phosphate.";
RL J. Biol. Chem. 276:44179-44184(2001).
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 INTERACTION WITH RBD2; YIF1; YIP1 AND YIP4; PHOSPHATIDYLINOSITOL
RP 3-PHOSPHATE-BINDING, AND MUTAGENESIS OF TYR-123.
RX PubMed=15263065; DOI=10.1074/mcp.m400081-mcp200;
RA Vollert C.S., Uetz P.;
RT "The phox homology (PX) domain protein interaction network in yeast.";
RL Mol. Cell. Proteomics 3:1053-1064(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65 AND SER-66, AND
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 [8]
RP FUNCTION, INTERACTION WITH VPS13, SUBCELLULAR LOCATION, DISRUPTION
RP PHENOTYPE, PXP MOTIF, AND MUTAGENESIS OF 5-ILE--LEU-15; ILE-5; LEU-8;
RP PRO-10; PRO-12; ILE-13 AND LEU-15.
RX PubMed=30018089; DOI=10.1083/jcb.201804111;
RA Bean B.D.M., Dziurdzik S.K., Kolehmainen K.L., Fowler C.M.S., Kwong W.K.,
RA Grad L.I., Davey M., Schluter C., Conibear E.;
RT "Competitive organelle-specific adaptors recruit Vps13 to membrane contact
RT sites.";
RL J. Cell Biol. 217:3593-3607(2018).
CC -!- FUNCTION: Recruits the lipid transfer protein VPS13 to endosomal and
CC vacuolar membranes. {ECO:0000269|PubMed:30018089}.
CC -!- SUBUNIT: Interacts (via PxP motif) with VPS13 (via SHR-BD domain)
CC (PubMed:30018089). Interacts with RBD2 (PubMed:15263065). Interacts
CC with YIF1 (PubMed:15263065). Interacts with YIP1 (PubMed:15263065).
CC Interacts with YIP4 (PubMed:15263065). {ECO:0000269|PubMed:15263065,
CC ECO:0000269|PubMed:30018089}.
CC -!- INTERACTION:
CC P38815; P53845: YIF1; NbExp=4; IntAct=EBI-24665, EBI-28230;
CC P38815; P53039: YIP1; NbExp=3; IntAct=EBI-24665, EBI-25295;
CC P38815; P53093: YIP4; NbExp=2; IntAct=EBI-24665, EBI-24124;
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:30018089}; Peripheral membrane protein
CC {ECO:0000269|PubMed:14562095}. Vacuole membrane
CC {ECO:0000269|PubMed:30018089}; Peripheral membrane protein
CC {ECO:0000305}. Note=Localizes to nuclear envelope-vacuole contact sites
CC during respiration. {ECO:0000269|PubMed:30018089}.
CC -!- DOMAIN: The PX domain binds phosphatidylinositol 3-phosphate
CC (PtdIns(3)P) which is necessary for peripheral membrane localization.
CC {ECO:0000269|PubMed:11557775}.
CC -!- DISRUPTION PHENOTYPE: Decreases VPS13 levels at endosomal membranes and
CC nuclear envelope-vacuole contact sites. {ECO:0000269|PubMed:30018089}.
CC -!- SIMILARITY: Belongs to the YPT35 family. {ECO:0000305}.
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DR EMBL; U00059; AAB68857.1; -; Genomic_DNA.
DR EMBL; AY557854; AAS56180.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06799.1; -; Genomic_DNA.
DR PIR; S48947; S48947.
DR RefSeq; NP_011973.1; NM_001179235.1.
DR AlphaFoldDB; P38815; -.
DR SMR; P38815; -.
DR BioGRID; 36538; 60.
DR DIP; DIP-1881N; -.
DR IntAct; P38815; 18.
DR MINT; P38815; -.
DR STRING; 4932.YHR105W; -.
DR iPTMnet; P38815; -.
DR MaxQB; P38815; -.
DR PaxDb; 4932-YHR105W; -.
DR PeptideAtlas; P38815; -.
DR EnsemblFungi; YHR105W_mRNA; YHR105W; YHR105W.
DR GeneID; 856505; -.
DR KEGG; sce:YHR105W; -.
DR AGR; SGD:S000001147; -.
DR SGD; S000001147; YPT35.
DR VEuPathDB; FungiDB:YHR105W; -.
DR eggNOG; ENOG502S40T; Eukaryota.
DR HOGENOM; CLU_1475537_0_0_1; -.
DR InParanoid; P38815; -.
DR OMA; FAVWKIT; -.
DR OrthoDB; 2041724at2759; -.
DR BioCyc; YEAST:G3O-31149-MONOMER; -.
DR BioGRID-ORCS; 856505; 8 hits in 10 CRISPR screens.
DR PRO; PR:P38815; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38815; Protein.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0071561; C:nucleus-vacuole junction; IDA:UniProtKB.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:SGD.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IMP:UniProtKB.
DR GO; GO:0036010; P:protein localization to endosome; IMP:UniProtKB.
DR GO; GO:0072657; P:protein localization to membrane; IMP:UniProtKB.
DR CDD; cd07280; PX_YPT35; 1.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR037917; Ypt35_PX.
DR PANTHER; PTHR10555:SF170; FI18122P1; 1.
DR PANTHER; PTHR10555; SORTING NEXIN; 1.
DR Pfam; PF00787; PX; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR PROSITE; PS50195; PX; 1.
PE 1: Evidence at protein level;
KW Endosome; Membrane; Phosphoprotein; Reference proteome; Vacuole.
FT CHAIN 1..214
FT /note="Endosomal/vacuolar adapter protein YPT35"
FT /id="PRO_0000202910"
FT DOMAIN 73..213
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 5..15
FT /note="PxP"
FT /evidence="ECO:0000269|PubMed:30018089"
FT COMPBIAS 31..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 5..15
FT /note="Missing: Disrupts interaction with VPS13."
FT /evidence="ECO:0000269|PubMed:30018089"
FT MUTAGEN 5
FT /note="I->A: Disrupts interaction with VPS13."
FT /evidence="ECO:0000269|PubMed:30018089"
FT MUTAGEN 8
FT /note="L->A: Disrupts interaction with VPS13."
FT /evidence="ECO:0000269|PubMed:30018089"
FT MUTAGEN 10
FT /note="P->A: Disrupts interaction with VPS13."
FT /evidence="ECO:0000269|PubMed:30018089"
FT MUTAGEN 12
FT /note="P->A: Disrupts interaction with VPS13."
FT /evidence="ECO:0000269|PubMed:30018089"
FT MUTAGEN 13
FT /note="I->A: Disrupts interaction with VPS13."
FT /evidence="ECO:0000269|PubMed:30018089"
FT MUTAGEN 15
FT /note="L->A: Disrupts interaction with VPS13."
FT /evidence="ECO:0000269|PubMed:30018089"
FT MUTAGEN 123
FT /note="Y->A: Abolishes partially PtdIns(3)P-binding."
FT /evidence="ECO:0000269|PubMed:15263065"
SQ SEQUENCE 214 AA; 24646 MW; 2ADD21AF107094DC CRC64;
MSDKISFLPP EPIQLLDEDS TEPELDIDSQ QENEGPISAS NSNDSTSHSN DCGATITRTR
PRRSSSINAN FSFQKAHVSD CTIVNGDHGT KFAVWRITVF LEPNLKAFAA KRESYKIQTY
KRYSDFVRLR ENLLTRIKTA KPEKLNCLQI PHLPPSVQWY SSWKYQEVNL NKDWLAKRQR
GLEYFLNHII LNSSLVEMTK DILIQFLEPS KRVA
//
