MVP1_YEAST
ID MVP1_YEAST Reviewed; 511 AA.
AC P40959; D6VZH9;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Sorting nexin MVP1;
GN Name=MVP1; OrderedLocusNames=YMR004W; ORFNames=YM8270.06;
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], FUNCTION, INTERACTION WITH VPS1, AND
RP SUBCELLULAR LOCATION.
RX PubMed=7862158; DOI=10.1128/mcb.15.3.1671;
RA Ekena K., Stevens T.H.;
RT "The Saccharomyces cerevisiae MVP1 gene interacts with VPS1 and is required
RT for vacuolar protein sorting.";
RL Mol. Cell. Biol. 15:1671-1678(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(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 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 [6]
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).
CC -!- FUNCTION: Required for vacuolar protein sorting.
CC {ECO:0000269|PubMed:7862158}.
CC -!- SUBUNIT: Interacts with VPS1. {ECO:0000269|PubMed:7862158}.
CC -!- INTERACTION:
CC P40959; P40959: MVP1; NbExp=3; IntAct=EBI-11636, EBI-11636;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7862158}. Membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}.
CC -!- DOMAIN: The PX domain binds phosphatidylinositol 3-phosphate which is
CC necessary for peripheral membrane localization. {ECO:0000250}.
CC -!- MISCELLANEOUS: Present with 2210 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
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DR EMBL; U16137; AAA67884.1; -; Genomic_DNA.
DR EMBL; Z48613; CAA88519.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09903.1; -; Genomic_DNA.
DR PIR; S53033; S53033.
DR RefSeq; NP_013717.1; NM_001182500.1.
DR PDB; 6Q0X; EM; 4.20 A; A/B/C/D=1-511.
DR PDBsum; 6Q0X; -.
DR AlphaFoldDB; P40959; -.
DR SMR; P40959; -.
DR BioGRID; 35174; 187.
DR DIP; DIP-1764N; -.
DR IntAct; P40959; 14.
DR MINT; P40959; -.
DR STRING; 4932.YMR004W; -.
DR iPTMnet; P40959; -.
DR MaxQB; P40959; -.
DR PaxDb; P40959; -.
DR PRIDE; P40959; -.
DR EnsemblFungi; YMR004W_mRNA; YMR004W; YMR004W.
DR GeneID; 855016; -.
DR KEGG; sce:YMR004W; -.
DR SGD; S000004606; MVP1.
DR VEuPathDB; FungiDB:YMR004W; -.
DR eggNOG; KOG2273; Eukaryota.
DR HOGENOM; CLU_009058_2_0_1; -.
DR InParanoid; P40959; -.
DR OMA; YLENKMV; -.
DR BioCyc; YEAST:G3O-32715-MON; -.
DR PRO; PR:P40959; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P40959; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005768; C:endosome; IDA:SGD.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:SGD.
DR GO; GO:0097320; P:plasma membrane tubulation; IDA:SGD.
DR GO; GO:0006623; P:protein targeting to vacuole; IMP:SGD.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IMP:SGD.
DR CDD; cd06866; PX_SNX8_Mvp1p_like; 1.
DR Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR028662; SNX8/Mvp1.
DR InterPro; IPR035704; SNX8/Mvp1_PX.
DR InterPro; IPR045734; Snx8_BAR_dom.
DR PANTHER; PTHR47554; PTHR47554; 1.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF19566; Snx8_BAR_dom; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50195; PX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Membrane; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..511
FT /note="Sorting nexin MVP1"
FT /id="PRO_0000213802"
FT DOMAIN 128..247
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 172
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT /evidence="ECO:0000250"
FT BINDING 174
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT /evidence="ECO:0000250"
FT BINDING 198
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT /evidence="ECO:0000250"
FT BINDING 213
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT /evidence="ECO:0000250"
FT CONFLICT 85
FT /note="Q -> N (in Ref. 1; AAA67884)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 511 AA; 59657 MW; 0EBB10FBCBB1DD78 CRC64;
MDNYEGSDPW NTSSNAWTKD DDHVVSTTNS EPSLNGISGE FNTLNFSTPL DTNEEDTGFL
PTNDVLEESI WDDSRNPLGA TGMSQTPNIA ANETVIDKND ARDQNIEESE ADLLDWTNNV
RKTYRPLDAD IIIIEEIPER EGLLFKHANY LVKHLIALPS TSPSEERTVV RRYSDFLWLR
EILLKRYPFR MIPELPPKRI GSQNADQLFL KKRRIGLSRF INLVMKHPKL SNDDLVLTFL
TVRTDLTSWR KQATYDTSNE FADKKISQEF MKMWKKEFAE QWNQAASCID TSMELWYRIT
LLLERHEKRI MQMVHERNFF ETLVDNFSEV TPKLYPVQQN DTILDINNNL SIIKKHLETT
SSICKQETEE ISGTLSPKFK IFTDILLSLR SLFERYKIMA ANNVVELQRH VELNKEKLES
MKGKPDVSGA EYDRIKKIIQ KDRRSIIEQS NRAWLIRQCI LEEFTIFQET QFLITRAFQD
WAKLNSNHAG LKLNEWEKLV TSIMDMPISR E
