DFG5_YEAST
ID DFG5_YEAST Reviewed; 458 AA.
AC Q05031; D6W064;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Mannan endo-1,6-alpha-mannosidase DFG5;
DE EC=3.2.1.101;
DE AltName: Full=Endo-alpha-1->6-D-mannanase DFG5;
DE Flags: Precursor;
GN Name=DFG5; OrderedLocusNames=YMR238W; ORFNames=YM9959.20;
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=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 [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 FUNCTION, GLYCOSYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=12421307; DOI=10.1046/j.1365-2958.2002.03244.x;
RA Kitagaki H., Wu H., Shimoi H., Ito K.;
RT "Two homologous genes, DCW1 (YKL046c) and DFG5, are essential for cell
RT growth and encode glycosylphosphatidylinositol (GPI)-anchored membrane
RT proteins required for cell wall biogenesis in Saccharomyces cerevisiae.";
RL Mol. Microbiol. 46:1011-1022(2002).
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 GLYCOSYLATION [LARGE SCALE ANALYSIS].
RX PubMed=19756047; DOI=10.1038/msb.2009.64;
RA Kung L.A., Tao S.-C., Qian J., Smith M.G., Snyder M., Zhu H.;
RT "Global analysis of the glycoproteome in Saccharomyces cerevisiae reveals
RT new roles for protein glycosylation in eukaryotes.";
RL Mol. Syst. Biol. 5:308-308(2009).
CC -!- FUNCTION: Required for normal synthesis of the cell wall.
CC {ECO:0000269|PubMed:12421307}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Random hydrolysis of (1->6)-alpha-D-mannosidic linkages in
CC unbranched (1->6)-mannans.; EC=3.2.1.101;
CC -!- INTERACTION:
CC Q05031; Q06144: ORM2; NbExp=3; IntAct=EBI-27512, EBI-34916;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12421307};
CC Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:12421307}. Note=GPI-
CC anchored plasma membrane protein (GPI-PMP).
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:12421307,
CC ECO:0000269|PubMed:19756047}.
CC -!- MISCELLANEOUS: Present with 2950 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 76 family. {ECO:0000305}.
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DR EMBL; Z49939; CAA90209.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10138.1; -; Genomic_DNA.
DR PIR; S57605; S57605.
DR RefSeq; NP_013965.1; NM_001182745.1.
DR AlphaFoldDB; Q05031; -.
DR SMR; Q05031; -.
DR BioGRID; 35416; 130.
DR DIP; DIP-2739N; -.
DR IntAct; Q05031; 15.
DR MINT; Q05031; -.
DR STRING; 4932.YMR238W; -.
DR CAZy; GH76; Glycoside Hydrolase Family 76.
DR MaxQB; Q05031; -.
DR PaxDb; Q05031; -.
DR PRIDE; Q05031; -.
DR EnsemblFungi; YMR238W_mRNA; YMR238W; YMR238W.
DR GeneID; 855278; -.
DR KEGG; sce:YMR238W; -.
DR SGD; S000004851; DFG5.
DR VEuPathDB; FungiDB:YMR238W; -.
DR eggNOG; ENOG502QWHG; Eukaryota.
DR HOGENOM; CLU_025694_1_2_1; -.
DR InParanoid; Q05031; -.
DR OMA; FASPNYW; -.
DR BioCyc; YEAST:G3O-32919-MON; -.
DR PRO; PR:Q05031; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q05031; protein.
DR GO; GO:0046658; C:anchored component of plasma membrane; ISA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0008496; F:mannan endo-1,6-alpha-mannosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0007117; P:budding cell bud growth; IGI:SGD.
DR GO; GO:0016052; P:carbohydrate catabolic process; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009272; P:fungal-type cell wall biogenesis; IDA:SGD.
DR GO; GO:0007124; P:pseudohyphal growth; IMP:SGD.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR005198; Glyco_hydro_76.
DR InterPro; IPR014480; Mannan-1_6-alpha_mannosidase.
DR PANTHER; PTHR12145; PTHR12145; 1.
DR Pfam; PF03663; Glyco_hydro_76; 1.
DR PIRSF; PIRSF016302; Man_a_manosd; 1.
DR SUPFAM; SSF48208; SSF48208; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell wall biogenesis/degradation; Glycoprotein; Glycosidase;
KW GPI-anchor; Hydrolase; Lipoprotein; Membrane; Reference proteome; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..437
FT /note="Mannan endo-1,6-alpha-mannosidase DFG5"
FT /id="PRO_0000012127"
FT PROPEP 438..458
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000012128"
FT REGION 399..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 437
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 245
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 273
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 417
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 458 AA; 50541 MW; 908D7E672333EC03 CRC64;
MIVNISAKMI LSICFTFLSF FKATHAMDLD TTSKTSICDA TALIQGGMLD YYEGTRYGGT
VGMFQSPYYW WHAGEAFGGM LENWFLCEND TYQELLYDAL LAQTGSNYDY IPSNQTMVEG
NDDQGIWGIT VMGAVERNFT DPGDGKPGWL AMVQAVFNTM YSRWDSEHCG GGLRWQIFTW
NSGYNYKNTV SNACLFQIAA RLGRYTGNTT YLEVAEQVFD WLVDVGYVVL NDTANVFDGA
EIDTNCTDIT KIEWTYNHGI VLGGLAYMYN ATNGTGEWET SLTKILNGAK SYFFKDSIMY
ESACQDYGTC NTDQRTFKSI FSRMLGLTSV MAPFTRDTID DLIKTSAEAA AKSCNGGTDG
HTCGLNWQKQ TNDGYYGLGE QMSALEVIQN LLIHDRPAPY KEDNGGTSKG DANAGMNSST
TNVLQNNLNI KKGDRAGAAI ITAVILSVLT GGAVWMLF
