MNL2_YEAST
ID MNL2_YEAST Reviewed; 849 AA.
AC Q12205; D6VY59; Q7LGY1;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Putative endoplasmic reticulum mannosidase MNL2;
DE EC=3.2.1.- {ECO:0000250|UniProtKB:P32906};
DE AltName: Full=Mannosidase-like protein 2;
GN Name=MNL2; OrderedLocusNames=YLR057W; ORFNames=L2153;
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=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(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 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 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 SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=21971548; DOI=10.1016/j.bbrc.2011.09.100;
RA Martinez Benitez E., Stolz A., Becher A., Wolf D.H.;
RT "Mnl2, a novel component of the ER associated protein degradation
RT pathway.";
RL Biochem. Biophys. Res. Commun. 414:528-532(2011).
CC -!- FUNCTION: Putative mannosidase involved in glycoprotein quality control
CC since it is involved in the targeting of misfolded glycoproteins for
CC ER-associated protein degradation (ERAD).
CC {ECO:0000269|PubMed:21971548}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P45700};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:P32906}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:21971548}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:21971548}.
CC -!- MISCELLANEOUS: Present with 71 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 47 family. {ECO:0000305}.
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DR EMBL; X94607; CAA64304.1; -; Genomic_DNA.
DR EMBL; Z73229; CAA97587.1; -; Genomic_DNA.
DR EMBL; Z73230; CAA97589.1; -; Genomic_DNA.
DR EMBL; AY692557; AAT92576.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09375.1; -; Genomic_DNA.
DR PIR; S61631; S61631.
DR RefSeq; NP_013158.1; NM_001181944.1.
DR AlphaFoldDB; Q12205; -.
DR BioGRID; 31332; 71.
DR DIP; DIP-8921N; -.
DR MINT; Q12205; -.
DR STRING; 4932.YLR057W; -.
DR CAZy; GH47; Glycoside Hydrolase Family 47.
DR iPTMnet; Q12205; -.
DR MaxQB; Q12205; -.
DR PaxDb; Q12205; -.
DR PRIDE; Q12205; -.
DR EnsemblFungi; YLR057W_mRNA; YLR057W; YLR057W.
DR GeneID; 850746; -.
DR KEGG; sce:YLR057W; -.
DR SGD; S000004047; MNL2.
DR VEuPathDB; FungiDB:YLR057W; -.
DR eggNOG; KOG2204; Eukaryota.
DR HOGENOM; CLU_022261_0_0_1; -.
DR InParanoid; Q12205; -.
DR OMA; NSYAENE; -.
DR BioCyc; YEAST:G3O-32212-MON; -.
DR Reactome; R-SCE-964827; Progressive trimming of alpha-1,2-linked mannose residues from Man9/8/7GlcNAc2 to produce Man5GlcNAc2.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q12205; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q12205; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004571; F:mannosyl-oligosaccharide 1,2-alpha-mannosidase activity; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006491; P:N-glycan processing; IBA:GO_Central.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IGI:SGD.
DR Gene3D; 1.50.10.10; -; 2.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR001382; Glyco_hydro_47.
DR InterPro; IPR036026; Seven-hairpin_glycosidases.
DR Pfam; PF01532; Glyco_hydro_47; 1.
DR PRINTS; PR00747; GLYHDRLASE47.
DR SUPFAM; SSF48225; SSF48225; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Glycosidase;
KW Hydrolase; Membrane; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..849
FT /note="Putative endoplasmic reticulum mannosidase MNL2"
FT /id="PRO_0000247229"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..32
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..849
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 56..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 559..598
FT /evidence="ECO:0000250|UniProtKB:P32906"
SQ SEQUENCE 849 AA; 96997 MW; A6B87AC32936A0D5 CRC64;
MSIARLVYSL FRRVRSVLLL FITISLLFYY TFQNEIDILN SYALNDSLPS INNYEHNTEG
SSKLDPPDLS STGSDRIATD KENGNVAVDL SDPATLREKN KYFPLLLKGS SHQIGSNLPI
SSLLTYKEKY PVLFEYSSPS LTSISQNDVH KIQPAMQLPP DVDMIKQIKD IFMKSWNQEQ
LLLKSNLRRE STWPIDLIDS LDTLYLCGET KLFQDSVNII EDFDFRVPPL AMEVIDIPDI
TTRVLEGLLS AYELSMDKRL LNKAKHVADF ILRSFDTPNR IPILKYFWKS DLRNRFPDRT
VPSGQLTTMA LAFIRLSQLT RLNKYFDAVE RVFTTIRQSY NEFDMEFMLP DVVDASGCQL
LTQEEIENGA HLKGSSIMKS INENFKFVHC QQLGKFLNPP IDDNSLQEQS QYQAYRINEK
TVPILENLFK INDLFQSSYD ILDGSSKNAN AATMDPSIGS EVEAVDEIIE KRNFKDGTKK
DSTKNTVGDK SLIDSQTFLT NSISNIFKFM TFRPMLPKQT ENKKFNFLNS ILTKSQFMPT
TNELDVTIRK SYDVSLYSCR LGGILGLSSR VPHRGGVNTK YILPSSLLEM SEIITESCFM
LMEEFDGLLP QKFELDPCTD ETNGNCEFNG ETKSRMIANG EYETFENDLD VGIKVSNYGK
GGNDQKAKRN VLSKDGITET QNIKGDTVGS SKSIAEIDGD EVTQIRRVFT LGKDIKPHIT
TDDTMGSQWK NHPDWPFWVN KVESRRLLDS NIIESIFYMY RISGEQKWRS MGKQSFGILM
QELMELNSGA KGLWQIKEFY ENGEKVNNDL PSYWFSRTLK YYLLLFSDGD KVSLDKHILT
QGGHIIKKK
