MNN1_YEAST
ID MNN1_YEAST Reviewed; 762 AA.
AC P39106; D3DLP7;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Alpha-1,3-mannosyltransferase MNN1;
DE EC=2.4.1.-;
GN Name=MNN1; OrderedLocusNames=YER001W;
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 26109 / X2180;
RX PubMed=8146181; DOI=10.1073/pnas.91.7.2723;
RA Yip C.L., Welch S.K., Klebl F., Gilbert T., Seidel P., Grant F.J.,
RA O'Hara P.J., Mackay V.L.;
RT "Cloning and analysis of the Saccharomyces cerevisiae MNN9 and MNN1 genes
RT required for complex glycosylation of secreted proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:2723-2727(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(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).
CC -!- FUNCTION: Responsible for addition of the terminal mannose residues to
CC the outer chain of core N-linked polysaccharides and to O-linked
CC mannotriose. Implicated in late Golgi modifications.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 1780 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the MNN1/MNT family. {ECO:0000305}.
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DR EMBL; L23753; AAA53676.1; -; Genomic_DNA.
DR EMBL; U18778; AAB64534.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07651.1; -; Genomic_DNA.
DR PIR; S50459; S50459.
DR RefSeq; NP_010916.1; NM_001178892.1.
DR AlphaFoldDB; P39106; -.
DR BioGRID; 36731; 53.
DR DIP; DIP-7589N; -.
DR IntAct; P39106; 3.
DR MINT; P39106; -.
DR STRING; 4932.YER001W; -.
DR CAZy; GT71; Glycosyltransferase Family 71.
DR SwissPalm; P39106; -.
DR MaxQB; P39106; -.
DR PaxDb; P39106; -.
DR PRIDE; P39106; -.
DR EnsemblFungi; YER001W_mRNA; YER001W; YER001W.
DR GeneID; 856718; -.
DR KEGG; sce:YER001W; -.
DR SGD; S000000803; MNN1.
DR VEuPathDB; FungiDB:YER001W; -.
DR eggNOG; ENOG502RZ48; Eukaryota.
DR GeneTree; ENSGT00940000176340; -.
DR HOGENOM; CLU_015387_1_1_1; -.
DR InParanoid; P39106; -.
DR OMA; GHINGED; -.
DR BioCyc; MetaCyc:YER001W-MON; -.
DR BioCyc; YEAST:YER001W-MON; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:P39106; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P39106; protein.
DR GO; GO:0005794; C:Golgi apparatus; IDA:SGD.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000033; F:alpha-1,3-mannosyltransferase activity; IMP:SGD.
DR GO; GO:0006491; P:N-glycan processing; IMP:SGD.
DR GO; GO:0006493; P:protein O-linked glycosylation; IDA:SGD.
DR InterPro; IPR022751; Alpha_mannosyltransferase.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF11051; Mannosyl_trans3; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..762
FT /note="Alpha-1,3-mannosyltransferase MNN1"
FT /id="PRO_0000080558"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 17..33
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..762
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 383
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 338
FT /note="S -> T (in Ref. 1; AAA53676)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 762 AA; 88529 MW; 7EF7967E2C60B185 CRC64;
MLALRRFILN QRSLRSCTIP ILVGALIIIL VLFQLVTHRN DALIRSSNVN STNKKTLKDA
DPKVLIEAFG SPEVDPVDTI PVSPLELVPF YDQSIDTKRS SSWLINKKGY YKHFNELSLT
DRCKFYFRTL YTLDDEWTNS VKKLEYSIND NEGVDEGKDA NGNPMDEKSE RLYRRKYDMF
QAFERIRAYD RCFMQANPVN IQEIFPKSDK MSKERVQSKL IKTLNATFPN YDPDNFKKYD
QFEFEHKMFP FINNFTTETF HEMVPKITSP FGKVLEQGFL PKFDHKTGKV QEYFKYEYDP
SKTFWANWRD MSAKVAGRGI VLSLGSNQFP LAVKFIASLR FEGNTLPIQV VYRGDELSQE
LVDKLIYAAR SPDFKPVENN YDNSTNVPQE IWFLDVSNTI HPKWRGDFGS YKSKWLVVLL
NLLQEFVFLD IDAISYEKID NYFKTTEYQK TGTVFYRERA LRENVNERCI ARYETLLPRN
LESKNFQNSL LIDPDHALNE CDNTLTTEEY IFKAFFHHRR QHQLEAGLFA VDKSKHTIPL
VLAAMIHLAK NTAHCTHGDK ENFWLGFLAA GHTYALQGVY SGAIGDYVKK TDLNGKRQEA
AVEICSGQIA HMSTDKKTLL WVNGGGTFCK HDNAAKDDWK KDGDFKKFKD QFKTFEEMEK
YYYITPISSK YVILPDPKSD DWHRASAGAC GGYIWCATHK TLLKPYSYNH RTTHGELITL
DEEQRLHIDA VNTVWSHANK DNTRSFTEEE IKELENSRHE QS
