ID   MNN5_YEAS7              Reviewed;         586 AA.
AC   A6ZQE9;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=Alpha-1,2-mannosyltransferase MNN5;
DE            EC=2.4.1.-;
DE   Flags: Precursor;
GN   Name=MNN5; ORFNames=SCY_3110;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
CC   -!- FUNCTION: Responsible for addition of first and second mannose residues
CC       to the outer chain of core N-linked polysaccharides and to O-linked
CC       mannotriose. Implicated in late Golgi modifications (By similarity).
CC       {ECO:0000250}.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network {ECO:0000250}.
CC   -!- PTM: Glycosylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the MNN1/MNT family. {ECO:0000305}.
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DR   EMBL; AAFW02000044; EDN63201.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6ZQE9; -.
DR   PRIDE; A6ZQE9; -.
DR   EnsemblFungi; EDN63201; EDN63201; SCY_3110.
DR   HOGENOM; CLU_013298_1_1_1; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000030; F:mannosyltransferase activity; IEA:UniProt.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR022751; Alpha_mannosyltransferase.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   Pfam; PF11051; Mannosyl_trans3; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Glycosyltransferase; Golgi apparatus; Signal; Transferase.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..586
FT                   /note="Alpha-1,2-mannosyltransferase MNN5"
FT                   /id="PRO_0000320340"
FT   CARBOHYD        113
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        136
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        259
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        264
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   586 AA;  67252 MW;  85DE1B8A9DB4C355 CRC64;
     MLIRLKKRKI LQVIVSAVVL ILFFCSVHND VSSSWLYGKK LRLPVLTRSN LKNNFYTTLV
     QAIVENKPTD SSPDLSKLHG AEGCSFANNV AAHDSGHDSD LSYESLSKCY NLNKTVQESL
     REVHSKFTDT LSGKLNFSIP QREALFSGSE GIVTIGGGKY SVLAYTMIKK LRDTGTTLPI
     EVIIPPQDEG EDDFCKNWLP KFNGKCIYFS DIVPSKPLSD LKLTHFQLKV FGLIISSFKR
     IIFLDADNYA VKNLDLAFNT TSFNDTGLIL WPDFWRRVTP PAFYNIIGSS IDIGKRVRFV
     SDDISPVSRY DPFVSNSNDY TPKERQEHFL KHVPLHDLDG TMPDLSSESG QMVIDKIRHF
     NTLLLALYYN VYGPTWYYKM ISQGTAGEGD KDTFVAAAHA LNMPYYQVRT KFEFDGFFYQ
     KDDYKGLALL QHDFEQDYKQ YQKAQQEVKA NIEEFSKLDP DYTLDNGFLK TLMVNDDGSD
     LDIMFIHASF YKADPWTLYH ENRFIGPNGE QVRGFRKPHR YGMDFELFLF NDMSKSFCTT
     PKSQVIKFKY FTDKVNTPEW DAMCEYLTNH VNYLESTHKE AMGEKN