MNN5_YEAST
ID MNN5_YEAST Reviewed; 586 AA.
AC P46982; D6VW04;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Alpha-1,2-mannosyltransferase MNN5;
DE EC=2.4.1.-;
DE Flags: Precursor;
GN Name=MNN5; OrderedLocusNames=YJL186W; ORFNames=J0409;
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=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 395.
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.
RX PubMed=6995454; DOI=10.1016/s0021-9258(19)43886-6;
RA Cohen R.E., Ballou L., Ballou C.E.;
RT "Saccharomyces cerevisiae mannoprotein mutants. Isolation of the mnn5
RT mutant and comparison with the mnn3 strain.";
RL J. Biol. Chem. 255:7700-7707(1980).
RN [4]
RP FUNCTION.
RX PubMed=6802821; DOI=10.1016/s0021-9258(19)83839-5;
RA Cohen R.E., Zhang W., Ballou C.E.;
RT "Effects of mannoprotein mutations on Saccharomyces cerevisiae core
RT oligosaccharide structure.";
RL J. Biol. Chem. 257:5730-5737(1982).
RN [5]
RP FUNCTION, GLYCOSYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=9756928; DOI=10.1074/jbc.273.41.26836;
RA Rayner J.C., Munro S.;
RT "Identification of the MNN2 and MNN5 mannosyltransferases required for
RT forming and extending the mannose branches of the outer chain mannans of
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 273:26836-26843(1998).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [7]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH SVP26.
RX PubMed=20236934; DOI=10.1074/jbc.m109.086272;
RA Noda Y., Yoda K.;
RT "Svp26 facilitates endoplasmic reticulum to Golgi transport of a set of
RT mannosyltransferases in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 285:15420-15429(2010).
RN [8]
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 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.
CC {ECO:0000269|PubMed:6802821, ECO:0000269|PubMed:6995454,
CC ECO:0000269|PubMed:9756928}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBUNIT: Interacts with SVP26. {ECO:0000269|PubMed:20236934}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:20236934,
CC ECO:0000269|PubMed:9756928}. Note=Golgi localization depends on SVP26.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:9756928}.
CC -!- MISCELLANEOUS: Present with 11400 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the MNN1/MNT family. {ECO:0000305}.
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DR EMBL; Z49461; CAA89481.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08620.2; -; Genomic_DNA.
DR PIR; S56969; S56969.
DR RefSeq; NP_012349.2; NM_001181619.2.
DR AlphaFoldDB; P46982; -.
DR BioGRID; 33576; 61.
DR DIP; DIP-2868N; -.
DR IntAct; P46982; 1.
DR MINT; P46982; -.
DR STRING; 4932.YJL186W; -.
DR CAZy; GT71; Glycosyltransferase Family 71.
DR MaxQB; P46982; -.
DR PaxDb; P46982; -.
DR PRIDE; P46982; -.
DR EnsemblFungi; YJL186W_mRNA; YJL186W; YJL186W.
DR GeneID; 853253; -.
DR KEGG; sce:YJL186W; -.
DR SGD; S000003722; MNN5.
DR VEuPathDB; FungiDB:YJL186W; -.
DR eggNOG; ENOG502QTWU; Eukaryota.
DR GeneTree; ENSGT00940000176544; -.
DR HOGENOM; CLU_013298_1_1_1; -.
DR InParanoid; P46982; -.
DR OMA; MFIHASF; -.
DR BioCyc; MetaCyc:YJL186W-MON; -.
DR BioCyc; YEAST:YJL186W-MON; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:P46982; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P46982; protein.
DR GO; GO:0005794; C:Golgi apparatus; IDA:SGD.
DR GO; GO:0000026; F:alpha-1,2-mannosyltransferase activity; IMP:SGD.
DR GO; GO:0046354; P:mannan biosynthetic process; IBA:GO_Central.
DR GO; GO:0006486; P:protein glycosylation; IMP:SGD.
DR GO; GO:0035268; P:protein mannosylation; IBA:GO_Central.
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 1: Evidence at protein level;
KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Reference proteome;
KW Signal; Transferase.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..586
FT /note="Alpha-1,2-mannosyltransferase MNN5"
FT /id="PRO_0000203019"
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"
FT CONFLICT 395
FT /note="V -> F (in Ref. 1; CAA89481)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 586 AA; 67204 MW; 4AE911B415E354E6 CRC64;
MLIRLKKRKI LQVIVSAVVL ILFFCSVHND VSSSWLYGKK LRLPVLTRSN LKNNFYTTLV
QAIVENKPAD SSPDLSKLHG AEGCSFANNV AAHDSGHDSD LSYESLSKCY NLNKTVQESL
REVHSKFTDT LSGKLNFSIP QREALFSGSE GIVTIGGGKY SVLAYTMIKK LRDTGTTLPI
EVIIPPQDEG EDDFCKNWLP KFNGKCIYFS DIVPSKPLSD LKLTHFQLKV FGLIISSFKR
IIFLDADNYA VKNLDLAFNT TSFNDTGLIL WPDFWRRVTP PAFYNIIGSS INIGKRVRFV
SDDISPVSRY DPFVSNSNDY TPKERQEHFL KHVPLHDLDG TMPDLSSESG QMVIDKIRHF
NTLLLALYYN VYGPTWYYKM ISQGTAGEGD KDTFVAAAHA LNMPYYQVRT NFEFDGFFYQ
KDDYKGLALL QHDFEQDYKQ YQKAQQKVKA NIEEFSKLDP DYTLDNGFLK TLMVNDDGSD
LDIMFIHASF YKADPWTLYH ENRFIGPNGE QVRGFRKPHR YGMDFELFLF NDMRGSFCTT
PKSQVIKFKY FTDKVNTPEW DAMCEYLTNH VNYLESTHKE AMGEKN
