MNN15_CANAL
ID MNN15_CANAL Reviewed; 763 AA.
AC Q59VL7; A0A1D8PDE6; Q59VI0;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Putative alpha-1,3-mannosyltransferase MNN15;
DE EC=2.4.1.-;
GN Name=MNN15; OrderedLocusNames=CAALFM_C104900WA;
GN ORFNames=CaO19.753, CaO19.8373;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP INDUCTION.
RX PubMed=20491945; DOI=10.1111/j.1567-1364.2010.00638.x;
RA Lis M., Liu T.T., Barker K.S., Rogers P.D., Bobek L.A.;
RT "Antimicrobial peptide MUC7 12-mer activates the calcium/calcineurin
RT pathway in Candida albicans.";
RL FEMS Yeast Res. 10:579-586(2010).
RN [5]
RP INDUCTION.
RX PubMed=22265407; DOI=10.1016/j.cell.2011.10.048;
RA Nobile C.J., Fox E.P., Nett J.E., Sorrells T.R., Mitrovich Q.M.,
RA Hernday A.D., Tuch B.B., Andes D.R., Johnson A.D.;
RT "A recently evolved transcriptional network controls biofilm development in
RT Candida albicans.";
RL Cell 148:126-138(2012).
RN [6]
RP IDENTIFICATION.
RX PubMed=23886038; DOI=10.1186/1756-0500-6-294;
RA Bates S., Hall R.A., Cheetham J., Netea M.G., MacCallum D.M., Brown A.J.,
RA Odds F.C., Gow N.A.;
RT "Role of the Candida albicans MNN1 gene family in cell wall structure and
RT virulence.";
RL BMC Res. Notes 6:294-294(2013).
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 (By similarity).
CC {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- INDUCTION: Induced during biofilm formation and Up-regulated in
CC response to treatment with MUC7 12-mer, a cationic antimicrobial
CC peptide derived from the N-terminal region of human low-molecular-
CC weight salivary mucin. {ECO:0000269|PubMed:20491945,
CC ECO:0000269|PubMed:22265407}.
CC -!- SIMILARITY: Belongs to the MNN1/MNT family. {ECO:0000305}.
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DR EMBL; CP017623; AOW26163.1; -; Genomic_DNA.
DR RefSeq; XP_713563.2; XM_708470.2.
DR STRING; 237561.Q59VL7; -.
DR GeneID; 3644794; -.
DR KEGG; cal:CAALFM_C104900WA; -.
DR CGD; CAL0000175887; MNN15.
DR VEuPathDB; FungiDB:C1_04900W_A; -.
DR eggNOG; ENOG502RZ48; Eukaryota.
DR HOGENOM; CLU_015387_0_1_1; -.
DR InParanoid; Q59VL7; -.
DR OrthoDB; 527450at2759; -.
DR UniPathway; UPA00378; -.
DR PHI-base; PHI:3694; -.
DR PRO; PR:Q59VL7; -.
DR Proteomes; UP000000559; Chromosome 1.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0046354; P:mannan biosynthetic process; IEA:UniProt.
DR GO; GO:0035268; P:protein mannosylation; IEA:UniProt.
DR GO; GO:0006493; P:protein O-linked glycosylation; IBA:GO_Central.
DR InterPro; IPR022751; Alpha_mannosyltransferase.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF11051; Mannosyl_trans3; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..763
FT /note="Putative alpha-1,3-mannosyltransferase MNN15"
FT /id="PRO_0000424328"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..763
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 617..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..646
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 763 AA; 89653 MW; ADF623EECEE32A74 CRC64;
MRFTLKKIFF VFLTLLIISI GYLLLQSVDL QRIRELLHDS EKFDLESLKQ ASLEIRKEIH
YTNYLFSGYD NFTQQFSDEE TLKQTSLNDK CKLVFTQWKE SHPDFEFKTF EPEYERYDKS
SDRKELFFKE RINQLRKRFE KDSNNKNKQF TLSRQDNKTI SQEYMEHVNR SKNVLQFMAD
FVSMMRLYGK CFFGRELDDE LKSIYNEFRG KLFPFISSQA PKFRKSGETE EFGWPIYDNE
NNIIDRKTEF GDNPIEFLQK NSKGKGIVIS VSTRYAKDAM RLIKILRALN NRLPIQIIYK
NDITKKNIEL LEFAAVATPE ELFDPETIRD GAKFMPELNL LEHYKNYGSE FPIQDLTFVN
IAGCVSRPYR FSFPGYSNKI LAMLYSSFEE IILFDADVVP TVNPQEFFDS KYYKSSGTYF
FQDRSLRDFN DFIETNFFST LFPSNEKSIE TIFDIPRVGE KTFNNKYMTG WRHYQEAGVV
AYNKMQHFLG ILMMFPLALW SEPVQSSIWG DKEMYWLGLS MAGDENYEFN KYAAASVGEK
TTEQKYKYYP NSDSNEVCST HPGHIDDNGR LLWINSGFSY CKKNGYFRDK GKFPFSTFEL
NDLVELYNSP IKIRAGLVPP DLPNQREPGS PPDTKPEMEF RKSWKSRKKD TDEINEKLPE
GQEPYDFISE WGPQKGWVKN GICSGYYYCA YDKITSYSSE KEFDTGTLFE FDTKSCELYD
YLSKIWHTGG SKMKPKVKLE TEKLGTGSDK EQXKDATTVR LRI
