MNN21_CANAL
ID MNN21_CANAL Reviewed; 660 AA.
AC Q59KJ7; A0A1D8PSY3;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Alpha-1,2-mannosyltransferase MNN21;
DE EC=2.4.1.-;
GN Name=MNN21; OrderedLocusNames=CAALFM_CR05300CA;
GN ORFNames=CaO19.1011, CaO19.8625;
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 FUNCTION.
RX PubMed=23633946; DOI=10.1371/journal.ppat.1003276;
RA Hall R.A., Bates S., Lenardon M.D., Maccallum D.M., Wagener J.,
RA Lowman D.W., Kruppa M.D., Williams D.L., Odds F.C., Brown A.J., Gow N.A.;
RT "The Mnn2 mannosyltransferase family modulates mannoprotein fibril length,
RT immune recognition and virulence of Candida albicans.";
RL PLoS Pathog. 9:E1003276-E1003276(2013).
CC -!- FUNCTION: Alpha-1,2-mannosyltransferase required for cell wall
CC integrity. Responsible for addition of the first alpha-1,2-linked
CC mannose to form the branches on the mannan backbone of
CC oligosaccharides. Addition of alpha-1,2-mannose is required for
CC stabilization of the alpha-1,6-mannose backbone and hence regulates
CC mannan fibril length; and is important for both immune recognition and
CC virulence. {ECO:0000269|PubMed:23633946}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MNN1/MNT family. {ECO:0000305}.
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DR EMBL; CP017630; AOW31255.1; -; Genomic_DNA.
DR RefSeq; XP_710276.1; XM_705184.1.
DR AlphaFoldDB; Q59KJ7; -.
DR STRING; 237561.Q59KJ7; -.
DR GeneID; 3648124; -.
DR KEGG; cal:CAALFM_CR05300CA; -.
DR CGD; CAL0000174283; MNN21.
DR VEuPathDB; FungiDB:CR_05300C_A; -.
DR eggNOG; ENOG502QQ16; Eukaryota.
DR HOGENOM; CLU_013298_1_0_1; -.
DR InParanoid; Q59KJ7; -.
DR OMA; KGYQYKA; -.
DR OrthoDB; 758358at2759; -.
DR UniPathway; UPA00378; -.
DR PHI-base; PHI:2884; -.
DR PRO; PR:Q59KJ7; -.
DR Proteomes; UP000000559; Chromosome R.
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:0000026; F:alpha-1,2-mannosyltransferase activity; IBA:GO_Central.
DR GO; GO:0046354; P:mannan biosynthetic process; IMP:CGD.
DR GO; GO:0035268; P:protein mannosylation; IMP:CGD.
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; Golgi apparatus; Membrane; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..660
FT /note="Alpha-1,2-mannosyltransferase MNN21"
FT /id="PRO_0000428635"
FT TOPO_DOM 1..17
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..660
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 75..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 657
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 660 AA; 76921 MW; 64CD8081982D6A43 CRC64;
MFQQLTYRLR LFRRRHKYIF INSIFLSVII IFLIYSYWSN LPAEDNSAII NEKGTYHRSL
WESITMALFP PKTKPFEEKK PQVNPNNNQE VGVESGASEI SQHKQQQQQQ QHAKEPTTKT
SSKSLVSDEA YQLNLKLINE QQEKYNRLHP FEQKRLQQGY EFFDNIFKIF YQAKPSVSQL
NTYPSKKRIY HARFDSLADD DTIFSEKYLS QFLQLSNEEL AAMKKSHKYV VENLPEDAPD
GLYKKNGIVY VAGGSFNWLT LLSIKSLRAV GCHLPIEVFI PKIEEYESDL CNRILPELDA
RCIYMKNQLM NPNKDNSDSF ANKFEFKGYQ YKALAILLSS FENVLLLDSD NIPAHSPEEL
FENDPFKSYG LVVWPDYWKR ATSPYYYNIA DIDVSEKYLG SKYNEVEGQY TDLSVEKGSV
ELDKIPLHQR LGSIPDPTSE SGQLLISKKT HLKPLLLALY YNLYGPSHYY PLFSQGSDGE
GDKETFLAAT VTLGKRYYQV AKFLVSLGHF KVPGGDFEGC GMGQFDPQQD LEYIKLREQY
AKIPEKDKEK QHKFKLQHQV LEKGPEILFV HANFPKLNPW KLKQEKKIFD AKGNRVRLYG
PGMIKRIGYD FEWFQWEGMK YLLCIYDVNL QIFQDVKKSD LCDEILEHLR FLESTQNITD
