MNN24_CANAL
ID MNN24_CANAL Reviewed; 709 AA.
AC Q5AD72; A0A1D8PGB3; Q5ADK0;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Alpha-1,2-mannosyltransferase MNN24;
DE EC=2.4.1.-;
GN Name=MNN24; Synonyms=MNN2, MNN22; OrderedLocusNames=CAALFM_C201300CA;
GN ORFNames=CaO19.1995, CaO19.9547;
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; CP017624; AOW27176.1; -; Genomic_DNA.
DR RefSeq; XP_719445.1; XM_714352.2.
DR AlphaFoldDB; Q5AD72; -.
DR STRING; 237561.Q5AD72; -.
DR GeneID; 3638789; -.
DR KEGG; cal:CAALFM_C201300CA; -.
DR CGD; CAL0000192056; MNN24.
DR VEuPathDB; FungiDB:C2_01300C_A; -.
DR eggNOG; ENOG502SJ0W; Eukaryota.
DR HOGENOM; CLU_013298_1_0_1; -.
DR InParanoid; Q5AD72; -.
DR OrthoDB; 758358at2759; -.
DR UniPathway; UPA00378; -.
DR PHI-base; PHI:2885; -.
DR PRO; PR:Q5AD72; -.
DR Proteomes; UP000000559; Chromosome 2.
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 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..709
FT /note="Alpha-1,2-mannosyltransferase MNN24"
FT /id="PRO_0000428638"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..709
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 709 AA; 83023 MW; 98EEADE8F6041821 CRC64;
MFSIPVSSKT VRLILVSLLL ITLINILAAF QRSTLSSWFP SSRHIINKFT DLRLALSSQE
SVLRDEEGEI YSLVGYHHDF DSNLVVVQKQ YLLEKTPNED TTEHFWNFLQ SNFETKSEYD
LNLIDGYNYK KLIKHLNEQN ELQLSHSFVE QYKMENQFIQ SFQNFFVQLI DTIEDCKPDL
DPINNDNHYP NGDKIVKYYE LRNKIPSENM KQFNIERLIH RNGRIPIYGG HLREQYKDEL
IRNKEFLSMY LTLSDSEISA LKKSHTKFLE TMMENWPENL FKFNKFNNFM KGDGIVYLGG
GKYNQLVLLS IKILRENGSR LPVEVIIPYK NDYDIQFCDR VLPTLNGKCK LMTDYLPQTF
VDKISGFQLK NIALLISSFE RILYLDADNI PIRNPDVLFT NAPFTTKHLV VWPDLWRRST
SPHYYTIAGI EVDPNFKVRN SYVDGDERGK YTDSMYYSYH DCKGSIPEAS SETGQLLINK
KIHFQTLILA MYYNYYGPDY YYPLFSQGAA GEGDKETFIA AAHKLDLPYY QVGEFNREFG
PINDNTRKHE FYGMGQYDPI IDYYMSTITT TQKDTKKKIN YNSPLPEKYA ANDEDDTCSN
YDFHLFQSSS LFFLHANWPK YYIEKLFLYS YDEDRGPVTN DGDKRRLYGN ELKKELGGYD
FELNIMKNLH WCFCEEPLID LIGIPVVGSK TRTDVCIAIK NHIEFLEIS
