MNN23_CANAL
ID MNN23_CANAL Reviewed; 606 AA.
AC Q5AP90; A0A1D8PES4;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 2.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Alpha-1,2-mannosyltransferase MNN23;
DE EC=2.4.1.-;
GN Name=MNN23; Synonyms=MNN3; OrderedLocusNames=CAALFM_C110070CA;
GN ORFNames=CaO19.12338, CaO19.4874;
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, AND DISRUPTION PHENOTYPE.
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 -!- DISRUPTION PHENOTYPE: Leads to hypersensitivity to toxic ergosterol
CC analog, amphotericin B, calcofluor white, and to thermosensitivity.
CC {ECO:0000269|PubMed:23633946}.
CC -!- SIMILARITY: Belongs to the MNN1/MNT family. {ECO:0000305}.
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DR EMBL; CP017623; AOW26638.1; -; Genomic_DNA.
DR RefSeq; XP_723558.2; XM_718465.2.
DR AlphaFoldDB; Q5AP90; -.
DR STRING; 237561.Q5AP90; -.
DR PRIDE; Q5AP90; -.
DR GeneID; 3634813; -.
DR KEGG; cal:CAALFM_C110070CA; -.
DR CGD; CAL0000193748; MNN23.
DR VEuPathDB; FungiDB:C1_10070C_A; -.
DR eggNOG; ENOG502S8HP; Eukaryota.
DR HOGENOM; CLU_013298_1_2_1; -.
DR InParanoid; Q5AP90; -.
DR OrthoDB; 758358at2759; -.
DR UniPathway; UPA00378; -.
DR PHI-base; PHI:2886; -.
DR PRO; PR:Q5AP90; -.
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: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 Golgi apparatus; Membrane; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..606
FT /note="Alpha-1,2-mannosyltransferase MNN23"
FT /id="PRO_0000428637"
FT TOPO_DOM 1..14
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 36..606
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 59..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 606 AA; 69650 MW; 04134431AC796400 CRC64;
MSINFLSIPR NRFKAIGVLS VTCILIYVIL HSSIITTDFD VSDYGDKFIP SIIFDDNNDN
GENLKDPQPE LDNDKGNGET DTTTSNSMTT AHTFWKGIFD TFDKYKMDLG QDPENAVSYV
DKLKQKQGPL NKEVLLSKAI VSSELMKHLK EKHSGVVEDL PSVMPGSVYN KGSKGVVIIG
GGKFSWLAYL ALVQLRNVGS KLPVEIVMPS RADYEKELEF CENTLPEMQA SCVVLPDVLG
EAVMKNRKFA SYQFKALALV VTSFEHILLL DSDNMIVSNP DEIFESKLYH QYGMITWPDY
WKRTISPLFY DVAEIEVNEN KRVRYNRFPL YNAPNVRSNI YTDQEREEVP FHDLQGSIAE
LSTESGQLII NKHTHGKTIL LALYYNFYGP NLFYKLFSLG EQGEGDKDTF VAAAVVTRQD
YYQVKSFIKT FGYADSDDKF QGVSMGQRNP LIDRKHYEDH VLALLEKDSF KSSSIADQIE
QMKKFENEDF DQHNSIPLFT VHCNYPKLDP KLYMSRDDLY DEKEKKLKYR LYGNLKYTKE
VVKDGETGTE ASTDKVQIDF ELQQWQHMQD ILCLKKIYFT HFIDNDMNEL CQFIENQVAW
LSKSQN
