MNN2_CANAL
ID MNN2_CANAL Reviewed; 597 AA.
AC Q59WF4; A0A1D8PEZ4; Q59WL2;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Alpha-1,2-mannosyltransferase MNN2;
DE EC=2.4.1.-;
GN Name=MNN2; Synonyms=MNN25, MNN5; OrderedLocusNames=CAALFM_C110720CA;
GN ORFNames=CaO19.2347, CaO19.9883;
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=15725072; DOI=10.1042/bj20050223;
RA Bai C., Chan F.Y., Wang Y.;
RT "Identification and functional characterization of a novel Candida albicans
RT gene CaMNN5 that suppresses the iron-dependent growth defect of
RT Saccharomyces cerevisiae aft1Delta mutant.";
RL Biochem. J. 389:27-35(2005).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=16467465; DOI=10.1128/ec.5.2.238-247.2006;
RA Bai C., Xu X.L., Chan F.Y., Lee R.T., Wang Y.;
RT "MNN5 encodes an iron-regulated alpha-1,2-mannosyltransferase important for
RT protein glycosylation, cell wall integrity, morphogenesis, and virulence in
RT Candida albicans.";
RL Eukaryot. Cell 5:238-247(2006).
RN [6]
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. Promotes iron uptake and usage along the endocytosis pathway
CC under iron-limiting conditions. {ECO:0000269|PubMed:15725072,
CC ECO:0000269|PubMed:16467465, ECO:0000269|PubMed:23633946}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:16467465};
CC -!- ACTIVITY REGULATION: Enzyme activity is regulated by iron.
CC {ECO:0000269|PubMed:16467465}.
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: Decreases the ability to extend O-linked, and
CC possibly also N-linked, mannans. Leads to hypersensitivity to cell
CC wall-damaging agents, and to a reduction of cell wall
CC mannosylphosphate. Leads also to resistance to killing by the iron-
CC chelating protein lactoferrin. {ECO:0000269|PubMed:16467465}.
CC -!- SIMILARITY: Belongs to the MNN1/MNT family. {ECO:0000305}.
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DR EMBL; CP017623; AOW26699.1; -; Genomic_DNA.
DR RefSeq; XP_713952.2; XM_708859.2.
DR AlphaFoldDB; Q59WF4; -.
DR STRING; 237561.Q59WF4; -.
DR PRIDE; Q59WF4; -.
DR GeneID; 3644405; -.
DR KEGG; cal:CAALFM_C110720CA; -.
DR CGD; CAL0000190919; MNN2.
DR VEuPathDB; FungiDB:C1_10720C_A; -.
DR eggNOG; ENOG502RGFY; Eukaryota.
DR HOGENOM; CLU_013298_2_0_1; -.
DR InParanoid; Q59WF4; -.
DR OrthoDB; 758358at2759; -.
DR UniPathway; UPA00378; -.
DR PHI-base; PHI:2883; -.
DR PRO; PR:Q59WF4; -.
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; IDA:CGD.
DR GO; GO:0009267; P:cellular response to starvation; IMP:CGD.
DR GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR GO; GO:0044182; P:filamentous growth of a population of unicellular organisms; IMP:CGD.
DR GO; GO:0036180; P:filamentous growth of a population of unicellular organisms in response to biotic stimulus; IMP:CGD.
DR GO; GO:0036178; P:filamentous growth of a population of unicellular organisms in response to neutral pH; IMP:CGD.
DR GO; GO:0036170; P:filamentous growth of a population of unicellular organisms in response to starvation; IMP:CGD.
DR GO; GO:0034755; P:iron ion transmembrane transport; IGI:CGD.
DR GO; GO:0046354; P:mannan biosynthetic process; IMP:CGD.
DR GO; GO:0006486; P:protein glycosylation; ISS: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 1: Evidence at protein level;
KW Glycoprotein; Golgi apparatus; Iron; Manganese; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..597
FT /note="Alpha-1,2-mannosyltransferase MNN2"
FT /id="PRO_0000428634"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..597
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 39..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..85
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 382
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 597 AA; 69165 MW; 0C19C9CEE85AF168 CRC64;
MIAKQKIKIL IGVIIVIATY HFIVSSNVRS KDLSDLVDLG SSDKSTTENE RPKNNIVTNN
RLDNPPNEDI PHAEPDSPPQ EPPKSGNKPD FSIFFEGLEK FAIKQPGIKD KYTSEKAKEK
FSTDDNFLFG KEYLENVLDI PQATFKELKD SHKRYVDEHI PKMLQRVKTF GSLAPSDKEW
ESYKGSSGYI IVGGGRFTWL SFLVIKQLRA TGAKLPVEMF IATESDYEKE FCEKVLPKYN
ARCNVFDYKL ADDLKKRFDI GGYQYKMLAL LSSKFENVLY LDSDNFPTRN VDYLFESDLY
KENNLLLWPD AWARTTNPKY YEIAGVPVKE NKLRYSKYDE KQAGGKDKLK PLSEYTFKDS
WYHDFEGTLP DPTSETGMFM VNKSSHLKTL LLCLYYNVFG PQYYYPLLTQ GSAGEGDKET
FIAAAHVMKE PWYQCARQFK WTGYVSKVDN KFTSKALAHY DPVQAQDTTR QDVDIIFMHL
SYPKFYPNWL ADNHDLVYAD TDEHIRMYSS INKNVGYDFD LRVMQFFTEG LCPNYYDSKT
GKPIENIPHI DYTNDYMGNH LMYVKDEEQN NIDRCNKVFI PHLKWLKETA EIPTVVS
