ID   MNN22_CANAL             Reviewed;         589 AA.
AC   Q5A687; A0A1D8PM49; Q5A6G7;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Alpha-1,2-mannosyltransferase MNN22;
DE            EC=2.4.1.-;
GN   Name=MNN22; Synonyms=MNN24; OrderedLocusNames=CAALFM_C404770CA;
GN   ORFNames=CaO19.11284, CaO19.3803;
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=16030247; DOI=10.1091/mbc.e05-05-0435;
RA   Hromatka B.S., Noble S.M., Johnson A.D.;
RT   "Transcriptional response of Candida albicans to nitric oxide and the role
RT   of the YHB1 gene in nitrosative stress and virulence.";
RL   Mol. Biol. Cell 16:4814-4826(2005).
RN   [5]
RP   INDUCTION.
RX   PubMed=16102003; DOI=10.1111/j.1365-2958.2005.04771.x;
RA   Urban C., Xiong X., Sohn K., Schroppel K., Brunner H., Rupp S.;
RT   "The moonlighting protein Tsa1p is implicated in oxidative stress response
RT   and in cell wall biogenesis in Candida albicans.";
RL   Mol. Microbiol. 57:1318-1341(2005).
RN   [6]
RP   INDUCTION.
RX   PubMed=16339080; DOI=10.1091/mbc.e05-06-0501;
RA   Enjalbert B., Smith D.A., Cornell M.J., Alam I., Nicholls S., Brown A.J.P.,
RA   Quinn J.;
RT   "Role of the Hog1 stress-activated protein kinase in the global
RT   transcriptional response to stress in the fungal pathogen Candida
RT   albicans.";
RL   Mol. Biol. Cell 17:1018-1032(2006).
RN   [7]
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   -!- INDUCTION: Expression is induced by nitric oxide (NO) and HOG1; and
CC       repressed by osmotic stress, oxidative stress, and heavy metal stress.
CC       Expression is also regulated by TSA1. {ECO:0000269|PubMed:16030247,
CC       ECO:0000269|PubMed:16102003, ECO:0000269|PubMed:16339080}.
CC   -!- SIMILARITY: Belongs to the MNN1/MNT family. {ECO:0000305}.
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DR   EMBL; CP017626; AOW29220.1; -; Genomic_DNA.
DR   RefSeq; XP_717208.1; XM_712115.2.
DR   AlphaFoldDB; Q5A687; -.
DR   STRING; 237561.Q5A687; -.
DR   GeneID; 3641117; -.
DR   KEGG; cal:CAALFM_C404770CA; -.
DR   CGD; CAL0000196006; MNN22.
DR   VEuPathDB; FungiDB:C4_04770C_A; -.
DR   eggNOG; ENOG502QQ16; Eukaryota.
DR   HOGENOM; CLU_013298_1_2_1; -.
DR   OrthoDB; 758358at2759; -.
DR   UniPathway; UPA00378; -.
DR   PHI-base; PHI:2887; -.
DR   PRO; PR:Q5A687; -.
DR   Proteomes; UP000000559; Chromosome 4.
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   2: Evidence at transcript level;
KW   Glycoprotein; Golgi apparatus; Membrane; Reference proteome; Signal-anchor;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..589
FT                   /note="Alpha-1,2-mannosyltransferase MNN22"
FT                   /id="PRO_0000428636"
FT   TOPO_DOM        1..16
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        17..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        34..589
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   REGION          50..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        64
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        332
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        530
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   589 AA;  68209 MW;  3A2D52B3612F4247 CRC64;
     MGSIFKDGRR ILVRPKSLII CLCLISIIFT QLIRYQYQLI ADEVQPTINE DHSSSQSLKN
     TKLNSTRSSS PISPPKSLNK LTSQEFWEHI FNIFEINKFD DGLKPLIKYT PKEQQLTTKI
     KTRDWLLSKA NIFHKDIIRQ YHESVLRNLP SKLPKSVYTP NTYGIVTIGG NFYSWMAYIQ
     LLQLRKLGSN LPVEILIPSI EDYYKEAHFC DHVLPQYNAK CILVPEKLGF NVAKHWKFSS
     YQFKALALCL SSFQHVLILD SDNVVLSKPE KVFDSPVYRD NGMVLWPDYW ERTISPEWYD
     IIGKPVVGNK QVRTGRFPVN IHNMLTSELE INETRFHDLE GALPDLSTES GQVMFNKKTH
     GKVMLMTLYY NIFGPEIYYK LFSLGALGEG DKDTFAAAAL ACGEKYYQVA SSIRTLGYFD
     TTPGGGFHGM AMAQKNPQLD YQLFQKTNQN FKDLHLDWDN EAKDQFSANN KIPIFTMHCN
     IKKINPAAYM KDEKIANMDE KRMNVRFYSN LKFKLNDDDI YSPDNEKEKN KSEKTDNDPN
     EIDFELSRWQ IVSEILCDQK ITFQFLKDEN MDEVCQFVKN TIAWLGKKT