MNN26_CANAL
ID MNN26_CANAL Reviewed; 756 AA.
AC Q59R28; A0A1D8PRD2; Q3MNZ7;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Alpha-1,2-mannosyltransferase MNN26;
DE EC=2.4.1.-;
GN Name=MNN26; Synonyms=MNN7; OrderedLocusNames=CAALFM_C703600WA;
GN ORFNames=CaO19.13984, CaO19.6692;
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 sensitivity to calcofluor white and SDS,
CC as well as to thermosensitivity. {ECO:0000269|PubMed:23633946}.
CC -!- SIMILARITY: Belongs to the MNN1/MNT family. {ECO:0000305}.
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DR EMBL; CP017629; AOW30702.1; -; Genomic_DNA.
DR RefSeq; XP_712145.1; XM_707052.1.
DR AlphaFoldDB; Q59R28; -.
DR SMR; Q59R28; -.
DR STRING; 237561.Q59R28; -.
DR CAZy; GT71; Glycosyltransferase Family 71.
DR PRIDE; Q59R28; -.
DR GeneID; 3646240; -.
DR KEGG; cal:CAALFM_C703600WA; -.
DR CGD; CAL0000182010; MNN26.
DR VEuPathDB; FungiDB:C7_03600W_A; -.
DR eggNOG; ENOG502QVWG; Eukaryota.
DR HOGENOM; CLU_013298_1_0_1; -.
DR InParanoid; Q59R28; -.
DR OMA; HVMNERY; -.
DR OrthoDB; 758358at2759; -.
DR UniPathway; UPA00378; -.
DR PHI-base; PHI:2888; -.
DR Proteomes; UP000000559; Chromosome 7.
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:0016020; C:membrane; IDA:CGD.
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..756
FT /note="Alpha-1,2-mannosyltransferase MNN26"
FT /id="PRO_0000428639"
FT TOPO_DOM 1..10
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..756
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 723..756
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 756 AA; 87222 MW; BD2438069E4C6CBC CRC64;
MSLRRLSPSH LILGTLVLGV IIFNLYVLTS THEDIKKVKG PTYHTSDNTK IQSHISNYDS
EEYVDRLTAE IEDAKKEELI SEIRKKLEIQ EKPGVIQKLK TELRMKYIDD IKNHLKQEIT
EQYSNEIFKQ YAFSFEIYSK KVDEYALQLE NSLKPASCLA ILQQAEKDTD SIPDLENYLT
KANDKYFKRQ EYWRYLLKDI LLNNKPKCEP LTKEEKGEKL NPTYQWDARI ISEQYLLGSK
LTIPGEKFRA LRSAHDQVVK QLKSLPDPPS QFISGHGIVV NGGGNMIGSA LTAIANMRER
GSQLPVELIL DTKQEYDKQI CEELLPKKLN GKCVIVEEQV GKEVFDIINE KFSRKIMGLL
VSSFDHIIAM DADNLAIKNV DNLLFTEPYL STKMILWPDL WVKLTSPLYY KIARIEPGEI
VDRFGIPNDA SFAEYITKDK QSEVHYHDLD NLPSTISVET GQMVFSKREH LKSLLLALYY
NINGKDFYID LLYQGAYGEG DRETIVPALH VMNERYSLTN HKVHILGYDA PNGKYSETTL
GQTDPRDGFE FYQDWRKFLT SRKLDTRLNP FQSGGYTSDL MKQFHDYKRQ IYQDKQYEDE
AAVHRMITYK LPSILFLHCN HPKIDPLKNS KEADAEFGVY SRRNMGLPDK VEKLLEGKDW
ELRFHTISQW VACEAISKSS LYWEKIAGKS QQQVCESVGK YIEFLKKDTF DNEATKLTIL
NQLGEKSQPK QPEINNNNNN NNNDDDNGKN KQGAAS
