MNN12_CANAL
ID MNN12_CANAL Reviewed; 828 AA.
AC Q5APQ8; A0A1D8PEX9; Q5AP62;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Putative alpha-1,3-mannosyltransferase MNN12;
DE EC=2.4.1.-;
GN Name=MNN12; OrderedLocusNames=CAALFM_C110300WA;
GN ORFNames=CaO19.12366, CaO19.4900;
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 IDENTIFICATION.
RX PubMed=23886038; DOI=10.1186/1756-0500-6-294;
RA Bates S., Hall R.A., Cheetham J., Netea M.G., MacCallum D.M., Brown A.J.,
RA Odds F.C., Gow N.A.;
RT "Role of the Candida albicans MNN1 gene family in cell wall structure and
RT virulence.";
RL BMC Res. Notes 6:294-294(2013).
CC -!- FUNCTION: Responsible for addition of the terminal mannose residues to
CC the outer chain of core N-linked polysaccharides and to O-linked
CC mannotriose. Implicated in late Golgi modifications (By similarity).
CC {ECO:0000250}.
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; CP017623; AOW26660.1; -; Genomic_DNA.
DR RefSeq; XP_723582.2; XM_718489.2.
DR AlphaFoldDB; Q5APQ8; -.
DR STRING; 237561.Q5APQ8; -.
DR GeneID; 3634904; -.
DR KEGG; cal:CAALFM_C110300WA; -.
DR CGD; CAL0000176287; MNN12.
DR VEuPathDB; FungiDB:C1_10300W_A; -.
DR eggNOG; ENOG502RZ48; Eukaryota.
DR HOGENOM; CLU_015387_0_0_1; -.
DR InParanoid; Q5APQ8; -.
DR OrthoDB; 527450at2759; -.
DR UniPathway; UPA00378; -.
DR PHI-base; PHI:3691; -.
DR PRO; PR:Q5APQ8; -.
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:0000033; F:alpha-1,3-mannosyltransferase activity; IBA:GO_Central.
DR GO; GO:0046354; P:mannan biosynthetic process; IEA:UniProt.
DR GO; GO:0035268; P:protein mannosylation; IEA:UniProt.
DR GO; GO:0006493; P:protein O-linked glycosylation; IBA:GO_Central.
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 3: Inferred from homology;
KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..828
FT /note="Putative alpha-1,3-mannosyltransferase MNN12"
FT /id="PRO_0000424325"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..828
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 80..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 437
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 591
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 828 AA; 97529 MW; 83E4D541791934AA CRC64;
MIEKLTIKRS RQKVIAYSVI IIWLMIVNIW LLNNYHLNSS TLTRHGNGDN LIDEDDDSSS
SSEYSIYNEL DTENYLGQQH QEEDVPNSQS TDNSLIKPTS PAKNSFKDDI TIKILQKHLQ
KQQNNPKDIR TKDSHAEIYN QIFENHPQID TILGNLNFNQ RCQLFFQNLF IKDNNWILNV
KDKKIKLENK NDFKFNDFKK SHLNEFKRQF KTMKKLLEPN KIIHNKDFDN SIEFQDFIKM
KYEQFWNRTM TYEQKIVDSI SILRIFNKCY LIEEATSTTT TKNNKQDFIK DQFKLVDGIR
RASKKNPSLP KFKPTKQEQM VNFDNENLSP SILEHRVYPW LSFEYPVYER WTGKVQYQPP
KMANYVKDGN QKTTKKTKYN NDKYLSSFFL NRLKQKCNGR GLVLSISDLH VDVTVRLIHL
LRALNNRYPI QIVYYDNLSK ETKEKIVTAA REVMSHVPKS FERVAKYFPD DYLDNDQGGL
PKQEIWFINT YNVIHADYKL QFRGFANKFL ATLFNSFDEF ILLDADTVLT QSPSYFFNLP
QYLETGTFFY KDRTTYETRP KSDSIFFEKL GPSVIDSVMF NIPIMTSYTL NRSFFKGLFH
YMESGLVVLN RDMHYSSFLT MVQMNFFEPV NSRIHGDKEI FWLAMAINGK QNYYFDENYA
AAVGVMTPDI ERTKPDKTLH ESKELCSPHP GHISHDDNSL VWLNSGFFYC GQNDKVKFVE
EFKHKSRLKH LNTLEAFKTF YYSPLRIENA IIPPMDLDIW AANNEDEPAK GWFGDPRYCS
GYMWCAYDKI GGKTKSGKNT RLEGKIINFD EQAQDLFNYY GDVWVGME
