ID   MNN14_CANAL             Reviewed;         685 AA.
AC   Q59YS7; A0A1D8PK92;
DT   13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Putative alpha-1,3-mannosyltransferase MNN14;
DE            EC=2.4.1.-;
GN   Name=MNN14; OrderedLocusNames=CAALFM_C305610WA; ORFNames=CaO19.6996;
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=22265407; DOI=10.1016/j.cell.2011.10.048;
RA   Nobile C.J., Fox E.P., Nett J.E., Sorrells T.R., Mitrovich Q.M.,
RA   Hernday A.D., Tuch B.B., Andes D.R., Johnson A.D.;
RT   "A recently evolved transcriptional network controls biofilm development in
RT   Candida albicans.";
RL   Cell 148:126-138(2012).
RN   [5]
RP   IDENTIFICATION, DISRUPTION PHENOTYPE, AND FUNCTION.
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       Involved in virulence. {ECO:0000250, ECO:0000269|PubMed:23886038}.
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: Induced during biofilm formation.
CC       {ECO:0000269|PubMed:22265407}.
CC   -!- DISRUPTION PHENOTYPE: Leads to small cell wall defects but displays a
CC       severe attenuation of virulence in a murine infection model.
CC       {ECO:0000269|PubMed:23886038}.
CC   -!- SIMILARITY: Belongs to the MNN1/MNT family. {ECO:0000305}.
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DR   EMBL; CP017625; AOW28572.1; -; Genomic_DNA.
DR   RefSeq; XP_714702.1; XM_709609.1.
DR   AlphaFoldDB; Q59YS7; -.
DR   STRING; 237561.Q59YS7; -.
DR   PRIDE; Q59YS7; -.
DR   GeneID; 3643651; -.
DR   KEGG; cal:CAALFM_C305610WA; -.
DR   CGD; CAL0000177565; MNN14.
DR   VEuPathDB; FungiDB:C3_05610W_A; -.
DR   eggNOG; ENOG502RZ48; Eukaryota.
DR   HOGENOM; CLU_015387_0_1_1; -.
DR   InParanoid; Q59YS7; -.
DR   OrthoDB; 527450at2759; -.
DR   UniPathway; UPA00378; -.
DR   PHI-base; PHI:3693; -.
DR   Proteomes; UP000000559; Chromosome 3.
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   2: Evidence at transcript level;
KW   Glycoprotein; Glycosyltransferase; Golgi apparatus; Membrane;
KW   Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW   Transmembrane helix; Virulence.
FT   CHAIN           1..685
FT                   /note="Putative alpha-1,3-mannosyltransferase MNN14"
FT                   /id="PRO_0000424327"
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..685
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        199
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        338
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        408
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        556
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   685 AA;  79713 MW;  31E3D6D9A900C5E7 CRC64;
     MGLLSIPYQS KSKLWIAIFL VVWSLISMHF IWQSQANSGL ILKNELSSTS SIPHEFEMLI
     DTNYPKFKPT SGHSGSQTYS NLFKNQDRNA AIFTILKNFD LEQRCQLYFK NVKNDKLIVD
     PDHDFKFDRF DYLNWDEYRD ESIKRLKGDN DEFVATSSDL DTIKKNFDKA KSRIASDLQL
     LHDYFSHIKI YNQCYIDRNT SFIKKQHELI DGLNWKTSFK RSSFLSGKQI VTEQQMYPWL
     SQKSPEYNCL ATGQTTKFAA NKNSFLNTLK NNLNGKGIVM TIADAHIDYC IRLIHLLRYL
     KNTLPIQIIY TSNDLSAESK SQLHQASVSD FDGLPQQNIT LVNVTPAIKP QYLHKFNEFG
     NKILAILFNT FEEMIFIDAD AILIENPEKF FQLTKYKNSG ALFFRDRNTS EYRPDHDIEM
     FLKLMNSQYD EIIFGLLQIT EKTMSIPLFD RKISHVMESG LVLLNRKVHF SQPLIMANMN
     FFEPIRERVY GDKEMFWLSL SIIGDENYQF NSHPAAAIGQ LTTYQERVKT FENPPSSFKS
     QEICANHPAH ISDEDNHTLL WFNSGFQFCN QLEKVNYEDE FSHKERYSQF DTIDKFKTFW
     QSSLVIESAI IPPENTNSNG GDGYEPSVSW KHMEPYCAGY TWCAYSSIGN GDQANDRGLV
     INYSPEEIEH FKKLGEIWMR GYNYL