MNN1_CANAL
ID MNN1_CANAL Reviewed; 800 AA.
AC Q5AGA0; A0A1D8PNH6; Q5AGN6;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Putative alpha-1,3-mannosyltransferase MNN1;
DE EC=2.4.1.-;
GN Name=MNN1; OrderedLocusNames=CAALFM_C502630CA;
GN ORFNames=CaO19.11755, CaO19.4279;
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=12912891; DOI=10.1128/ec.2.4.718-728.2003;
RA Ramon A.M., Fonzi W.A.;
RT "Diverged binding specificity of Rim101p, the Candida albicans ortholog of
RT PacC.";
RL Eukaryot. Cell 2:718-728(2003).
RN [5]
RP INDUCTION.
RX PubMed=14734021; DOI=10.1016/s1567-1356(03)00201-0;
RA Kruppa M., Jabra-Rizk M.A., Meiller T.F., Calderone R.;
RT "The histidine kinases of Candida albicans: regulation of cell wall mannan
RT biosynthesis.";
RL FEMS Yeast Res. 4:409-416(2004).
RN [6]
RP INDUCTION.
RX PubMed=18799621; DOI=10.1091/mbc.e08-05-0479;
RA Alvarez F.J., Douglas L.M., Rosebrock A., Konopka J.B.;
RT "The Sur7 protein regulates plasma membrane organization and prevents
RT intracellular cell wall growth in Candida albicans.";
RL Mol. Biol. Cell 19:5214-5225(2008).
RN [7]
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 -!- INDUCTION: Expression is negatively regulated by RIM101. Expression is
CC also increased in absence of SUR7, as well as CHK1 and NIK1.
CC {ECO:0000269|PubMed:12912891, ECO:0000269|PubMed:14734021,
CC ECO:0000269|PubMed:18799621}.
CC -!- SIMILARITY: Belongs to the MNN1/MNT family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP017627; AOW29688.1; -; Genomic_DNA.
DR RefSeq; XP_720587.1; XM_715494.1.
DR AlphaFoldDB; Q5AGA0; -.
DR STRING; 237561.Q5AGA0; -.
DR GeneID; 3637784; -.
DR KEGG; cal:CAALFM_C502630CA; -.
DR CGD; CAL0000201916; MNN1.
DR VEuPathDB; FungiDB:C5_02630C_A; -.
DR eggNOG; ENOG502RZ48; Eukaryota.
DR HOGENOM; CLU_015387_0_0_1; -.
DR InParanoid; Q5AGA0; -.
DR OrthoDB; 527450at2759; -.
DR UniPathway; UPA00378; -.
DR PHI-base; PHI:3690; -.
DR PRO; PR:Q5AGA0; -.
DR Proteomes; UP000000559; Chromosome 5.
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 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.
FT CHAIN 1..800
FT /note="Putative alpha-1,3-mannosyltransferase MNN1"
FT /id="PRO_0000424324"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..800
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 545
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 656
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 767
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 800 AA; 94231 MW; 765ADFB93BB42B8C CRC64;
MIQKLIKNRQ RSKWVLFTGA SLWIFFILDF MNSNYYNTES HISSYSIYNV YDNLHEETES
PPKSALSSSL LEPSTNQQTS DFKNHLLYKS LISSLFQNTT KQTKDLNSNI YDDIFSNHKL
ETVLGTLSFK ERCDLYFKNV FAEDVNWHFN PDTRYDMHFD KNTKEFKDFI KVKELVIQEK
FDKMKEKFKE EDYNRELSKL KKSMFTDFLN EKFEQEIVNR LSTFRIFNKC YITNDETPQI
NKINQFITNQ QKLVQDIHRD ESGNFYKSKI DKLKLTNKEA LVDLMVTKSS TFEHRVYPWI
SKEYPVYERW TGKVYHEPPN YYEILNHDPM QKTPKKIQQS NNAAQPFLKQ FKNKFNGRGI
VLTIGNQHSD YAVSLIHLLR ALDNKLPIQI VYYDDVNEES KRKIVTAAQE DFRSLPHSFE
KVAHLFGDKY INSQGKGLQP QEVWFVNAYN SIHKNYRGKF SRFGNKLLAS LFNSFSEFML
IDVDTVLMQP PEYFFQLKNY QTTGTYFFKD RSVLQRRTVE DGKFFERMGP STVDQMMFDI
PIMTNYTTTR ELFRGLQHYM ESGLVMINKD KHLNSILMIT QINLIGPITG KVWGDKELFW
LGFAINGDEE YYFDDNFAAA IGELTPPQDR ARKDGTWHHS KEICSPHPGH VSGDDNHSLL
WINSGFRFCH QADEVNFEKE AKKKTRLKHL HTADQFRTFY YNPLRITHAV VPPLDQDLQD
RKNAMDEPTS GWLWESGYCK RYMWCAYSSV GGPQKRPDEK DDTVDNNETK DNTLDGILVE
YNQDEIALFN YLGDIWVGTE
