OCH1_CANAL
ID OCH1_CANAL Reviewed; 385 AA.
AC Q5A4E3; A0A1D8PKE6;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Initiation-specific alpha-1,6-mannosyltransferase {ECO:0000305};
DE EC=2.4.1.232 {ECO:0000250|UniProtKB:P31755};
DE AltName: Full=Outer chain elongation protein 1 {ECO:0000250|UniProtKB:P31755};
GN Name=OCH1 {ECO:0000303|PubMed:16263704};
GN OrderedLocusNames=CAALFM_C306090CA; ORFNames=CaO19.7391;
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 DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=16263704; DOI=10.1074/jbc.m510360200;
RA Bates S., Hughes H.B., Munro C.A., Thomas W.P., MacCallum D.M., Bertram G.,
RA Atrih A., Ferguson M.A., Brown A.J., Odds F.C., Gow N.A.;
RT "Outer chain N-glycans are required for cell wall integrity and virulence
RT of Candida albicans.";
RL J. Biol. Chem. 281:90-98(2006).
RN [5]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=16710478; DOI=10.1172/jci27114;
RA Netea M.G., Gow N.A., Munro C.A., Bates S., Collins C., Ferwerda G.,
RA Hobson R.P., Bertram G., Hughes H.B., Jansen T., Jacobs L., Buurman E.T.,
RA Gijzen K., Williams D.L., Torensma R., McKinnon A., MacCallum D.M.,
RA Odds F.C., Van der Meer J.W., Brown A.J., Kullberg B.J.;
RT "Immune sensing of Candida albicans requires cooperative recognition of
RT mannans and glucans by lectin and Toll-like receptors.";
RL J. Clin. Invest. 116:1642-1650(2006).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=16855023; DOI=10.1091/mbc.e06-02-0143;
RA Rida P.C., Nishikawa A., Won G.Y., Dean N.;
RT "Yeast-to-hyphal transition triggers formin-dependent Golgi localization to
RT the growing tip in Candida albicans.";
RL Mol. Biol. Cell 17:4364-4378(2006).
RN [7]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=18644880; DOI=10.1128/iai.00368-08;
RA Fradin C., Slomianny M.C., Mille C., Masset A., Robert R., Sendid B.,
RA Ernst J.F., Michalski J.C., Poulain D.;
RT "Beta-1,2 oligomannose adhesin epitopes are widely distributed over the
RT different families of Candida albicans cell wall mannoproteins and are
RT associated through both N- and O-glycosylation processes.";
RL Infect. Immun. 76:4509-4517(2008).
RN [8]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=19222370; DOI=10.1086/597274;
RA van de Veerdonk F.L., Joosten L.A., Devesa I., Mora-Montes H.M.,
RA Kanneganti T.D., Dinarello C.A., van der Meer J.W., Gow N.A.,
RA Kullberg B.J., Netea M.G.;
RT "Bypassing pathogen-induced inflammasome activation for the regulation of
RT interleukin-1beta production by the fungal pathogen Candida albicans.";
RL J. Infect. Dis. 199:1087-1096(2009).
RN [9]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=21254968; DOI=10.3109/13693786.2010.551425;
RA Sheth C.C., Hall R., Lewis L., Brown A.J., Odds F.C., Erwig L.P., Gow N.A.;
RT "Glycosylation status of the C. albicans cell wall affects the efficiency
RT of neutrophil phagocytosis and killing but not cytokine signaling.";
RL Med. Mycol. 49:513-524(2011).
RN [10]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=23608318; DOI=10.1016/j.fgb.2013.03.009;
RA Shahana S., Mora-Montes H.M., Castillo L., Bohovych I., Sheth C.C.,
RA Odds F.C., Gow N.A., Brown A.J.;
RT "Reporters for the analysis of N-glycosylation in Candida albicans.";
RL Fungal Genet. Biol. 56:107-115(2013).
CC -!- FUNCTION: Mannosyltransferase involved in outer chain elongation of
CC asparagine-linked oligosaccharides of the type Man(9)GlcNAc(2). Adds
CC the first alpha-1,6-mannose to the Man(8)GlcNAc(2) and Man(9)GlcNAc(2),
CC but not Man(5)GlcNAc(2), endoplasmic reticulum intermediates (By
CC similarity). Represents the first enzymatic event required for
CC synthesis of outer chain mannose linkages on yeast secretory proteins.
CC N-glycan outer chain epitopes play a crucial role in the host-fungal
CC interaction, virulence, and host immune response such as interleukin
CC synthesis or phagocytosis by neutrophils.
CC {ECO:0000250|UniProtKB:P31755, ECO:0000269|PubMed:16263704,
CC ECO:0000269|PubMed:16710478, ECO:0000269|PubMed:18644880,
CC ECO:0000269|PubMed:19222370, ECO:0000269|PubMed:21254968,
CC ECO:0000269|PubMed:23608318}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Transfers an alpha-D-mannosyl residue from GDP-mannose into
CC lipid-linked oligosaccharide, forming an alpha-(1->6)-D-mannosyl-D-
CC mannose linkage.; EC=2.4.1.232;
CC Evidence={ECO:0000250|UniProtKB:P31755};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P31755};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P31755}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:P31755}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:16855023}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:P31755}. Note=Is recycled between the trans-
CC Golgi network and a late compartment of the endoplasmic reticulum.
CC {ECO:0000250|UniProtKB:P31755}.
CC -!- DOMAIN: The conserved DXD motif is involved in enzyme activity.
CC {ECO:0000250|UniProtKB:P31755}.
CC -!- DISRUPTION PHENOTYPE: Results in a temperature-sensitive growth defect,
CC cellular aggregation, loss of outer chain elongation of N-glycans,
CC hypersensitivity to a range of cell wall perturbing agents, as well as
CC to constitutively activated cell wall integrity pathway. Finally, leads
CC to attenuated virulence in a mouse model of systemic infection and
CC affects inflammatory response and the efficiency of neutrophil
CC phagocytosis by the host. {ECO:0000269|PubMed:16263704,
CC ECO:0000269|PubMed:16710478, ECO:0000269|PubMed:18644880,
CC ECO:0000269|PubMed:19222370, ECO:0000269|PubMed:21254968,
CC ECO:0000269|PubMed:23608318}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 32 family.
CC {ECO:0000305}.
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DR EMBL; CP017625; AOW28617.1; -; Genomic_DNA.
DR RefSeq; XP_716632.1; XM_711539.1.
DR AlphaFoldDB; Q5A4E3; -.
DR BioGRID; 1224845; 2.
DR STRING; 237561.Q5A4E3; -.
DR GeneID; 3641751; -.
DR KEGG; cal:CAALFM_C306090CA; -.
DR CGD; CAL0000174808; OCH1.
DR VEuPathDB; FungiDB:C3_06090C_A; -.
DR eggNOG; ENOG502QW2I; Eukaryota.
DR HOGENOM; CLU_022381_5_0_1; -.
DR InParanoid; Q5A4E3; -.
DR OMA; AFVKHNF; -.
DR OrthoDB; 1507715at2759; -.
DR Proteomes; UP000000559; Chromosome 3.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:CGD.
DR GO; GO:0000136; C:mannan polymerase complex; IBA:GO_Central.
DR GO; GO:0000009; F:alpha-1,6-mannosyltransferase activity; IBA:GO_Central.
DR GO; GO:0033164; F:glycolipid 1,6-alpha-mannosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0034605; P:cellular response to heat; IMP:CGD.
DR GO; GO:0009267; P:cellular response to starvation; IMP:CGD.
DR GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR GO; GO:0036170; P:filamentous growth of a population of unicellular organisms in response to starvation; IMP:CGD.
DR GO; GO:0006491; P:N-glycan processing; IMP:CGD.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR InterPro; IPR007577; GlycoTrfase_DXD_sugar-bd_CS.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR039367; Och1-like.
DR PANTHER; PTHR31834; PTHR31834; 1.
DR Pfam; PF04488; Gly_transf_sug; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Glycosyltransferase; Golgi apparatus; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix; Virulence.
FT CHAIN 1..385
FT /note="Initiation-specific alpha-1,6-mannosyltransferase"
FT /id="PRO_0000430618"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P31755"
FT TRANSMEM 16..36
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..385
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P31755"
FT MOTIF 189..191
FT /note="DXD motif"
FT /evidence="ECO:0000250|UniProtKB:P31755"
SQ SEQUENCE 385 AA; 44828 MW; BD0616E650AB1700 CRC64;
MLQLREPQMV HKHLKLAVLG IVVIFTTYFI ISSLSSPTST HKTEYNSPKL QLAKELELNS
NWKELGLNFQ PNKKYSLPDE STLRQQLSYQ FPYDESKPFP KNIWQTWKVG IDEKSFPKRY
LKYQQTWEDK NPDYKHYVVP DKQCDLLIEQ LYSQVPDVAK AYRIMPKSIL KADFFRYLIL
FARGGVYTDI DTVGLKPVDE WISNSEMILE KKNRSGLVVG IEADPDRPDW ADWYARRIQF
CQWTIQSKRG HPMLRELIAK ITDITLTRHK KGQLKKVLGK NEGGDIMNWT GPGIFTDTVF
EYMNNILQSP EVFKNKKKWA TIIDWKLFTG MEQPIAIDDV LVLPITSFSP DVNQMGAKDS
HDPMAYAKHM FSGSWKDDGM PEMEQ
