PMT6_CANAL
ID PMT6_CANAL Reviewed; 832 AA.
AC Q5A688; A0A1D8PM65;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Dolichyl-phosphate-mannose--protein mannosyltransferase 6 {ECO:0000305};
DE Short=Protein mannosyltransferase 6;
DE EC=2.4.1.109 {ECO:0000250|UniProtKB:P33775};
GN Name=PMT6; Synonyms=PMT3; OrderedLocusNames=CAALFM_C404780WA;
GN ORFNames=CaO19.11283, CaO19.3802;
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=10809683; DOI=10.1128/jb.182.11.3063-3071.2000;
RA Timpel C., Zink S., Strahl-Bolsinger S., Schroppel K., Ernst J.;
RT "Morphogenesis, adhesive properties, and antifungal resistance depend on
RT the Pmt6 protein mannosyltransferase in the fungal pathogen candida
RT albicans.";
RL J. Bacteriol. 182:3063-3071(2000).
RN [5]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=16040968; DOI=10.1128/iai.73.8.4571-4580.2005;
RA Rouabhia M., Schaller M., Corbucci C., Vecchiarelli A., Prill S.K.,
RA Giasson L., Ernst J.F.;
RT "Virulence of the fungal pathogen Candida albicans requires the five
RT isoforms of protein mannosyltransferases.";
RL Infect. Immun. 73:4571-4580(2005).
RN [6]
RP INDUCTION.
RX PubMed=21592964; DOI=10.1074/jbc.m111.233569;
RA Singh R.P., Prasad H.K., Sinha I., Agarwal N., Natarajan K.;
RT "Cap2-HAP complex is a critical transcriptional regulator that has dual but
RT contrasting roles in regulation of iron homeostasis in Candida albicans.";
RL J. Biol. Chem. 286:25154-25170(2011).
RN [7]
RP INDUCTION.
RX PubMed=23563485; DOI=10.1128/ec.00071-13;
RA Srikantha T., Daniels K.J., Pujol C., Kim E., Soll D.R.;
RT "Identification of genes upregulated by the transcription factor Bcr1 that
RT are involved in impermeability, impenetrability, and drug resistance of
RT Candida albicans a/alpha biofilms.";
RL Eukaryot. Cell 12:875-888(2013).
CC -!- FUNCTION: Protein mannosyltransferase (PMT) involved in hyphal
CC morphogenesis and drug sensitivity. Transfers mannose from Dol-P-
CC mannose to Ser or Thr residues on proteins. PMT1, PMT2 and PMT4 account
CC for most of the protein-O-glycosylation activity, while PMT5 and PMT6
CC may specifically modulate a much narrower spectrum of target proteins.
CC Required for biofilm formation and virulence.
CC {ECO:0000250|UniProtKB:P33775, ECO:0000269|PubMed:10809683,
CC ECO:0000269|PubMed:16040968}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl beta-D-mannosyl phosphate + L-seryl-[protein] = 3-
CC O-(alpha-D-mannosyl)-L-seryl-[protein] + a dolichyl phosphate + H(+);
CC Xref=Rhea:RHEA:17377, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527,
CC Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:13546, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29999, ChEBI:CHEBI:57683, ChEBI:CHEBI:58211,
CC ChEBI:CHEBI:137321; EC=2.4.1.109;
CC Evidence={ECO:0000250|UniProtKB:P33775};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl beta-D-mannosyl phosphate + L-threonyl-[protein] =
CC 3-O-(alpha-D-mannosyl)-L-threonyl-[protein] + a dolichyl phosphate +
CC H(+); Xref=Rhea:RHEA:53396, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527,
CC Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:13547, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30013, ChEBI:CHEBI:57683, ChEBI:CHEBI:58211,
CC ChEBI:CHEBI:137323; EC=2.4.1.109;
CC Evidence={ECO:0000250|UniProtKB:P33775};
CC -!- PATHWAY: Protein modification; protein glycosylation. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P33775}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- INDUCTION: Expression is repressed by HAP4 and BCR1.
CC {ECO:0000269|PubMed:21592964, ECO:0000269|PubMed:23563485}.
CC -!- DISRUPTION PHENOTYPE: Leads to supersensitivity to hygromycin B.
CC Impairs filamentation, significantly reduces adherence to endothelial
CC cells, and shows reduced virulence in a mouse model of hematogenously
CC disseminated candidiasis (HDC) and using reconstituted human epithelium
CC (RHE). {ECO:0000269|PubMed:10809683, ECO:0000269|PubMed:16040968}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 39 family.
CC {ECO:0000305}.
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DR EMBL; CP017626; AOW29221.1; -; Genomic_DNA.
DR RefSeq; XP_717207.1; XM_712114.2.
DR AlphaFoldDB; Q5A688; -.
DR SMR; Q5A688; -.
DR BioGRID; 1224140; 2.
DR STRING; 237561.Q5A688; -.
DR PRIDE; Q5A688; -.
DR GeneID; 3641116; -.
DR KEGG; cal:CAALFM_C404780WA; -.
DR CGD; CAL0000189855; PMT6.
DR VEuPathDB; FungiDB:C4_04780W_A; -.
DR eggNOG; KOG3359; Eukaryota.
DR HOGENOM; CLU_008438_5_0_1; -.
DR InParanoid; Q5A688; -.
DR OrthoDB; 203029at2759; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q5A688; -.
DR Proteomes; UP000000559; Chromosome 4.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004169; F:dolichyl-phosphate-mannose-protein mannosyltransferase activity; IBA:GO_Central.
DR GO; GO:0036244; P:cellular response to neutral pH; 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:0044182; P:filamentous growth of a population of unicellular organisms; IMP:CGD.
DR GO; GO:0036178; P:filamentous growth of a population of unicellular organisms in response to neutral pH; IMP:CGD.
DR GO; GO:0036170; P:filamentous growth of a population of unicellular organisms in response to starvation; IMP:CGD.
DR GO; GO:0035269; P:protein O-linked mannosylation; IBA:GO_Central.
DR GO; GO:0044011; P:single-species biofilm formation on inanimate substrate; IMP:CGD.
DR InterPro; IPR027005; GlyclTrfase_39-like.
DR InterPro; IPR003342; Glyco_trans_39/83.
DR InterPro; IPR036300; MIR_dom_sf.
DR InterPro; IPR016093; MIR_motif.
DR InterPro; IPR032421; PMT_4TMC.
DR PANTHER; PTHR10050; PTHR10050; 1.
DR Pfam; PF02815; MIR; 1.
DR Pfam; PF02366; PMT; 1.
DR Pfam; PF16192; PMT_4TMC; 1.
DR SMART; SM00472; MIR; 3.
DR SUPFAM; SSF82109; SSF82109; 1.
DR PROSITE; PS50919; MIR; 3.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Membrane;
KW Reference proteome; Repeat; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..832
FT /note="Dolichyl-phosphate-mannose--protein
FT mannosyltransferase 6"
FT /id="PRO_0000430576"
FT TRANSMEM 135..155
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..194
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..227
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 232..252
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..311
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..347
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TRANSMEM 676..696
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TRANSMEM 723..743
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TRANSMEM 755..775
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TRANSMEM 787..807
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT DOMAIN 383..437
FT /note="MIR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 466..522
FT /note="MIR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 537..595
FT /note="MIR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 20
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 357
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 453
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 832 AA; 94913 MW; 7F552DB123233DB3 CRC64;
MATGYSTGVS PFDLDENNHN DSIHHRHQNH HSQSHDSSGE RDDTEIEDII QKTSKLNINT
STSTKIKNFF FQSSNRHDSS NSPPLREVFI KTINPLILTA ISSFVRLYRI DVANSVVWDE
AHFGKFGSQY LKRQFYFDVH PPLGKLLIGL SGYLADYDGN FDFESSNVYP DNVNYVFMRI
FNCFFGILVT PLAYKTAVIL GYNQFTCWLI AFMVIFEQLS LTLSKFILLD SMLLFFTVLT
MYCLVKVHTL AIARVGSNSK TPLTKLEIKW YILTGISIGC VCSVKWVGLF VTALVGFYTI
VDLWIKFYQT FAIDKKSPKK MSVVNYLIHW VVRIFTLIII PMTIYVATFK VHFMVLNHTG
PDDGTLSTLL QGSLIGNDLQ SGPRSVAFGS LVTIRSQGLS PNLIHSHPHN YPQGSQEQQV
TTYGFKDDNN EFLFEFGVDA GLRNQHATLE NENSTRNGGN DDDYYHVIIH DGDTVRINHK
NTGSYLRANA VGAPITSSSY EVSCFGDVES NDWADEWVIE IQSQDQSPDP MFQDEDPSEI
HSVSTSFRLK HKQLGCYLAT TGKSYPAWGY QQGEVVCKYS VFSRDKNTWW NIEKHVNNKL
PLPATEYVPP KPKFWKEFIL LNYAMMASNN ALIPDPDRFD KLSSEWWEWP ILNTGLRMNS
WGDADIKYFL LGNPLITWIS TIALIVCPLY LLVVGIKYQR QWILLSATDT SNANPANSQS
LSLLAARALL PLAGWVLHYV PFILMGRVKY LHHYVPALYF AIFVAGFIVD AILNLDFSYH
NNKFQYIFKV VIYSTLYLVI CISFWYFKDL SFGMEGSSVD YRHLRLLGSW MI
