PMT2_CANAL
ID PMT2_CANAL Reviewed; 769 AA.
AC Q5ADM9; A0A1D8PKL8;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Dolichyl-phosphate-mannose--protein mannosyltransferase 2 {ECO:0000305};
DE Short=Protein mannosyltransferase 2;
DE EC=2.4.1.109 {ECO:0000250|UniProtKB:P33775, ECO:0000303|PubMed:15659169};
GN Name=PMT2 {ECO:0000303|PubMed:15659169};
GN OrderedLocusNames=CAALFM_C306890WA; ORFNames=CaO19.14104, CaO19.6812;
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=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 [5]
RP IDENTIFICATION, DISRUPTION PHENOTYPE, AND INDUCTION.
RX PubMed=15659169; DOI=10.1111/j.1365-2958.2004.04401.x;
RA Prill S.K., Klinkert B., Timpel C., Gale C.A., Schroppel K., Ernst J.F.;
RT "PMT family of Candida albicans: five protein mannosyltransferase isoforms
RT affect growth, morphogenesis and antifungal resistance.";
RL Mol. Microbiol. 55:546-560(2005).
RN [6]
RP INDUCTION.
RX PubMed=16455273; DOI=10.1016/j.fgb.2005.12.002;
RA Castillo L., Martinez A.I., Garcera A., Garcia-Martinez J.,
RA Ruiz-Herrera J., Valentin E., Sentandreu R.;
RT "Genomic response programs of Candida albicans following protoplasting and
RT regeneration.";
RL Fungal Genet. Biol. 43:124-134(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=16534748; DOI=10.1002/pmic.200500465;
RA Insenser M., Nombela C., Molero G., Gil C.;
RT "Proteomic analysis of detergent-resistant membranes from Candida
RT albicans.";
RL Proteomics 6:S74-81(2006).
RN [8]
RP INDUCTION.
RX PubMed=21375589; DOI=10.1111/j.1365-2958.2011.07604.x;
RA Cantero P.D., Ernst J.F.;
RT "Damage to the glycoshield activates PMT-directed O-mannosylation via the
RT Msb2-Cek1 pathway in Candida albicans.";
RL Mol. Microbiol. 80:715-725(2011).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=22662216; DOI=10.1371/journal.pone.0037768;
RA Wang L., Jia Y., Tang R.J., Xu Z., Cao Y.B., Jia X.M., Jiang Y.Y.;
RT "Proteomic analysis of Rta2p-dependent raft-association of detergent-
RT resistant membranes in Candida albicans.";
RL PLoS ONE 7:E37768-E37768(2012).
CC -!- FUNCTION: Protein mannosyltransferase (PMT) involved in hyphal growth
CC and drug sensitivity. Transfers mannose from Dol-P-mannose to Ser or
CC Thr residues on proteins. PMT1, PMT2 and PMT4 account for most of the
CC protein-O-glycosylation activity, while PMT5 and PMT6 may specifically
CC modulate a much narrower spectrum of target proteins. Essential protein
CC that plays an important role in virulence.
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, ECO:0000303|PubMed:15659169};
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, ECO:0000303|PubMed:15659169};
CC -!- PATHWAY: Protein modification; protein glycosylation. {ECO:0000305}.
CC -!- SUBUNIT: PMT1 and PMT2 form a functional heterodimer.
CC {ECO:0000250|UniProtKB:P31382}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P31382}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Associates with lipid rafts in a RTA2-dependent
CC manner. {ECO:0000269|PubMed:16534748, ECO:0000269|PubMed:22662216}.
CC -!- INDUCTION: Transcribed in the yeast form, but expression is increased
CC two to threefold during hyphal induction. Also induced during cell wall
CC regeneration. Up-regulated more than twofold when PMT1 expression is
CC impaired. MSB2 functions not only to secure basal levels of the PMT2
CC transcripts but is needed also for up-regulation of both transcripts
CC upon PMT1 inhibition. {ECO:0000269|PubMed:15659169,
CC ECO:0000269|PubMed:16455273, ECO:0000269|PubMed:21375589}.
CC -!- DISRUPTION PHENOTYPE: Disruption of both alleles leads to letality.
CC Disruption of only one allele impairs filamentation and leads to an
CC altered cell wall composition with reduced amounts of beta-1,6-glucan
CC and shows reduced virulence in a mouse model of hematogenously
CC disseminated candidiasis (HDC) and using reconstituted human epithelium
CC (RHE). {ECO:0000269|PubMed:15659169, ECO:0000269|PubMed:16040968}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 39 family.
CC {ECO:0000305}.
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DR EMBL; CP017625; AOW28694.1; -; Genomic_DNA.
DR RefSeq; XP_719907.1; XM_714814.1.
DR AlphaFoldDB; Q5ADM9; -.
DR SMR; Q5ADM9; -.
DR STRING; 237561.Q5ADM9; -.
DR PRIDE; Q5ADM9; -.
DR GeneID; 3638538; -.
DR KEGG; cal:CAALFM_C306890WA; -.
DR CGD; CAL0000187219; PMT2.
DR VEuPathDB; FungiDB:C3_06890W_A; -.
DR eggNOG; KOG3359; Eukaryota.
DR HOGENOM; CLU_008438_5_0_1; -.
DR InParanoid; Q5ADM9; -.
DR OMA; DANDVWR; -.
DR OrthoDB; 203029at2759; -.
DR BRENDA; 2.4.1.109; 1096.
DR UniPathway; UPA00378; -.
DR PHI-base; PHI:454; -.
DR PRO; PR:Q5ADM9; -.
DR Proteomes; UP000000559; Chromosome 3.
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:0016020; C:membrane; IDA:CGD.
DR GO; GO:0005886; C:plasma membrane; IDA:CGD.
DR GO; GO:0004169; F:dolichyl-phosphate-mannose-protein mannosyltransferase activity; IBA:GO_Central.
DR GO; GO:0036178; P:filamentous growth of a population of unicellular organisms in response to neutral pH; 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 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Membrane;
KW Reference proteome; Repeat; Transferase; Transmembrane;
KW Transmembrane helix; Virulence.
FT CHAIN 1..769
FT /note="Dolichyl-phosphate-mannose--protein
FT mannosyltransferase 2"
FT /id="PRO_0000430577"
FT TRANSMEM 59..79
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..169
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..194
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..218
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..272
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..308
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TRANSMEM 615..635
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TRANSMEM 655..675
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TRANSMEM 679..699
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TRANSMEM 718..738
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT DOMAIN 342..397
FT /note="MIR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 412..468
FT /note="MIR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 474..534
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..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 8
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 408
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"
FT CARBOHYD 462
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 769 AA; 88372 MW; 4E847200A44585C0 CRC64;
MSTSVEPNET EALLRKQNDL STTASIEEKY PHQQGEAAED DDDTLKRTQY DEAKETAESL
KQVESILAPI VFTALSFFVR FYRISVNDHV VWDEAHFGKF GSYYLRHEFY HDVHPPLGKM
LVGLSGYLAG YNGSWDFPSG EKYPDYIDYT KMRLFNATFS ALCVPLAYFT GKEVGFSMFT
TWLFTLMVAL ESSYVTLGKF ILLDSMLLFF TVATVFCFSR FNNFNNKSQE FSRKWWKWIL
LTGVSIGCTC SVKMVGLFVT TLVGIYTVVD LWNKLSDKSI SWTKYIQHWF ARIVALILVP
IFIFMLSFKV HFDLLYKSGT GDANMSSLFQ ANLAGSDVGG GPREVSMFHS VITLKNQGLS
GGLLHSHVQT FPEGSKQQQV TTYGHKDSNN NWIFQRARGQ PYYDTSGNTT DIEYIFDGMH
VRLMHPQTGR NLHTHDIPAP VSKSEYEVAC YGNLTIGDPK DNWTVEIMEQ ASDEDKMRLH
PLTSSFRLKN EVMNCYLGVT GTTLPQWGFR QGEVVCYKNP FKKDKRTWWN IENNRNAVLP
PAPEDFKLPK TKFIRDFIQL NLAMMATNNA LVPDTEKQDD LASSFWQWPT LNVGIRMCGW
GPENPKYYMI GSPATTWTST VGVILFAFIV LYYLIRWQRQ YVDFPSTNPH KLKLFLMGGI
YPMFGWGLHF LPFAIMGRVT YVHHYVPALY FAMLVFCYEV ESFSSRLNKP NASPVSKLLY
LAIYIGLLSL VAGTFWYFRY LSWGMEGPKE DWKHLKLLES WRVSDDQYT
