PMT5_CANAL
ID PMT5_CANAL Reviewed; 725 AA.
AC Q5ACU3; A0A1D8PU16;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Dolichyl-phosphate-mannose--protein mannosyltransferase 5 {ECO:0000305};
DE Short=Protein mannosyltransferase 5;
DE EC=2.4.1.109 {ECO:0000250|UniProtKB:P33775, ECO:0000303|PubMed:15659169};
GN Name=PMT5 {ECO:0000303|PubMed:15659169};
GN OrderedLocusNames=CAALFM_CR09770CA; ORFNames=CaO19.7549;
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, INDUCTION, DISRUPTION PHENOTYPE, AND FUNCTION.
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).
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. {ECO:0000269|PubMed:16040968,
CC ECO:0000303|PubMed:15659169}.
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 -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P33775}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- INDUCTION: Expressed at very low levels. {ECO:0000269|PubMed:15659169}.
CC -!- DISRUPTION PHENOTYPE: Shows altered cell wall composition with a
CC significant decrease in wall mannoproteins, and reduced virulence in a
CC mouse model of hematogenously disseminated candidiasis (HDC) and using
CC reconstituted human epithelium (RHE). {ECO:0000269|PubMed:15659169,
CC ECO:0000269|PubMed:16040968}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 39 family.
CC {ECO:0000305}.
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DR EMBL; CP017630; AOW31634.1; -; Genomic_DNA.
DR RefSeq; XP_719311.1; XM_714218.1.
DR AlphaFoldDB; Q5ACU3; -.
DR SMR; Q5ACU3; -.
DR BioGRID; 1222105; 2.
DR STRING; 237561.Q5ACU3; -.
DR GeneID; 3639011; -.
DR KEGG; cal:CAALFM_CR09770CA; -.
DR CGD; CAL0000185574; PMT5.
DR VEuPathDB; FungiDB:CR_09770C_A; -.
DR eggNOG; KOG3359; Eukaryota.
DR HOGENOM; CLU_008438_2_1_1; -.
DR InParanoid; Q5ACU3; -.
DR OMA; IPNTLWY; -.
DR OrthoDB; 203029at2759; -.
DR BRENDA; 2.4.1.109; 1096.
DR UniPathway; UPA00378; -.
DR PHI-base; PHI:453; -.
DR Proteomes; UP000000559; Chromosome R.
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:0005886; C:plasma membrane; IDA:CGD.
DR GO; GO:0004169; F:dolichyl-phosphate-mannose-protein mannosyltransferase activity; IBA:GO_Central.
DR GO; GO:0035269; P:protein O-linked mannosylation; IBA:GO_Central.
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; IPR027004; PMT1/PTM5.
DR InterPro; IPR032421; PMT_4TMC.
DR PANTHER; PTHR10050; PTHR10050; 1.
DR PANTHER; PTHR10050:SF50; PTHR10050:SF50; 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..725
FT /note="Dolichyl-phosphate-mannose--protein
FT mannosyltransferase 5"
FT /id="PRO_0000430575"
FT TRANSMEM 34..54
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..212
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..276
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TRANSMEM 570..590
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TRANSMEM 619..639
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TRANSMEM 644..664
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TRANSMEM 673..693
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT DOMAIN 303..356
FT /note="MIR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 368..427
FT /note="MIR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 439..495
FT /note="MIR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT CARBOHYD 409
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 725 AA; 84506 MW; DE260F25789203F7 CRC64;
MTKELPSGYF QGPFRPYKTF QPSLTERPLS KFEQFAVFSI LLISLIRLYK LYIPDRVVFD
EIHLIKYIKN YYDGSIFVDI HPPLGKLIYF YITKLFSFDK DFQIDIIGDL YPEDFPYLWL
RLFSGICGIG HVLLTFFTLR ITCNSVISIV ITILICLENS MVTVSRLILL EGPSLFVQSL
VIYNYKAFTT RIPFTGCWYF NLFVTGIALG LNISLKISGL FTFAWVGILT CVQLWEILGD
LRISIWQFIK HLVLRVVAFI MVPLTIYCSV FYIHFENLPN EGPGSGFLTP HFRSTLDDYQ
QQPLQVLYGS TITIKHNALE KYLHSHDLTY PRGSNLQQVT LYDFPDVNNE WVIETKQKYN
EEKLMTDQRE VKDGDVVRLY HKATGHYLHV NDIRPPISEH EYSYEVNGNE TRGLLGNEDY
EFKIRMLVKK PHAENDLPLI KLRTTETIFQ LIHQATRCNL MSHEQKLPDW GEYQNEVLCV
KEPTIPNTLW YVESSSHPLL KDTKKLKTFP KFSFWSKLIE THKVMFNLNK GFTNPHPYAS
KPLDWPLLSR GIAFFSNYNL KSIDEESSLI YYLGNVAIYY SVFFVGLIAI FKCAIYSFIK
LNPYASPPSS SKSSPYANFY NNSWPYLVGW FINYIPYCLM SRNLYLHHYL SALNFGILLL
SQYLNYRVAK NKIIGGIITA TIFVSAIYCF YEFIPITYGL PWTLDQCNSH KWFPNWDIDC
MTYTG
