ID A0A1E3QHM0_LIPST Unreviewed; 749 AA.
AC A0A1E3QHM0;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 03-MAY-2023, entry version 20.
DE RecName: Full=Dolichyl-phosphate-mannose--protein mannosyltransferase {ECO:0000256|ARBA:ARBA00012839, ECO:0000256|RuleBase:RU367007};
DE EC=2.4.1.109 {ECO:0000256|ARBA:ARBA00012839, ECO:0000256|RuleBase:RU367007};
GN ORFNames=LIPSTDRAFT_67537 {ECO:0000313|EMBL:ODQ76592.1};
OS Lipomyces starkeyi NRRL Y-11557.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Lipomycetaceae; Lipomyces.
OX NCBI_TaxID=675824 {ECO:0000313|EMBL:ODQ76592.1, ECO:0000313|Proteomes:UP000094385};
RN [1] {ECO:0000313|EMBL:ODQ76592.1, ECO:0000313|Proteomes:UP000094385}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-11557 {ECO:0000313|EMBL:ODQ76592.1,
RC ECO:0000313|Proteomes:UP000094385};
RX PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
CC -!- FUNCTION: Transfers mannose from Dol-P-mannose to Ser or Thr residues
CC on proteins. {ECO:0000256|RuleBase:RU367007}.
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:0000256|ARBA:ARBA00034032,
CC ECO:0000256|RuleBase:RU367007};
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:0000256|ARBA:ARBA00033990,
CC ECO:0000256|RuleBase:RU367007};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922, ECO:0000256|RuleBase:RU367007}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU367007}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004477,
CC ECO:0000256|RuleBase:RU367007}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 39 family.
CC {ECO:0000256|ARBA:ARBA00007222, ECO:0000256|RuleBase:RU367007}.
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DR EMBL; KV454289; ODQ76592.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E3QHM0; -.
DR STRING; 675824.A0A1E3QHM0; -.
DR OrthoDB; 5489060at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000094385; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004169; F:dolichyl-phosphate-mannose-protein mannosyltransferase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 2.80.10.50; -; 1.
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; DOLICHYL-PHOSPHATE-MANNOSE--PROTEIN MANNOSYLTRANSFERASE; 1.
DR PANTHER; PTHR10050:SF50; DOLICHYL-PHOSPHATE-MANNOSE--PROTEIN MANNOSYLTRANSFERASE 1-RELATED; 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; MIR domain; 1.
DR PROSITE; PS50919; MIR; 3.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU367007};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU367007};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367007};
KW Reference proteome {ECO:0000313|Proteomes:UP000094385};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU367007};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU367007};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU367007}.
FT TRANSMEM 102..121
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 128..146
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 152..171
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 183..202
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 237..261
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 555..576
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 620..641
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 653..675
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT DOMAIN 290..344
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
FT DOMAIN 356..415
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
FT DOMAIN 425..481
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
FT REGION 726..749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 749 AA; 84771 MW; A8E0C68DD08D27F5 CRC64;
MASTSTKFST LPPKDKAAIL SITGLAVLVR LYKIWQPSSV VFDEVHFGGF ASKYIKGRYF
MDVHPPLAKL LITLAGYLAG YDGNFDFKDI GKDYIEDGVP YVAMRLLPAT LGVLVIPLSF
LTLKAYGCTS LTASLGALLV LFENALTTQS RFILLDSPLV FFTALTAYAW SNFQNQPAFQ
SSWYWYLFLT GLSLGATVSV KWVGLFTIAW VGVTTISGLW QLLGDLAVTP KQYAKHFFWR
AVFLIVVPII FYMLMFGIHF ICLVNPGDGD GFMSSEFQAT FNNKKMADTP ADVAFGSHIT
IRHWNTQGGY LHSHDHLYPG GSKQQQVTLY PHKDDNNLWL VENSTEVEVE ARALPPVYLK
DGDVIKLQHV KTYRRLHSHD LRPPVTEADW QNEVSAYGYK GFAGDANDNF RIEILESKSK
PGKAQEYVRA IETKFRLIHT ITGCALFSHK VKLPSWAFEQ QEVTCSKQGT LPNSIWYIEY
NEHPTLPADA EKINYPKVGF FKKFAELQKV MWETNAGLIA AHNWDSRPEA WPYLRRGINF
WIKDQRQVYL IGNVFVWWLS TAGLVIYVLF KIMTIIRWQR GYNDYSLPSV QAFNGKVGTN
VVAWALHYFP FYLMKRQLFL HHYLPALYFA ILAVVVAWDL FCKNVLRQKA ITTVATIGLL
AIAVYIFVTL SPLAYGEPWT KDECENARLM KHWDFECNTF PTDMSSYDAS TIANVSSVNG
SIVGERSTAS SFQSPEDLSG EEAPPRDEL
//
