ID A7TPV8_VANPO Unreviewed; 753 AA.
AC A7TPV8;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 03-MAY-2023, entry version 70.
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=Kpol_1000p18 {ECO:0000313|EMBL:EDO15706.1};
OS Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX NCBI_TaxID=436907 {ECO:0000313|Proteomes:UP000000267};
RN [1] {ECO:0000313|EMBL:EDO15706.1, ECO:0000313|Proteomes:UP000000267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 /
RC NRRL Y-8283 / UCD 57-17 {ECO:0000313|Proteomes:UP000000267};
RX PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT species descended from a whole-genome duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
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; DS480448; EDO15706.1; -; Genomic_DNA.
DR RefSeq; XP_001643564.1; XM_001643514.1.
DR AlphaFoldDB; A7TPV8; -.
DR STRING; 436907.A7TPV8; -.
DR GeneID; 5543796; -.
DR KEGG; vpo:Kpol_1000p18; -.
DR eggNOG; KOG3359; Eukaryota.
DR HOGENOM; CLU_008438_0_0_1; -.
DR InParanoid; A7TPV8; -.
DR OMA; NCHLNAP; -.
DR OrthoDB; 5489060at2759; -.
DR PhylomeDB; A7TPV8; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000000267; 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:SF51; PROTEIN O-MANNOSYL-TRANSFERASE 1; 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:UP000000267};
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 135..153
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 218..235
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 280..301
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 594..615
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 636..653
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 665..684
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 705..729
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT DOMAIN 327..387
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
FT DOMAIN 395..454
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
FT DOMAIN 461..517
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
SQ SEQUENCE 753 AA; 86979 MW; 5C9B9F612EFDBC84 CRC64;
MAGVMKKRVT SKVDVDEPGN KYSKGAEKYQ FLAERWLTSP LPDKEEVYKF WLYIVTGIAF
VTRFYKIWYP KEVVFDEVHF GKFASYYLER TYYFDVHPPF AKMLIAFVGW LSGYDGAFKF
DDIGLSYKKN PAPYIAYRSL NAILGTLTIP LMFNTMKELN FKAITCAFAS LLVAVDNAHV
TETRLILLDA TLVISIAASI YCYVKFYKVQ LTAPFSHAWY IWLYLTGLSL SFVISSKYVG
VMTYAAIGTA VVVNLWQLLD IRAGLSLANF ARHFIRRLSG LVFAPFVVYL FWFWCHFAIL
VNSGPGDPFM SQDFQETLLE SPLAKESKQV QYYDIVTIKH RDTDAFLHSH DAFYPLRYDD
GRVSSQGQQV TGYSHDDINN QWEILPVKEL ASKNGHPVLQ GEQIRLRHVQ SNTYLLTHDV
ASPLYPTNEE VTTVSEEIAN GENYKETLFT FQNLNKNDVN KQIKTKGTNF RIFHVDTSVA
LWTHNDELLP EWAFSQQEVN GNKKVTESSN NWFIDTIVNI DEARLKHIPK KTGTLPFLTK
WLELQRLMFE HNNKLSSEHP FASQPYSWPG SLSGVSFWTK DDERKQIYFI GNIIGWWFQV
VSLAAFIGIV IADMLTRQRG YFALNSITRE KLYGPVMYLF VGWACHYFPF YLMGRQKFLH
HYLPAHLIAS LFSAAIWEII FSDTKSIDVH KDEKNDDVPE IKTKYYTIFL AVVSFAVIAF
FIYFAPFVYG DVSLTPEQVA QRKWLNMELH FAK
//
