ID T1GJJ7_MEGSC Unreviewed; 332 AA.
AC T1GJJ7;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Dolichyl-phosphate-mannose--protein mannosyltransferase {ECO:0000256|RuleBase:RU367007};
DE EC=2.4.1.109 {ECO:0000256|RuleBase:RU367007};
OS Megaselia scalaris (Humpbacked fly) (Phora scalaris).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Platypezoidea;
OC Phoridae; Megaseliini; Megaselia.
OX NCBI_TaxID=36166 {ECO:0000313|EnsemblMetazoa:MESCA003646-PA, ECO:0000313|Proteomes:UP000015102};
RN [1] {ECO:0000313|Proteomes:UP000015102}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Durham, NC isolate 2 -- Noor lab
RC {ECO:0000313|Proteomes:UP000015102};
RA Hughes D.;
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:MESCA003646-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) to UniProtKB.
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|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|RuleBase:RU367007};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|RuleBase:RU367007}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|RuleBase:RU367007}; Multi-pass membrane protein
CC {ECO:0000256|RuleBase:RU367007}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 39 family.
CC {ECO:0000256|RuleBase:RU367007}.
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DR EMBL; CAQQ02173422; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; T1GJJ7; -.
DR STRING; 36166.T1GJJ7; -.
DR EnsemblMetazoa; MESCA003646-RA; MESCA003646-PA; MESCA003646.
DR HOGENOM; CLU_837556_0_0_1; -.
DR OMA; INTACDL; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000015102; 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; 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; 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|RuleBase:RU367007};
KW Glycosyltransferase {ECO:0000256|RuleBase:RU367007};
KW Reference proteome {ECO:0000313|Proteomes:UP000015102};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|RuleBase:RU367007}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..332
FT /note="Dolichyl-phosphate-mannose--protein
FT mannosyltransferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004577423"
FT DOMAIN 53..114
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
FT DOMAIN 126..183
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
FT DOMAIN 189..245
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
SQ SEQUENCE 332 AA; 38094 MW; 779FFD13EDF200D6 CRC64;
MVSIRLHTYC NLLAIFYIHL NTLTKAGPHD HVMTSAFQAS LEGGLSSITK GQPVKVTHGS
QVTLRHTYGR PCWLHSHAHV YPVKYPDKRG SSHQQQVTCY SFKDVNNWWI VKKPDANSLV
VNFDDPEPIR HGDVIQLVHG LTMRALNSHD VAAPVTPTCQ EVTCYIDYNI SMKADILWRV
EIANKETGGD EWNAINSHVR LIHLGTKAAL RFTGRQLPAW GFHQHEVAAD KNIVQKDTIW
NVEEHKYTKV DDKKERDRQL HLSEMIPTKK TKFSFLEKFI ELQYKMLTFA DHLSPEEHLY
SSSPLEWPLL DKTIAYWLDN KSNGQIHLVG NM
//
