ID A0A0L7R9R8_9HYME Unreviewed; 711 AA.
AC A0A0L7R9R8;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 13-SEP-2023, entry version 23.
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=WH47_10354 {ECO:0000313|EMBL:KOC67579.1};
OS Habropoda laboriosa.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Habropoda.
OX NCBI_TaxID=597456 {ECO:0000313|EMBL:KOC67579.1, ECO:0000313|Proteomes:UP000053825};
RN [1] {ECO:0000313|EMBL:KOC67579.1, ECO:0000313|Proteomes:UP000053825}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0110345459 {ECO:0000313|EMBL:KOC67579.1};
RA Pan H., Kapheim K.;
RT "The genome of Habropoda laboriosa.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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; KQ414621; KOC67579.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L7R9R8; -.
DR STRING; 597456.A0A0L7R9R8; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000053825; 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; 2.
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 Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU367007};
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:UP000053825};
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 116..137
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 172..205
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 225..248
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 559..580
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 600..618
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 624..645
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 657..677
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT DOMAIN 281..342
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
FT DOMAIN 353..410
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
FT DOMAIN 415..472
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
SQ SEQUENCE 711 AA; 82004 MW; 7B2363CA2C0956D0 CRC64;
MLSNATEKFK IVKESVSDAP RSRIKISLEI DLISVILLVT GLITRLYRLE EPRSIVFDEL
HYGKYVGLYM KRIFFFDSHP PLGKQLISAA AYLAGFNGQF KFDRIGNSYA DIVPLFALRL
VPALCGSLLI PTVYHLILEL GLKQWTAALA GFLLLLGNSL KVMDQPTSLS WWIWLILGIA
NLTCALCVKY VGLYSLVLAL LLIVYDYWKL IPKKSLSNTV LCFHLAIRIF VILSVICTIY
LTVFYIHLTI LSKAGPHDSV MTSAFQASLD GGLASITKGQ PLEVIHGSQI TLRHTYGRAC
WLHSHNHMYP LKYPDGRGSS HQQQVTCYSF KDVNNWWIVK KPERNDLVVT KPSESIKHGD
VIQLIHGITS RALNSHDVAA PMTPQSQEVS CYIDYNVSMP AQNLWRVEIT NKDSTDHVWH
AIQSQIRLIH VNTDYALKFS GRQLSDWGFN QHEVVADKLV DQTDSIWNVE EHRYTKSEDQ
KQRERELINA EMIPLQATTL SFWEKFVELQ IKMFLSGQEG QNSHMYSSDP LDWPLMSRGI
AYWVSNDSNA QVHLLGNIAI WYSGTVCVII YTFLLIFYML RRRRMCFDIA HEEWNKFSNI
GSILLTGYLL HFLPFIFVER TLFLHHYLPA FVFKLLLTSA TIEHLHYLIG NRYKHNFLMY
ILKFSTVIWM IFIIYVFKKF AVLSYGTTHL SAKEVLKLRW RDTWDFIIHK T
//