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Database: UniProt
Entry: A0A0L7R9R8_9HYME
LinkDB: A0A0L7R9R8_9HYME
Original site: A0A0L7R9R8_9HYME 
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
//
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