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Database: UniProt
Entry: A0A2A4J5U6_HELVI
LinkDB: A0A2A4J5U6_HELVI
Original site: A0A2A4J5U6_HELVI 
ID   A0A2A4J5U6_HELVI        Unreviewed;       958 AA.
AC   A0A2A4J5U6;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
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=B5V51_7233 {ECO:0000313|EMBL:PCG66793.1};
OS   Heliothis virescens (Tobacco budworm moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC   Noctuidae; Heliothinae; Heliothis.
OX   NCBI_TaxID=7102 {ECO:0000313|EMBL:PCG66793.1, ECO:0000313|Proteomes:UP000218220};
RN   [1] {ECO:0000313|EMBL:PCG66793.1, ECO:0000313|Proteomes:UP000218220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HvINT- {ECO:0000313|EMBL:PCG66793.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:PCG66793.1};
RA   Fritz M.L., Deyonke A.M., Papanicolaou A., Micinski S., Westbrook J.,
RA   Gould F.;
RT   "Contemporary evolution of a Lepidopteran species, Heliothis virescens, in
RT   response to modern agricultural practices.";
RL   Submitted (SEP-2017) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PCG66793.1}.
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DR   EMBL; NWSH01003201; PCG66793.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A4J5U6; -.
DR   STRING; 7102.A0A2A4J5U6; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000218220; 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; -; 2.
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; 2.
DR   Pfam; PF02366; PMT; 1.
DR   Pfam; PF16192; PMT_4TMC; 1.
DR   SMART; SM00472; MIR; 6.
DR   SUPFAM; SSF82109; MIR domain; 2.
DR   PROSITE; PS50919; MIR; 6.
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:UP000218220};
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        160..179
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        185..204
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        211..231
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        237..270
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        291..314
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        574..592
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   TRANSMEM        612..634
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367007"
FT   DOMAIN          347..408
FT                   /note="MIR"
FT                   /evidence="ECO:0000259|PROSITE:PS50919"
FT   DOMAIN          419..476
FT                   /note="MIR"
FT                   /evidence="ECO:0000259|PROSITE:PS50919"
FT   DOMAIN          480..538
FT                   /note="MIR"
FT                   /evidence="ECO:0000259|PROSITE:PS50919"
FT   DOMAIN          664..725
FT                   /note="MIR"
FT                   /evidence="ECO:0000259|PROSITE:PS50919"
FT   DOMAIN          736..793
FT                   /note="MIR"
FT                   /evidence="ECO:0000259|PROSITE:PS50919"
FT   DOMAIN          797..855
FT                   /note="MIR"
FT                   /evidence="ECO:0000259|PROSITE:PS50919"
SQ   SEQUENCE   958 AA;  108390 MW;  7AB7B991FBD4547A CRC64;
     MDVSSDIKNR HDKKKIKEVS ELARNSYFKD ILNNETQSTD DISAAVETEP IQKEILSSKT
     EQGLSGVYLH LEINLVFLGL LALALCTRLP NLEEPHYIVF DELHYGRYVS LYTKGIFFFD
     AHPPLGKQLL YLAGRAAGYD GNFTFDRIGT PYTDNVPVKA LRLIPALAGS MLVAVTYQLM
     MEISFYHWTA VLAGLLVLFE NCFLAQSRFM LLESIQILFG LYGILCAIKS TRRTGFASFV
     WLCIAALALG CCFSVKYSGV YSYFLAVFLV GRQIWKRIGS TKSVLRLTWS ALWRLLVLTV
     IPFAVYVSVF YAHLAMLPKA GPHDSVMTSA FQASLQGGLA SITRGQPLHV AHGSQITLRH
     THGRTCWLHS HAHVYPVRYT DGRGSSHQQQ VTCYSFKDVN NWWIVKRPDQ ASLSVSRPPD
     AIRHGDVVQL LHGITSRALN SHDVAAPVSP QSQEVSCYID YNVSMPAQNL WRVDIVNRDS
     EDATWDSIRS LVRLVHVDSG SALRFSGRQL PSWGFHQHEV VADKVLTHQD TVWNVEEHRY
     TKAEDRKERE RELVSAEMIP TAVTQLTFWE KVKYSGVYSY FLAVFLVGRQ IWKRIGSTKS
     VLRLTWSALW RLLVLTVIPF AVYVSVFYAH LAMLPKAGPH DSVMTSAFQA SLQGGLASIT
     RGQPLHVAHG SQITLRHTHG RTCWLHSHAH VYPVRYTDGR GSSHQQQVTC YSFKDVNNWW
     IVKRPDQASL SVSRPPDAIR HGDVVQLLHG ITSRALNSHD VAAPVSPQSQ EVSCYIDYNV
     SMPAQNLWRV DIVNRDSEDA TWDSIRSLVR LVHVDSGSAL RFSGRQLPSW GFHQHEVVAD
     KVLTHQDTVW NVEEHRYTKA EDRKEREREL VSAEMIPTAV TQLTFWEKFA ELQYKMIAHA
     PDAPHGHMFA SDPSEWPLLI RSIAYWLSPN SNCLPRTVRY PSASRLRGPT TMCNEEIL
//
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