ID A0A182F7X3_ANOAL Unreviewed; 693 AA.
AC A0A182F7X3;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=dolichyl-phosphate-mannose--protein mannosyltransferase {ECO:0000256|ARBA:ARBA00012839};
DE EC=2.4.1.109 {ECO:0000256|ARBA:ARBA00012839};
OS Anopheles albimanus (New world malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7167 {ECO:0000313|EnsemblMetazoa:AALB002594-PA, ECO:0000313|Proteomes:UP000069272};
RN [1] {ECO:0000313|EnsemblMetazoa:AALB002594-PA}
RP IDENTIFICATION.
RC STRAIN=STECLA/ALBI9_A {ECO:0000313|EnsemblMetazoa:AALB002594-PA};
RG EnsemblMetazoa;
RL Submitted (AUG-2022) to UniProtKB.
CC -!- FUNCTION: Transfers mannosyl residues to the hydroxyl group of serine
CC or threonine residues. {ECO:0000256|ARBA:ARBA00003582}.
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 -!- 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 -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000256|ARBA:ARBA00004240}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the TMTC family.
CC {ECO:0000256|ARBA:ARBA00007882}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A182F7X3; -.
DR STRING; 7167.A0A182F7X3; -.
DR EnsemblMetazoa; AALB002594-RA; AALB002594-PA; AALB002594.
DR VEuPathDB; VectorBase:AALB002594; -.
DR VEuPathDB; VectorBase:AALB20_028260; -.
DR OrthoDB; 155869at2759; -.
DR Proteomes; UP000069272; Chromosome 2R.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004169; F:dolichyl-phosphate-mannose-protein mannosyltransferase activity; IEA:UniProtKB-EC.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 3.
DR InterPro; IPR013618; TMTC_DUF1736.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR013105; TPR_2.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR44227; -; 1.
DR PANTHER; PTHR44227:SF3; PROTEIN O-MANNOSYL-TRANSFERASE TMTC4; 1.
DR Pfam; PF08409; TMTC_DUF1736; 1.
DR Pfam; PF13424; TPR_12; 1.
DR Pfam; PF13432; TPR_16; 1.
DR Pfam; PF07719; TPR_2; 1.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00028; TPR; 6.
DR SUPFAM; SSF48452; TPR-like; 2.
DR PROSITE; PS50005; TPR; 5.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW TPR repeat {ECO:0000256|ARBA:ARBA00022803}.
FT DOMAIN 260..332
FT /note="DUF1736"
FT /evidence="ECO:0000259|Pfam:PF08409"
SQ SEQUENCE 693 AA; 78692 MW; F7F726A1E532C58E CRC64;
MSSARQQTIV QYSILVAASL FAYGGSLHGT FVFDDSAAIV KNMDVRNVAT PFRTLLRHDF
WGNNLTDPTS HKSFRPLTVL SYQLESRFLG LNAGHMKKLN LALHTICSLL VLRLFQILCS
EDGHRFRTAF WGAFLFTVHP VHTEAVVGIV GRADLLAAIG YLTIMLLYLR WIESDHCQRW
GFIVYPVLFA LTIISMLCKE TGIMALVSCG AVDILKRIKW PLRGTVHELL HAHRTSLGRV
IILAALSLGA LALRLWIMDF ESPRFHRMDN PVGASNSTLA RVLSQSYLYW INLWLLVCPD
WLSFDWALGS IPLIEGLSDL RLLLVALFYG FIALLLLRVP STKRNEVTLS LVLAIIPFVP
ACGIVRVGFV IAERLLYLPS VGFCYLIAIG CRRLIKRSFL FYIPLCFLCT VFILKTQSRA
HEWTNEDLLF RSALRVCPGN AKVYYNIARL ATDQGDRKTA FAFYRHAIAL HPDYEAAHMN
LGNLYRETGD LDTAETHLLK AIQIHEPFPS AWMNLGIVQA AQRNHDAALQ SYQRALQLKP
NYANCLYNLG NLYIDMQNST MALRYWREAI QQNPRHSKAW ANILALYDNR GRTEDIIRTS
ELALSFLPND TAILFTRANA YGKLAQYEKA ESLYRQIIAA RPDYAVYRAN LGVLYHRWGQ
RESQAIEQYR AALRIDPNLR SAKTNLLKLM GTT
//
