ID A0A0V0XHA3_TRIPS Unreviewed; 476 AA.
AC A0A0V0XHA3;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=dolichyl-phosphate-mannose--protein mannosyltransferase {ECO:0000256|ARBA:ARBA00012839};
DE EC=2.4.1.109 {ECO:0000256|ARBA:ARBA00012839};
DE Flags: Fragment;
GN Name=TMTC2 {ECO:0000313|EMBL:KRX87391.1};
GN ORFNames=T4E_10725 {ECO:0000313|EMBL:KRX87391.1};
OS Trichinella pseudospiralis (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6337 {ECO:0000313|EMBL:KRX87391.1, ECO:0000313|Proteomes:UP000054815};
RN [1] {ECO:0000313|EMBL:KRX87391.1, ECO:0000313|Proteomes:UP000054815}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS141 {ECO:0000313|EMBL:KRX87391.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:KRX87391.1}.
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DR EMBL; JYDU01000290; KRX87391.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0XHA3; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000054815; Unassembled WGS sequence.
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; 2.
DR InterPro; IPR013618; TMTC_DUF1736.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR44216; PROTEIN O-MANNOSYL-TRANSFERASE TMTC2; 1.
DR PANTHER; PTHR44216:SF3; PROTEIN O-MANNOSYL-TRANSFERASE TMTC2; 1.
DR Pfam; PF08409; TMTC_DUF1736; 1.
DR Pfam; PF13176; TPR_7; 1.
DR Pfam; PF13181; TPR_8; 2.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50005; TPR; 3.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000054815};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..22
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 83..101
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 219..243
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 249..266
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 278..300
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 21..93
FT /note="DUF1736"
FT /evidence="ECO:0000259|Pfam:PF08409"
FT REPEAT 321..354
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 355..388
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 431..464
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX87391.1"
SQ SEQUENCE 476 AA; 53700 MW; 215AE4AACFB31DE5 CRC64;
LWMLIFGAAS ALFFRLWVMN FQSPNFSAFD NPASHCPNRL IRILTFLFLP IFNFKLALCP
TVLSFDWSMN SIPLVESVTD SRVFVTCAGY LALASLGVQL YRFITEREEL TPVAKLCTSL
PCSPYTPQTR RFVDLCNNND SEDAIVNCCL NVHAWSKENH SATAARLNIK SREKSNCTPI
INRMYANDCQ QVAAKFRAKF KGQPLKLESS ILKDPSSEMA FLALLLMVIT FIPASNLFFY
VGFVVAERVL YLPSVGFCCL VAVGACKLLE IAKRQNRAIF YSVHVILCIS LVSLAVRSWL
RNMDWMDEKS LYSSGVSVCP VKALANLANV YAQEGTLEKA EQLYKIALNQ KSDTSDTWYN
YGLFLQNAGR LREASNAYRN SIQRRPWFAL AYLNFGIVLG EMGRTEEAKQ GHIVEAREKF
ELATRLQIES VQALEHLGHF YLDTGNLELA IETFVKALKL EPHNFSLVFA LATAQR
//
