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Database: UniProt
Entry: A0A1A9Z7Q0_GLOPL
LinkDB: A0A1A9Z7Q0_GLOPL
Original site: A0A1A9Z7Q0_GLOPL 
ID   A0A1A9Z7Q0_GLOPL        Unreviewed;      1055 AA.
AC   A0A1A9Z7Q0;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-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   Glossina pallidipes (Tsetse fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC   Glossinidae; Glossina.
OX   NCBI_TaxID=7398 {ECO:0000313|EnsemblMetazoa:GPAI006342-PA, ECO:0000313|Proteomes:UP000092445};
RN   [1] {ECO:0000313|Proteomes:UP000092445}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IAEA {ECO:0000313|Proteomes:UP000092445};
RA   Aksoy S., Warren W., Wilson R.K.;
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:GPAI006342-PA}
RP   IDENTIFICATION.
RC   STRAIN=IAEA {ECO:0000313|EnsemblMetazoa:GPAI006342-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) 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}.
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DR   AlphaFoldDB; A0A1A9Z7Q0; -.
DR   STRING; 7398.A0A1A9Z7Q0; -.
DR   EnsemblMetazoa; GPAI006342-RA; GPAI006342-PA; GPAI006342.
DR   VEuPathDB; VectorBase:GPAI006342; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000092445; 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; 4.
DR   InterPro; IPR013618; TMTC_DUF1736.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR001440; TPR_1.
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; PF00515; TPR_1; 1.
DR   Pfam; PF13374; TPR_10; 1.
DR   Pfam; PF13181; TPR_8; 1.
DR   Pfam; PF17874; TPR_MalT; 1.
DR   SMART; SM00028; TPR; 8.
DR   SUPFAM; SSF48452; TPR-like; 2.
DR   PROSITE; PS50005; TPR; 5.
DR   PROSITE; PS50293; TPR_REGION; 2.
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   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW   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        46..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        153..170
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        176..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        212..229
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        235..252
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        259..280
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        583..602
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        608..633
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          284..354
FT                   /note="DUF1736"
FT                   /evidence="ECO:0000259|Pfam:PF08409"
FT   REPEAT          692..725
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          726..759
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          831..864
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          869..902
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          1006..1039
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REGION          522..557
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1055 AA;  118176 MW;  4CD4C11C6C2D9B28 CRC64;
     MIDFLRESQC FTENGLKSLI YTEGTWLLDS EQQAYRHNYV HYGMDYISLG CCSLAFILYL
     NTLNSGFVYD DRRAILSNMD VSGSSPWQNA FVNDFWGTAL TDSGSHGSYR PLCVLSFRLN
     FILSGYSPWG FHLVNNMLHC VATGLVVKVA RQLLSSMWGV IVTGALFAVH PIHTEAIAGI
     VGRADAATSI CYMLAFLAYL RHMNWRIRND QRQWLALAFA IATSVIALLF KETGITALLL
     CVIFDLICTL CGQCDKNRLR SICIVLSSLV CVAFSRLALI PKPQASFSSA DNPISKTTSA
     WTRLLTFIYL PVFNFKLLVS PHVLSFDWGM DAIPRIISIF DERNILSVTF YGAITYLMWY
     SYQALLVRRN CGAGKQRSQT YVVNGCDPGS HYHLQPKIQR KSRTKHKYVQ RQCQSSEGLY
     VMNCTSSNVS YPPGNSTTNF WKKGWLRPYS SGQICTDCKQ EINSGQHSAS CRALNNNNVL
     TYNTPNVLNS ECCCHQLMSS GGTAAPQLFS LALQIIARSS RSSSSCSNST TASNKSSDSS
     ASSTYSSSSS SSKSSSSQLS IVSPYEDQWI QHREYIFSHA SNSCANACVL ITSLAFLILP
     FLPATNLFFY VGFVVAERLL YLPSVGFCLI VGFGLSKIMD FLRTRRMQRT KQMMVISLCV
     LLCTLSARTV LRNRDWKDEE SLYRSAVRVN PPKALGNLGS VLSSQARYTE AEEILLEAIK
     YRPNMADVHF NLGILYQNQK KYNFAIESFK NALNFRPSLA GITFKYHCIC RCINEKFMWA
     LVAPFPVAYL NLGISLIALG KCQEAAQVLQ DGSRLNGTGV RDRNSHENAR ISSYLQLGAL
     YADQGKLQRA LAVYREALHE LPHNYHMRDV LYYRIGDIFG RLQKWDEAEK HHRAALNLRP
     KEAGVHLSYG ITLARNSSRA SEAEFWFKRA LKLAPEQASV YHHYAEFLTS QSRNAEAVSY
     RVRAARLAPN DYSLVVAAAT ALRLMDRKAE AEVLYRKAVY LRPYDAHAHT NLGAILHLLG
     HTSKAAASYK EALRLQPGDI TTLSNLAKLG LRNTE
//
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