TMTC1_CAEEL
ID TMTC1_CAEEL Reviewed; 690 AA.
AC Q20144;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Protein O-mannosyl-transferase TMTC1;
DE EC=2.4.1.109;
DE AltName: Full=Transmembrane and TPR repeat-containing protein F38B6.6;
GN ORFNames=F38B6.6;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Transfers mannosyl residues to the hydroxyl group of serine
CC or threonine residues. {ECO:0000250|UniProtKB:Q8IUR5}.
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:0000250|UniProtKB:Q8IUR5};
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:0000250|UniProtKB:Q8IUR5};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:Q8IUR5}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q8IUR5}.
CC -!- SIMILARITY: Belongs to the TMTC family. {ECO:0000305}.
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DR EMBL; FO080973; CCD68214.1; -; Genomic_DNA.
DR PIR; T16298; T16298.
DR RefSeq; NP_509123.2; NM_076722.5.
DR AlphaFoldDB; Q20144; -.
DR SMR; Q20144; -.
DR STRING; 6239.F38B6.6.1; -.
DR PaxDb; Q20144; -.
DR EnsemblMetazoa; F38B6.6.1; F38B6.6.1; WBGene00018175.
DR GeneID; 185454; -.
DR KEGG; cel:CELE_F38B6.6; -.
DR UCSC; F38B6.6; c. elegans.
DR CTD; 185454; -.
DR WormBase; F38B6.6; CE30976; WBGene00018175; -.
DR eggNOG; KOG1124; Eukaryota.
DR GeneTree; ENSGT00940000158521; -.
DR HOGENOM; CLU_011615_2_0_1; -.
DR InParanoid; Q20144; -.
DR OMA; KAWANIL; -.
DR OrthoDB; 1320023at2759; -.
DR PhylomeDB; Q20144; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q20144; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00018175; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004169; F:dolichyl-phosphate-mannose-protein mannosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0000030; F:mannosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IBA:GO_Central.
DR GO; GO:0035269; P:protein O-linked mannosylation; ISS:UniProtKB.
DR Gene3D; 1.25.40.10; -; 2.
DR InterPro; IPR013618; TMTC_DUF1736.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF08409; DUF1736; 1.
DR Pfam; PF13176; TPR_7; 1.
DR Pfam; PF13181; TPR_8; 2.
DR SMART; SM00028; TPR; 7.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50005; TPR; 7.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Glycoprotein; Membrane; Reference proteome; Repeat;
KW TPR repeat; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..690
FT /note="Protein O-mannosyl-transferase TMTC1"
FT /id="PRO_0000280297"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 308..328
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 342..362
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 366..386
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 398..431
FT /note="TPR 1"
FT REPEAT 433..465
FT /note="TPR 2"
FT REPEAT 466..499
FT /note="TPR 3"
FT REPEAT 501..533
FT /note="TPR 4"
FT REPEAT 534..567
FT /note="TPR 5"
FT REPEAT 602..635
FT /note="TPR 6"
FT REPEAT 637..669
FT /note="TPR 7"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 559
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 600
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 617
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 686
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 690 AA; 77737 MW; 2FC7FDFA59551E60 CRC64;
MKKHLHHKVS GSCDPGDRSP KEKGRSQGIR NLLILISLSI IPYLSCLGGD FVFDDAESIV
NNPIVNGKDP LLQIFSRDFW GRSISSSNSH KSYRPVTTFT FWLNYKLHET STLGYHVVNI
ICHTVATLVF YKLGKQLEHI FDFFNIAFSA SILFAVHPVH TEAVANITGR AELLMTIFSL
AALILHVKNR EINCKFVLLV ILSTLSKEQG LMTIPIAICI DFLAHRSCRS NFVRMICLLV
AIGFLRMMVN GFEAAKFTKL DNPTAFLNSK FYRMINYTYI WLYHAYLLVI PVNLCFDYSM
GCISSITTMW DLRALSPVLI FTIVIIGVKF QNECRAFTLS SLMGIISFLP ASNIFFTVGF
SIAERVLYLP SAGFCLLCAI IFKKLSVHFK NADVLSITLI LLLISKTYRR SGEWKTELSL
YSSGLSVCPT NAKIHYNLGK VLGDNGLTKD AEKNYWNAIK LDPSYEQALN NLGNLLEKSG
DSKTAESLLA RAVTLRPSFA VAWMNLGISQ MNLKKYYEAE KSLKNSLLIR PNSAHCLFNL
GVLYQRTNRD EMAMSAWKNA TRIDPSHSQS WTNLFVVLDH LSQCSQVIDL SYQALSSVPN
ESRVHMQIGS CHAKHSNFTA AENHIKSAID LNPTSVLFHA NLGILYQRMS RHKEAESQYR
IVLALDSKNI VAKQNLQKLE EHNCYNSTLP
