TMTC2_XENLA
ID TMTC2_XENLA Reviewed; 836 AA.
AC Q6DCD5;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Protein O-mannosyl-transferase TMTC2 {ECO:0000250|UniProtKB:Q8N394};
DE EC=2.4.1.109 {ECO:0000250|UniProtKB:Q8N394};
DE AltName: Full=Transmembrane and TPR repeat-containing protein 2;
GN Name=tmtc2;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transfers mannosyl residues to the hydroxyl group of serine
CC or threonine residues. {ECO:0000250|UniProtKB:Q8N394}.
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:Q8N394};
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:Q8N394};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:Q8N394}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q8N394}.
CC -!- SIMILARITY: Belongs to the TMTC family. {ECO:0000305}.
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DR EMBL; BC078113; AAH78113.1; -; mRNA.
DR RefSeq; NP_001087168.1; NM_001093699.1.
DR AlphaFoldDB; Q6DCD5; -.
DR SMR; Q6DCD5; -.
DR DNASU; 447057; -.
DR GeneID; 447057; -.
DR KEGG; xla:447057; -.
DR CTD; 447057; -.
DR Xenbase; XB-GENE-948543; tmtc2.S.
DR OrthoDB; 1320023at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000186698; Chromosome 3S.
DR Bgee; 447057; Expressed in blastula and 13 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
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:0035269; P:protein O-linked mannosylation; ISS:UniProtKB.
DR Gene3D; 1.25.40.10; -; 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 Pfam; PF08409; DUF1736; 1.
DR Pfam; PF00515; TPR_1; 1.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00028; TPR; 9.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS50005; TPR; 8.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Glycoprotein; Membrane; Reference proteome; Repeat;
KW TPR repeat; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..836
FT /note="Protein O-mannosyl-transferase TMTC2"
FT /id="PRO_0000280292"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 313..333
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 393..413
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 415..435
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 450..470
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 460..492
FT /note="TPR 1"
FT REPEAT 493..526
FT /note="TPR 2"
FT REPEAT 527..560
FT /note="TPR 3"
FT REPEAT 562..594
FT /note="TPR 4"
FT REPEAT 606..639
FT /note="TPR 5"
FT REPEAT 643..676
FT /note="TPR 6"
FT REPEAT 677..710
FT /note="TPR 7"
FT REPEAT 712..744
FT /note="TPR 8"
FT REPEAT 746..778
FT /note="TPR 9"
FT REPEAT 779..812
FT /note="TPR 10"
FT CARBOHYD 221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 836 AA; 94404 MW; F7B3BF11EAE912A5 CRC64;
MIAELLSSAL GLLLYLNTLG ADFCYDDSRA IKTNQDLLPE TPWNHIFFND FWGTLLTHSG
SHKSYRPLCT LSFRLNYLFG GLDPWNYHLV NVLLHSAVTG LFTNLCKALF GSGCWTLIAG
LLFASHPIHT EAVSGIVGRA DVGSGLFFLL SLLCYMKHCS TRGYSLSSWC WILCAGFWAA
CSMLWKEQGV TVLAVSAVYD VFVFHKLKMN QIISVVFKEK NVSFFFSVGL LFAWGVILLG
ARFYWMGNTP PSFSNSDNPA ADCEVLLTRT LTFFYLPTKN LWLLFCPDTL SFDWSMDAVP
LIKTITDWRN IHTVAFYILL ILLAYSSLKG SAIKRDCNGK VFMNGKQNTN GHSCQSDLEH
KNAEQNPVIA SKLENGVKHH NSHEMQLPST ENIVVLALSL LIVPFVPASN LFFYVGFVIA
ERVLYIPSMG FCLLVTVGAR ALYIKAQKNI LKNLLFYATA ALIVFYGLKT VVRNGDWKNE
EMLYRSGIKV NPAKAWGNLG NVLKSQSKID EAENAYRNAL YYRSNMADML YNLGLLLQEN
SKFSEALHYY KLAIGSRPTL ASGYLNTGII LMNQGRTEEA RRTFLKCSEI PDENLKDPNA
HKSSVTSCLY NLGKLYHEQG QYEDALIVYK EAIQKMPRQF SPQSLYNMMG EAYMRLNVVS
EAEHWYTESL KSKPDHIPAH LTYGKLLTLT GRKNEAERYF LKAIQLDPNK GNCYMHYGQF
LLEEGRILEA AEMAKKAAEL DSSEFDVVFN AAHMLRQASL NEEAEKFYKL AAGLRQNYPA
ALMNLGAILH LNGKLEEAEY NYLRALQLKP DDAITQSNLR KLWNIMEKQG LKNSKT
