TMTC1_DROME
ID TMTC1_DROME Reviewed; 859 AA.
AC Q9VQE9; D3PFE4; Q7KU17; Q8T3V2;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 3.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Protein O-mannosyl-transferase TMTC1 {ECO:0000250|UniProtKB:Q8IUR5};
DE EC=2.4.1.109 {ECO:0000250|UniProtKB:Q8IUR5};
DE AltName: Full=Transmembrane and TPR repeat-containing protein CG31690;
GN ORFNames=CG31690;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Testis;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL90222.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact giving rise to incorrect N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE014134; AAS64621.2; -; Genomic_DNA.
DR EMBL; BT120303; ADC53520.1; -; mRNA.
DR EMBL; AY089484; AAL90222.1; ALT_SEQ; mRNA.
DR RefSeq; NP_995615.2; NM_205893.3.
DR AlphaFoldDB; Q9VQE9; -.
DR SMR; Q9VQE9; -.
DR STRING; 7227.FBpp0290896; -.
DR GlyGen; Q9VQE9; 2 sites.
DR PaxDb; Q9VQE9; -.
DR PRIDE; Q9VQE9; -.
DR EnsemblMetazoa; FBtr0301682; FBpp0290896; FBgn0051690.
DR GeneID; 33455; -.
DR KEGG; dme:Dmel_CG31690; -.
DR UCSC; CG31690-RA; d. melanogaster.
DR FlyBase; FBgn0051690; CG31690.
DR VEuPathDB; VectorBase:FBgn0051690; -.
DR eggNOG; KOG1124; Eukaryota.
DR HOGENOM; CLU_011615_4_0_1; -.
DR InParanoid; Q9VQE9; -.
DR OMA; STHHHYA; -.
DR OrthoDB; 1320023at2759; -.
DR PhylomeDB; Q9VQE9; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 33455; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 33455; -.
DR PRO; PR:Q9VQE9; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0051690; Expressed in central nervous system and 5 other tissues.
DR ExpressionAtlas; Q9VQE9; baseline and differential.
DR Genevisible; Q9VQE9; DM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; 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: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; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF08409; DUF1736; 1.
DR Pfam; PF00515; TPR_1; 1.
DR SMART; SM00028; TPR; 7.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50005; TPR; 7.
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..859
FT /note="Protein O-mannosyl-transferase TMTC1"
FT /id="PRO_0000280298"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 246..266
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 329..349
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 423..443
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 447..467
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 474..493
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 485..517
FT /note="TPR 1"
FT REPEAT 518..551
FT /note="TPR 2"
FT REPEAT 552..585
FT /note="TPR 3"
FT REPEAT 587..620
FT /note="TPR 4"
FT REPEAT 632..665
FT /note="TPR 5"
FT REPEAT 671..704
FT /note="TPR 6"
FT REPEAT 705..739
FT /note="TPR 7"
FT REPEAT 740..773
FT /note="TPR 8"
FT REPEAT 774..807
FT /note="TPR 9"
FT REPEAT 808..841
FT /note="TPR 10"
FT CARBOHYD 363
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 471
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 17
FT /note="H -> Q (in Ref. 4; AAL90222)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="M -> V (in Ref. 4; AAL90222)"
FT /evidence="ECO:0000305"
FT CONFLICT 222
FT /note="E -> K (in Ref. 4; AAL90222)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="V -> T (in Ref. 4; AAL90222)"
FT /evidence="ECO:0000305"
FT CONFLICT 229
FT /note="D -> Y (in Ref. 3; ADC53520)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="G -> A (in Ref. 4; AAL90222)"
FT /evidence="ECO:0000305"
FT CONFLICT 319
FT /note="S -> P (in Ref. 4; AAL90222)"
FT /evidence="ECO:0000305"
FT CONFLICT 544
FT /note="T -> A (in Ref. 4; AAL90222)"
FT /evidence="ECO:0000305"
FT CONFLICT 570
FT /note="S -> T (in Ref. 4; AAL90222)"
FT /evidence="ECO:0000305"
FT CONFLICT 761
FT /note="G -> S (in Ref. 4; AAL90222)"
FT /evidence="ECO:0000305"
FT CONFLICT 762
FT /note="L -> F (in Ref. 3; ADC53520)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 859 AA; 94857 MW; 7104901AF76C2CA8 CRC64;
MHTPKCRRPS MSATLSHKDL AGLAGCSALA FVLYLNTLNA GFVYDDRRAI LANGDVTGAR
PLANLLRNDF WGTPLVDSGS HGSWRPLCVL SFRLNYLAGG MTPLGYHLVN VMLHCVATWL
VFLVARTLLP SRMGVLAAGA LFAVHPAHTE AVAGLVGRAD LASCVCYLLA YLSYRRHMLN
REWGSLILTI MLALAALLCK ETAITALLLC GLCDVLSPVG RENSDKVCDG SISGLASFNF
QRRFRSLSIL GFTLLCGLYC RLSLLPRPST AFSAADNPTA HESCFWTRTL TFLYLPVANF
GILLWPQELS FDWGMEAVSR IRTLWDARNI LTAGFYGSLV AILWKGSGLR SAASPMDFAE
VANISLPLLR RLGGNSCHTW LGLTCDCHHQ LSAPSYRSAS AIYSTSSKSK SASWTAAPIL
GTAFLVLPFL PASNLLFYVG FVMAERVLYL PSVGYCLLFG LGFGHLWQRV NSSWRSRLML
LCGLALLLGV HGVRTFRRNL DWRDEEQLFR SAISINPPKA LGNLGSVLSA QGRYEEAELT
LRMTLGHRPT MADAHFNLGV VHQKQLNFSS AIPCFRRAIE LRPQLAVAYL NLGTSLISLG
DHRQEAISVL RTGARLEGSG VRDRGAHVEA RYTCYLQLSV LYRSDGRLQD AAAALRESLK
ALPLLPQKQR AVLHLRLGEI LAELQDWNEA EHQQRLAMQL QPEQGAAYVT YGQTLARNGS
RLAEAESWFK RALQLAPLEP SSHHHYADFL EQQERHHEAL GLRLRAAALA PQDYTLQSCV
ADALRLLNRL AEAELWYRKA VTLQPMAAHA HANLGAILQM RGLRKEAVAC YHKALELQPG
HAISRANLAR MNVHKHENE
