TMTC2_DROME
ID TMTC2_DROME Reviewed; 938 AA.
AC Q9V3X5;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 148.
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 CG4341;
GN ORFNames=CG4341;
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; TISSUE=Head;
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).
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; AE014134; AAF51432.1; -; Genomic_DNA.
DR EMBL; AF181645; AAD55431.1; -; mRNA.
DR RefSeq; NP_608558.1; NM_134714.5.
DR AlphaFoldDB; Q9V3X5; -.
DR SMR; Q9V3X5; -.
DR BioGRID; 59530; 1.
DR STRING; 7227.FBpp0077614; -.
DR GlyGen; Q9V3X5; 5 sites.
DR PaxDb; Q9V3X5; -.
DR PRIDE; Q9V3X5; -.
DR EnsemblMetazoa; FBtr0077949; FBpp0077614; FBgn0028481.
DR GeneID; 33276; -.
DR KEGG; dme:Dmel_CG4341; -.
DR UCSC; CG4341-RA; d. melanogaster.
DR FlyBase; FBgn0028481; CG4341.
DR VEuPathDB; VectorBase:FBgn0028481; -.
DR eggNOG; KOG1124; Eukaryota.
DR GeneTree; ENSGT00940000166588; -.
DR InParanoid; Q9V3X5; -.
DR OrthoDB; 1320023at2759; -.
DR PhylomeDB; Q9V3X5; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 33276; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 33276; -.
DR PRO; PR:Q9V3X5; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0028481; Expressed in brain and 6 other tissues.
DR ExpressionAtlas; Q9V3X5; baseline and differential.
DR Genevisible; Q9V3X5; 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:FlyBase.
DR GO; GO:0035269; P:protein O-linked mannosylation; IBA:GO_Central.
DR Gene3D; 1.25.40.10; -; 4.
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; PF13181; TPR_8; 1.
DR SMART; SM00028; TPR; 8.
DR SUPFAM; SSF48452; SSF48452; 2.
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..938
FT /note="Protein O-mannosyl-transferase TMTC2"
FT /id="PRO_0000280299"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 250..270
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..312
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 511..531
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 534..554
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 563..580
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 569..601
FT /note="TPR 1"
FT REPEAT 602..635
FT /note="TPR 2"
FT REPEAT 636..669
FT /note="TPR 3"
FT REPEAT 671..703
FT /note="TPR 4"
FT REPEAT 715..748
FT /note="TPR 5"
FT REPEAT 753..786
FT /note="TPR 6"
FT REPEAT 788..821
FT /note="TPR 7"
FT REPEAT 823..855
FT /note="TPR 8"
FT REPEAT 857..889
FT /note="TPR 9"
FT REPEAT 890..923
FT /note="TPR 10"
FT REGION 450..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 418
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 419
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 457
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 460
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 938 AA; 103091 MW; 4856B2543FD4A134 CRC64;
MPSLEPWLWG DSCSWLGMLA MLRLRLHKSN MDFTCLFCCS LAFVLYLNTL GAGFVYDDRR
AILANADVSG GTPWQRSFSN DFWGTPLTDS GSHGSWRPLC VLSFRLNYLI GGGFAPWGFH
LVNNLLHCVA TALVVRVART LLASVWAVLA AGALFAAHPI HTEAVAGVVG RADLAACVCY
LLTYLSYLRH MRWRESGDPR QWLALGATLI LAAAGLLCKE TAITALLVCA LFDVMRGLSG
QVDKQRLRSV CIVLGALFCM AYCRLVIVPG PQTAFSSADN PIARTPSAWT RLLTFLYLPV
FNLRLLLQPN VLSFDWGMDA LPRVTSLWDR RNAQSACFYS VLVGVAWGSC RQLLSGSKEV
THCGVSSTFP QYHIQKVASR KSRSKRKRLA NNTKYQAFEA AYHQQQQEAL PCRDCNNNNS
SGYVYEGSSP VAQAPAQAPH LVSSAFRGSR SSSSCSNSTN SSSSSSSSSS SSSSSSSSLS
GGFQCSSKDY ALEGMSPANR HACVLIMSLS FLALPFLPAS NLLFYVGFVV AERLLYLPSV
GFCLLVGYGV SKLMSCNQRT RNILLLSFSL LLAAMSLRTL RRNADWRDEE SLYRSAIAIN
PPKALGNLGS VLSSQGRYEE AKQVLQEAIR FRPNMADVHF NLGILHQNQQ VYPAAVECFQ
RAIKFRPNLA VAYLNLGISF IALGKRQQAI EILQAGSNLD GAAVRDRTAH DQARSSAYLQ
LGALYVEQGK LQRALAIYRE ALSSLPGLPQ QREILYQRIG DVLGRLQQWD EAERHHRAAL
ELQPNQVAAH LSYGITLARN SSRASEAEMW FKRALKLAPE QASVYHHYAE FLSLQSRHHE
SAIYHRRAAE LAPNDYTLVV AAATAMRLLD RKVDAEMWYR KAVALRPGDA HAHTNLGAIL
HLLGRTNHAA ASYKAALRLQ PGDAITLGNL AKLGVTNV
