TMTC3_DROME
ID TMTC3_DROME Reviewed; 926 AA.
AC Q7K4B6; O02435; Q24581;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Protein O-mannosyl-transferase Tmtc3 {ECO:0000250|UniProtKB:Q6ZXV5};
DE EC=2.4.1.109 {ECO:0000250|UniProtKB:Q6ZXV5};
DE AltName: Full=Transmembrane and TPR repeat-containing protein 3 {ECO:0000312|FlyBase:FBgn0020312};
GN Name=Tmtc3 {ECO:0000312|FlyBase:FBgn0020312};
GN ORFNames=CG4050 {ECO:0000312|FlyBase:FBgn0020312};
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=Embryo;
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 [MRNA] OF 674-926.
RA Davis T.;
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transfers mannosyl residues to the hydroxyl group of serine
CC or threonine residues. {ECO:0000250|UniProtKB:Q6ZXV5}.
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:Q6ZXV5};
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:Q6ZXV5};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:Q6ZXV5}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q6ZXV5}.
CC -!- SIMILARITY: Belongs to the TMTC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA63344.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AE013599; AAF46676.2; -; Genomic_DNA.
DR EMBL; AY052013; AAK93437.1; -; mRNA.
DR EMBL; X92653; CAA63344.1; ALT_FRAME; mRNA.
DR RefSeq; NP_477246.2; NM_057898.4.
DR RefSeq; NP_726030.1; NM_166426.2.
DR AlphaFoldDB; Q7K4B6; -.
DR SMR; Q7K4B6; -.
DR BioGRID; 63038; 1.
DR STRING; 7227.FBpp0071560; -.
DR GlyGen; Q7K4B6; 2 sites.
DR PaxDb; Q7K4B6; -.
DR DNASU; 37401; -.
DR EnsemblMetazoa; FBtr0071637; FBpp0071560; FBgn0020312.
DR EnsemblMetazoa; FBtr0071638; FBpp0071561; FBgn0020312.
DR GeneID; 37401; -.
DR KEGG; dme:Dmel_CG4050; -.
DR UCSC; CG4050-RA; d. melanogaster.
DR CTD; 160418; -.
DR FlyBase; FBgn0020312; Tmtc3.
DR VEuPathDB; VectorBase:FBgn0020312; -.
DR eggNOG; KOG1124; Eukaryota.
DR GeneTree; ENSGT00940000157538; -.
DR HOGENOM; CLU_011615_1_0_1; -.
DR InParanoid; Q7K4B6; -.
DR OMA; SDYVQAY; -.
DR OrthoDB; 1320023at2759; -.
DR PhylomeDB; Q7K4B6; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 37401; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 37401; -.
DR PRO; PR:Q7K4B6; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0020312; Expressed in eye disc (Drosophila) and 28 other tissues.
DR ExpressionAtlas; Q7K4B6; baseline and differential.
DR Genevisible; Q7K4B6; DM.
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:0035269; P:protein O-linked mannosylation; ISS:UniProtKB.
DR Gene3D; 1.25.40.10; -; 3.
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; 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..926
FT /note="Protein O-mannosyl-transferase Tmtc3"
FT /id="PRO_0000280300"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 223..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 304..324
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 346..366
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 385..405
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 420..440
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 443..463
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 514..547
FT /note="TPR 1"
FT REPEAT 549..581
FT /note="TPR 2"
FT REPEAT 596..630
FT /note="TPR 3"
FT REPEAT 631..664
FT /note="TPR 4"
FT REPEAT 665..698
FT /note="TPR 5"
FT REPEAT 736..769
FT /note="TPR 6"
FT REPEAT 771..803
FT /note="TPR 7"
FT REPEAT 804..838
FT /note="TPR 8"
FT REPEAT 840..872
FT /note="TPR 9"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 609
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 645
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 732
FT /note="D -> H (in Ref. 4; CAA63344)"
FT /evidence="ECO:0000305"
FT CONFLICT 916
FT /note="D -> V (in Ref. 4; CAA63344)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 926 AA; 105361 MW; 495C4DBCC3C05F71 CRC64;
MSTNPNPGIH QYAPSTLPRE REREGATNSP QRNLLEFLCI CVACIVCYYN STQCGLVFDD
ISAIRDNKDL RPHTPLINVF LNDFWGTPMR KEQSHKSYRP LTVLTFRFNY LLHALEPFGY
HLVNLLLHLS VCLLWRRVCR LLLRQCAASG SNAISAPSSS SVSQLNTCAF VASLLFAVHP
VHTEAVTGVV GRAELLSSIC FLAAFLSYAK SVGDSGCPRR TNWLTLFGCF GSCLLASMLC
KEQGITIAGI CVVYELFVVH QLRPLHLCHF VLRLFDERTE QQSPKLANPS GIRRWSSSTL
WKRLSFLVGI TLTLLVGRVY VMGSQLPIFT RFDNPASAAD TPERQLTYGY LIYLNCWLLL
CPSLLCCDWT MGTVPLLQGF TDSRNITTLL TFLALGAMVA KTCFTRNLAL SRTLIMCLGW
MVLPFLPASN LFFPVGFVVA ERILYMPSMG YCLLVAYGFE QLQRRGSLSW QRFSQAALAI
LLLTHALKTH QRNLDWRTEY SLFMSGVHVN QRNAKLYNNV GHALENEGKF EEALLYFQQA
VRIQTDDIGA HINVGRTFNN LKRYAEAEQA YVQAKALFPQ AKPGVSYHAR IAPNHLNVFI
NLANLIAKNQ TRLEEADHLY RQAISMRSDY VQAYINRGDI LMKLNRTAQA QEVYEQALLY
DNENADIYYN LGVVFLEQGK SQQAQVYFNK AIELYPEHEQ ALLNSAILLQ ELGGEEARRV
SRSRLYKVLE NDDQNEKVYF NLGMLAMDES SFDEAEQFFK RAIHLKADFR SALFNLALLL
ADTKRPLDAV PFLNQLIRHH PSHVKGLILL GDIYINHMKD LDEAEKCYRS ILHYDPHNTQ
GLHNLCVVFV ERKRLAKAAA CLQYAQRLAP AEDYIGRHLQ IVLARLQKIN KLPESAPERK
LAYEDYDPLE FKLPQDRPTH KSRKRS
