TMTC3_MOUSE
ID TMTC3_MOUSE Reviewed; 920 AA.
AC Q8BRH0; Q3TMN6;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 133.
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;
GN Name=Tmtc3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-753 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Transfers mannosyl residues to the hydroxyl group of serine
CC or threonine residues. The 4 members of the TMTC family are O-mannosyl-
CC transferases dedicated primarily to the cadherin superfamily, each
CC member seems to have a distinct role in decorating the cadherin domains
CC with O-linked mannose glycans at specific regions. Also acts as O-
CC mannosyl-transferase on other proteins such as PDIA3. Involved in the
CC positive regulation of proteasomal protein degradation in the
CC endoplasmic reticulum (ER), and the control of ER stress response.
CC {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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BRH0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BRH0-2; Sequence=VSP_023620, VSP_023621;
CC -!- SIMILARITY: Belongs to the TMTC family. {ECO:0000305}.
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DR EMBL; AK044857; BAC32122.1; -; mRNA.
DR EMBL; AK165838; BAE38405.1; -; mRNA.
DR EMBL; AC153501; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS24150.1; -. [Q8BRH0-2]
DR CCDS; CCDS48684.1; -. [Q8BRH0-1]
DR RefSeq; NP_001028504.1; NM_001033332.2.
DR RefSeq; NP_001103483.1; NM_001110013.1.
DR AlphaFoldDB; Q8BRH0; -.
DR SMR; Q8BRH0; -.
DR BioGRID; 231882; 4.
DR STRING; 10090.ENSMUSP00000061470; -.
DR GlyConnect; 2781; 1 N-Linked glycan (1 site).
DR GlyGen; Q8BRH0; 2 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q8BRH0; -.
DR PhosphoSitePlus; Q8BRH0; -.
DR MaxQB; Q8BRH0; -.
DR PaxDb; Q8BRH0; -.
DR PeptideAtlas; Q8BRH0; -.
DR PRIDE; Q8BRH0; -.
DR ProteomicsDB; 259052; -. [Q8BRH0-1]
DR ProteomicsDB; 259053; -. [Q8BRH0-2]
DR DNASU; 237500; -.
DR GeneID; 237500; -.
DR KEGG; mmu:237500; -.
DR CTD; 160418; -.
DR MGI; MGI:3036255; Tmtc3.
DR eggNOG; KOG1124; Eukaryota.
DR InParanoid; Q8BRH0; -.
DR OrthoDB; 1320023at2759; -.
DR PhylomeDB; Q8BRH0; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 237500; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Tmtc3; mouse.
DR PRO; PR:Q8BRH0; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8BRH0; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
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:0060447; P:bud outgrowth involved in lung branching; IMP:MGI.
DR GO; GO:0030154; P:cell differentiation; IMP:MGI.
DR GO; GO:0048286; P:lung alveolus development; IMP:MGI.
DR GO; GO:0030324; P:lung development; IMP:MGI.
DR GO; GO:0055001; P:muscle cell development; IMP:MGI.
DR GO; GO:1901800; P:positive regulation of proteasomal protein catabolic process; ISS:UniProtKB.
DR GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR GO; GO:0035269; P:protein O-linked mannosylation; ISS:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; 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; PF13174; TPR_6; 1.
DR Pfam; PF13181; TPR_8; 6.
DR SMART; SM00028; TPR; 9.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS50005; TPR; 9.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Glycoprotein; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; TPR repeat; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..920
FT /note="Protein O-mannosyl-transferase TMTC3"
FT /id="PRO_0000280294"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 326..346
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 359..379
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 382..402
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 417..450
FT /note="TPR 1"
FT REPEAT 451..484
FT /note="TPR 2"
FT REPEAT 486..518
FT /note="TPR 3"
FT REPEAT 533..567
FT /note="TPR 4"
FT REPEAT 568..601
FT /note="TPR 5"
FT REPEAT 602..635
FT /note="TPR 6"
FT REPEAT 673..706
FT /note="TPR 7"
FT REPEAT 708..740
FT /note="TPR 8"
FT REPEAT 741..775
FT /note="TPR 9"
FT REPEAT 777..809
FT /note="TPR 10"
FT REGION 829..897
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 839..858
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 861..883
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 508
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZXV5"
FT CARBOHYD 499
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 651..658
FT /note="EVKLRPEA -> KFPENVSI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023620"
FT VAR_SEQ 659..920
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023621"
FT CONFLICT 501
FT /note="S -> T (in Ref. 1; BAE38405)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 920 AA; 104198 MW; EAEE8BD242C5EC3C CRC64;
MLEGKMADIN FKEVTLIVSV VAACYWNSLF CGFVFDDVSA ILDNKDLHPS TPLKTLFQND
FWGTPMSEER SHKSYRPLTV LTFRLNYLLS ELKPMSYHLL NTVFHAVVSV IFLKVCRLFL
DKRSSMIAAL LFAVHPIHTE AVTGVVGRAE LLSSVFFLAA FLSYTKSKGP DNSIVWTPIV
LTVFLVAVAT LCKEQGITVV GICCVYEVFV AQGYTLPMLC TVAGQFLRGK GSIPLSMLQT
LVKLIVLMLS TLLLVVVRVQ VIQSQLPVFT RFDNPAAVSP TPTRQLTFNY LLPVNAWLLL
NPSELCCDWT MGTIPLIESF LDVRNLATFA FFCFLGALGI FSLRYPGDSS KTVLMALCLM
ALPFIPASNL FFPVGFVVAE RVLYVPSMGF CILVAHGWQK ISNKSVLKKL SWVCLSMVIL
THALKTLHRN WDWESEYTLF MSALKVNKNN AKLWNNVGHA LENEKNFEKA LKYFLQATHV
QPDDIGAHMN VGRTYKNLNR SREAEASYML AKSLMPQIIP GKKYAARIAP NHLNVYINLA
NLIRANESRL EEADQLYRQA ISMRPDFKQA YISRGELLLK MNKPLKAKEA YLKALELDRN
NADLWYNLAI VYIELKEPNE ALKNFNRALE LNPKHKLALF NSAILMQESG EVKLRPEARK
RLLNYVNEEP QDANGYFNLG MLAMDDKKDS EAESWMKKAI KLQPDFRSAL FNLALLYSQT
AKELKALPIL EELLKYYPDH TKGLILKGDI LMNQKKDIPG AKKCFEKILE MDPSNVQGKH
NLCVVYFEEK ELLKAERCLV ETLALAPHEE YIQRHLSIVR DRISSSGIVE QPLAPADKTP
GTEEREEIPS EDVKEISSES RPPQILKTNN NRNSKSNKQS TENADQDAPH KTTKDIKEIE
KKRVAALKRL EEIERILNGE
