TMTC1_MOUSE
ID TMTC1_MOUSE Reviewed; 942 AA.
AC Q3UV71; E9QM13; Q8BQV5;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 117.
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 1 {ECO:0000312|MGI:MGI:3039590};
GN Name=Tmtc1 {ECO:0000312|MGI:MGI:3039590};
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Bone, and Corpora quadrigemina;
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).
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.
CC {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 -!- SUBUNIT: May interact with FAM168B. {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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3UV71-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UV71-2; Sequence=VSP_023618;
CC -!- SIMILARITY: Belongs to the TMTC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC32703.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK046396; BAC32703.1; ALT_FRAME; mRNA.
DR EMBL; AK137545; BAE23402.1; -; mRNA.
DR EMBL; AC126683; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC142274; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS51960.1; -. [Q3UV71-1]
DR CCDS; CCDS85189.1; -. [Q3UV71-2]
DR RefSeq; NP_001334447.1; NM_001347518.1. [Q3UV71-2]
DR RefSeq; NP_945318.2; NM_198967.5. [Q3UV71-1]
DR AlphaFoldDB; Q3UV71; -.
DR SMR; Q3UV71; -.
DR BioGRID; 239881; 1.
DR STRING; 10090.ENSMUSP00000056353; -.
DR iPTMnet; Q3UV71; -.
DR PhosphoSitePlus; Q3UV71; -.
DR MaxQB; Q3UV71; -.
DR PaxDb; Q3UV71; -.
DR PRIDE; Q3UV71; -.
DR ProteomicsDB; 259050; -. [Q3UV71-1]
DR ProteomicsDB; 259051; -. [Q3UV71-2]
DR Antibodypedia; 12772; 93 antibodies from 21 providers.
DR DNASU; 387314; -.
DR Ensembl; ENSMUST00000060095; ENSMUSP00000056353; ENSMUSG00000030306. [Q3UV71-1]
DR Ensembl; ENSMUST00000100772; ENSMUSP00000098335; ENSMUSG00000030306. [Q3UV71-2]
DR GeneID; 387314; -.
DR KEGG; mmu:387314; -.
DR UCSC; uc009eti.2; mouse. [Q3UV71-2]
DR UCSC; uc009etj.2; mouse. [Q3UV71-1]
DR CTD; 83857; -.
DR MGI; MGI:3039590; Tmtc1.
DR VEuPathDB; HostDB:ENSMUSG00000030306; -.
DR eggNOG; KOG1124; Eukaryota.
DR GeneTree; ENSGT00940000158027; -.
DR HOGENOM; CLU_011615_1_1_1; -.
DR InParanoid; Q3UV71; -.
DR OMA; YANFLMD; -.
DR OrthoDB; 1320023at2759; -.
DR PhylomeDB; Q3UV71; -.
DR TreeFam; TF328339; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 387314; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Tmtc1; mouse.
DR PRO; PR:Q3UV71; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q3UV71; protein.
DR Bgee; ENSMUSG00000030306; Expressed in secondary oocyte and 204 other tissues.
DR ExpressionAtlas; Q3UV71; baseline and differential.
DR Genevisible; Q3UV71; MM.
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:0005739; C:mitochondrion; HDA:MGI.
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 GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR Gene3D; 1.25.40.10; -; 4.
DR InterPro; IPR003107; HAT.
DR InterPro; IPR013618; TMTC_DUF1736.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF08409; DUF1736; 1.
DR SMART; SM00386; HAT; 4.
DR SMART; SM00028; TPR; 11.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS50005; TPR; 10.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Endoplasmic reticulum; Membrane; Reference proteome;
KW Repeat; TPR repeat; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..942
FT /note="Protein O-mannosyl-transferase TMTC1"
FT /id="PRO_0000280289"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 332..352
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 374..394
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 415..435
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 442..462
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 464..484
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 499..519
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 543..576
FT /note="TPR 1"
FT REPEAT 577..607
FT /note="TPR 2"
FT REPEAT 608..641
FT /note="TPR 3"
FT REPEAT 642..675
FT /note="TPR 4"
FT REPEAT 676..709
FT /note="TPR 5"
FT REPEAT 710..742
FT /note="TPR 6"
FT REPEAT 743..776
FT /note="TPR 7"
FT REPEAT 811..844
FT /note="TPR 8"
FT REPEAT 849..882
FT /note="TPR 9"
FT REPEAT 883..916
FT /note="TPR 10"
FT REGION 245..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 534..571
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023618"
FT CONFLICT 171
FT /note="A -> P (in Ref. 1; BAC32703)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="P -> T (in Ref. 1; BAE23402)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 942 AA; 105811 MW; 19BB548FC43A4339 CRC64;
MLVTRGDRGG GERAPSRRPR CGLVPAGAAA LLAGASCLCY GRSLRGEFVH DDVWAIVNNP
DVRPGTPLRW AIFANDFWGK GLADSTSHKS YRPLCVLSFR LNIFLTGMNP FYFHAVNVIL
HCLVTLVLMY TCDKTVFKNR GLAFVTALLF AVHPVHTEAV AGIVGRADVL ACLLFLLAFL
SYQRSLDQGC AGQCFPTTAS PFFLLLSLFL GTCAMLVKET GITVFGVCLV YDLFSPSHKQ
DKLSNGAVCQ HSSGQPGSPQ PSSQQAHPHR ESRKQRFPHK DSWGGCHSPL PPEPKSSGFP
MSPRAMWSLM RCLTGSTNRN FLLTLRPFLK RAILVISYVT VILYFRLWIM GGTMPLFSEQ
DNPASFSPYI LTRFLTYSYL LAFNVWLLLA PITLCYDWQV GSIPLVETIW DVRNLATILL
AVVMALLSLH CVAAFKRLEH KEVLAGLLFL VFPFIPASNL FFRVGFVVAE RVLYMPSMGY
CILFVHGLSK LCAGLSRCGA TSLMASTVLL LLLFSWKTVK QNEIWLSRES LFRSGVQTLP
HNAKVHYNYA NFLKDQGRNK EAIYHYRTAL KLYPRHASAL NNLGTLTKDM AEAKMYYQKA
LQLHPQHNRA LFNLGNLLKS QEKTEEAIML LKESIKYGPD FADAYSSLAS LLAEQERFKE
AEDIYQAGIK NCPDSSDLHN NYAVFLVDSG FPEKAVAHYQ QAIQLSPSHH VAVVNLGRLY
RSLGENSKAE EWYRRALKVA RTAEVLSPLG ALYYNTGRHK EALEVYREAV SLQPSQRELR
LALAQVLAVM GQTKEAEKIT SHIVSEEPRC LECYRLLSAI HSKQEHHGKA LEAIEKALQL
KPKDPKVISE LFFTKGNQLR EQNLLDKAFE SYEAAVTLDP DQAQAWMNMG GIRHIQGSYV
SARAYYERAL KLVPDSKLLK ENLAKLDRLE RRLQEVRERD QT
