TMTC2_MOUSE
ID TMTC2_MOUSE Reviewed; 836 AA.
AC Q56A06; B2RRD8; Q5U620; Q8C787;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Protein O-mannosyl-transferase TMTC2;
DE EC=2.4.1.109;
DE AltName: Full=Transmembrane and TPR repeat-containing protein 2;
GN Name=Tmtc2;
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).
RC STRAIN=C57BL/6J; TISSUE=Heart;
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 MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and Czech II; TISSUE=Brain, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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: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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q56A06-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q56A06-2; Sequence=VSP_023628, VSP_023629;
CC -!- SIMILARITY: Belongs to the TMTC family. {ECO:0000305}.
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DR EMBL; AK052344; BAC34946.1; -; mRNA.
DR EMBL; BC034657; AAH34657.1; -; mRNA.
DR EMBL; BC092226; AAH92226.1; -; mRNA.
DR EMBL; BC138362; AAI38363.1; -; mRNA.
DR EMBL; BC138363; AAI38364.1; -; mRNA.
DR CCDS; CCDS24157.1; -. [Q56A06-1]
DR RefSeq; NP_796342.2; NM_177368.4. [Q56A06-1]
DR AlphaFoldDB; Q56A06; -.
DR SMR; Q56A06; -.
DR STRING; 10090.ENSMUSP00000061919; -.
DR TCDB; 8.A.95.1.3; the transmembrane and tpr repeat-containing protein 3 (tmtc3) family.
DR GlyGen; Q56A06; 1 site.
DR iPTMnet; Q56A06; -.
DR PhosphoSitePlus; Q56A06; -.
DR MaxQB; Q56A06; -.
DR PaxDb; Q56A06; -.
DR PRIDE; Q56A06; -.
DR ProteomicsDB; 260713; -. [Q56A06-1]
DR ProteomicsDB; 260714; -. [Q56A06-2]
DR Antibodypedia; 29839; 51 antibodies from 16 providers.
DR Ensembl; ENSMUST00000061506; ENSMUSP00000061919; ENSMUSG00000036019. [Q56A06-1]
DR GeneID; 278279; -.
DR KEGG; mmu:278279; -.
DR UCSC; uc007gym.1; mouse. [Q56A06-1]
DR UCSC; uc007gyn.1; mouse. [Q56A06-2]
DR CTD; 160335; -.
DR MGI; MGI:1914057; Tmtc2.
DR VEuPathDB; HostDB:ENSMUSG00000036019; -.
DR eggNOG; KOG1124; Eukaryota.
DR GeneTree; ENSGT00940000156144; -.
DR HOGENOM; CLU_011615_4_0_1; -.
DR InParanoid; Q56A06; -.
DR OMA; DYTCLFC; -.
DR OrthoDB; 1320023at2759; -.
DR PhylomeDB; Q56A06; -.
DR TreeFam; TF328339; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 278279; 0 hits in 75 CRISPR screens.
DR ChiTaRS; Tmtc2; mouse.
DR PRO; PR:Q56A06; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q56A06; protein.
DR Bgee; ENSMUSG00000036019; Expressed in manus and 241 other tissues.
DR Genevisible; Q56A06; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; 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:0055074; P:calcium ion homeostasis; 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; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF08409; DUF1736; 1.
DR Pfam; PF00515; TPR_1; 1.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00028; TPR; 9.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS50005; TPR; 9.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Endoplasmic reticulum; Glycoprotein; Membrane;
KW Reference proteome; Repeat; TPR repeat; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..836
FT /note="Protein O-mannosyl-transferase TMTC2"
FT /id="PRO_0000280304"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 313..333
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 400..420
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 423..443
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 450..470
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 460..492
FT /note="TPR 1"
FT REPEAT 493..526
FT /note="TPR 2"
FT REPEAT 527..560
FT /note="TPR 3"
FT REPEAT 562..594
FT /note="TPR 4"
FT REPEAT 606..639
FT /note="TPR 5"
FT REPEAT 643..676
FT /note="TPR 6"
FT REPEAT 677..710
FT /note="TPR 7"
FT REPEAT 712..744
FT /note="TPR 8"
FT REPEAT 746..778
FT /note="TPR 9"
FT REPEAT 779..812
FT /note="TPR 10"
FT CARBOHYD 221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 719..721
FT /note="QFL -> EWR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023628"
FT VAR_SEQ 722..836
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023629"
SQ SEQUENCE 836 AA; 94176 MW; 57E5A7AF66F8568A CRC64;
MIAELVSSAL GLALYLNTLS ADFCYDDSRA IKTNQDLLPE TPWTHIFYND FWGTLLTHSG
SHKSYRPLCT LSFRLNHAIG GLNPWSYHLV NVLLHAAVTG LFTRFSKALL GDGYWTFMAG
LMFASHPIHT EAVAGIVGRA DVGASLFFLL SLLCYIKHCS TRGYSARTWG WFLGTGLCAG
CSMLWKEQGV TVLAVSAVYD VFVFHRLKMK QILPTIYKRK NLSLFLSISL LTFWGTCLLG
ARLYWMGNKP PSFSNSDNPA ADSDSLLART LTFLYLPTKN LWLLLCPDTL SFDWSMDAVP
LLKTVCDWRN LHTVAFYSGL LLLAYCGLKN PSLEGECNGK ALTNGKQNAN GHSCHSDVEY
RNSEMKPSFA SKVENGIKNC VPQRTQLPST ENIVILSLSL LIIPFIPATN LFFYVGFVIA
ERVLYIPSMG FCLLITVGAR ALYVKVQKRF LKSLVFYATA TLIVFYGVKT AIRNGDWQNE
EMLYRSGIKV NPAKAWGNLG NVLKSQSKIS EAESAYRNAL FYRSNMADML YNLGLLLQEN
SRFAEALHYY KLAIGSRPTL ASAYLNTGII LMNQGKTEEA RRTFLKCSEI PDENLKDPHA
HKSSVTSCLY NLGKLYHEQG RYEEALSVYR EAIQKMPRHF APQSLYNMMG EAYMRLSKLP
EAEHWYMESL RSKTDHIPAH LTYGKLLALT GRKSEAEKFF LKAIELDPTK GNCYMHYGQF
LLEESRLTEA AEMAKKAAEL DNTEFDVVFN AAHMLRQASL NEAAEKYYDL AARLRPNYPA
ALMNLGAILH LNGRLQKAEA NYLRALQLKP DDVITQSNLR KLWNIMEKQG LKTSKT
