TRDN_MOUSE
ID TRDN_MOUSE Reviewed; 693 AA.
AC E9Q9K5; Q8VIN7; Q8VIN8; Q8VIN9; Q9CV36;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Triadin;
GN Name=Trdn {ECO:0000312|MGI:MGI:1924007};
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 {ECO:0000312|Ensembl:ENSMUSP00000093436};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Heart;
RX PubMed=11707337; DOI=10.1016/s0378-1119(01)00718-1;
RA Hong C.-S., Ji J.H., Kim J.P., Jung D.H., Kim D.H.;
RT "Molecular cloning and characterization of mouse cardiac triadin
RT isoforms.";
RL Gene 278:193-199(2001).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-190.
RC STRAIN=C57BL/6J; TISSUE=Tongue;
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 [4]
RP DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY, AND ALTERNATIVE
RP SPLICING.
RX PubMed=19843516; DOI=10.1074/jbc.m109.022442;
RA Oddoux S., Brocard J., Schweitzer A., Szentesi P., Giannesini B.,
RA Brocard J., Faure J., Pernet-Gallay K., Bendahan D., Lunardi J.,
RA Csernoch L., Marty I.;
RT "Triadin deletion induces impaired skeletal muscle function.";
RL J. Biol. Chem. 284:34918-34929(2009).
RN [5]
RP DISRUPTION PHENOTYPE, FUNCTION, GLYCOSYLATION, AND TISSUE SPECIFICITY.
RX PubMed=19383796; DOI=10.1073/pnas.0902919106;
RA Chopra N., Yang T., Asghari P., Moore E.D., Huke S., Akin B.,
RA Cattolica R.A., Perez C.F., Hlaing T., Knollmann-Ritschel B.E., Jones L.R.,
RA Pessah I.N., Allen P.D., Franzini-Armstrong C., Knollmann B.C.;
RT "Ablation of triadin causes loss of cardiac Ca2+ release units, impaired
RT excitation-contraction coupling, and cardiac arrhythmias.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:7636-7641(2009).
RN [6]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=22768324; DOI=10.1371/journal.pone.0039962;
RA Boncompagni S., Thomas M., Lopez J.R., Allen P.D., Yuan Q., Kranias E.G.,
RA Franzini-Armstrong C., Perez C.F.;
RT "Triadin/junctin double null mouse reveals a differential role for triadin
RT and junctin in anchoring CASQ to the jSR and regulating Ca(2+)
RT homeostasis.";
RL PLoS ONE 7:E39962-E39962(2012).
CC -!- FUNCTION: Contributes to the regulation of lumenal Ca2+ release via the
CC sarcoplasmic reticulum calcium release channels RYR1 and RYR2, a key
CC step in triggering skeletal and heart muscle contraction. Required for
CC normal organization of the triad junction, where T-tubules and the
CC sarcoplasmic reticulum terminal cisternae are in close contact.
CC Required for normal skeletal muscle strength (PubMed:19843516). Plays a
CC role in excitation-contraction coupling in the heart and in regulating
CC the rate of heart beats. {ECO:0000269|PubMed:19383796,
CC ECO:0000269|PubMed:19843516, ECO:0000269|PubMed:22768324}.
CC -!- SUBUNIT: Homooligomer of variable subunit number; disulfide-linked.
CC Interacts with CASQ1 and RYR1 in skeletal muscle. Interacts with CASQ2.
CC {ECO:0000250|UniProtKB:Q13061, ECO:0000250|UniProtKB:Q28820}.
CC -!- SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane
CC {ECO:0000269|PubMed:11707337}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q28820}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=E9Q9K5-1; Sequence=Displayed;
CC Name=2; Synonyms=Cardiac triadin 1;
CC IsoId=E9Q9K5-2; Sequence=VSP_056796, VSP_056797;
CC Name=3; Synonyms=Cardiac triadin 2;
CC IsoId=E9Q9K5-3; Sequence=VSP_056798, VSP_056799;
CC Name=4; Synonyms=Cardiac triadin 3, Trisk 32;
CC IsoId=E9Q9K5-4; Sequence=VSP_056795, VSP_056800, VSP_056801;
CC -!- TISSUE SPECIFICITY: Detected in heart (at protein level). Detected in
CC heart. {ECO:0000269|PubMed:11707337, ECO:0000269|PubMed:19383796,
CC ECO:0000269|PubMed:19843516}.
CC -!- PTM: Phosphorylated by CaMK2. {ECO:0000250|UniProtKB:Q28820}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:19383796}.
CC -!- DISRUPTION PHENOTYPE: Mice appear normal; they are viable and fertile
CC but have reduced muscular strength, due to defects in the structure of
CC the triad junction, where T-tubules and the sarcoplasmic reticulum
CC terminal cisternae are in close contact. In mutant mice, about 25% of
CC the triads are in oblique or longitudinal orientation, instead of the
CC normal transversal orientation (PubMed:19843516). Similar structural
CC defects are seen in the heart, leading to impaired excitation-
CC contraction coupling. Mutant mice are subject to stress-induced
CC ventricular tachycardia (PubMed:19383796).
CC {ECO:0000269|PubMed:19383796, ECO:0000269|PubMed:19843516,
CC ECO:0000269|PubMed:22768324}.
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DR EMBL; AF223415; AAL33876.1; -; mRNA.
DR EMBL; AF223416; AAL33877.1; -; mRNA.
DR EMBL; AF223417; AAL33878.1; -; mRNA.
DR EMBL; AC109214; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC153965; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC153966; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC157017; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK009816; BAB26520.1; -; mRNA.
DR CCDS; CCDS48532.1; -. [E9Q9K5-1]
DR CCDS; CCDS87985.1; -. [E9Q9K5-3]
DR CCDS; CCDS87986.1; -. [E9Q9K5-2]
DR RefSeq; NP_084002.2; NM_029726.2. [E9Q9K5-1]
DR AlphaFoldDB; E9Q9K5; -.
DR BioGRID; 218297; 4.
DR IntAct; E9Q9K5; 1.
DR STRING; 10090.ENSMUSP00000093436; -.
DR GlyGen; E9Q9K5; 2 sites.
DR iPTMnet; E9Q9K5; -.
DR PhosphoSitePlus; E9Q9K5; -.
DR MaxQB; E9Q9K5; -.
DR PaxDb; E9Q9K5; -.
DR PRIDE; E9Q9K5; -.
DR ProteomicsDB; 259306; -. [E9Q9K5-1]
DR ProteomicsDB; 259307; -. [E9Q9K5-2]
DR ProteomicsDB; 259308; -. [E9Q9K5-3]
DR ProteomicsDB; 259309; -. [E9Q9K5-4]
DR Antibodypedia; 51878; 47 antibodies from 12 providers.
DR DNASU; 76757; -.
DR Ensembl; ENSMUST00000095762; ENSMUSP00000093436; ENSMUSG00000019787. [E9Q9K5-1]
DR Ensembl; ENSMUST00000217779; ENSMUSP00000151583; ENSMUSG00000019787. [E9Q9K5-3]
DR Ensembl; ENSMUST00000219931; ENSMUSP00000151999; ENSMUSG00000019787. [E9Q9K5-4]
DR Ensembl; ENSMUST00000219982; ENSMUSP00000152042; ENSMUSG00000019787. [E9Q9K5-2]
DR GeneID; 76757; -.
DR KEGG; mmu:76757; -.
DR UCSC; uc007etz.2; mouse. [E9Q9K5-2]
DR UCSC; uc007eua.2; mouse. [E9Q9K5-3]
DR UCSC; uc007eub.2; mouse. [E9Q9K5-4]
DR UCSC; uc011xcl.1; mouse. [E9Q9K5-1]
DR CTD; 10345; -.
DR MGI; MGI:1924007; Trdn.
DR VEuPathDB; HostDB:ENSMUSG00000019787; -.
DR eggNOG; ENOG502S0X4; Eukaryota.
DR GeneTree; ENSGT00510000049207; -.
DR HOGENOM; CLU_023557_0_0_1; -.
DR InParanoid; E9Q9K5; -.
DR OMA; EKADMKH; -.
DR OrthoDB; 1200049at2759; -.
DR TreeFam; TF350396; -.
DR Reactome; R-MMU-2672351; Stimuli-sensing channels.
DR Reactome; R-MMU-5578775; Ion homeostasis.
DR BioGRID-ORCS; 76757; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Trdn; mouse.
DR PRO; PR:E9Q9K5; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; E9Q9K5; protein.
DR Bgee; ENSMUSG00000019787; Expressed in tarsal region and 103 other tissues.
DR ExpressionAtlas; E9Q9K5; baseline and differential.
DR Genevisible; E9Q9K5; MM.
DR GO; GO:0034704; C:calcium channel complex; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0030314; C:junctional membrane complex; ISO:MGI.
DR GO; GO:0014701; C:junctional sarcoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0016020; C:membrane; TAS:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0016529; C:sarcoplasmic reticulum; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR GO; GO:0044325; F:transmembrane transporter binding; IBA:GO_Central.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; ISO:MGI.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; ISO:MGI.
DR GO; GO:0090158; P:endoplasmic reticulum membrane organization; ISO:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0060047; P:heart contraction; IMP:BHF-UCL.
DR GO; GO:0051280; P:negative regulation of release of sequestered calcium ion into cytosol; ISO:MGI.
DR GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; ISO:MGI.
DR GO; GO:0060316; P:positive regulation of ryanodine-sensitive calcium-release channel activity; IBA:GO_Central.
DR GO; GO:0086036; P:regulation of cardiac muscle cell membrane potential; IBA:GO_Central.
DR GO; GO:0010880; P:regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; ISO:MGI.
DR GO; GO:0014808; P:release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; IMP:MGI.
DR GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR InterPro; IPR007943; Asp-B-hydro/Triadin_dom.
DR InterPro; IPR010798; Triadin.
DR PANTHER; PTHR14106; PTHR14106; 3.
DR Pfam; PF05279; Asp-B-Hydro_N; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Membrane;
KW Phosphoprotein; Reference proteome; Sarcoplasmic reticulum; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..693
FT /note="Triadin"
FT /id="PRO_0000430562"
FT TOPO_DOM 1..47
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 48..68
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 69..693
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 117..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 666..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..132
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..352
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..507
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..576
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..642
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..693
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QX75"
FT CARBOHYD 515
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 584
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 268
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:Q28820"
FT DISULFID 655
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:Q28820"
FT VAR_SEQ 263..282
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_056795"
FT VAR_SEQ 263..277
FT /note="DQYAFCRYMIDMFVH -> GKHSRRRRQQEVQRE (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_056796"
FT VAR_SEQ 278..693
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_056797"
FT VAR_SEQ 284..293
FT /note="QSPVMPPPSL -> IPNNSYCCLS (in isoform 3)"
FT /id="VSP_056798"
FT VAR_SEQ 294..693
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_056799"
FT VAR_SEQ 307..325
FT /note="EKEKEEKKKMEKKDTSDTK -> GKYLVLWCFLPHKYFHYIF (in
FT isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_056800"
FT VAR_SEQ 326..693
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_056801"
FT CONFLICT 34
FT /note="R -> K (in Ref. 1; AAL33876/AAL33877/AAL33878)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 693 AA; 77844 MW; 6DD93304D5509F62 CRC64;
MTEITAEGNA STTTTVIDNK NGCIPKSPGK VLKRSVTEDI VTTFSSPAAW LLVIALIITW
SAVAIVMFDL VDYKNFSASS IAKIGSDPLK LVNDAVEETT DWIYGFFSLL SDIISSEGDE
DDEDADEDID KGEIEEPPLK RKEIHQEKAE KEEKPEKKIQ TKASHREREK GKEKLKGEKP
EKTATHKEKL EKKERPETKM MAKEDKKIKT KEKTEEKAKK EMKVGKQEKV KPTAAKAKET
PKTPPKARKK DDKEMPAVHE QKDQYAFCRY MIDMFVHGDL KPGQSPVMPP PSLTPSKPAL
STTALEEKEK EEKKKMEKKD TSDTKKKEKE VKKKSEETTI DGKGKEPGKP PETKQMTAKL
TTQAAARKDE KKEESKKMRK PTEEQPKGKK QEKKEKHIEP AKTPKKEHPG PSEKLKKAKA
EQAKEEIAAA STKKALHGKK EEKAKTVEQE VKKEKSGKSS SDLKDKEVKK EKSGKSSSDL
KDKEPQLKNE EKSKPQVKKE AKLASSDKGQ TRKQNITRPE QVIPHVKPEK AEHQEKGHPS
IKKDKPKPSS KGAPEVPDSG KKKIEKSEKE SKVPTREENL QVYNVTKAEK PGKIPKDSKE
APASKKDKED SKEAPTSKKD KEDSKDVPHS KKDKEVTDDV SSPKKQTRPI SFFQCVYLNG
YNGYGFQFPV TPVQQPGENP GKTNSPGQKQ QEQ
