TRDN_RAT
ID TRDN_RAT Reviewed; 687 AA.
AC Q9QX75; E9PTN7; Q5DVI6; Q5DVI7; Q9JKZ5; Q9JKZ6; Q9QX76;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Triadin;
GN Name=Trdn {ECO:0000312|RGD:619856};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000312|EMBL:CAB64604.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING,
RP GLYCOSYLATION, AND TISSUE SPECIFICITY.
RC STRAIN=Wistar; TISSUE=Skeletal muscle;
RX PubMed=10713145; DOI=10.1074/jbc.275.11.8206;
RA Marty I., Thevenon D., Scotto C., Groh S., Sainnier S., Robert M.,
RA Grunwald D., Villaz M.;
RT "Cloning and characterization of a new isoform of skeletal muscle
RT triadin.";
RL J. Biol. Chem. 275:8206-8212(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), ALTERNATIVE SPLICING,
RP SUBCELLULAR LOCATION, INTERACTION WITH RYR1, AND TISSUE SPECIFICITY.
RC STRAIN=Wistar {ECO:0000312|EMBL:CAH23274.1};
RX PubMed=15927957; DOI=10.1074/jbc.m501484200;
RA Vassilopoulos S., Thevenon D., Smida Rezgui S., Urbani-Brocard J.,
RA Chapel A., Lacampagne A., Lunardi J., Dewaard M., Marty I.;
RT "Triadins are not triad-specific proteins: two new skeletal muscle triadins
RT possibly involved in the architecture of sarcoplasmic reticulum.";
RL J. Biol. Chem. 280:28601-28609(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE [MRNA] OF
RP 1-310 (ISOFORM 1/2/4).
RC STRAIN=Wistar {ECO:0000312|EMBL:AAF29539.1};
RC TISSUE=Heart {ECO:0000312|EMBL:AAF29539.1};
RA You H.J., Kim D.H.;
RT "Study of molecular characterization and subcellular localization of
RT cardiac triadin in rat.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303 AND SER-306, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(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. Plays a role in
CC excitation-contraction coupling in the heart and in regulating the rate
CC of heart beats. {ECO:0000250|UniProtKB:E9Q9K5}.
CC -!- SUBUNIT: Homooligomer of variable subunit number; disulfide-linked.
CC Interacts with CASQ1 in skeletal muscle. Interacts with CASQ2 (By
CC similarity). Interacts with RYR1 in skeletal muscle.
CC {ECO:0000250|UniProtKB:Q13061, ECO:0000250|UniProtKB:Q28820,
CC ECO:0000269|PubMed:15927957}.
CC -!- SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q28820}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q28820}. Microsome
CC {ECO:0000269|PubMed:15927957}. Cell membrane, sarcolemma
CC {ECO:0000269|PubMed:15927957}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=Triadin 95kDa, Trisk 95 {ECO:0000303|PubMed:10713145};
CC IsoId=Q9QX75-1; Sequence=Displayed;
CC Name=2; Synonyms=Triadin 51 kDa, Trisk 51
CC {ECO:0000303|PubMed:10713145};
CC IsoId=Q9QX75-2; Sequence=VSP_056806, VSP_056807;
CC Name=3; Synonyms=Triadin 32 kDa, Trisk 32
CC {ECO:0000303|PubMed:15927957};
CC IsoId=Q9QX75-3; Sequence=VSP_056802, VSP_056803;
CC Name=4; Synonyms=Triadin 49 kDa, Trisk 49
CC {ECO:0000303|PubMed:15927957};
CC IsoId=Q9QX75-4; Sequence=VSP_056804, VSP_056805;
CC -!- TISSUE SPECIFICITY: Detected in skeletal muscle (at protein level).
CC Detected in skeletal muscle. {ECO:0000269|PubMed:10713145,
CC ECO:0000269|PubMed:15927957}.
CC -!- PTM: Phosphorylated by CaMK2. {ECO:0000250|UniProtKB:Q28820}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:10713145}.
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; AJ243303; CAB64603.1; -; mRNA.
DR EMBL; AJ243304; CAB64604.1; -; mRNA.
DR EMBL; AJ812275; CAH23273.1; -; mRNA.
DR EMBL; AJ812276; CAH23274.1; -; mRNA.
DR EMBL; AF220558; AAF29539.1; -; mRNA.
DR EMBL; AF220559; AAF29540.1; -; mRNA.
DR EMBL; AABR06001232; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06001233; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06001234; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06001235; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06001236; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06001237; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06001238; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06001239; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06001240; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06001241; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06001242; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06001243; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH474002; EDL87717.1; -; Genomic_DNA.
DR RefSeq; NP_067698.1; NM_021666.2. [Q9QX75-1]
DR AlphaFoldDB; Q9QX75; -.
DR STRING; 10116.ENSRNOP00000041570; -.
DR GlyGen; Q9QX75; 1 site.
DR iPTMnet; Q9QX75; -.
DR PhosphoSitePlus; Q9QX75; -.
DR PaxDb; Q9QX75; -.
DR PRIDE; Q9QX75; -.
DR GeneID; 59299; -.
DR KEGG; rno:59299; -.
DR UCSC; RGD:619856; rat.
DR CTD; 10345; -.
DR RGD; 619856; Trdn.
DR VEuPathDB; HostDB:ENSRNOG00000012609; -.
DR eggNOG; ENOG502S0X4; Eukaryota.
DR OrthoDB; 1200049at2759; -.
DR TreeFam; TF350396; -.
DR Reactome; R-RNO-2672351; Stimuli-sensing channels.
DR Reactome; R-RNO-5578775; Ion homeostasis.
DR PRO; PR:Q9QX75; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Proteomes; UP000234681; Chromosome 1.
DR Bgee; ENSRNOG00000012609; Expressed in quadriceps femoris and 17 other tissues.
DR ExpressionAtlas; Q9QX75; baseline and differential.
DR GO; GO:0034704; C:calcium channel complex; IGI:BHF-UCL.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0030314; C:junctional membrane complex; IDA:RGD.
DR GO; GO:0014701; C:junctional sarcoplasmic reticulum membrane; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR GO; GO:0016529; C:sarcoplasmic reticulum; IDA:RGD.
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; IMP:RGD.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IMP:RGD.
DR GO; GO:0090158; P:endoplasmic reticulum membrane organization; IMP:RGD.
DR GO; GO:0060047; P:heart contraction; ISO:RGD.
DR GO; GO:0014902; P:myotube differentiation; IEP:RGD.
DR GO; GO:0051280; P:negative regulation of release of sequestered calcium ion into cytosol; IMP:RGD.
DR GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; IMP:RGD.
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; IMP:RGD.
DR GO; GO:0014808; P:release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; ISO:RGD.
DR GO; GO:0009617; P:response to bacterium; ISO:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
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; Cell membrane; Disulfide bond; Endoplasmic reticulum;
KW Glycoprotein; Membrane; Microsome; Phosphoprotein; Reference proteome;
KW Sarcoplasmic reticulum; Transmembrane; Transmembrane helix.
FT CHAIN 1..687
FT /note="Triadin"
FT /id="PRO_0000430563"
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..687
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 117..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..687
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..265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..356
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..506
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..584
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..634
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 303
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 514
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 270
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:Q28820"
FT DISULFID 649
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:Q28820"
FT VAR_SEQ 265..287
FT /note="DQYAFCRYMIDMFVHGDLKPGQS -> GKLSKEEKEAVGGPKRILDKKQI
FT (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_056802"
FT VAR_SEQ 288..687
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_056803"
FT VAR_SEQ 439..442
FT /note="ALHG -> GKHS (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_056804"
FT VAR_SEQ 443..687
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_056805"
FT VAR_SEQ 456..461
FT /note="DVKPKL -> KKSEAG (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_056806"
FT VAR_SEQ 462..687
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_056807"
FT CONFLICT 95
FT /note="A -> V (in Ref. 1; CAB64603, 2; CAH23274/CAH23273
FT and 3; AAF29540)"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="E -> D (in Ref. 1; CAB64603, 2; CAH23274/CAH23273
FT and 3; AAF29540)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 687 AA; 77200 MW; 52C52CF9410DDCE7 CRC64;
MTEITAEGNA SITTTVIDNK NGSVPKSPGK VLKRTVTEDI VTTFSSPAAW LLVIALIITW
SAVAIVMFDL VDYKNFSASS IAKIGSDPLK LVNDAVEETT DWIYGFFSLL SDIISSDGDE
DDEDADEDID KGEIEEPPLK RKEIQKEKAE KQEKPEKKIQ TKVSHREKEK GKEKLKGEKP
EKKATHKEKL EKKERTETKM AAKEDKKIKT KEKTEEKAKK EMKVGKQEKA KPAAAKAKET
PKTTPKAREK DDKETPAVPK HEQKDQYAFC RYMIDMFVHG DLKPGQSPAV PPPSLTASRP
ALSTPSLEEK EKEEKKKVEK KVTSDTKKKE KGEAKKKSEK ETVIDGKGKE PGKPPETKQT
TTKLTTQAAA TKDEKKEDSK KMKKPPEEKP KGKKQEKKEK HIEPAKTPKK EHPAPSEKHR
KAKAEQAKEE IAPASTKKAL HGKKEEKAKT VEQGKDVKPK LPQPQLKKEE KSEPQPKKEV
KLETQLKKEE KSEPQVKKEA KLASSEKGQT RKQNITRPEQ VIPHGKPEQK VPKQIKAITA
EKTEKAERQE KYHPSIKTEG KPEVTDSGKK KIEKPEKESK VPPKQENLQV RNVTRAEKRG
KISKDSKDAP APKKDKDSKD VLHSKKDKEV TNNVSSPKKQ KSPISFFQCV YLDGYNGYGF
QFPVTPVQHS GENPGKSNSP GQKQQEQ
