TRDN_CANLF
ID TRDN_CANLF Reviewed; 701 AA.
AC P82179;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Triadin;
GN Name=TRDN;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS SKELETAL; CARDIAC 1 AND CARDIAC 3),
RP ALTERNATIVE SPLICING, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, TOPOLOGY,
RP GLYCOSYLATION AT ASN-75, AND MUTAGENESIS OF ASN-75.
RC TISSUE=Heart, and Skeletal muscle;
RX PubMed=10497235; DOI=10.1074/jbc.274.40.28660;
RA Kobayashi Y.M., Jones L.R.;
RT "Identification of triadin 1 as the predominant triadin isoform expressed
RT in mammalian myocardium.";
RL J. Biol. Chem. 274:28660-28668(1999).
RN [2]
RP INTERACTION WITH CASQ2.
RX PubMed=20302875; DOI=10.1016/j.yjmcc.2010.03.006;
RA Kirchhefer U., Wehrmeister D., Postma A.V., Pohlentz G., Mormann M.,
RA Kucerova D., Muller F.U., Schmitz W., Schulze-Bahr E., Wilde A.A.,
RA Neumann J.;
RT "The human CASQ2 mutation K206N is associated with hyperglycosylation and
RT altered cellular calcium handling.";
RL J. Mol. Cell. Cardiol. 49:95-105(2010).
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 and RYR1 in skeletal muscle (By similarity).
CC Interacts with CASQ2. {ECO:0000250|UniProtKB:Q28820,
CC ECO:0000269|PubMed:20302875}.
CC -!- SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane; Single-pass type
CC II membrane protein {ECO:0000269|PubMed:10497235}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=Skeletal;
CC IsoId=P82179-1; Sequence=Displayed;
CC Name=Cardiac 1;
CC IsoId=P82179-2; Sequence=VSP_004001, VSP_004002;
CC Name=Cardiac 3;
CC IsoId=P82179-3; Sequence=VSP_004003, VSP_004004;
CC -!- TISSUE SPECIFICITY: Detected in heart (at protein level). Skeletal and
CC cardiac muscle. {ECO:0000269|PubMed:10497235}.
CC -!- PTM: Phosphorylated by CaMK2. {ECO:0000250|UniProtKB:Q28820}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:10497235}.
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DR EMBL; AF165916; AAF00222.1; -; mRNA.
DR EMBL; AF165915; AAF00221.1; -; mRNA.
DR EMBL; AF165917; AAF00223.1; -; mRNA.
DR RefSeq; NP_001003154.2; NM_001003154.2. [P82179-1]
DR AlphaFoldDB; P82179; -.
DR CORUM; P82179; -.
DR iPTMnet; P82179; -.
DR GeneID; 403776; -.
DR CTD; 10345; -.
DR InParanoid; P82179; -.
DR OrthoDB; 1200049at2759; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0014701; C:junctional sarcoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0016529; C:sarcoplasmic reticulum; IDA:BHF-UCL.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IPI:BHF-UCL.
DR GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:BHF-UCL.
DR GO; GO:0060047; P:heart contraction; IBA:GO_Central.
DR GO; GO:1901846; P:positive regulation of cell communication by electrical coupling involved in cardiac conduction; IDA:BHF-UCL.
DR GO; GO:0060316; P:positive regulation of ryanodine-sensitive calcium-release channel activity; IDA:BHF-UCL.
DR GO; GO:0086036; P:regulation of cardiac muscle cell membrane potential; IDA:BHF-UCL.
DR GO; GO:0010880; P:regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; IDA:BHF-UCL.
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..701
FT /note="Triadin"
FT /id="PRO_0000065625"
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..701
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 676..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
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..256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..293
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..351
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..651
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..701
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10497235"
FT CARBOHYD 617
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 263
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:Q28820"
FT DISULFID 663
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:Q28820"
FT VAR_SEQ 258..278
FT /note="DQYAFCRYMIDMFVHGDLRPG -> GKHSEEVAGGSKRTLGKKQIQ (in
FT isoform Cardiac 1)"
FT /evidence="ECO:0000305"
FT /id="VSP_004001"
FT VAR_SEQ 279..701
FT /note="Missing (in isoform Cardiac 1)"
FT /evidence="ECO:0000305"
FT /id="VSP_004002"
FT VAR_SEQ 467
FT /note="E -> EPIKGKEVKVPGSLKEKE (in isoform Cardiac 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_004003"
FT VAR_SEQ 525..580
FT /note="EEKVVKQVKATEKAAIEKTVKPKPAKKAEHQEKESPTIKTDKPKPTSKETPE
FT VTES -> GILQVVPVVLNCLFLVQFQQDEELNVESKVFRMIHVLSHPTSRTSPILVIS
FT TTCRT (in isoform Cardiac 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_004004"
FT MUTAGEN 75
FT /note="N->A: Loss of glycosylation site."
FT /evidence="ECO:0000269|PubMed:10497235"
SQ SEQUENCE 701 AA; 78284 MW; 04D5AF8763775C0A CRC64;
MTEITAEGNA STTTTVIDSK NGSVPKSPGK VLKRTVTEDI VTTFSSPAAW LLVIALIITW
SAVAVVMFDL VDYKNFSASS LSKIGSDPLK LVHDAVEETT DWVYGFFSLL SDIISSDGDE
DDDDGDEDTD KGEIEEPPLK QKEIHKEKAE KEEKPERKIL AKVAHREKEK VKEKEKSEKK
ATHKEKIEKK EKPETKTMAK EERKAKTEEK IKKEVKGGKQ EKVKPTAAKV KEVQKTPPKA
KEKEGKETAA VAKHEQKDQY AFCRYMIDMF VHGDLRPGQS PALPPPLPTV QASRPTPASP
TLEGKEEEEK KKAEKKVTSE TKKKEKEDVK KKSDKDTAID VEKKEPGKAP ETKQGTIKVV
AQAAAKKDEK KEDSKKTKTP VEEHPKGKKQ EKKEKYVEPA KSSKKEHSAP SEKQVKAKTE
RAKEETSAAS TKKAVPGKKE EKTTKTVEQE IRKEKSGKTS TASKDKEPEI KKDEKMPKAD
KEVKPKPPQS QVKKEEKSES QVKKEAKPEQ DIAKPEKTVS HGKPEEKVVK QVKATEKAAI
EKTVKPKPAK KAEHQEKESP TIKTDKPKPT SKETPEVTES GKKKIEKSEK ESKEKAEMKH
LKEEKVSTRK ESLQSHNVTK AEKPARVSRE DLEDVSASKK AKEEAEDVSS TKRQKSPISF
FQCVYLDGYN GYGFQFPVTP AYRPGESSGQ PSSPGQKQQG Q
