TRDN_RABIT
ID TRDN_RABIT Reviewed; 706 AA.
AC Q28820; Q28636; Q28637; Q28643;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=Triadin;
GN Name=TRDN;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SKELETAL 1), PARTIAL PROTEIN SEQUENCE,
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND TOPOLOGY.
RC STRAIN=New Zealand white; TISSUE=Skeletal muscle;
RX PubMed=7685347; DOI=10.1016/s0021-9258(18)31437-6;
RA Knudson C.M., Stang K.K., Moomaw C.R., Slaughter C.A., Campbell K.P.;
RT "Primary structure and topological analysis of a skeletal muscle-specific
RT junctional sarcoplasmic reticulum glycoprotein (triadin).";
RL J. Biol. Chem. 268:12646-12654(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS SKELETAL 1; SKELETAL 2 AND SKELETAL
RP 3), PARTIAL PROTEIN SEQUENCE, AND TISSUE SPECIFICITY.
RC TISSUE=Skeletal muscle;
RX PubMed=8026576; DOI=10.1016/0014-5793(94)00556-7;
RA Peng M., Fan H., Kirley T.L., Caswell A.H., Schwartz A.;
RT "Structural diversity of triadin in skeletal muscle and evidence of its
RT existence in heart.";
RL FEBS Lett. 348:17-20(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS CARDIAC 1; CARDIAC 2 AND CARDIAC 3),
RP PARTIAL PROTEIN SEQUENCE, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
RP TOPOLOGY.
RC TISSUE=Heart muscle;
RX PubMed=8550602; DOI=10.1074/jbc.271.18.10545;
RA Guo W., Jorgensen A.O., Jones L.R., Campbell K.P.;
RT "Biochemical characterization and molecular cloning of cardiac triadin.";
RL J. Biol. Chem. 271:458-465(1996).
RN [4]
RP GLYCOSYLATION AT ASN-625, SUBUNIT, AND DISULFIDE BOND.
RX PubMed=7578102; DOI=10.1021/bi00045a035;
RA Fan H., Brandt N.R., Caswell A.H.;
RT "Disulfide bonds, N-glycosylation and transmembrane topology of skeletal
RT muscle triadin.";
RL Biochemistry 34:14902-14908(1995).
RN [5]
RP INTERACTION WITH RYR1 AND CASQ1, FUNCTION, SUBCELLULAR LOCATION, AND
RP TOPOLOGY.
RX PubMed=7721813; DOI=10.1074/jbc.270.16.9027;
RA Guo W., Campbell K.P.;
RT "Association of triadin with the ryanodine receptor and calsequestrin in
RT the lumen of the sarcoplasmic reticulum.";
RL J. Biol. Chem. 270:9027-9030(1995).
RN [6]
RP PHOSPHORYLATION BY CAMK2.
RX PubMed=11681715; DOI=10.1023/a:1017987015807;
RA Colpo P., Nori A., Sacchetto R., Damiani E., Margreth A.;
RT "Phosphorylation of the triadin cytoplasmic domain by CaM protein kinase in
RT rabbit fast-twitch muscle sarcoplasmic reticulum.";
RL Mol. Cell. Biochem. 223:139-145(2001).
RN [7]
RP FUNCTION, INTERACTION WITH RYR1, AND TISSUE SPECIFICITY.
RX PubMed=17846166; DOI=10.1085/jgp.200709790;
RA Goonasekera S.A., Beard N.A., Groom L., Kimura T., Lyfenko A.D.,
RA Rosenfeld A., Marty I., Dulhunty A.F., Dirksen R.T.;
RT "Triadin binding to the C-terminal luminal loop of the ryanodine receptor
RT is important for skeletal muscle excitation contraction coupling.";
RL J. Gen. Physiol. 130:365-378(2007).
RN [8]
RP INTERACTION WITH CASQ1, AND SUBCELLULAR LOCATION.
RX PubMed=19230141; DOI=10.1016/j.ceca.2008.01.005;
RA Beard N.A., Wei L., Cheung S.N., Kimura T., Varsanyi M., Dulhunty A.F.;
RT "Phosphorylation of skeletal muscle calsequestrin enhances its Ca2+ binding
RT capacity and promotes its association with junctin.";
RL Cell Calcium 44:363-373(2008).
RN [9]
RP FUNCTION, INTERACTION WITH CASQ1, AND SUBCELLULAR LOCATION.
RX PubMed=19398037; DOI=10.1016/j.biocel.2009.04.017;
RA Wei L., Gallant E.M., Dulhunty A.F., Beard N.A.;
RT "Junctin and triadin each activate skeletal ryanodine receptors but junctin
RT alone mediates functional interactions with calsequestrin.";
RL Int. J. Biochem. Cell Biol. 41:2214-2224(2009).
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
CC (PubMed:19398037, PubMed:17846166 and PubMed:7721813). 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 (By similarity). {ECO:0000250|UniProtKB:E9Q9K5,
CC ECO:0000269|PubMed:17846166, ECO:0000269|PubMed:19398037,
CC ECO:0000269|PubMed:7721813}.
CC -!- SUBUNIT: Interacts with CASQ2 (By similarity). Homooligomer of variable
CC subunit number; disulfide-linked. Interacts with CASQ1 and RYR1 in
CC skeletal muscle. {ECO:0000250|UniProtKB:Q13061,
CC ECO:0000269|PubMed:17846166, ECO:0000269|PubMed:19230141,
CC ECO:0000269|PubMed:19398037, ECO:0000269|PubMed:7578102,
CC ECO:0000269|PubMed:7721813}.
CC -!- SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane; Single-pass type
CC II membrane protein {ECO:0000269|PubMed:19230141,
CC ECO:0000269|PubMed:19398037, ECO:0000269|PubMed:7685347,
CC ECO:0000269|PubMed:7721813, ECO:0000269|PubMed:8550602}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Comment=Additional isoforms seem to exist.;
CC Name=Skeletal 1; Synonyms=ST1;
CC IsoId=Q28820-1; Sequence=Displayed;
CC Name=Cardiac 1; Synonyms=CT1;
CC IsoId=Q28820-2; Sequence=VSP_004458, VSP_004460;
CC Name=Cardiac 2; Synonyms=CT2;
CC IsoId=Q28820-3; Sequence=VSP_004459, VSP_004461;
CC Name=Cardiac 3; Synonyms=CT3;
CC IsoId=Q28820-4; Sequence=VSP_004466;
CC Name=Skeletal 2; Synonyms=ST2;
CC IsoId=Q28820-5; Sequence=VSP_004462, VSP_004463, VSP_004464,
CC VSP_004465;
CC Name=Skeletal 3; Synonyms=ST3;
CC IsoId=Q28820-6; Sequence=VSP_004464, VSP_004465;
CC -!- TISSUE SPECIFICITY: Detected in skeletal muscle and in heart (at
CC protein level). Detected in skeletal muscle and in heart.
CC {ECO:0000269|PubMed:17846166, ECO:0000269|PubMed:7685347,
CC ECO:0000269|PubMed:8026576, ECO:0000269|PubMed:8550602}.
CC -!- PTM: Phosphorylated by CaMK2. {ECO:0000269|PubMed:11681715}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:7578102}.
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DR EMBL; U31540; AAC48496.1; -; mRNA.
DR EMBL; L10065; AAA31488.1; -; mRNA.
DR EMBL; U31555; AAC48497.1; -; mRNA.
DR EMBL; U34201; AAC48498.1; -; mRNA.
DR PIR; A45990; A45990.
DR RefSeq; NP_001076212.1; NM_001082743.1. [Q28820-1]
DR AlphaFoldDB; Q28820; -.
DR IntAct; Q28820; 1.
DR MINT; Q28820; -.
DR STRING; 9986.ENSOCUP00000024583; -.
DR iPTMnet; Q28820; -.
DR PRIDE; Q28820; -.
DR GeneID; 100009519; -.
DR KEGG; ocu:100009519; -.
DR CTD; 10345; -.
DR InParanoid; Q28820; -.
DR OrthoDB; 1200049at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
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; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Membrane; Phosphoprotein; Reference proteome;
KW Sarcoplasmic reticulum; Transmembrane; Transmembrane helix.
FT CHAIN 1..706
FT /note="Triadin"
FT /id="PRO_0000065627"
FT TOPO_DOM 1..47
FT /note="Cytoplasmic"
FT TRANSMEM 48..68
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 69..706
FT /note="Lumenal"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 684..706
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..131
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..302
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..358
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..618
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..659
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..706
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 625
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:7578102"
FT DISULFID 270
FT /note="Interchain"
FT /evidence="ECO:0000303|PubMed:7578102"
FT DISULFID 671
FT /note="Interchain"
FT /evidence="ECO:0000303|PubMed:7578102"
FT VAR_SEQ 265..308
FT /note="DQYAFCRYMIDIFVHGDLKPGQSPAIPPPSPTEQASRPTPALPT -> ECIF
FT LSAATPQGIPNRQQLNDIHHCFLKTKKGGNGQHAFCLKGC (in isoform
FT Cardiac 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_004459"
FT VAR_SEQ 265..286
FT /note="DQYAFCRYMIDIFVHGDLKPGQ -> GGKQSEEAAGCFKRTLGKKQMQ (in
FT isoform Cardiac 1)"
FT /evidence="ECO:0000305"
FT /id="VSP_004458"
FT VAR_SEQ 287..706
FT /note="Missing (in isoform Cardiac 1)"
FT /evidence="ECO:0000305"
FT /id="VSP_004460"
FT VAR_SEQ 309..706
FT /note="Missing (in isoform Cardiac 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_004461"
FT VAR_SEQ 416
FT /note="A -> E (in isoform Skeletal 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_004462"
FT VAR_SEQ 417..425
FT /note="Missing (in isoform Skeletal 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_004463"
FT VAR_SEQ 585
FT /note="D -> E (in isoform Skeletal 2 and isoform Skeletal
FT 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_004464"
FT VAR_SEQ 586..592
FT /note="Missing (in isoform Skeletal 2 and isoform Skeletal
FT 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_004465"
FT VAR_SEQ 646..706
FT /note="SKKAKEEAEEVSSTKKQKSPISFFQCVYLDGYNGYGFQFPVTPAQYPGESSG
FT KPNSPGPKQ -> LLATVGIWGMNQWMEDLSVTLPSK (in isoform Cardiac
FT 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_004466"
SQ SEQUENCE 706 AA; 79134 MW; 2F1352C33BEEF52D CRC64;
MTEITAEGNA STTTTVIDSK NGSVPKSPGK VLKRTVTEDL VTTFSSPAAW LLVIALIITW
SAVAVVMFDL VDYKNFSASS IAKMGSDPLK LVHDAVEETT DWIYGFFSLL SDIISSDGDE
EDDEGDEDTA KGEIEEPPLK RKDIHKEKIE KQEKPERKIP TKVVHKEKEK EKEKVKEKEK
PEKKATHKEK LEKKEKPETK TVTKEEKKAR TKEKIEEKTK KEVKGVKQEK VKQTVAKAKE
VQKTPKPKEK ESKETAAVSK QEQKDQYAFC RYMIDIFVHG DLKPGQSPAI PPPSPTEQAS
RPTPALPTPE EKEGEKKKAE KKVTTETKKK AEKEDAKKKS EKETDIDMKK KEPGKSPDTK
PGTVKVTTQA ATKKDEKKED SKKAKKPAEE QPKGKKQEKK EKHEEPAKST KKEHAAPSEK
QAKAKIERKE EVSAASTKKA VPAKKEEKTT KTVEQETRKE KPGKISSVLK DKELTKEKEV
KVPASLKEKG SETKKDEKTS KPEPQIKKEE KPGKEVKPKP PQPQIKKEEK PEQDIMKPEK
TALHGKPEEK VLKQVKAVTT EKHVKPKPAK KAEHQEKEPP SIKTDKPKST SKGMPEVTES
GKKKIEKSEK EIKVPARRES HQLQNVTKAE KPARGSKEGF EDVPASKKAK EEAEEVSSTK
KQKSPISFFQ CVYLDGYNGY GFQFPVTPAQ YPGESSGKPN SPGPKQ
