GenomeNet

Database: UniProt
Entry: A0A0G2JU95_RAT
LinkDB: A0A0G2JU95_RAT
Original site: A0A0G2JU95_RAT 
ID   A0A0G2JU95_RAT          Unreviewed;       688 AA.
AC   A0A0G2JU95;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 3.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=Triadin {ECO:0000256|ARBA:ARBA00016711};
GN   Name=Trdn {ECO:0000313|Ensembl:ENSRNOP00000069016.3,
GN   ECO:0000313|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:0000313|Ensembl:ENSRNOP00000069016.3, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000069016.3, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000069016.3,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
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   [2] {ECO:0007829|PubMed:22673903}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903;
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).
RN   [3] {ECO:0000313|Ensembl:ENSRNOP00000069016.3}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000069016.3};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-
CC       pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
CC       Sarcoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004157};
CC       Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004157}.
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DR   AlphaFoldDB; A0A0G2JU95; -.
DR   Ensembl; ENSRNOT00000090388.3; ENSRNOP00000069016.3; ENSRNOG00000012609.10.
DR   RGD; 619856; Trdn.
DR   VEuPathDB; HostDB:ENSRNOG00000012609; -.
DR   GeneTree; ENSGT00510000049207; -.
DR   OMA; QIHKQDI; -.
DR   OrthoDB; 5363225at2759; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000012609; Expressed in quadriceps femoris and 17 other cell types or tissues.
DR   ExpressionAtlas; A0A0G2JU95; baseline and differential.
DR   GO; GO:0033017; C:sarcoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR   GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR   GO; GO:0060047; P:heart contraction; IEA:Ensembl.
DR   GO; GO:0014808; P:release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; IEA:Ensembl.
DR   GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
DR   InterPro; IPR007943; Asp-B-hydro/Triadin_dom.
DR   InterPro; IPR010798; Triadin.
DR   PANTHER; PTHR14106; TRIADIN; 1.
DR   PANTHER; PTHR14106:SF0; TRIADIN; 1.
DR   Pfam; PF05279; Asp-B-Hydro_N; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW   Sarcoplasmic reticulum {ECO:0000256|ARBA:ARBA00022951};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        48..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          46..76
FT                   /note="Aspartyl beta-hydroxylase/Triadin"
FT                   /evidence="ECO:0000259|Pfam:PF05279"
FT   REGION          117..265
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          280..644
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          662..688
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..635
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        672..688
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   688 AA;  77343 MW;  4178F79363915215 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 HIETAKTPKK EHPAPSEKHR
     KAKAEQAKEE IAPASTKKAL HGKKEEKAKT VEQGKDVKPK LPQPQLKKEE KSEPQPKKEV
     KLETQLKKEE KSEPQVKKEA KLASSEKGQT RKQNITRPEQ VIPHGKPEQK VPKQIKAITA
     EKTEKAERQE KYHPSIKTEG KPEVTDSGKK KIEKPEKESK VPPKQENLQV RNVTRAEKRG
     KISKDSKDAP APKKDKEDSK DVLHSKKDKE VTNNVSSPKK QKSPISFFQC VYLDGYNGYG
     FQFPVTPVQH PGENPGKSNS PGQKQQEQ
//
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