ID   TTHY_MOUSE              Reviewed;         147 AA.
AC   P07309;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   27-MAR-2024, entry version 188.
DE   RecName: Full=Transthyretin;
DE   AltName: Full=Prealbumin;
DE   Flags: Precursor;
GN   Name=Ttr;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND THYROID HORMONE-BINDING SITES LYS-35 AND
RP   GLU-74.
RC   TISSUE=Liver;
RX   PubMed=3005251; DOI=10.1093/oxfordjournals.jbchem.a135442;
RA   Wakasugi S., Maeda S., Shimada K., Nakashima H., Migita S.;
RT   "Structural comparisons between mouse and human prealbumin.";
RL   J. Biochem. 98:1707-1714(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=3020014; DOI=10.1093/oxfordjournals.jbchem.a121705;
RA   Wakasugi S., Maeda S., Shimada K.;
RT   "Structure and expression of the mouse prealbumin gene.";
RL   J. Biochem. 100:49-58(1986).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Choroid plexus;
RA   Kita H., Kawamoto S., Okubo K., Matsubara K.;
RL   Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-118.
RC   STRAIN=C57BL/6J; TISSUE=Plasma;
RX   PubMed=17330941; DOI=10.1021/pr0604559;
RA   Bernhard O.K., Kapp E.A., Simpson R.J.;
RT   "Enhanced analysis of the mouse plasma proteome using cysteine-containing
RT   tryptic glycopeptides.";
RL   J. Proteome Res. 6:987-995(2007).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 21-147, INCREASED STABILITY OF
RP   THE MOUSE PROTEIN, AND SUBUNIT.
RX   PubMed=18006495; DOI=10.1074/jbc.m708028200;
RA   Reixach N., Foss T.R., Santelli E., Pascual J., Kelly J.W., Buxbaum J.N.;
RT   "Human-murine transthyretin heterotetramers are kinetically stable and non-
RT   amyloidogenic. A lesson in the generation of transgenic models of diseases
RT   involving oligomeric proteins.";
RL   J. Biol. Chem. 283:2098-2107(2008).
CC   -!- FUNCTION: Thyroid hormone-binding protein. Probably transports
CC       thyroxine from the bloodstream to the brain.
CC   -!- SUBUNIT: Homotetramer. Dimer of dimers. In the homotetramer, subunits
CC       assemble around a central channel that can accommodate two ligand
CC       molecules. Interacts with RBP4 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Detected in plasma (at protein level). Detected in
CC       liver.
CC   -!- PTM: Sulfonation of the reactive cysteine Cys-30 enhances the stability
CC       of the native conformation of TTR, avoiding misassembly of the protein
CC       leading to amyloid formation. {ECO:0000250|UniProtKB:P02766}.
CC   -!- MISCELLANEOUS: The mouse protein shows increased stability and much
CC       reduced propensity to form amyloid fibrils, compared to the human
CC       protein.
CC   -!- SIMILARITY: Belongs to the transthyretin family. {ECO:0000305}.
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DR   EMBL; X03351; CAA27057.1; -; mRNA.
DR   EMBL; D00073; BAA00050.1; -; Genomic_DNA.
DR   EMBL; D89076; BAA13757.1; -; mRNA.
DR   EMBL; AK018701; BAB31352.1; -; mRNA.
DR   EMBL; BC024702; AAH24702.1; -; mRNA.
DR   CCDS; CCDS29085.1; -.
DR   PIR; A24132; VBMS.
DR   RefSeq; NP_038725.1; NM_013697.5.
DR   PDB; 2QPF; X-ray; 2.05 A; A/B/C/D/E/F/G/H=21-147.
DR   PDBsum; 2QPF; -.
DR   AlphaFoldDB; P07309; -.
DR   SMR; P07309; -.
DR   BioGRID; 204369; 20.
DR   DIP; DIP-29726N; -.
DR   IntAct; P07309; 3.
DR   MINT; P07309; -.
DR   STRING; 10090.ENSMUSP00000074783; -.
DR   ChEMBL; CHEMBL5169111; -.
DR   GlyCosmos; P07309; 1 site, No reported glycans.
DR   GlyGen; P07309; 2 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; P07309; -.
DR   PhosphoSitePlus; P07309; -.
DR   SwissPalm; P07309; -.
DR   CPTAC; non-CPTAC-3625; -.
DR   CPTAC; non-CPTAC-5622; -.
DR   jPOST; P07309; -.
DR   PaxDb; 10090-ENSMUSP00000074783; -.
DR   PeptideAtlas; P07309; -.
DR   ProteomicsDB; 298011; -.
DR   ABCD; P07309; 2 sequenced antibodies.
DR   Antibodypedia; 650; 1558 antibodies from 45 providers.
DR   DNASU; 22139; -.
DR   Ensembl; ENSMUST00000075312.5; ENSMUSP00000074783.4; ENSMUSG00000061808.5.
DR   GeneID; 22139; -.
DR   KEGG; mmu:22139; -.
DR   UCSC; uc008eet.2; mouse.
DR   AGR; MGI:98865; -.
DR   CTD; 7276; -.
DR   MGI; MGI:98865; Ttr.
DR   VEuPathDB; HostDB:ENSMUSG00000061808; -.
DR   eggNOG; KOG3006; Eukaryota.
DR   GeneTree; ENSGT00940000153229; -.
DR   HOGENOM; CLU_115536_2_0_1; -.
DR   InParanoid; P07309; -.
DR   OMA; TWEPFAT; -.
DR   OrthoDB; 5352684at2759; -.
DR   PhylomeDB; P07309; -.
DR   TreeFam; TF300210; -.
DR   Reactome; R-MMU-2453902; The canonical retinoid cycle in rods (twilight vision).
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   Reactome; R-MMU-975634; Retinoid metabolism and transport.
DR   BioGRID-ORCS; 22139; 1 hit in 77 CRISPR screens.
DR   ChiTaRS; Ttr; mouse.
DR   EvolutionaryTrace; P07309; -.
DR   PRO; PR:P07309; -.
DR   Proteomes; UP000000589; Chromosome 18.
DR   RNAct; P07309; Protein.
DR   Bgee; ENSMUSG00000061808; Expressed in choroid plexus epithelium and 219 other cell types or tissues.
DR   ExpressionAtlas; P07309; baseline and differential.
DR   GO; GO:0005615; C:extracellular space; ISO:MGI.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   GO; GO:0042562; F:hormone binding; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR   GO; GO:0070324; F:thyroid hormone binding; IBA:GO_Central.
DR   GO; GO:0006144; P:purine nucleobase metabolic process; IBA:GO_Central.
DR   CDD; cd05821; TLP_Transthyretin; 1.
DR   Gene3D; 2.60.40.180; Transthyretin/hydroxyisourate hydrolase domain; 1.
DR   InterPro; IPR023418; Thyroxine_BS.
DR   InterPro; IPR000895; Transthyretin/HIU_hydrolase.
DR   InterPro; IPR023416; Transthyretin/HIU_hydrolase_d.
DR   InterPro; IPR036817; Transthyretin/HIU_hydrolase_sf.
DR   InterPro; IPR023419; Transthyretin_CS.
DR   PANTHER; PTHR10395:SF12; TRANSTHYRETIN; 1.
DR   PANTHER; PTHR10395; URICASE AND TRANSTHYRETIN-RELATED; 1.
DR   Pfam; PF00576; Transthyretin; 1.
DR   PRINTS; PR00189; TRNSTHYRETIN.
DR   SMART; SM00095; TR_THY; 1.
DR   SUPFAM; SSF49472; Transthyretin (synonym: prealbumin); 1.
DR   PROSITE; PS00768; TRANSTHYRETIN_1; 1.
DR   PROSITE; PS00769; TRANSTHYRETIN_2; 1.
DR   UCD-2DPAGE; P07309; -.
DR   Genevisible; P07309; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Gamma-carboxyglutamic acid; Glycoprotein; Hormone;
KW   Phosphoprotein; Reference proteome; Secreted; Signal; Sulfation;
KW   Thyroid hormone; Transport.
FT   SIGNAL          1..20
FT   CHAIN           21..147
FT                   /note="Transthyretin"
FT                   /id="PRO_0000035760"
FT   BINDING         35
FT                   /ligand="L-thyroxine"
FT                   /ligand_id="ChEBI:CHEBI:58448"
FT                   /evidence="ECO:0000250|UniProtKB:P02766"
FT   BINDING         74
FT                   /ligand="L-thyroxine"
FT                   /ligand_id="ChEBI:CHEBI:58448"
FT                   /evidence="ECO:0000250|UniProtKB:P02766"
FT   BINDING         137
FT                   /ligand="L-thyroxine"
FT                   /ligand_id="ChEBI:CHEBI:58448"
FT                   /evidence="ECO:0000250|UniProtKB:P02766"
FT   MOD_RES         30
FT                   /note="Sulfocysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P02766"
FT   MOD_RES         62
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P02766"
FT   MOD_RES         72
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P02767"
FT   CARBOHYD        118
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:17330941"
FT   STRAND          32..38
FT                   /evidence="ECO:0007829|PDB:2QPF"
FT   TURN            39..42
FT                   /evidence="ECO:0007829|PDB:2QPF"
FT   STRAND          49..55
FT                   /evidence="ECO:0007829|PDB:2QPF"
FT   STRAND          61..68
FT                   /evidence="ECO:0007829|PDB:2QPF"
FT   STRAND          73..75
FT                   /evidence="ECO:0007829|PDB:2QPF"
FT   TURN            81..83
FT                   /evidence="ECO:0007829|PDB:2QPF"
FT   STRAND          86..93
FT                   /evidence="ECO:0007829|PDB:2QPF"
FT   HELIX           95..101
FT                   /evidence="ECO:0007829|PDB:2QPF"
FT   STRAND          107..109
FT                   /evidence="ECO:0007829|PDB:2QPF"
FT   STRAND          111..118
FT                   /evidence="ECO:0007829|PDB:2QPF"
FT   STRAND          124..132
FT                   /evidence="ECO:0007829|PDB:2QPF"
FT   STRAND          135..143
FT                   /evidence="ECO:0007829|PDB:2QPF"
SQ   SEQUENCE   147 AA;  15776 MW;  9803CCC3024BA911 CRC64;
     MASLRLFLLC LAGLVFVSEA GPAGAGESKC PLMVKVLDAV RGSPAVDVAV KVFKKTSEGS
     WEPFASGKTA ESGELHGLTT DEKFVEGVYR VELDTKSYWK TLGISPFHEF ADVVFTANDS
     GHRHYTIAAL LSPYSYSTTA VVSNPQN
//