THRSP_MOUSE
ID THRSP_MOUSE Reviewed; 150 AA.
AC Q62264;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Thyroid hormone-inducible hepatic protein;
DE AltName: Full=Spot 14 protein;
DE Short=S14;
DE Short=SPOT14;
GN Name=Thrsp; Synonyms=S14;
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 [GENOMIC DNA].
RC STRAIN=BALB/cJ;
RX PubMed=9003802; DOI=10.1016/s0014-5793(96)01433-0;
RA Grillasca J.-P., Gastaldi M., Khiri H., Dace A., Peyrol N., Reynier P.,
RA Torresani J., Planells R.;
RT "Cloning and initial characterization of human and mouse Spot 14 genes.";
RL FEBS Lett. 401:38-42(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary 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 [3]
RP DISRUPTION PHENOTYPE.
RX PubMed=11564699; DOI=10.1210/endo.142.10.8431;
RA Zhu Q., Mariash A., Margosian M.R., Gopinath S., Fareed M.T.,
RA Anderson G.W., Mariash C.N.;
RT "Spot 14 gene deletion increases hepatic de novo lipogenesis.";
RL Endocrinology 142:4363-4370(2001).
RN [4]
RP DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15890771; DOI=10.1210/en.2005-0204;
RA Zhu Q., Anderson G.W., Mucha G.T., Parks E.J., Metkowski J.K.,
RA Mariash C.N.;
RT "The Spot 14 protein is required for de novo lipid synthesis in the
RT lactating mammary gland.";
RL Endocrinology 146:3343-3350(2005).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=19356628; DOI=10.1016/j.mce.2009.01.005;
RA Anderson G.W., Zhu Q., Metkowski J., Stack M.J., Gopinath S., Mariash C.N.;
RT "The Thrsp null mouse (Thrsp(tm1cnm)) and diet-induced obesity.";
RL Mol. Cell. Endocrinol. 302:99-107(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, and
RC Pancreas;
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 [7]
RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS), FUNCTION, INTERACTION WITH MID1IP1,
RP AND SUBCELLULAR LOCATION.
RX PubMed=20952656; DOI=10.1073/pnas.1012736107;
RA Colbert C.L., Kim C.W., Moon Y.A., Henry L., Palnitkar M., McKean W.B.,
RA Fitzgerald K., Deisenhofer J., Horton J.D., Kwon H.J.;
RT "Crystal structure of Spot 14, a modulator of fatty acid synthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:18820-18825(2010).
CC -!- FUNCTION: Plays a role in the regulation of lipogenesis, especially in
CC lactating mammary gland. Important for the biosynthesis of
CC triglycerides with medium-length fatty acid chains. May modulate
CC lipogenesis by interacting with MID1IP1 and preventing its interaction
CC with ACACA. May function as transcriptional coactivator. May modulate
CC the transcription factor activity of THRB (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:15890771,
CC ECO:0000269|PubMed:20952656}.
CC -!- SUBUNIT: Homodimer. Heterodimer with MID1IP1. Interacts with THRB and
CC PLAGL1 (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q62264; Q62264: Thrsp; NbExp=3; IntAct=EBI-15853187, EBI-15853187;
CC Q62264; G3H9D1: I79_006999; Xeno; NbExp=2; IntAct=EBI-15853187, EBI-15884821;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20952656}. Cytoplasm
CC {ECO:0000269|PubMed:20952656}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in tissues that synthesize
CC triglycerides. {ECO:0000269|PubMed:15890771}.
CC -!- DISRUPTION PHENOTYPE: Decreased lipid synthesis in the lactating
CC mammary gland. Milk has reduced triglyceride content, causing reduced
CC weight gain in nursing pups. Adults exhibit reduced body fat content.
CC No effect on lipid synthesis in liver. No effect on the expression of
CC thyroid hormone-induced lipogenic genes. {ECO:0000269|PubMed:11564699,
CC ECO:0000269|PubMed:15890771, ECO:0000269|PubMed:19356628}.
CC -!- SIMILARITY: Belongs to the SPOT14 family. {ECO:0000305}.
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DR EMBL; X95279; CAA64600.1; -; Genomic_DNA.
DR EMBL; BC009165; AAH09165.1; -; mRNA.
DR CCDS; CCDS21458.1; -.
DR RefSeq; NP_033407.1; NM_009381.3.
DR PDB; 3ONT; X-ray; 2.65 A; A=1-150.
DR PDBsum; 3ONT; -.
DR AlphaFoldDB; Q62264; -.
DR SMR; Q62264; -.
DR DIP; DIP-59527N; -.
DR IntAct; Q62264; 2.
DR STRING; 10090.ENSMUSP00000042988; -.
DR iPTMnet; Q62264; -.
DR PhosphoSitePlus; Q62264; -.
DR SwissPalm; Q62264; -.
DR jPOST; Q62264; -.
DR MaxQB; Q62264; -.
DR PaxDb; Q62264; -.
DR PRIDE; Q62264; -.
DR ProteomicsDB; 258874; -.
DR Antibodypedia; 31292; 211 antibodies from 31 providers.
DR DNASU; 21835; -.
DR Ensembl; ENSMUST00000043077; ENSMUSP00000042988; ENSMUSG00000035686.
DR GeneID; 21835; -.
DR KEGG; mmu:21835; -.
DR UCSC; uc009ije.1; mouse.
DR CTD; 7069; -.
DR MGI; MGI:109126; Thrsp.
DR VEuPathDB; HostDB:ENSMUSG00000035686; -.
DR eggNOG; ENOG502S7IQ; Eukaryota.
DR GeneTree; ENSGT00500000044890; -.
DR HOGENOM; CLU_066079_1_0_1; -.
DR InParanoid; Q62264; -.
DR OMA; MDRYSAT; -.
DR OrthoDB; 1326063at2759; -.
DR PhylomeDB; Q62264; -.
DR TreeFam; TF326826; -.
DR Reactome; R-MMU-200425; Carnitine metabolism.
DR BioGRID-ORCS; 21835; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Thrsp; mouse.
DR EvolutionaryTrace; Q62264; -.
DR PRO; PR:Q62264; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q62264; protein.
DR Bgee; ENSMUSG00000035686; Expressed in aorta tunica adventitia and 216 other tissues.
DR ExpressionAtlas; Q62264; baseline and differential.
DR Genevisible; Q62264; MM.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0046890; P:regulation of lipid biosynthetic process; IMP:UniProtKB.
DR GO; GO:0010866; P:regulation of triglyceride biosynthetic process; IMP:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR DisProt; DP02820; -.
DR InterPro; IPR009786; Spot_14.
DR PANTHER; PTHR14315; PTHR14315; 1.
DR Pfam; PF07084; Spot_14; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Lipid biosynthesis; Lipid metabolism; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..150
FT /note="Thyroid hormone-inducible hepatic protein"
FT /id="PRO_0000123774"
FT REGION 83..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04143"
FT HELIX 13..30
FT /evidence="ECO:0007829|PDB:3ONT"
FT HELIX 34..37
FT /evidence="ECO:0007829|PDB:3ONT"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:3ONT"
FT HELIX 56..71
FT /evidence="ECO:0007829|PDB:3ONT"
FT HELIX 108..111
FT /evidence="ECO:0007829|PDB:3ONT"
FT HELIX 113..145
FT /evidence="ECO:0007829|PDB:3ONT"
SQ SEQUENCE 150 AA; 17093 MW; C0CAACD39DBF8E31 CRC64;
MQVLTKRYPK NCLLTVMDRY SAVVRNMEQV VMIPSLLRDV QLSGPGGSVQ DGAPDLYTYF
TMLKSICVEV DHGLLPREEW QAKVAGNETS EAENDAAETE EAEEDRISEE LDLEAQFHLH
FCSLHHILTH LTRKAQEVTR KYQEMTGQVL
