THRSP_RAT
ID THRSP_RAT Reviewed; 150 AA.
AC P04143; Q63536;
DT 01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1986, sequence version 1.
DT 25-MAY-2022, entry version 101.
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 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;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6327713; DOI=10.1016/s0021-9258(17)39865-4;
RA Liaw C.W., Towle H.C.;
RT "Characterization of a thyroid hormone-responsive gene from rat.";
RL J. Biol. Chem. 259:7253-7260(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC TISSUE=Liver;
RX PubMed=2303455; DOI=10.1016/s0021-9258(19)39792-3;
RA Jump D.B., Bell A., Santiago V.;
RT "Thyroid hormone and dietary carbohydrate interact to regulate rat liver
RT S14 gene transcription and chromatin structure.";
RL J. Biol. Chem. 265:3474-3478(1990).
RN [3]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=4065033; DOI=10.1210/endo-117-6-2259;
RA Jump D.B., Oppenheimer J.H.;
RT "High basal expression and 3,5,3'-triiodothyronine regulation of messenger
RT ribonucleic acid S14 in lipogenic tissues.";
RL Endocrinology 117:2259-2266(1985).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=1446647; DOI=10.1210/endo.131.6.1446647;
RA Kinlaw W.B., Tron P., Friedmann A.S.;
RT "Nuclear localization and hepatic zonation of rat 'spot 14' protein:
RT immunohistochemical investigation employing anti-fusion protein
RT antibodies.";
RL Endocrinology 131:3120-3122(1992).
RN [5]
RP FUNCTION, AND INDUCTION.
RX PubMed=8999918; DOI=10.1074/jbc.272.46.28939;
RA Brown S.B., Maloney M., Kinlaw W.B.;
RT "'Spot 14' protein functions at the pretranslational level in the
RT regulation of hepatic metabolism by thyroid hormone and glucose.";
RL J. Biol. Chem. 272:2163-2166(1997).
RN [6]
RP FUNCTION.
RX PubMed=20233797; DOI=10.1210/en.2009-1058;
RA Aipoalani D.L., O'Callaghan B.L., Mashek D.G., Mariash C.N., Towle H.C.;
RT "Overlapping roles of the glucose-responsive genes, S14 and S14R, in
RT hepatic lipogenesis.";
RL Endocrinology 151:2071-2077(2010).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
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).
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:20233797, ECO:0000269|PubMed:8999918}.
CC -!- SUBUNIT: Homodimer. Heterodimer with MID1IP1. Interacts with THRB and
CC PLAGL1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:1446647}. Cytoplasm
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in liver, lactating mammary gland,
CC epididymal, retroperitoneal and brown fat. Mainly expressed in tissues
CC that synthesize triglycerides. {ECO:0000269|PubMed:4065033}.
CC -!- INDUCTION: The mRNA levels in rat liver are up-regulated in response to
CC thyroid hormone (T3) and a carbohydrate-rich diet. Up-regulated in
CC liver at the time of weaning, when pups switch from a high-fat milk
CC diet to having to synthesize their own fatty acids. Down-regulated by
CC fasting. Levels of mRNA increase within 20 minutes of T3
CC administration. {ECO:0000269|PubMed:2303455,
CC ECO:0000269|PubMed:4065033, ECO:0000269|PubMed:8999918}.
CC -!- SIMILARITY: Belongs to the SPOT14 family. {ECO:0000305}.
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DR EMBL; K01934; AAA96608.1; -; Genomic_DNA.
DR EMBL; M33553; AAA42099.1; -; Genomic_DNA.
DR PIR; A05173; A05173.
DR AlphaFoldDB; P04143; -.
DR SMR; P04143; -.
DR STRING; 10116.ENSRNOP00000016540; -.
DR iPTMnet; P04143; -.
DR PaxDb; P04143; -.
DR UCSC; RGD:3859; rat.
DR RGD; 3859; Thrsp.
DR eggNOG; ENOG502S7IQ; Eukaryota.
DR InParanoid; P04143; -.
DR PhylomeDB; P04143; -.
DR Reactome; R-RNO-200425; Carnitine metabolism.
DR PRO; PR:P04143; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0009617; P:response to bacterium; ISO:RGD.
DR InterPro; IPR009786; Spot_14.
DR PANTHER; PTHR14315; PTHR14315; 1.
DR Pfam; PF07084; Spot_14; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Lipid biosynthesis; Lipid metabolism; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..150
FT /note="Thyroid hormone-inducible hepatic protein"
FT /id="PRO_0000123775"
FT REGION 83..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CONFLICT 43
FT /note="S -> M (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 45
FT /note="S -> Y (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 150 AA; 17009 MW; 15812D18DDFB12DE CRC64;
MQVLTKRYPK NCLLKVMDRY SAVVRNMEQV VMIPSLLRDV ELSGSGGSVQ DGAPDLYTYF
TMLKSICVEV DHGLLPREEW QAKVAGNEGS EAENEAAETE EAEEDRLSEE LDLEAQFHLH
FSSLHHILTH LTQKAQEVTQ KYQEMTGQVL
