NOCT_MOUSE
ID NOCT_MOUSE Reviewed; 429 AA.
AC O35710; Q9QZG9;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2001, sequence version 3.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Nocturnin {ECO:0000312|MGI:MGI:109382};
DE EC=3.1.3.108 {ECO:0000250|UniProtKB:Q9UK39};
DE AltName: Full=Carbon catabolite repression 4-like protein;
DE Flags: Precursor;
GN Name=Noct {ECO:0000312|MGI:MGI:109382}; Synonyms=Ccr4, Ccrn4l, Noc;
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] (ISOFORM 2).
RC STRAIN=DBA/2J; TISSUE=Liver;
RX PubMed=9038221; DOI=10.1074/jbc.272.9.5995;
RA Puech A., Dupressoir A., Loireau M.-P., Mattei M.-G., Heidmann T.;
RT "Characterization of two age-induced intracisternal A-particle-related
RT transcripts in the mouse liver. Transcriptional read-through into an open
RT reading frame with similarities to the yeast ccr4 transcription factor.";
RL J. Biol. Chem. 272:5995-6003(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=10521507; DOI=10.1074/jbc.274.43.31068;
RA Dupressoir A., Barbot W., Loireau M.-P., Heidmann T.;
RT "Characterization of a mammalian gene related to the yeast CCR4 general
RT transcription factor and revealed by transposon insertion.";
RL J. Biol. Chem. 274:31068-31075(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CIRCADIAN EXPRESSION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Retina;
RX PubMed=11394964; DOI=10.1186/1471-213x-1-9;
RA Wang Y., Osterbur D.L., Megaw P.L., Tosini G., Fukuhara C., Green C.B.,
RA Besharse J.C.;
RT "Rhythmic expression of nocturnin mRNA in multiple tissues of the mouse.";
RL BMC Dev. Biol. 1:9-9(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Ovary;
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 INDUCTION.
RX PubMed=17400819; DOI=10.1261/rna.286507;
RA Garbarino-Pico E., Niu S., Rollag M.D., Strayer C.A., Besharse J.C.,
RA Green C.B.;
RT "Immediate early response of the circadian polyA ribonuclease nocturnin to
RT two extracellular stimuli.";
RL RNA 13:745-755(2007).
RN [6]
RP INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=20392228; DOI=10.1111/j.1749-6632.2009.05221.x;
RA Kawai M., Green C.B., Horowitz M., Ackert-Bicknell C., Lecka-Czernik B.,
RA Rosen C.J.;
RT "Nocturnin: a circadian target of Pparg-induced adipogenesis.";
RL Ann. N. Y. Acad. Sci. 1192:131-138(2010).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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 FUNCTION, AND INDUCTION.
RX PubMed=20685873; DOI=10.1210/en.2010-0407;
RA Kawai M., Delany A.M., Green C.B., Adamo M.L., Rosen C.J.;
RT "Nocturnin suppresses igf1 expression in bone by targeting the 3'
RT untranslated region of igf1 mRNA.";
RL Endocrinology 151:4861-4870(2010).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND INTERACTION WITH
RP PPARG.
RX PubMed=20498072; DOI=10.1073/pnas.1000788107;
RA Kawai M., Green C.B., Lecka-Czernik B., Douris N., Gilbert M.R., Kojima S.,
RA Ackert-Bicknell C., Garg N., Horowitz M.C., Adamo M.L., Clemmons D.R.,
RA Rosen C.J.;
RT "A circadian-regulated gene, Nocturnin, promotes adipogenesis by
RT stimulating PPAR-gamma nuclear translocation.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:10508-10513(2010).
RN [10]
RP FUNCTION.
RX PubMed=22082366; DOI=10.1111/j.1749-6632.2011.06213.x;
RA Guntur A.R., Kawai M., Le P., Bouxsein M.L., Bornstein S., Green C.B.,
RA Rosen C.J.;
RT "An essential role for the circadian-regulated gene nocturnin in
RT osteogenesis: the importance of local timekeeping in skeletal
RT homeostasis.";
RL Ann. N. Y. Acad. Sci. 1237:58-63(2011).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21820310; DOI=10.1016/j.cub.2011.07.018;
RA Douris N., Kojima S., Pan X., Lerch-Gaggl A.F., Duong S.Q., Hussain M.M.,
RA Green C.B.;
RT "Nocturnin regulates circadian trafficking of dietary lipid in intestinal
RT enterocytes.";
RL Curr. Biol. 21:1347-1355(2011).
RN [12]
RP FUNCTION, AND INDUCTION.
RX PubMed=22073225; DOI=10.1371/journal.pone.0026954;
RA Niu S., Shingle D.L., Garbarino-Pico E., Kojima S., Gilbert M., Green C.B.;
RT "The circadian deadenylase Nocturnin is necessary for stabilization of the
RT iNOS mRNA in mice.";
RL PLoS ONE 6:E26954-E26954(2011).
RN [13]
RP FUNCTION.
RX PubMed=22331129; DOI=10.1038/oby.2012.37;
RA Hee S.W., Tsai S.H., Chang Y.C., Chang C.J., Yu I.S., Lee P.C., Lee W.J.,
RA Yun-Chia Chang E., Chuang L.M.;
RT "The role of nocturnin in early adipogenesis and modulation of systemic
RT insulin resistance in human.";
RL Obesity 20:1558-1565(2012).
RN [14]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=23449310; DOI=10.1262/jrd.2013-001;
RA Nishikawa S., Hatanaka Y., Tokoro M., Shin S.W., Shimizu N., Nishihara T.,
RA Kato R., Takemoto A., Amano T., Anzai M., Kishigami S., Hosoi Y.,
RA Matsumoto K.;
RT "Functional analysis of nocturnin, a circadian deadenylase, at maternal-to-
RT zygotic transition in mice.";
RL J. Reprod. Dev. 59:258-265(2013).
RN [15]
RP LACK OF ADENYLASE ACTIVITY.
RX PubMed=29860338; DOI=10.1093/nar/gky412;
RA Abshire E.T., Chasseur J., Bohn J.A., Del Rizzo P.A., Freddolino P.L.,
RA Goldstrohm A.C., Trievel R.C.;
RT "The structure of human Nocturnin reveals a conserved ribonuclease domain
RT that represses target transcript translation and abundance in cells.";
RL Nucleic Acids Res. 46:6257-6270(2018).
CC -!- FUNCTION: Phosphatase which catalyzes the conversion of NADP(+) to
CC NAD(+) and of NADPH to NADH (By similarity). Shows a small preference
CC for NADPH over NADP(+) (By similarity). Represses translation and
CC promotes degradation of target mRNA molecules (By similarity). Plays an
CC important role in post-transcriptional regulation of metabolic genes
CC under circadian control (PubMed:20685873, PubMed:20498072). Exerts a
CC rhythmic post-transcriptional control of genes necessary for metabolic
CC functions including nutrient absorption, glucose/insulin sensitivity,
CC lipid metabolism, adipogenesis, inflammation and osteogenesis
CC (PubMed:20498072, PubMed:22082366, PubMed:21820310, PubMed:22073225,
CC PubMed:22331129). Plays an important role in favoring adipogenesis over
CC osteoblastogenesis and acts as a key regulator of the
CC adipogenesis/osteogenesis balance (PubMed:20498072, PubMed:22082366).
CC Promotes adipogenesis by facilitating PPARG nuclear translocation which
CC activates its transcriptional activity (PubMed:20498072). Regulates
CC circadian expression of NOS2 in the liver and negatively regulates the
CC circadian expression of IGF1 in the bone (PubMed:22073225,
CC PubMed:20685873). Critical for proper development of early embryos
CC (PubMed:23449310). {ECO:0000250|UniProtKB:Q9UK39,
CC ECO:0000269|PubMed:20498072, ECO:0000269|PubMed:20685873,
CC ECO:0000269|PubMed:21820310, ECO:0000269|PubMed:22073225,
CC ECO:0000269|PubMed:22082366, ECO:0000269|PubMed:22331129,
CC ECO:0000269|PubMed:23449310}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NADP(+) = NAD(+) + phosphate; Xref=Rhea:RHEA:28050,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:58349; EC=3.1.3.108;
CC Evidence={ECO:0000250|UniProtKB:Q9UK39};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28051;
CC Evidence={ECO:0000250|UniProtKB:Q9UK39};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NADPH = NADH + phosphate; Xref=Rhea:RHEA:60664,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:57945; EC=3.1.3.108;
CC Evidence={ECO:0000250|UniProtKB:Q9UK39};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60665;
CC Evidence={ECO:0000250|UniProtKB:Q9UK39};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9UK39};
CC Note=Binds 2 magnesium ions, but the ions are only loosely bound to the
CC protein. {ECO:0000250|UniProtKB:Q9UK39};
CC -!- SUBUNIT: Interacts with PPARG. {ECO:0000269|PubMed:20498072}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23449310}. Nucleus
CC {ECO:0000269|PubMed:23449310}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:20498072}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q9UK39}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O35710-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O35710-2; Sequence=VSP_016677;
CC -!- TISSUE SPECIFICITY: Highly expressed in the differentiated adipocyte
CC (at protein level). Ubiquitous. {ECO:0000269|PubMed:10521507,
CC ECO:0000269|PubMed:11394964, ECO:0000269|PubMed:20392228}.
CC -!- DEVELOPMENTAL STAGE: Expression is highest in oocytes, begins to
CC decrease after fertilization by the 4-cell stage and then slightly
CC increases up to the blastocyst stage. {ECO:0000269|PubMed:23449310}.
CC -!- INDUCTION: Immediate early gene (IEG) showing acute responses to
CC several stimuli including serum shock, phorbol ester,
CC lipopolysaccharide (LPS) and rosiglitazone, a PPARG agonist. Exhibits a
CC high amplitude circadian rhythm with maximal levels in early evening.
CC In constant darkness or constant light, the amplitude of the rhythm
CC decreases. Expression is regulated by both light and food-entrained
CC cues and by the CLOCK-ARNTL/BMAL1 heterodimer and PPARG. Up-regulated
CC in cells undergoing adipogenesis. {ECO:0000269|PubMed:17400819,
CC ECO:0000269|PubMed:20392228, ECO:0000269|PubMed:20685873,
CC ECO:0000269|PubMed:22073225}.
CC -!- DISRUPTION PHENOTYPE: Mice exhibit metabolic defects including a
CC resistance to diet-induced obesity, decreased fat storage, changes in
CC lipid-related gene expression profiles in the liver, and altered
CC glucose and insulin sensitivities. Exhibit a delayed early embryo
CC development and at 12 weeks of age show enhanced skeletal mass and
CC increased osteoblastogenesis. {ECO:0000269|PubMed:20498072,
CC ECO:0000269|PubMed:21820310, ECO:0000269|PubMed:23449310}.
CC -!- SIMILARITY: Belongs to the CCR4/nocturin family. {ECO:0000305}.
CC -!- CAUTION: Was initially shown to have low deadenylase activity that was
CC lost when the metal-binding Glu was mutated (PubMed:17400819). Later
CC studies showed that the purified protein lacked deadenylase activity
CC (PubMed:29860338). Was subsequently shown to act as a phosphatase (By
CC similarity). {ECO:0000250|UniProtKB:Q9UK39,
CC ECO:0000269|PubMed:17400819, ECO:0000269|PubMed:29860338}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB62717.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U70139; AAB62717.1; ALT_FRAME; mRNA.
DR EMBL; AF183960; AAD56547.1; -; mRNA.
DR EMBL; AF199491; AAG01384.1; -; mRNA.
DR EMBL; AK087790; BAC40004.1; -; mRNA.
DR CCDS; CCDS17336.1; -. [O35710-1]
DR RefSeq; NP_033964.1; NM_009834.2. [O35710-1]
DR AlphaFoldDB; O35710; -.
DR SMR; O35710; -.
DR DIP; DIP-60436N; -.
DR IntAct; O35710; 1.
DR STRING; 10090.ENSMUSP00000023849; -.
DR iPTMnet; O35710; -.
DR PhosphoSitePlus; O35710; -.
DR EPD; O35710; -.
DR MaxQB; O35710; -.
DR PaxDb; O35710; -.
DR PRIDE; O35710; -.
DR ProteomicsDB; 252916; -. [O35710-1]
DR ProteomicsDB; 252917; -. [O35710-2]
DR Antibodypedia; 16153; 129 antibodies from 30 providers.
DR DNASU; 12457; -.
DR Ensembl; ENSMUST00000023849; ENSMUSP00000023849; ENSMUSG00000023087. [O35710-1]
DR Ensembl; ENSMUST00000144826; ENSMUSP00000141416; ENSMUSG00000023087. [O35710-2]
DR Ensembl; ENSMUST00000167780; ENSMUSP00000130347; ENSMUSG00000023087. [O35710-1]
DR GeneID; 12457; -.
DR KEGG; mmu:12457; -.
DR UCSC; uc008pdm.2; mouse. [O35710-1]
DR CTD; 25819; -.
DR MGI; MGI:109382; Noct.
DR VEuPathDB; HostDB:ENSMUSG00000023087; -.
DR eggNOG; KOG0620; Eukaryota.
DR GeneTree; ENSGT00940000155249; -.
DR HOGENOM; CLU_016428_1_2_1; -.
DR InParanoid; O35710; -.
DR OMA; FRLKRDC; -.
DR PhylomeDB; O35710; -.
DR TreeFam; TF323175; -.
DR BRENDA; 3.1.13.4; 3474.
DR BRENDA; 3.1.3.108; 3474.
DR BioGRID-ORCS; 12457; 2 hits in 41 CRISPR screens.
DR ChiTaRS; Noct; mouse.
DR PRO; PR:O35710; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; O35710; protein.
DR Bgee; ENSMUSG00000023087; Expressed in secondary oocyte and 262 other tissues.
DR ExpressionAtlas; O35710; baseline and differential.
DR Genevisible; O35710; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000932; C:P-body; IDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR GO; GO:0019178; F:NADP phosphatase activity; ISS:UniProtKB.
DR GO; GO:0102757; F:NADPH phosphatase activity; ISS:UniProtKB.
DR GO; GO:0004535; F:poly(A)-specific ribonuclease activity; IDA:UniProtKB.
DR GO; GO:0032922; P:circadian regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0007623; P:circadian rhythm; IEP:UniProtKB.
DR GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IGI:MGI.
DR GO; GO:0048255; P:mRNA stabilization; IMP:UniProtKB.
DR GO; GO:0006739; P:NADP metabolic process; ISS:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; IMP:UniProtKB.
DR GO; GO:0033962; P:P-body assembly; IGI:MGI.
DR GO; GO:0045600; P:positive regulation of fat cell differentiation; IMP:UniProtKB.
DR GO; GO:0042752; P:regulation of circadian rhythm; IMP:UniProtKB.
DR GO; GO:0045995; P:regulation of embryonic development; IMP:UniProtKB.
DR GO; GO:0009991; P:response to extracellular stimulus; IDA:UniProtKB.
DR GO; GO:0032496; P:response to lipopolysaccharide; IDA:UniProtKB.
DR CDD; cd09096; Deadenylase_nocturnin; 1.
DR Gene3D; 3.60.10.10; -; 1.
DR InterPro; IPR034965; Deadenylase_nocturnin.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR InterPro; IPR040109; Nocturnin.
DR PANTHER; PTHR12121:SF45; PTHR12121:SF45; 1.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR SUPFAM; SSF56219; SSF56219; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Biological rhythms; Cytoplasm; Hydrolase; Magnesium;
KW Metal-binding; Mitochondrion; Nucleus; Reference proteome; Repressor;
KW RNA-binding; Transit peptide.
FT TRANSIT 1..73
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 74..429
FT /note="Nocturnin"
FT /evidence="ECO:0000255"
FT /id="PRO_0000218569"
FT REGION 21..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..351
FT /note="Interaction with PPARG"
FT /evidence="ECO:0000269|PubMed:20498072"
FT BINDING 193
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9UK39"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UK39"
FT BINDING 217..219
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UK39"
FT BINDING 261
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UK39"
FT BINDING 284..287
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UK39"
FT BINDING 322..324
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UK39"
FT BINDING 412
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UK39"
FT VAR_SEQ 1..64
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9038221"
FT /id="VSP_016677"
SQ SEQUENCE 429 AA; 48301 MW; CB9FB55D84E13942 CRC64;
MYQSPRRLCS ALLLRDAPGL RRTLVPGPRR TLAPPVLGSR PKSPQLQAAA ASGAARSRPR
TVSSMGNGTS RLYSALAKTV NSSAAAQHPE YLVSTDPEHL EPIDPKELLE ECRAVLHTRP
PRYQRDFVDL RTDCSSSHSP IRVMQWNILA QALGEGKDNF VQCPVEALKW EERKCLILEE
ILAYQPDILC LQEVDHYFDT FQPLLSRLGY QGTFFPKPWS PCLDVEHNNG PDGCALFFLQ
NRFKLISSTN IRLTAMTLKT NQVAIAQTLE CKESGRQFCI AVTHLKARTG WERFRSAQGC
DLLQNLQNIT QGAKIPLIVC GDFNAEPTEE VYKHFASSSL NLNSAYKLLS PDGQSEPPYT
TWKIRTSGEC RHTLDYIWYS RHALSVTSAL DLLTEEQIGP NRLPSFHYPS DHLSLVCDFS
FNEEPHELF
