NOCT_RAT
ID NOCT_RAT Reviewed; 428 AA.
AC Q9ET55; G3V7F4;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 11-DEC-2013, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Nocturnin {ECO:0000312|RGD:1587344};
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|RGD:1587344}; Synonyms=Ccr4, Ccrn4l, Noc;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Li P.W., Adams M.D., Amanatides P.G., Baden-Tillson H.,
RA Barnstead M., Chin S.H., Dew I., Evans C.A., Ferriera S., Flanigan M.,
RA Fosler C., Glodek A., Gu Z., Holt R.A., Jennings D., Kraft C.L., Lu F.,
RA Nguyen T., Nusskern D.R., Pfannkoch C.M., Sitter C., Sutton G.G.,
RA Venter J.C., Wang Z., Woodage T., Zheng X.H., Zhong F.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 74-326.
RC TISSUE=Retina;
RA Wang Y., Osterbur D.L., Green C.B., Besharse J.C.;
RT "Mammalian homologs of Xenopus nocturnin: conservation of structure and
RT circadian regulation.";
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). Exerts a rhythmic post-
CC transcriptional control of genes necessary for metabolic functions
CC including nutrient absorption, glucose/insulin sensitivity, lipid
CC metabolism, adipogenesis, inflammation and osteogenesis (By
CC similarity). Plays an important role in favoring adipogenesis over
CC osteoblastogenesis and acts as a key regulator of the
CC adipogenesis/osteogenesis balance (By similarity). Promotes
CC adipogenesis by facilitating PPARG nuclear translocation which
CC activates its transcriptional activity (By similarity). Regulates
CC circadian expression of NOS2 in the liver and negatively regulates the
CC circadian expression of IGF1 in the bone (By similarity). Critical for
CC proper development of early embryos (By similarity).
CC {ECO:0000250|UniProtKB:O35710, ECO:0000250|UniProtKB:Q9UK39}.
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:0000250|UniProtKB:O35710}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O35710}. Nucleus
CC {ECO:0000250|UniProtKB:O35710}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:O35710}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q9UK39}.
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 (By similarity). Later
CC studies showed that the purified protein lacked deadenylase activity
CC (By similarity). Was subsequently shown to act as a phosphatase (By
CC similarity). {ECO:0000250|UniProtKB:O35710,
CC ECO:0000250|UniProtKB:Q9UK39}.
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DR EMBL; AABR06016602; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH474003; EDM15000.1; -; Genomic_DNA.
DR EMBL; AF199495; AAG01390.1; -; mRNA.
DR RefSeq; NP_612535.1; NM_138526.1.
DR AlphaFoldDB; Q9ET55; -.
DR SMR; Q9ET55; -.
DR STRING; 10116.ENSRNOP00000014348; -.
DR PaxDb; Q9ET55; -.
DR PRIDE; Q9ET55; -.
DR Ensembl; ENSRNOT00000014348; ENSRNOP00000014348; ENSRNOG00000010799.
DR GeneID; 310395; -.
DR KEGG; rno:310395; -.
DR UCSC; RGD:1587344; rat.
DR CTD; 25819; -.
DR RGD; 1587344; Noct.
DR eggNOG; KOG0620; Eukaryota.
DR GeneTree; ENSGT00940000155249; -.
DR HOGENOM; CLU_016428_1_2_1; -.
DR InParanoid; Q9ET55; -.
DR OMA; FRLKRDC; -.
DR OrthoDB; 1387401at2759; -.
DR TreeFam; TF323175; -.
DR PRO; PR:Q9ET55; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Proteomes; UP000234681; Chromosome 2.
DR Bgee; ENSRNOG00000010799; Expressed in quadriceps femoris and 20 other tissues.
DR Genevisible; Q9ET55; RN.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000932; C:P-body; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS: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; ISS: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; ISS:UniProtKB.
DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0007623; P:circadian rhythm; ISO:RGD.
DR GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; ISO:RGD.
DR GO; GO:0048255; P:mRNA stabilization; ISS:UniProtKB.
DR GO; GO:0006739; P:NADP metabolic process; ISS:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; ISS:UniProtKB.
DR GO; GO:0033962; P:P-body assembly; ISO:RGD.
DR GO; GO:0045600; P:positive regulation of fat cell differentiation; ISS:UniProtKB.
DR GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
DR GO; GO:0045995; P:regulation of embryonic development; ISS:UniProtKB.
DR GO; GO:0009991; P:response to extracellular stimulus; ISS:UniProtKB.
DR GO; GO:0032496; P:response to lipopolysaccharide; ISS: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 2: Evidence at transcript level;
KW Biological rhythms; Cytoplasm; Hydrolase; Magnesium; Metal-binding;
KW Mitochondrion; Nucleus; Reference proteome; Repressor; RNA-binding;
KW Transit peptide.
FT TRANSIT 1..72
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 73..428
FT /note="Nocturnin"
FT /evidence="ECO:0000255"
FT /id="PRO_0000424685"
FT REGION 21..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..350
FT /note="Interaction with PPARG"
FT /evidence="ECO:0000250|UniProtKB:O35710"
FT BINDING 192
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9UK39"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UK39"
FT BINDING 216..218
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UK39"
FT BINDING 260
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UK39"
FT BINDING 283..286
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UK39"
FT BINDING 321..323
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UK39"
FT BINDING 411
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UK39"
FT CONFLICT 94
FT /note="A -> P (in Ref. 3; AAG01390)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="F -> L (in Ref. 3; AAG01390)"
FT /evidence="ECO:0000305"
FT CONFLICT 304
FT /note="N -> S (in Ref. 3; AAG01390)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 428 AA; 48122 MW; 44D116EA73D17B74 CRC64;
MYQSPRRLCS ALLLRDAPGL RRTLVPGPRR TLAPPVLGSR PASPQLQAAA SGAARSRPRT
VSPMGNGTSR LYSALAKTIN SSAAAQHPEY LVSADPEHLE PIDPKELLEE CRAVLHTRPP
RYQRDFVDLR TDCSSSHPPI RVMQWNILAQ ALGEGKDNFV QCPVEALKWE ERKCLILEEI
LAYQPDILCL QEVDHYFDTF QPLLSRLGYQ GTFFPKPWSP CLDVEHNNGP DGCALFFLQS
RFKLINSTNI RLTAMTLKTN QVAIAQTLEC KESGRQFCIA VTHLKARTGW ERFRSAQGCD
LLQNLQNITE GAKIPLIVCG DFNAEPTEEV YKHFASSSLN LNSAYKLLSP DGQSEPPYTT
WKIRTSGECR HTLDYIWYSR HALSVTSALD LLTEEQIGPN RLPSFHYPSD HLSLVCDFSF
NEEPDELL
