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O35710

- NOCT_MOUSE

UniProt

O35710 - NOCT_MOUSE

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Protein

Nocturnin

Gene

Ccrn4l

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Circadian deadenylase which plays an important role in post-transcriptional regulation of metabolic genes under circadian control. Degrades poly(A) tails of specific target mRNAs leading to their degradation and suppression of translation. Exerts a rhythmic post-transcriptional control of genes necessary for metabolic functions including nutrient absorption, glucose/insulin sensitivity, lipid metabolism, adipogenesis, inflammation and osteogenesis. Plays an important role in favoring adipogenesis over osteoblastogenesis and acts as a key regulator of the adipogenesis/osteogenesis balance. Promotes adipogenesis by activating PPARG transcriptional activity in a deadenylase-independent manner by facilitating its nuclear translocation. Regulates circadian expression of NOS2 in the liver and negatively regulates the circadian expression of IGF1 in the bone. Critical for proper development of early embryos.8 Publications

Catalytic activityi

Exonucleolytic cleavage of poly(A) to 5'-AMP.

Cofactori

Mg2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei193 – 1931By similarity
Metal bindingi193 – 1931Magnesium 1By similarity
Metal bindingi322 – 3221Magnesium 2By similarity
Metal bindingi324 – 3241Magnesium 2By similarity
Active sitei375 – 3751By similarity
Active sitei412 – 4121By similarity
Metal bindingi412 – 4121Magnesium 2By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. mRNA binding Source: UniProtKB
  3. poly(A)-specific ribonuclease activity Source: UniProtKB

GO - Biological processi

  1. circadian regulation of gene expression Source: UniProtKB
  2. circadian rhythm Source: UniProtKB
  3. cytoplasmic mRNA processing body assembly Source: MGI
  4. deadenylation-dependent decapping of nuclear-transcribed mRNA Source: MGI
  5. mRNA processing Source: UniProtKB-KW
  6. mRNA stabilization Source: UniProtKB
  7. negative regulation of gene expression Source: UniProtKB
  8. negative regulation of osteoblast differentiation Source: UniProtKB
  9. positive regulation of fat cell differentiation Source: UniProtKB
  10. regulation of circadian rhythm Source: UniProtKB
  11. regulation of embryonic development Source: UniProtKB
  12. response to extracellular stimulus Source: UniProtKB
  13. response to lipopolysaccharide Source: UniProtKB
  14. RNA phosphodiester bond hydrolysis, exonucleolytic Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Exonuclease, Hydrolase, Nuclease

Keywords - Biological processi

Biological rhythms, mRNA processing

Keywords - Ligandi

Magnesium, Metal-binding, RNA-binding

Enzyme and pathway databases

BRENDAi3.1.13.4. 3474.
ReactomeiREACT_198620. BMAL1:CLOCK,NPAS2 activates circadian gene expression.

Names & Taxonomyi

Protein namesi
Recommended name:
Nocturnin (EC:3.1.13.4)
Alternative name(s):
Carbon catabolite repression 4-like protein
Circadian deadenylase NOC
Gene namesi
Name:Ccrn4l
Synonyms:Ccr4, Noc
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 3

Organism-specific databases

MGIiMGI:109382. Ccrn4l.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytoplasmic mRNA processing body Source: MGI
  3. nucleus Source: UniProtKB
  4. perinuclear region of cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Mice exhibit metabolic defects including a resistance to diet-induced obesity, decreased fat storage, changes in lipid-related gene expression profiles in the liver, and altered glucose and insulin sensitivities. Exhibit a delayed early embryo development and at 12 weeks of age show enhanced skeletal mass and increased osteoblastogenesis.3 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 429429NocturninPRO_0000218569Add
BLAST

Proteomic databases

MaxQBiO35710.
PaxDbiO35710.
PRIDEiO35710.

PTM databases

PhosphoSiteiO35710.

Expressioni

Tissue specificityi

Highly expressed in the differentiated adipocyte (at protein level). Ubiquitous.3 Publications

Developmental stagei

Expression is highest in oocytes, begins to decrease after fertilization by the 4-cell stage and then slightly increases up to the blastocyst stage.1 Publication

Inductioni

Immediate early gene (IEG) showing acute responses to several stimuli including serum shock, phorbol ester, lipopolysaccharide (LPS) and rosiglitazone, a PPARG agonist. Exhibits a high amplitude circadian rhythm with maximal levels in early evening. In constant darkness or constant light, the amplitude of the rhythm decreases. Expression is regulated by both light and food-entrained cues and by the CLOCK-ARNTL/BMAL1 heterodimer and PPARG. Up-regulated in cells undergoing adipogenesis.4 Publications

Gene expression databases

BgeeiO35710.
CleanExiMM_CCR4.
ExpressionAtlasiO35710. baseline and differential.
GenevestigatoriO35710.

Interactioni

Subunit structurei

Interacts with PPARG.1 Publication

Protein-protein interaction databases

DIPiDIP-60436N.

Structurei

3D structure databases

ProteinModelPortaliO35710.
SMRiO35710. Positions 120-422.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni341 – 35111Interaction with PPARGAdd
BLAST

Sequence similaritiesi

Belongs to the CCR4/nocturin family.Curated

Phylogenomic databases

eggNOGiCOG5239.
GeneTreeiENSGT00550000074364.
HOGENOMiHOG000237357.
HOVERGENiHBG006512.
InParanoidiO35710.
OMAiPEYLVSP.
OrthoDBiEOG7Z95MC.
PhylomeDBiO35710.
TreeFamiTF323175.

Family and domain databases

Gene3Di3.60.10.10. 1 hit.
InterProiIPR005135. Endo/exonuclease/phosphatase.
[Graphical view]
PfamiPF03372. Exo_endo_phos. 1 hit.
[Graphical view]
SUPFAMiSSF56219. SSF56219. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O35710-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MYQSPRRLCS ALLLRDAPGL RRTLVPGPRR TLAPPVLGSR PKSPQLQAAA
60 70 80 90 100
ASGAARSRPR TVSSMGNGTS RLYSALAKTV NSSAAAQHPE YLVSTDPEHL
110 120 130 140 150
EPIDPKELLE ECRAVLHTRP PRYQRDFVDL RTDCSSSHSP IRVMQWNILA
160 170 180 190 200
QALGEGKDNF VQCPVEALKW EERKCLILEE ILAYQPDILC LQEVDHYFDT
210 220 230 240 250
FQPLLSRLGY QGTFFPKPWS PCLDVEHNNG PDGCALFFLQ NRFKLISSTN
260 270 280 290 300
IRLTAMTLKT NQVAIAQTLE CKESGRQFCI AVTHLKARTG WERFRSAQGC
310 320 330 340 350
DLLQNLQNIT QGAKIPLIVC GDFNAEPTEE VYKHFASSSL NLNSAYKLLS
360 370 380 390 400
PDGQSEPPYT TWKIRTSGEC RHTLDYIWYS RHALSVTSAL DLLTEEQIGP
410 420
NRLPSFHYPS DHLSLVCDFS FNEEPHELF
Length:429
Mass (Da):48,301
Last modified:November 2, 2001 - v3
Checksum:iCB9FB55D84E13942
GO
Isoform 2 (identifier: O35710-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-64: Missing.

Note: No experimental confirmation available.

Show »
Length:365
Mass (Da):41,500
Checksum:i762CA86E0F907EB8
GO

Sequence cautioni

The sequence AAB62717.1 differs from that shown. Reason: Frameshift at position 125. Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6464Missing in isoform 2. 1 PublicationVSP_016677Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U70139 mRNA. Translation: AAB62717.1. Frameshift.
AF183960 mRNA. Translation: AAD56547.1.
AF199491 mRNA. Translation: AAG01384.1.
AK087790 mRNA. Translation: BAC40004.1.
CCDSiCCDS17336.1. [O35710-1]
RefSeqiNP_033964.1. NM_009834.2. [O35710-1]
XP_006501020.1. XM_006500957.1. [O35710-2]
UniGeneiMm.86541.

Genome annotation databases

EnsembliENSMUST00000023849; ENSMUSP00000023849; ENSMUSG00000023087. [O35710-1]
ENSMUST00000167780; ENSMUSP00000130347; ENSMUSG00000023087. [O35710-1]
GeneIDi12457.
KEGGimmu:12457.
UCSCiuc008pdm.2. mouse. [O35710-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U70139 mRNA. Translation: AAB62717.1 . Frameshift.
AF183960 mRNA. Translation: AAD56547.1 .
AF199491 mRNA. Translation: AAG01384.1 .
AK087790 mRNA. Translation: BAC40004.1 .
CCDSi CCDS17336.1. [O35710-1 ]
RefSeqi NP_033964.1. NM_009834.2. [O35710-1 ]
XP_006501020.1. XM_006500957.1. [O35710-2 ]
UniGenei Mm.86541.

3D structure databases

ProteinModelPortali O35710.
SMRi O35710. Positions 120-422.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-60436N.

PTM databases

PhosphoSitei O35710.

Proteomic databases

MaxQBi O35710.
PaxDbi O35710.
PRIDEi O35710.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000023849 ; ENSMUSP00000023849 ; ENSMUSG00000023087 . [O35710-1 ]
ENSMUST00000167780 ; ENSMUSP00000130347 ; ENSMUSG00000023087 . [O35710-1 ]
GeneIDi 12457.
KEGGi mmu:12457.
UCSCi uc008pdm.2. mouse. [O35710-1 ]

Organism-specific databases

CTDi 25819.
MGIi MGI:109382. Ccrn4l.

Phylogenomic databases

eggNOGi COG5239.
GeneTreei ENSGT00550000074364.
HOGENOMi HOG000237357.
HOVERGENi HBG006512.
InParanoidi O35710.
OMAi PEYLVSP.
OrthoDBi EOG7Z95MC.
PhylomeDBi O35710.
TreeFami TF323175.

Enzyme and pathway databases

BRENDAi 3.1.13.4. 3474.
Reactomei REACT_198620. BMAL1:CLOCK,NPAS2 activates circadian gene expression.

Miscellaneous databases

ChiTaRSi Ccrn4l. mouse.
NextBioi 281308.
PROi O35710.
SOURCEi Search...

Gene expression databases

Bgeei O35710.
CleanExi MM_CCR4.
ExpressionAtlasi O35710. baseline and differential.
Genevestigatori O35710.

Family and domain databases

Gene3Di 3.60.10.10. 1 hit.
InterProi IPR005135. Endo/exonuclease/phosphatase.
[Graphical view ]
Pfami PF03372. Exo_endo_phos. 1 hit.
[Graphical view ]
SUPFAMi SSF56219. SSF56219. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of two age-induced intracisternal A-particle-related transcripts in the mouse liver. Transcriptional read-through into an open reading frame with similarities to the yeast ccr4 transcription factor."
    Puech A., Dupressoir A., Loireau M.-P., Mattei M.-G., Heidmann T.
    J. Biol. Chem. 272:5995-6003(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Strain: DBA/2J.
    Tissue: Liver.
  2. "Characterization of a mammalian gene related to the yeast CCR4 general transcription factor and revealed by transposon insertion."
    Dupressoir A., Barbot W., Loireau M.-P., Heidmann T.
    J. Biol. Chem. 274:31068-31075(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Strain: BALB/c.
    Tissue: Brain.
  3. "Rhythmic expression of nocturnin mRNA in multiple tissues of the mouse."
    Wang Y., Osterbur D.L., Megaw P.L., Tosini G., Fukuhara C., Green C.B., Besharse J.C.
    BMC Dev. Biol. 1:9-9(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CIRCADIAN EXPRESSION, TISSUE SPECIFICITY.
    Strain: BALB/c.
    Tissue: Retina.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Ovary.
  5. "Immediate early response of the circadian polyA ribonuclease nocturnin to two extracellular stimuli."
    Garbarino-Pico E., Niu S., Rollag M.D., Strayer C.A., Besharse J.C., Green C.B.
    RNA 13:745-755(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION.
  6. Cited for: INDUCTION, TISSUE SPECIFICITY.
  7. "Nocturnin suppresses igf1 expression in bone by targeting the 3' untranslated region of igf1 mRNA."
    Kawai M., Delany A.M., Green C.B., Adamo M.L., Rosen C.J.
    Endocrinology 151:4861-4870(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION.
  8. "A circadian-regulated gene, Nocturnin, promotes adipogenesis by stimulating PPAR-gamma nuclear translocation."
    Kawai M., Green C.B., Lecka-Czernik B., Douris N., Gilbert M.R., Kojima S., Ackert-Bicknell C., Garg N., Horowitz M.C., Adamo M.L., Clemmons D.R., Rosen C.J.
    Proc. Natl. Acad. Sci. U.S.A. 107:10508-10513(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, INTERACTION WITH PPARG.
  9. "An essential role for the circadian-regulated gene nocturnin in osteogenesis: the importance of local timekeeping in skeletal homeostasis."
    Guntur A.R., Kawai M., Le P., Bouxsein M.L., Bornstein S., Green C.B., Rosen C.J.
    Ann. N. Y. Acad. Sci. 1237:58-63(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "Nocturnin regulates circadian trafficking of dietary lipid in intestinal enterocytes."
    Douris N., Kojima S., Pan X., Lerch-Gaggl A.F., Duong S.Q., Hussain M.M., Green C.B.
    Curr. Biol. 21:1347-1355(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  11. "The circadian deadenylase Nocturnin is necessary for stabilization of the iNOS mRNA in mice."
    Niu S., Shingle D.L., Garbarino-Pico E., Kojima S., Gilbert M., Green C.B.
    PLoS ONE 6:E26954-E26954(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION.
  12. "The role of nocturnin in early adipogenesis and modulation of systemic insulin resistance in human."
    Hee S.W., Tsai S.H., Chang Y.C., Chang C.J., Yu I.S., Lee P.C., Lee W.J., Yun-Chia Chang E., Chuang L.M.
    Obesity 20:1558-1565(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "Functional analysis of nocturnin, a circadian deadenylase, at maternal-to-zygotic transition in mice."
    Nishikawa S., Hatanaka Y., Tokoro M., Shin S.W., Shimizu N., Nishihara T., Kato R., Takemoto A., Amano T., Anzai M., Kishigami S., Hosoi Y., Matsumoto K.
    J. Reprod. Dev. 59:258-265(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiNOCT_MOUSE
AccessioniPrimary (citable) accession number: O35710
Secondary accession number(s): Q9QZG9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 2, 2001
Last modified: November 26, 2014
This is version 111 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3