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Q91YB0 (CLOCK_NANGA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Circadian locomoter output cycles protein kaput
EC=2.3.1.48
Gene names
Name:Clock
OrganismNannospalax galili (Northern Israeli blind subterranean mole rat) (Spalax galili)
Taxonomic identifier1026970 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Spalacidae › Spalacinae › Nannospalax

Protein attributes

Sequence length865 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

ARNTL/2-CLOCK heterodimers activate E-box element (5'-CACGTG-3') transcription of a number of proteins of the circadian clock. Activates transcription of PER1 and PER2. This transcription is inhibited in a feedback loop by PER and CRY proteins. Has intrinsic histone acetyltransferase activity and this enzymatic function contributes to chromatin-remodeling events implicated in circadian control of gene expression. Acetylates primarily histones H3 and H4. Acetylates also a non-histone substrate: ARNTL. Plays a role in DNA damage response (DDR) signaling during the S phase By similarity. Ref.1

Catalytic activity

Acetyl-CoA + [histone] = CoA + acetyl-[histone].

Subunit structure

Component of the circadian clock oscillator which includes the CRY proteins, CLOCK or NPAS2, ARNTL or ARNTL2, CSNK1D and/or CSNK1E, TIMELESS and the PER proteins. Efficient DNA binding requires dimerization with another bHLH protein. Heterodimerization with ARNTL is required for E-box-dependent transactivation, for CLOCK nuclear translocation and degradation, and, for phosphorylation of both CLOCK and ARNTL. Interaction with PER and CRY proteins requires translocation to the nucleus. Interaction of the CLOCK-ARNTL heterodimer with PER or CRY inhibits transcription activation. Binds weakly ARNTL and ARNTL2 to form heterodimers which bind poorly to the E-box motif By similarity.

Subcellular location

Cytoplasm. Nucleus. Chromosome By similarity. Note: Localizes to sites of DNA damage in a H2AX-independent manner. Shuffling between the cytoplasm and the nucleus is under circadian regulation and is ARNTL-dependent By similarity.

Tissue specificity

Expressed in brain, retina and harderian gland as well as in peripheral tissues, kidney and liver. Localizes in the brain to the suprachiasmatic nucleus (SCN). Ref.1

Induction

Exhibits no circadian rhythm expression. Ref.1

Post-translational modification

Phosphorylation is dependent on CLOCK-ARNTL heterodimer formation By similarity.

Sequence similarities

Contains 1 bHLH (basic helix-loop-helix) domain.

Contains 1 PAC (PAS-associated C-terminal) domain.

Contains 2 PAS (PER-ARNT-SIM) domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 865865Circadian locomoter output cycles protein kaput
PRO_0000262640

Regions

Domain34 – 8451bHLH
Domain107 – 17771PAS 1
Domain262 – 33271PAS 2
Domain336 – 37944PAC
Region514 – 56451Implicated in the circadian rhythmicity By similarity
Compositional bias483 – 847365Gln-rich

Amino acid modifications

Modified residue4081Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q91YB0 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: E5003191B7578C21

FASTA86597,437
        10         20         30         40         50         60 
MLFTVSCSKM SSIVDRDDSS IFDGLVEEDD KDKAKRVSRN KSEKKRRDQF NVLIKELGSM 

        70         80         90        100        110        120 
LPGNARKMDK STVLQKSIDF LRKHKEITAQ SDASEIRQDW KPTFLSNEEF TQLMLEALDG 

       130        140        150        160        170        180 
FFLAIMTDGS IIYVSESVTS LLEHLPSDLV DQSVFNFIPE GEHSEVYKIL STHLLESDSL 

       190        200        210        220        230        240 
TPEYLKSKNQ LEFCCHMLRG TVDPKEPSTY EYVRFIGNFK SLNSVPTSAH NGFEGTIQRT 

       250        260        270        280        290        300 
HRPSYEDRVC FVATVRLATP QFIKEMCTVE EPNEEFTSRH SLEWKFLFLD HRAPPIIGYL 

       310        320        330        340        350        360 
PFEVLGTSGY DYYHVDDLEN LAKCHEHLMQ YGKGKSCYYR FLTKGQQWIW LQTHYYITYH 

       370        380        390        400        410        420 
QWNSRPEFIV CTHTVVSYAE VRAERRRELG IEESLPDAAA DKSQDSGSDN RINTVSLKEA 

       430        440        450        460        470        480 
LERFDHSPTP SASSRSSRKS SHTAVSDPSS TPTKIPTDTS TPPRQHLPAH EKMAQRRSSF 

       490        500        510        520        530        540 
SSQSMNSQSV GPSLTQPVMS QAANLPVPQG MSQFQFSAQL GAMQHLKDQL EQRTRMIEAN 

       550        560        570        580        590        600 
IHRQQEELRK IQEQLQMVHG QGLQMFLQQS NPGLNFGSVQ LSSGNSSNIQ QLTPINMQGQ 

       610        620        630        640        650        660 
VVPTNQIQSG MNAGHIGTSQ HLIQQQSLQS TSTQQSQQSV MSGHSQQTSL ASQTQSTLTA 

       670        680        690        700        710        720 
PLYNTMVISQ PAPGSMVQIP SSMPQNSTQS ATVTTFTQDR QIRFSQGQQL VTKLVTAPVA 

       730        740        750        760        770        780 
CGAVMVPSTM LMGQVVTAYP TFATQQQQAQ TLSVTQQQPQ QQQPQQQQPQ QQQPQQQQQS 

       790        800        810        820        830        840 
SQEQQLPSVP QPSQAQLTQS PQQFLQTSRL LHGNPSTQLI LSAAFPLQQS TFPPSHHQQH 

       850        860 
QSQQQQQLSR HRTDSLTDPS KVQPQ

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References

[1]"Biological clock in total darkness: the Clock/MOP3 circadian system of the blind subterranean mole rat."
Avivi A., Albrecht U., Oster H., Joel A., Beiles A., Nevo E.
Proc. Natl. Acad. Sci. U.S.A. 98:13751-13756(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH ARNTL, INDUCTION, TISSUE SPECIFICITY, FUNCTION.
Tissue: Brain.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AJ318057 mRNA. Translation: CAC85403.1.

3D structure databases

HSSPHSSP built from PDB template 1AM9 based on UniProtKB P36956.
ProteinModelPortalQ91YB0.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG050997.

Family and domain databases

Gene3D4.10.280.10. 1 hit.
InterProIPR011598. bHLH_dom.
IPR001067. Nuc_translocat.
IPR001610. PAC.
IPR000014. PAS.
IPR013767. PAS_fold.
IPR013655. PAS_fold_3.
[Graphical view]
PfamPF00010. HLH. 1 hit.
PF00989. PAS. 1 hit.
PF08447. PAS_3. 1 hit.
[Graphical view]
PRINTSPR00785. NCTRNSLOCATR.
SMARTSM00353. HLH. 1 hit.
SM00086. PAC. 1 hit.
SM00091. PAS. 2 hits.
[Graphical view]
SUPFAMSSF47459. HLH_basic. 1 hit.
PROSITEPS50888. BHLH. 1 hit.
PS50113. PAC. False negative.
PS50112. PAS. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCLOCK_NANGA
AccessionPrimary (citable) accession number: Q91YB0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: December 1, 2001
Last modified: May 1, 2013
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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