Reviewed, UniProtKB/Swiss-Prot Q91YA8 (CLOCK_SPAJD)

Names and origin

Protein names

Recommended name:
    Circadian locomoter output cycles protein kaput
    EC=2.3.1.48

Gene names

Name:

Clock

Organism

Spalax judaei (Blind subterranean mole rat)

Taxonomic identifier

134510 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Spalacidae › Spalacinae › Spalax

Protein attributes

Sequence length	865 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	ARNTL/2-CLOCK heterodimers activate E-box element (3'-CACGTG-5') 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 By similarity.
Catalytic activity	Acetyl-CoA + histone = CoA + acetylhistone.
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 By similarity. Nucleus By similarity. Note: Shuffling between the cytoplasm and the nucleus is under circadian regulation and is ARNTL-dependent By similarity.
Post-translational modification	Phosphorylation is dependent on CLOCK-ARNTL heterodimer formation By similarity.
Sequence similarities	Contains 1 basic helix-loop-helix (bHLH) domain. Contains 1 PAC (PAS-associated C-terminal) domain. Contains 2 PAS (PER-ARNT-SIM) domains.

Ontologies

Keywords
Biological process	Biological rhythms Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Domain	Repeat
Ligand	DNA-binding
Molecular function	Activator Transferase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW rhythmic process Inferred from electronic annotation. Source: UniProtKB-KW signal transduction Inferred from electronic annotation. Source: InterPro transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	histone acetyltransferase activity Inferred from electronic annotation. Source: EC signal transducer activity Inferred from electronic annotation. Source: InterPro transcription factor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 865	865	Circadian locomoter output cycles protein kaput		PRO_0000262641
Regions
	Domain	48 – 85	38	Helix-loop-helix motif
	Domain	107 – 177	71	PAS 1
	Domain	262 – 332	71	PAS 2
	Domain	336 – 379	44	PAC
	DNA binding	35 – 47	13	Basic motif
	Region	514 – 564	51	Implicated in the circadian rhythmicity By similarity
	Compositional bias	483 – 847	365	Gln-rich
Amino acid modifications
	Modified residue	408	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q91YA8-1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: B85AB1B359A5750B	FASTA	865	97,421
	10 20 30 40 50 60 MLFTVSCSKM SSIVDRDDSS IFDGLVEEDD KNKAKRVSRN KSEKKRRDQF NVLIKELGSM 70 80 90 100 110 120 LPGNAREMDK 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 TIDPKEPSTY EYMRFIGNFK SLNSVPTSAH NGFEGTIQRT 250 260 270 280 290 300 HRLSYEDRVC SVATVRLATP 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 IEESLPDATA DKGQDSGSDN RINTVSLKEA 430 440 450 460 470 480 LERFDHSPTP SASSRSSRKS SHTAVSDPSS TPTKIPTDTS TPPRQHLPAH EKMAQRRSSF 490 500 510 520 530 540 SSQSMNSQSV GPSLTQPVIS 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

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: 11707566] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AJ318059 mRNA. Translation: CAC85405.1.
3D structure databases
HSSP	HSSP built from PDB template 1P97 based on UniProtKB Q99814.
ModBase	Search...
Phylogenomic databases
HOVERGEN	Q91YA8.
Family and domain databases
InterPro	IPR001092. HLH_basic. IPR011598. HLH_DNA_bd. IPR001067. Nuc_translocat. IPR001610. PAC. IPR000014. PAS. IPR013767. PAS_fold. IPR013655. PAS_fold_3. [Graphical view]
Gene3D	G3DSA:4.10.280.10. HLH_DNA_bd. 1 hit.
Pfam	PF00010. HLH. 1 hit. PF00989. PAS. 1 hit. PF08447. PAS_3. 1 hit. [Graphical view]
PRINTS	PR00785. NCTRNSLOCATR.
SMART	SM00353. HLH. 1 hit. SM00086. PAC. 1 hit. SM00091. PAS. 2 hits. [Graphical view]
PROSITE	PS50888. HLH. 1 hit. PS50113. PAC. False negative. PS50112. PAS. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CLOCK_SPAJD

Accession

Primary (citable) accession number: Q91YA8

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2006
Last sequence update:	December 1, 2001
Last modified:	June 16, 2009
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)