Nucleobindin-1 (NUCB1), also known as calnuc, is a
protein
Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residue (biochemistry), residues. Proteins perform a vast array of functions within organisms, including Enzyme catalysis, catalysing metab ...
that in humans is encoded by the ''NUCB1''
gene
In biology, the word gene has two meanings. The Mendelian gene is a basic unit of heredity. The molecular gene is a sequence of nucleotides in DNA that is transcribed to produce a functional RNA. There are two types of molecular genes: protei ...
.
Structure
The human calnuc protein contains 461 amino acids and has a pI of 4.9.
The protein contains the following regions and
domain
A domain is a geographic area controlled by a single person or organization. Domain may also refer to:
Law and human geography
* Demesne, in English common law and other Medieval European contexts, lands directly managed by their holder rather ...
s:
*
Signal peptide
A signal peptide (sometimes referred to as signal sequence, targeting signal, localization signal, localization sequence, transit peptide, leader sequence or leader peptide) is a short peptide (usually 16–30 amino acids long) present at the ...
*
Leucine-zipper
A leucine zipper (or leucine scissors) is a common three-dimensional structural motif in proteins. They were first described by Landschulz and collaborators in 1988 when they found that an enhancer binding protein had a very characteristic 30-ami ...
The leucine-zipper of calnuc may be responsible for its dimerization.
* aa 347-389 –
Nuclear localization signal
A nuclear localization signal ''or'' sequence (NLS) is an amino acid sequence that 'tags' a protein for import into the cell nucleus by nuclear transport. Typically, this signal consists of one or more short sequences of positively charged lysin ...
* 2 zinc binding sites
with high affinity (K
d = 20 nM)
*
carboxypeptidase
A carboxypeptidase ( EC number 3.4.16 - 3.4.18) is a protease enzyme that hydrolyzes (cleaves) a peptide bond at the carboxy-terminal (C-terminal) end of a protein or peptide. This is in contrast to an aminopeptidases, which cleave peptide b ...
-like motifs : HFREXnH (aa 66) and HFTEXnH (aa 146)
* 2
EF-hands
The EF hand is a helix–loop–helix structural domain or ''motif'' found in a large family of calcium-binding proteins.
The EF-hand motif contains a helix–loop–helix topology, much like the spread thumb and forefinger of the human hand, i ...
* Potential anchor region
– 15-aa hydrophobic region at its COOH terminus that may be sufficient for membrane anchoring
References
Further reading
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EF-hand-containing proteins
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