WordNet

the 3rd letter of the Roman alphabet (同)c
(music) the keynote of the scale of C major
a general-purpose programing language closely associated with the UNIX operating system
(architecture) a statue or a human bust or an animal carved out of the top of a square pillar; originally used as a boundary marker in ancient Rome (同)terminal figure, term
either end of a railroad or bus route

PrepTutorEJDIC

carbonの化学記号
目的,終結 / (鉄道・バスの)終点,終着駅
cesiumの化学記号
cadmiumの化学記号

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2014/04/07 23:11:17」(JST)

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A tetrapeptide (example: Val-Gly-Ser-Ala) with green highlighted N-terminal α-amino acid (example: L-valine) and blue marked C-terminal α-amino acid (example: L-alanine).

The C-terminus (also known as the carboxyl-terminus, carboxy-terminus, C-terminal tail, C-terminal end, or COOH-terminus) is the end of an amino acid chain (protein or polypeptide), terminated by a free carboxyl group (-COOH). When the protein is translated from messenger RNA, it is created from N-terminus to C-terminus. The convention for writing peptide sequences is to put the C-terminal end on the right and write the sequence from N- to C-terminus.

Chemistry

Each amino acid has a carboxyl group and an amine group, and amino acids link to one another to form a chain by a dehydration reaction by joining the amine group of one amino acid to the carboxyl group of the next. Thus polypeptide chains have an end with an unbound carboxyl group, the C-terminus, and an end with an amine group, the N-terminus. Proteins are naturally synthesized starting from the N-terminus and ending at the C-terminus.

Function

C-terminal retention signals

While the N-terminus of a protein often contains targeting signals, the C-terminus can contain retention signals for protein sorting. The most common ER retention signal is the amino acid sequence -KDEL (or -HDEL) at the C-terminus, which keeps the protein in the endoplasmic reticulum and prevents it from entering the secretory pathway.

C-terminal modifications

The C-terminus of proteins can be modified posttranslationally, most commonly by the addition of a lipid anchor to the C-terminus that allows the protein to be inserted into a membrane without having a transmembrane domain.

Prenylation

Main article: Prenylation

One form of C-terminal modification is prenylation. During prenylation, a farnesyl- or geranylgeranyl-isoprenoid membrane anchor is added to a cysteine residue near the C-terminus. Small, membrane-bound G proteins are often modified this way.

GPI anchors

Main article: Glycosylphosphatidylinositol

Another form of C-terminal modification is the addition of a phosphoglycan, glycosylphosphatidylinositol (GPI), as a membrane anchor. The GPI anchor is attached to the C-terminus after proteolytic cleavage of a C-terminal propeptide. The most prominent example for this type of modification is the prion protein.

C-terminal domain

RNA POL II in action.

The C-terminal domain (or carboxyl tail domain, CTD) of some proteins has specialized functions. The CTD of RNA polymerase II typically consists of up to 52 repeats of the sequence Tyr-Ser-Pro-Thr-Ser-Pro-Ser.^[1] Other proteins often bind the C-terminal domain of RNA polymerase in order to activate polymerase activity. It is the protein domain which is involved in the initiation of DNA transcription, the capping of the RNA transcript, and attachment to the spliceosome for RNA splicing.^[2]

References

^ Meinhart A, Cramer P (July 2004). "Recognition of RNA polymerase II carboxy-terminal domain by 3'-RNA-processing factors". Nature 430 (6996): 223–6. doi:10.1038/nature02679. PMID 15241417.
^ Brickey WJ, Greenleaf AL (June 1995). "Functional studies of the carboxy-terminal repeat domain of Drosophila RNA polymerase II in vivo". Genetics 140 (2): 599–613. PMC 1206638. PMID 7498740.

UpToDate Contents

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English Journal

Phylogenetic analysis of receptor FgfrL1 shows divergence of the C-terminal end in rodents.

Zhuang L1, Bluteau G1, Trueb B2.
Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology.Comp Biochem Physiol B Biochem Mol Biol.2015 Aug;186:43-50. doi: 10.1016/j.cbpb.2015.04.009. Epub 2015 Apr 28.
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PMID 25934085

Segmental expression and C-terminal labeling of protein ERp44 through protein trans-splicing.

Dai X1, Liu XQ2, Meng Q3.
Protein expression and purification.Protein Expr Purif.2015 Aug;112:29-36. doi: 10.1016/j.pep.2015.04.005. Epub 2015 Apr 20.
Endoplasmic reticulum resident protein 44 (ERp44) is a member of the protein disulfide isomerase family and functions in oxidative protein folding in the endoplasmic reticulum. A structurally flexible C-terminal tail (C-tail) of ERp44 plays critical roles in dynamically regulating ERp44's function i
PMID 25907381

Multiplex diagnosis of viral infectious diseases (AIDS, hepatitis C, and hepatitis A) based on point of care lateral flow assay using engineered proteinticles.

Lee JH1, Seo HS1, Kwon JH1, Kim HT1, Kwon KC1, Sim SJ1, Cha YJ2, Lee J3.
Biosensors & bioelectronics.Biosens Bioelectron.2015 Jul 15;69:213-25. doi: 10.1016/j.bios.2015.02.033. Epub 2015 Feb 25.
Lateral flow assay (LFA) is an attractive method for rapid, simple, and cost-effective point of care diagnosis. For LFA-based multiplex diagnosis of three viral intractable diseases (acquired immune deficiency syndrome and hepatitis C and A), here we developed proteinticle-based 7 different 3D probe
PMID 25747506

Japanese Journal

Electrostatic engineering of the interface between heavy and light chains promotes antibody Fab fragment production

Cytotechnology 69(3), 469-475, 2017-06
NAID 120006323719

Selections, frameshift mutations, and copy number variation detected on the surf 4.1 gene in the western Kenyan Plasmodium falciparum population

Malaria Journal 16, 98, 2017-03-02
NAID 120006221052

NBS1 and multiple regulations of DNA damage response

Journal of Radiation Research 57(S1), i11-i17, 2016-08-16
NAID 120006027205

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