C-terminal domain

• C末端領域、C末端ドメイン、C末領域

関

C-terminal region、C-terminal tail

WordNet

1. relating to or occurring in a term or fixed period of time; "terminal examinations"; "terminal payments"
2. a contact on an electrical device (such as a battery) at which electric current enters or leaves (同)pole
3. station where transport vehicles load or unload passengers or goods (同)terminus, depot
4. electronic equipment consisting of a device providing access to a computer; has a keyboard and display
5. being or situated at an end; "the endmost pillar"; "terminal buds on a branch"; "a terminal station"; "the terminal syllable"
6. causing or ending in or approaching death; "a terminal patient"; "terminal cancer"
7. of or relating to or situated at the ends of a delivery route; "freight pickup is a terminal service"; "terminal charges"
8. territory over which rule or control is exercised; "his domain extended into Europe"; "he made it the law of the land" (同)demesne, land
9. (mathematics) the set of values of the independent variable for which a function is defined (同)domain of a function
10. the 3rd letter of the Roman alphabet (同)c
11. (music) the keynote of the scale of C major
12. a general-purpose programing language closely associated with the UNIX operating system

PrepTutorEJDIC

1. 『終りの』,末端の / 毎期の,定期の;学期末の / 『死に至る』, / 末端 / (電池の)端子 / (町の中心に近い)空港バス発着場;(一般に,鉄道・バスの)終点,終着駅
2. (国の)領地,領土;(個人の)所有地 / (関心・活動などの)範囲,分野 / (個人・一族の)所有地 / (数学で)変域(関数の独立変数がとる値の集合)
3. carbonの化学記号
4. cesiumの化学記号
5. cadmiumの化学記号

Wikipedia preview

出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/03/03 12:08:22」(JST)

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[Wiki en表示]

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. Amino acids link to one another to form a chain by a dehydration reaction which joins 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 unbound 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. 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.

See also

• N-terminus
• TopFIND, a scientific database covering proteases, their cleavage site specificity, substrates, inhibitors and protein termini originating from their activity

References

UpToDate Contents

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• 1. インスリン受容体の構造および機能 structure and function of the insulin receptor
• 2. 第VIII因子および第IX因子の生物学と正常な機能 biology and normal function of factor viii and factor ix
• 3. 脊髄小脳変性症 the spinocerebellar ataxias
• 4. 末期進行癌における生存期間の推定 survival estimates in advanced terminal cancer
• 5. 心不全におけるナトリウム利尿ペプチド測定 natriuretic peptide measurement in heart failure

English Journal

• Activation of Aicda gene transcription by Pax5 in plasmacytoma cells.

• Dege C, Hagman J.SourceIntegrated Department of Immunology, National Jewish Health, Denver, CO, 80206, USA.
• Immunologic research.Immunol Res.2013 Mar;55(1-3):155-61. doi: 10.1007/s12026-012-8357-8.
• Activation-induced deaminase (AID) is an enzyme responsible for somatic hypermutation and immunoglobulin heavy chain class switch recombination. Because AID causes double-stranded breaks in DNA, its expression is highly regulated and is normally restricted to germinal-center B cells. Dysregulated AI
• PMID 22956488

• DNA-binding regulates site-specific ubiquitination of IRF-1.

• Landré V, Pion E, Narayan V, Xirodimas DP, Ball KL.Source*Cell Signalling Unit, Edinburgh Cancer Research Centre, MRC Institute of Genetics and Molecular Medicine, University of Edinburgh, Crewe Rd South, Edinburgh EH4 2XR, U.K.
• The Biochemical journal.Biochem J.2013 Feb 1;449(3):707-17. doi: 10.1042/BJ20121076.
• Understanding the determinants for site-specific ubiquitination by E3 ligase components of the ubiquitin machinery is proving to be a challenge. In the present study we investigate the role of an E3 ligase docking site (Mf2 domain) in an intrinsically disordered domain of IRF-1 [IFN (interferon) reg
• PMID 23134341

• The glycolipid transfer protein (GLTP) domain of phosphoinositol 4-phosphate adaptor protein-2 (FAPP2): Structure drives preference for simple neutral glycosphingolipids.

• Kamlekar RK, Simanshu DK, Gao YG, Kenoth R, Pike HM, Prendergast FG, Malinina L, Molotkovsky JG, Venyaminov SY, Patel DJ, Brown RE.SourceThe Hormel Institute, University of Minnesota, Austin, MN, USA.
• Biochimica et biophysica acta.Biochim Biophys Acta.2013 Feb;1831(2):417-27. doi: 10.1016/j.bbalip.2012.10.010. Epub 2012 Nov 16.
• Phosphoinositol 4-phosphate adaptor protein-2 (FAPP2) plays a key role in glycosphingolipid (GSL) production using its C-terminal domain to transport newly synthesized glucosylceramide away from the cytosol-facing glucosylceramide synthase in the cis-Golgi for further anabolic processing. Structural
• PMID 23159414

Japanese Journal

• Recognition of CpG oligodeoxynucleotides by human Toll-like receptor 9 and subsequent cytokine induction

• Suwarti Suwarti,Yamazaki Tomohiko,Svetlana Chechetka,Hanagata Nobutaka
• Biochemical and Biophysical Research Communications 430(4), 1234-1239, 2013-01-25
• … We clarified that both the C- and N-termini of the extracellular domain (ECD) are necessary for the function of TLR9 in human cells, even if only the C-terminal region of mouse TLR9-ECD was activated by CpG ODNs. … Next, we identified residues in the C-terminus of TLR9-ECD (H505 in leucine-rich repeat (LRR)-16, H530 in LRR-17, and Y554 in LRR-18) that are essential for hTLR9 activation. …
• NAID 120005228348

• Functional Characterization of Domains of IPS-1 Using an Inducible Oligomerization System.

• Takamatsu Shiori,Onoguchi Kazuhide,Onomoto Koji,Narita Ryo,Takahasi Kiyohiro,Ishidate Fumiyoshi,Fujiwara Takahiro K,Yoneyama Mitsutoshi,Kato Hiroki,Fujita Takashi
• PloS one 8(1), 2013-01-07
• … IPS-1 is composed of N-terminal Caspase Activation and Recruitment Domain (CARD), proline-rich domain, intermediate domain, and C-terminal transmembrane (TM) domain. … The TM domain of IPS-1 anchors it to the mitochondrial outer membrane. … Using this system, we investigated the domain-requirement of IPS-1 for its signaling. …
• NAID 120005241348

• A C-Terminal Membrane Association Domain of Phototropin 2 is Necessary for Chloroplast Movement (Special Focus Issue : Blue light responses mediated by LOV)

• Kong Sam-Geun,Kagawa Takatoshi,Wada Masamitsu [他]
• Plant and Cell Physiology 54(1), 57-68, 2013-01-00
• NAID 40019558461

Related Pictures

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★リンクテーブル★

リンク元	「C末端領域」「C-terminal tail」「C-terminal region」「C末領域」「C末端ドメイン」
関連記事	「terminal」「C」「domain」「terminal domain」「Cs」

「C末端領域」

　　[★]

英

C-terminal domain、C-terminal region、C-terminal tail

関

C末端ドメイン、C末領域、C末端部、C末端部分、C末尾

「C-terminal tail」

　　[★]

• C末尾、C末端部、C末端領域

関

C-tail、C-terminal domain、C-terminal portion、C-terminal region

「C-terminal region」

　　[★]

• C末端領域、C末端部、C末端部分

関

C-terminal domain、C-terminal portion、C-terminal tail

「C末領域」

　　[★]

英

C-terminal domain

関

C末端ドメイン、C末端領域

「C末端ドメイン」

　　[★]

英

C-terminal domain

関

C末端領域、C末領域

「terminal」

　　[★]

• n.

• 末端、末端側、ターミナル

• adj.

• 終端の、終末の、末期の

関

distal、end、end stage、ending、extremity、full-blown、terminal region、terminal stage、terminally、termini、terminus

　 　 　 　 　 　 　 　

「C」

　　[★]

• 炭素 carbon
• シトシン cytosine
• システイン cysteine
• シチジン
• セルシウス度 摂氏 degrees Celsius degree C
• 産婦人科領域で「子宮外頚 子宮外頚部 exocervix」を表現するための略語

　 　 　 　

「domain」

　　[★]

• n.

• ドメイン、(分子内の)領域、分域

関

area、realm、region、regional、segregation、territory、universe

　 　 　

「terminal domain」

　　[★]

• 末端領域、末端ドメイン

関

distal region、terminal region

「Cs」

　　[★] セシウム, caesium, cesium