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{{Infobox_gene}}
{{PBB_Controls
'''Acetylcholinesterase collagenic tail peptide''' also known as '''AChE Q subunit''', '''acetylcholinesterase-associated collagen''', or '''ColQ''' is the collagen-tail subunit of [[acetylcholinesterase]] found in the [[neuromuscular junction]]. In humans it is encoded by the ''COLQ'' [[gene]].<ref name="pmid9689136">{{cite journal |vauthors=Ohno K, Brengman J, Tsujino A, Engel AG | title = Human endplate acetylcholinesterase deficiency caused by mutations in the collagen-like tail subunit (ColQ) of the asymmetric enzyme | journal = Proc Natl Acad Sci U S A | volume = 95 | issue = 16 | pages = 9654–9 |date=Sep 1998 | pmid = 9689136 | pmc = 21394 | doi =10.1073/pnas.95.16.9654  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: COLQ collagen-like tail subunit (single strand of homotrimer) of asymmetric acetylcholinesterase| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8292| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Collagen-like tail subunit (single strand of homotrimer) of asymmetric acetylcholinesterase
| HGNCid = 2226
| Symbol = COLQ
| AltSymbols =; EAD
| OMIM = 603033
| ECnumber = 
| Homologene = 10437
| MGIid = 1338761
| GeneAtlas_image1 = PBB_GE_COLQ_206073_at_tn.png
| Function =  
| Component = {{GNF_GO|id=GO:0005605 |text = basal lamina}} {{GNF_GO|id=GO:0005615 |text = extracellular space}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0045202 |text = synapse}}
| Process = {{GNF_GO|id=GO:0001507 |text = acetylcholine catabolic process in synaptic cleft}} {{GNF_GO|id=GO:0006817 |text = phosphate transport}} {{GNF_GO|id=GO:0008105 |text = asymmetric protein localization}} {{GNF_GO|id=GO:0042135 |text = neurotransmitter catabolic process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 8292
    | Hs_Ensembl = ENSG00000206561
    | Hs_RefseqProtein = NP_005668
    | Hs_RefseqmRNA = NM_005677
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 3
    | Hs_GenLoc_start = 15466645
    | Hs_GenLoc_end = 15538262
    | Hs_Uniprot = Q9Y215
    | Mm_EntrezGene = 382864
    | Mm_Ensembl = ENSMUSG00000057606
    | Mm_RefseqmRNA = XM_356716
    | Mm_RefseqProtein = XP_356716
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 14
    | Mm_GenLoc_start = 30353422
    | Mm_GenLoc_end = 30382865
    | Mm_Uniprot = Q3KNA4
  }}
}}
'''Collagen-like tail subunit (single strand of homotrimer) of asymmetric acetylcholinesterase''', also known as '''COLQ''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: COLQ collagen-like tail subunit (single strand of homotrimer) of asymmetric acetylcholinesterase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8292| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
This gene encodes the subunit of a [[collagen]]-like molecule associated with [[acetylcholinesterase]] in skeletal muscle. Each molecule is composed of three identical subunits. Each subunit contains a [[proline]]-rich attachment domain (PRAD) that binds an acetylcholinesterase [[tetramer]] to anchor the catalytic subunit of the enzyme to the basal lamina. Multiple [[transcript variants]] encoding different [[isoforms]] have been found for this gene.<ref name="entrez" />
{{PBB_Summary
 
| section_title =
== Clinical significance ==
| summary_text = This gene encodes the subunit of a collagen-like molecule associated with acetylcholinesterase in skeletal muscle. Each molecule is composed of three identical subunits. Each subunit contains a proline-rich attachment domain (PRAD) that binds an acetylcholinesterase tetramer to anchor the catalytic subunit of the enzyme to the basal lamina. Mutations in this gene are associated with endplate acetylcholinesterase deficiency. Multiple transcript variants encoding different isoforms have been found for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: COLQ collagen-like tail subunit (single strand of homotrimer) of asymmetric acetylcholinesterase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8292| accessdate = }}</ref>
 
}}
Mutations in this gene are associated with endplate acetylcholinesterase deficiency.<ref name="entrez"/>


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==External links==
* {{UCSC gene info|COLQ}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
*{{cite journal  | author=Donger C |title=Mutation in the human acetylcholinesterase-associated collagen gene, COLQ, is responsible for congenital myasthenic syndrome with end-plate acetylcholinesterase deficiency (Type Ic) |journal=Am. J. Hum. Genet. |volume=63 |issue= 4 |pages= 967–75 |year= 1998 |pmid= 9758617 |doi=10.1086/302059  | pmc=1377491  |name-list-format=vanc| author2=Krejci E  | author3=Serradell AP  | display-authors=3  | last4=Eymard  | first4=Bruno  | last5=Bon  | first5=Suzanne  | last6=Nicole  | first6=Sophie  | last7=Chateau  | first7=Danielle  | last8=Gary  | first8=Françoise  | last9=Fardeau  | first9=Michel }}
| citations =
*{{cite journal  | author=Ohno K |title=Congenital end-plate acetylcholinesterase deficiency caused by a nonsense mutation and an A-->G splice-donor-site mutation at position +3 of the collagenlike-tail-subunit gene (COLQ): how does G at position +3 result in aberrant splicing? |journal=Am. J. Hum. Genet. |volume=65 |issue= 3 |pages= 635–44 |year= 1999 |pmid= 10441569 |doi=10.1086/302551  | pmc=1377969  |name-list-format=vanc| author2=Brengman JM  | author3=Felice KJ  | display-authors=3  | last4=Cornblath  | first4=D  | last5=Engel  | first5=A }}
*{{cite journal  | author=Ohno K, Brengman J, Tsujino A, Engel AG |title=Human endplate acetylcholinesterase deficiency caused by mutations in the collagen-like tail subunit (ColQ) of the asymmetric enzyme. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 16 |pages= 9654-9 |year= 1998 |pmid= 9689136 |doi=  }}
*{{cite journal  |vauthors=Altamirano CV, Lockridge O |title=Conserved aromatic residues of the C-terminus of human butyrylcholinesterase mediate the association of tetramers |journal=Biochemistry |volume=38 |issue= 40 |pages= 13414–22 |year= 1999 |pmid= 10529218 |doi=10.1021/bi991475 }}
*{{cite journal  | author=Donger C, Krejci E, Serradell AP, ''et al.'' |title=Mutation in the human acetylcholinesterase-associated collagen gene, COLQ, is responsible for congenital myasthenic syndrome with end-plate acetylcholinesterase deficiency (Type Ic). |journal=Am. J. Hum. Genet. |volume=63 |issue= 4 |pages= 967-75 |year= 1998 |pmid= 9758617 |doi=  }}
*{{cite journal  | author=Ohno K |title=The spectrum of mutations causing end-plate acetylcholinesterase deficiency |journal=Ann. Neurol. |volume=47 |issue= 2 |pages= 162–70 |year= 2000 |pmid= 10665486 |doi=10.1002/1531-8249(200002)47:2<162::AID-ANA5>3.0.CO;2-Q  |name-list-format=vanc| author2=Engel AG  | author3=Brengman JM  | display-authors=3  | last4=Shen  | first4=Xin-Ming  | last5=Heidenreich  | first5=Fedor  | last6=Vincent  | first6=Angela  | last7=Milone  | first7=Margherita  | last8=Tan  | first8=Ersin  | last9=Demirci  | first9=Mehmet }}
*{{cite journal  | author=Ohno K, Brengman JM, Felice KJ, ''et al.'' |title=Congenital end-plate acetylcholinesterase deficiency caused by a nonsense mutation and an A-->G splice-donor-site mutation at position +3 of the collagenlike-tail-subunit gene (COLQ): how does G at position +3 result in aberrant splicing? |journal=Am. J. Hum. Genet. |volume=65 |issue= 3 |pages= 635-44 |year= 1999 |pmid= 10441569 |doi=  }}
*{{cite journal  |vauthors=Deprez P, Inestrosa NC |title=Molecular modeling of the collagen-like tail of asymmetric acetylcholinesterase |journal=Protein Eng. |volume=13 |issue= 1 |pages= 27–34 |year= 2000 |pmid= 10679527 |doi=10.1093/protein/13.1.27 }}
*{{cite journal  | author=Altamirano CV, Lockridge O |title=Conserved aromatic residues of the C-terminus of human butyrylcholinesterase mediate the association of tetramers. |journal=Biochemistry |volume=38 |issue= 40 |pages= 13414-22 |year= 1999 |pmid= 10529218 |doi=  }}
*{{cite journal  | author=Shapira YA |title=Three novel COLQ mutations and variation of phenotypic expressivity due to G240X |journal=Neurology |volume=58 |issue= 4 |pages= 603–9 |year= 2002 |pmid= 11865139 |doi= 10.1212/wnl.58.4.603|name-list-format=vanc| author2=Sadeh ME  | author3=Bergtraum MP  | display-authors=3  | last4=Tsujino  | first4=A  | last5=Ohno  | first5=K  | last6=Shen  | first6=XM  | last7=Brengman  | first7=J  | last8=Edwardson  | first8=S  | last9=Matoth  | first9=I }}
*{{cite journal  | author=Ohno K, Engel AG, Brengman JM, ''et al.'' |title=The spectrum of mutations causing end-plate acetylcholinesterase deficiency. |journal=Ann. Neurol. |volume=47 |issue= 2 |pages= 162-70 |year= 2000 |pmid= 10665486 |doi=  }}
*{{cite journal  | author=Strausberg RL |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241  |name-list-format=vanc| author2=Feingold EA  | author3=Grouse LH  | display-authors=3  | last4=Derge  | first4=JG  | last5=Klausner  | first5=RD  | last6=Collins  | first6=FS  | last7=Wagner  | first7=L  | last8=Shenmen  | first8=CM  | last9=Schuler  | first9=GD }}
*{{cite journal  | author=Deprez P, Inestrosa NC |title=Molecular modeling of the collagen-like tail of asymmetric acetylcholinesterase. |journal=Protein Eng. |volume=13 |issue= 1 |pages= 27-34 |year= 2000 |pmid= 10679527 |doi=  }}
*{{cite journal  | author=Ishigaki K |title=Two novel mutations in the COLQ gene cause endplate acetylcholinesterase deficiency |journal=Neuromuscul. Disord. |volume=13 |issue= 3 |pages= 236–44 |year= 2003 |pmid= 12609505 |doi=10.1016/s0960-8966(02)00243-2  |name-list-format=vanc| author2=Nicolle D  | author3=Krejci E  | display-authors=3  | last4=Leroy  | first4=Jean-Paul  | last5=Koenig  | first5=Jeanine  | last6=Fardeau  | first6=Michel  | last7=Eymard  | first7=Bruno  | last8=Hantaı̈  | first8=Daniel }}
*{{cite journal  | author=Shapira YA, Sadeh ME, Bergtraum MP, ''et al.'' |title=Three novel COLQ mutations and variation of phenotypic expressivity due to G240X. |journal=Neurology |volume=58 |issue= 4 |pages= 603-9 |year= 2002 |pmid= 11865139 |doi=  }}
*{{cite journal  |vauthors=Hillman RT, Green RE, Brenner SE |title=An unappreciated role for RNA surveillance |journal=Genome Biol. |volume=5 |issue= 2 |pages= R8 |year= 2005 |pmid= 14759258 |doi= 10.1186/gb-2004-5-2-r8 | pmc=395752 }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | author=Cartaud A |title=MuSK is required for anchoring acetylcholinesterase at the neuromuscular junction |journal=J. Cell Biol. |volume=165 |issue= 4 |pages= 505–15 |year= 2004 |pmid= 15159418 |doi= 10.1083/jcb.200307164 | pmc=2172359  |name-list-format=vanc| author2=Strochlic L  | author3=Guerra M  | display-authors=3  | last4=Blanchard  | first4=B  | last5=Lambergeon  | first5=M  | last6=Krejci  | first6=E  | last7=Cartaud  | first7=J  | last8=Legay  | first8=C }}
*{{cite journal  | author=Ishigaki K, Nicolle D, Krejci E, ''et al.'' |title=Two novel mutations in the COLQ gene cause endplate acetylcholinesterase deficiency. |journal=Neuromuscul. Disord. |volume=13 |issue= 3 |pages= 236-44 |year= 2003 |pmid= 12609505 |doi=  }}
*{{cite journal  | author=Gerhard DS |title=The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928  |name-list-format=vanc| author2=Wagner L  | author3=Feingold EA  | display-authors=3  | last4=Shenmen  | first4=CM  | last5=Grouse  | first5=LH  | last6=Schuler  | first6=G  | last7=Klein  | first7=SL  | last8=Old  | first8=S  | last9=Rasooly  | first9=R }}
*{{cite journal  | author=Hillman RT, Green RE, Brenner SE |title=An unappreciated role for RNA surveillance. |journal=Genome Biol. |volume=5 |issue= 2 |pages= R8 |year= 2005 |pmid= 14759258 |doi= 10.1186/gb-2004-5-2-r8 }}
*{{cite journal  | author=Dvir H |title=The synaptic acetylcholinesterase tetramer assembles around a polyproline II helix |journal=EMBO J. |volume=23 |issue= 22 |pages= 4394–405 |year= 2005 |pmid= 15526038 |doi= 10.1038/sj.emboj.7600425 | pmc=526459  |name-list-format=vanc| author2=Harel M  | author3=Bon S  | display-authors=3  | last4=Liu  | first4=Wang-Qing  | last5=Vidal  | first5=Michel  | last6=Garbay  | first6=Christiane  | last7=Sussman  | first7=Joel L  | last8=Massoulié  | first8=Jean  | last9=Silman  | first9=Israel }}
*{{cite journal  | author=Cartaud A, Strochlic L, Guerra M, ''et al.'' |title=MuSK is required for anchoring acetylcholinesterase at the neuromuscular junction. |journal=J. Cell Biol. |volume=165 |issue= 4 |pages= 505-15 |year= 2004 |pmid= 15159418 |doi= 10.1083/jcb.200307164 }}
*{{cite journal  |vauthors=Ting AK, Siow NL, Kong LW, Tsim KW |title=Transcriptional regulation of acetylcholinesterase-associated collagen ColQ in fast- and slow-twitch muscle fibers |journal=Chem. Biol. Interact. |volume=157-158 |issue=  |pages= 63–70 |year= 2006 |pmid= 16256971 |doi= 10.1016/j.cbi.2005.10.009 }}
*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal  | author=Schreiner F |title=Novel COLQ mutation 950delC in synaptic congenital myasthenic syndrome and symptomatic heterozygous relatives |journal=Neuromuscul. Disord. |volume=17 |issue= 3 |pages= 262–5 |year= 2007 |pmid= 17300939 |doi= 10.1016/j.nmd.2006.11.010 |name-list-format=vanc| author2=Hoppenz M  | author3=Klaeren R  | display-authors=3  | last4=Reimann  | first4=Jens  | last5=Woelfle  | first5=Joachim }}
*{{cite journal  | author=Dvir H, Harel M, Bon S, ''et al.'' |title=The synaptic acetylcholinesterase tetramer assembles around a polyproline II helix. |journal=EMBO J. |volume=23 |issue= 22 |pages= 4394-405 |year= 2005 |pmid= 15526038 |doi= 10.1038/sj.emboj.7600425 }}
*{{cite journal  | author=Ting AK, Siow NL, Kong LW, Tsim KW |title=Transcriptional regulation of acetylcholinesterase-associated collagen ColQ in fast- and slow-twitch muscle fibers. |journal=Chem. Biol. Interact. |volume=157-158 |issue=  |pages= 63-70 |year= 2006 |pmid= 16256971 |doi= 10.1016/j.cbi.2005.10.009 }}
*{{cite journal  | author=Schreiner F, Hoppenz M, Klaeren R, ''et al.'' |title=Novel COLQ mutation 950delC in synaptic congenital myasthenic syndrome and symptomatic heterozygous relatives. |journal=Neuromuscul. Disord. |volume=17 |issue= 3 |pages= 262-5 |year= 2007 |pmid= 17300939 |doi= 10.1016/j.nmd.2006.11.010 }}
}}
{{refend}}
{{refend}}


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Latest revision as of 09:54, 30 August 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Acetylcholinesterase collagenic tail peptide also known as AChE Q subunit, acetylcholinesterase-associated collagen, or ColQ is the collagen-tail subunit of acetylcholinesterase found in the neuromuscular junction. In humans it is encoded by the COLQ gene.[1][2]

Function

This gene encodes the subunit of a collagen-like molecule associated with acetylcholinesterase in skeletal muscle. Each molecule is composed of three identical subunits. Each subunit contains a proline-rich attachment domain (PRAD) that binds an acetylcholinesterase tetramer to anchor the catalytic subunit of the enzyme to the basal lamina. Multiple transcript variants encoding different isoforms have been found for this gene.[2]

Clinical significance

Mutations in this gene are associated with endplate acetylcholinesterase deficiency.[2]

References

  1. ↑ Ohno K, Brengman J, Tsujino A, Engel AG (Sep 1998). "Human endplate acetylcholinesterase deficiency caused by mutations in the collagen-like tail subunit (ColQ) of the asymmetric enzyme". Proc Natl Acad Sci U S A. 95 (16): 9654–9. doi:10.1073/pnas.95.16.9654. PMC 21394. PMID 9689136.
  2. ↑ 2.0 2.1 2.2 "Entrez Gene: COLQ collagen-like tail subunit (single strand of homotrimer) of asymmetric acetylcholinesterase".

External links

Further reading


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