Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9Y215 (COLQ_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acetylcholinesterase collagenic tail peptide
Alternative name(s):
AChE Q subunit
Acetylcholinesterase-associated collagen
Gene names
Name:COLQ
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length455 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Anchors the catalytic subunits of asymmetric AChE to the synaptic basal lamina.

Subunit structure

Homotrimer. Component of the asymmetric form of AChE, a disulfide-bonded oligomer composed of the collagenic subunits (Q) and a variable number of asymmetric catalytic subunits (T). The N-terminal of a collagenic subunit (Q) associates with the C-terminal of a catalytic subunit (T).

Subcellular location

Cell junctionsynapse.

Tissue specificity

Found at the end plate of skeletal muscle.

Domain

The proline-rich attachment domain (PRAD) binds the AChE catalytic subunits.

Post-translational modification

The triple-helical tail is stabilized by disulfide bonds at each end.

Involvement in disease

Myasthenic syndrome, congenital, Engel type (CMSE) [MIM:603034]: A rare autosomal recessive congenital myasthenic syndrome characterized by onset during childhood, generalized weakness, abnormal fatigability on exertion, refrectoriness to acetylcholinesterase drugs, decremental electromyographic response and morphological abnormalities of the neuromuscular junctions.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.9

Sequence similarities

Belongs to the COLQ family.

Contains 2 collagen-like domains.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ACHEP223032EBI-1637847,EBI-1637793

Alternative products

This entry describes 8 isoforms produced by alternative splicing. [Align] [Select]
Isoform I (identifier: Q9Y215-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform II (identifier: Q9Y215-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-35: MVVLNPMTLGIYLQLFFLSIVSQPTFINSVLPISA → MTGSSFSLAHLLIISGLLCYSAGCL
Isoform III (identifier: Q9Y215-3)

The sequence of this isoform differs from the canonical sequence as follows:
     74-107: Missing.
Isoform IV (identifier: Q9Y215-4)

The sequence of this isoform differs from the canonical sequence as follows:
     73-76: Missing.
Isoform V (identifier: Q9Y215-5)

The sequence of this isoform differs from the canonical sequence as follows:
     124-132: Missing.
Isoform VI (identifier: Q9Y215-6)

The sequence of this isoform differs from the canonical sequence as follows:
     240-291: GQKGDSGVMG...RGFPGPPGRC → SSRTPCTLPR...DYISSGTERG
     292-455: Missing.
Isoform VII (identifier: Q9Y215-7)

The sequence of this isoform differs from the canonical sequence as follows:
     272-281: GQLIMGPKGE → DFCGQQPGGA
     282-455: Missing.
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Isoform VIII (identifier: Q9Y215-8)

The sequence of this isoform differs from the canonical sequence as follows:
     273-329: QLIMGPKGER...FVVNNQEELE → HMETCNAPST...VLAPSPPTFV
     330-455: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 455433Acetylcholinesterase collagenic tail peptide
PRO_0000005854

Regions

Domain96 – 269174Collagen-like 1
Domain277 – 29115Collagen-like 2
Region51 – 6717PRAD
Region130 – 1334Heparan sulfate proteoglycan binding Potential
Region235 – 2384Heparan sulfate proteoglycan binding Potential

Amino acid modifications

Disulfide bond51Interchain (with T subunit) Potential
Disulfide bond52Interchain (with T subunit) Potential
Disulfide bond93Interchain Potential
Disulfide bond291Interchain Potential
Disulfide bond293Interchain Potential

Natural variations

Alternative sequence1 – 3535MVVLN…LPISA → MTGSSFSLAHLLIISGLLCY SAGCL in isoform II.
VSP_001175
Alternative sequence73 – 764Missing in isoform IV.
VSP_001176
Alternative sequence74 – 10734Missing in isoform III.
VSP_001177
Alternative sequence124 – 1329Missing in isoform V.
VSP_001178
Alternative sequence240 – 29152GQKGD…PPGRC → SSRTPCTLPRRPPVPCGQGS RSPVTVVAGNESQACLLPRF EEDYISSGTERG in isoform VI.
VSP_001179
Alternative sequence272 – 28110GQLIMGPKGE → DFCGQQPGGA in isoform VII.
VSP_001180
Alternative sequence273 – 32957QLIMG…QEELE → HMETCNAPSTATSTPRPAAT SPEGREEKVGCAPQNWQQLL HCHQTGHVLAPSPPTFV in isoform VIII.
VSP_001181
Alternative sequence282 – 455174Missing in isoform VII.
VSP_001182
Alternative sequence292 – 455164Missing in isoform VI.
VSP_001183
Alternative sequence330 – 455126Missing in isoform VIII.
VSP_001184
Natural variant591P → Q in CMSE; abrogates binding to T subunit. Ref.9
VAR_010133
Natural variant3121S → G.
Corresponds to variant rs6782980 [ dbSNP | Ensembl ].
VAR_048809
Natural variant3421D → E in CMSE; impairs anchoring to the basal lamina. Ref.9
VAR_010134
Natural variant4101R → Q in CMSE. Ref.9
VAR_010135
Natural variant4301Y → S in CMSE. Ref.1
VAR_010136
Natural variant4441C → Y in CMSE. Ref.9
VAR_010137

Experimental info

Sequence conflict3701D → N in AAO06818. Ref.3
Sequence conflict3991R → RD in CAA12648. Ref.1
Sequence conflict3991R → RD in AAO06814. Ref.3
Sequence conflict3991R → RD in AAO06816. Ref.3
Sequence conflict3991R → RD in AAO06817. Ref.3
Sequence conflict3991R → RD in AAO06818. Ref.3
Sequence conflict3991R → RD in AAO06819. Ref.3
Sequence conflict4001C → Y in AAO06816. Ref.3
Sequence conflict4041Y → D in AAO06817. Ref.3
Sequence conflict4231G → V in AAO06819. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform I [UniParc].

Last modified October 17, 2006. Version 2.
Checksum: A95D3E5D5ECDBE55

FASTA45547,766
        10         20         30         40         50         60 
MVVLNPMTLG IYLQLFFLSI VSQPTFINSV LPISAALPSL DQKKRGGHKA CCLLTPPPPP 

        70         80         90        100        110        120 
LFPPPFFRGG RSPLLSPDMK NLMLELETSQ SPCMQGSLGS PGPPGPQGPP GLPGKTGPKG 

       130        140        150        160        170        180 
EKGELGRPGR KGRPGPPGVP GMPGPIGWPG PEGPRGEKGD LGMMGLPGSR GPMGSKGYPG 

       190        200        210        220        230        240 
SRGEKGSRGE KGDLGPKGEK GFPGFPGMLG QKGEMGPKGE PGIAGHRGPT GRPGKRGKQG 

       250        260        270        280        290        300 
QKGDSGVMGP PGKPGPSGQP GRPGPPGPPP AGQLIMGPKG ERGFPGPPGR CLCGPTMNVN 

       310        320        330        340        350        360 
NPSYGESVYG PSSPRVPVIF VVNNQEELER LNTQNAIAFR RDQRSLYFKD SLGWLPIQLT 

       370        380        390        400        410        420 
PFYPVDYTAD QHGTCGDGLL QPGEECDDGN SDVGDDCIRC HRAYCGDGHR HEGVEDCDGS 

       430        440        450 
DFGYLTCETY LPGSYGDLQC TQYCYIDSTP CRYFT 

« Hide

Isoform II [UniParc].

Checksum: 8677E75D64046DE7
Show »

FASTA44546,457
Isoform III [UniParc].

Checksum: 490EE07243B21B03
Show »

FASTA42144,243
Isoform IV [UniParc].

Checksum: 82557E51EC65241E
Show »

FASTA45147,356
Isoform V [UniParc].

Checksum: C3D9F2E1C1FFA6F4
Show »

FASTA44646,815
Isoform VI [UniParc].

Checksum: 7DFC921C5B98D84B
Show »

FASTA29130,024
Isoform VII [UniParc].

Checksum: FE0A55A8FAE0E135
Show »

FASTA28128,354
Isoform VIII [UniParc].

Checksum: A3ECE29DEDE5766F
Show »

FASTA32933,538

References

« Hide 'large scale' references
[1]"Mutation in the human acetylcholinesterase-associated collagen gene, COLQ, is responsible for congenital myasthenic syndrome with end-plate acetylcholinesterase deficiency (Type Ic)."
Donger C., Krejci E., Serradell A.P., Eymard B., Bon S., Nicole S., Chateau D., Gary F., Fardeau M., Massoulie J., Guicheney P.
Am. J. Hum. Genet. 63:967-975(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT CMSE SER-430.
Tissue: Blood and Skeletal muscle.
[2]"Human endplate acetylcholinesterase deficiency caused by mutations in the collagen-like tail subunit (ColQ) of the asymmetric enzyme."
Ohno K., Brengman J., Tsujino A., Engel A.G.
Proc. Natl. Acad. Sci. U.S.A. 95:9654-9659(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], ALTERNATIVE SPLICING.
Tissue: Skeletal muscle.
[3]Arredondo J., DeLeon M.
Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM II).
Tissue: Thymus.
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung.
[7]"An unappreciated role for RNA surveillance."
Hillman R.T., Green R.E., Brenner S.E.
Genome Biol. 5:R8.1-R8.16(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
[8]"The synaptic acetylcholinesterase tetramer assembles around a polyproline II helix."
Dvir H., Harel M., Bon S., Liu W.-Q., Vidal M., Garbay C., Sussman J.L., Massoulie J., Silman I.
EMBO J. 23:4394-4405(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 53-67 IN COMPLEX WITH ACHE.
[9]"The spectrum of mutations causing end-plate acetylcholinesterase deficiency."
Ohno K., Engel A.G., Brengman J.M., Shen X.-M., Heidenreich F., Vincent A., Milone M., Tan E., Demirci M., Walsh P., Nakano S., Akiguchi I.
Ann. Neurol. 47:162-170(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CMSE GLN-59; GLU-342; GLN-410 AND TYR-444.
Tissue: Blood and Muscle.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ225895 mRNA. Translation: CAA12648.1.
AF057036 mRNA. Translation: AAC39927.1.
AF229126 expand/collapse EMBL AC list , AF229117, AF229118, AF229119, AF229120, AF229121, AF229122, AF229123, AF229124, AF229125 Genomic DNA. Translation: AAF43195.1.
AF229126 expand/collapse EMBL AC list , AF229118, AF229119, AF229120, AF229121, AF229122, AF229123, AF229124, AF229125 Genomic DNA. Translation: AAF43196.1.
AF229126 expand/collapse EMBL AC list , AF229117, AF229118, AF229119, AF229120, AF229121, AF229122, AF229123, AF229124, AF229125 Genomic DNA. Translation: AAF43197.1.
AF229126 expand/collapse EMBL AC list , AF229117, AF229118, AF229119, AF229120, AF229121, AF229122, AF229123, AF229124, AF229125 Genomic DNA. Translation: AAF43198.1.
AF229126 expand/collapse EMBL AC list , AF229117, AF229118, AF229119, AF229120, AF229121, AF229122, AF229123, AF229124, AF229125 Genomic DNA. Translation: AAF43199.1.
AF229122 expand/collapse EMBL AC list , AF229117, AF229118, AF229119, AF229120, AF229121 Genomic DNA. Translation: AAF43200.1.
AF229124 expand/collapse EMBL AC list , AF229117, AF229118, AF229119, AF229120, AF229121, AF229122 Genomic DNA. Translation: AAF43201.1.
AF229126 expand/collapse EMBL AC list , AF229117, AF229118, AF229119, AF229120, AF229121, AF229122 Genomic DNA. Translation: AAF43202.1.
AY150334 mRNA. Translation: AAO06814.1.
AY150336 mRNA. Translation: AAO06816.1.
AY150337 mRNA. Translation: AAO06817.1.
AY150338 mRNA. Translation: AAO06818.1.
AY150339 mRNA. Translation: AAO06819.1.
AK128401 mRNA. Translation: BAG54671.1.
CH471055 Genomic DNA. Translation: EAW64250.1.
BC074828 mRNA. Translation: AAH74828.1.
BC074829 mRNA. Translation: AAH74829.1.
CCDSCCDS33709.1. [Q9Y215-1]
CCDS43057.1. [Q9Y215-3]
CCDS46768.1. [Q9Y215-2]
RefSeqNP_005668.2. NM_005677.3. [Q9Y215-1]
NP_536799.1. NM_080538.2. [Q9Y215-2]
NP_536800.2. NM_080539.3. [Q9Y215-3]
UniGeneHs.146735.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1VZJX-ray2.35I/J53-67[»]
ProteinModelPortalQ9Y215.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113897. 2 interactions.
IntActQ9Y215. 1 interaction.

PTM databases

PhosphoSiteQ9Y215.

Polymorphism databases

DMDM116241309.

Proteomic databases

PaxDbQ9Y215.
PRIDEQ9Y215.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000383781; ENSP00000373291; ENSG00000206561. [Q9Y215-2]
ENST00000383786; ENSP00000373296; ENSG00000206561. [Q9Y215-3]
ENST00000383787; ENSP00000373297; ENSG00000206561. [Q9Y215-5]
ENST00000383788; ENSP00000373298; ENSG00000206561. [Q9Y215-1]
ENST00000603808; ENSP00000474271; ENSG00000206561.
GeneID8292.
KEGGhsa:8292.
UCSCuc003bzv.3. human. [Q9Y215-2]
uc003bzx.3. human. [Q9Y215-1]
uc010heo.3. human. [Q9Y215-3]

Organism-specific databases

CTD8292.
GeneCardsGC03M015491.
GeneReviewsCOLQ.
HGNCHGNC:2226. COLQ.
MIM603033. gene.
603034. phenotype.
neXtProtNX_Q9Y215.
Orphanet98915. Synaptic congenital myasthenic syndromes.
PharmGKBPA26743.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG329823.
HOVERGENHBG102052.
InParanoidQ9Y215.
PhylomeDBQ9Y215.
TreeFamTF331890.

Gene expression databases

ArrayExpressQ9Y215.
BgeeQ9Y215.
GenevestigatorQ9Y215.

Family and domain databases

InterProIPR008160. Collagen.
IPR011936. Myxo_disulph_rpt.
[Graphical view]
PfamPF01391. Collagen. 1 hit.
[Graphical view]
TIGRFAMsTIGR02232. myxo_disulf_rpt. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ9Y215.
GeneWikiCOLQ.
GenomeRNAi8292.
NextBio31075.
PROQ9Y215.
SOURCESearch...

Entry information

Entry nameCOLQ_HUMAN
AccessionPrimary (citable) accession number: Q9Y215
Secondary accession number(s): B3KY09 expand/collapse secondary AC list , Q6DK18, Q6YH18, Q6YH19, Q6YH20, Q6YH21, Q9NP18, Q9NP19, Q9NP20, Q9NP21, Q9NP22, Q9NP23, Q9NP24, Q9UP88
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: October 17, 2006
Last modified: July 9, 2014
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM