COLQ_HUMAN
ID COLQ_HUMAN Reviewed; 455 AA.
AC Q9Y215; B3KY09; Q6DK18; Q6YH18; Q6YH19; Q6YH20; Q6YH21; Q9NP18; Q9NP19;
AC Q9NP20; Q9NP21; Q9NP22; Q9NP23; Q9NP24; Q9UP88;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Acetylcholinesterase collagenic tail peptide;
DE AltName: Full=AChE Q subunit;
DE AltName: Full=Acetylcholinesterase-associated collagen;
DE Flags: Precursor;
GN Name=COLQ;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT CMS5 SER-430.
RC TISSUE=Blood, and Skeletal muscle;
RX PubMed=9758617; DOI=10.1086/302059;
RA Donger C., Krejci E., Serradell A.P., Eymard B., Bon S., Nicole S.,
RA Chateau D., Gary F., Fardeau M., Massoulie J., Guicheney P.;
RT "Mutation in the human acetylcholinesterase-associated collagen gene, COLQ,
RT is responsible for congenital myasthenic syndrome with end-plate
RT acetylcholinesterase deficiency (Type Ic).";
RL Am. J. Hum. Genet. 63:967-975(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND ALTERNATIVE SPLICING.
RC TISSUE=Skeletal muscle;
RX PubMed=9689136; DOI=10.1073/pnas.95.16.9654;
RA Ohno K., Brengman J., Tsujino A., Engel A.G.;
RT "Human endplate acetylcholinesterase deficiency caused by mutations in the
RT collagen-like tail subunit (ColQ) of the asymmetric enzyme.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:9654-9659(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Arredondo J., DeLeon M.;
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM II).
RC TISSUE=Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP INVOLVEMENT IN CMS5.
RX PubMed=11865139; DOI=10.1212/wnl.58.4.603;
RA Shapira Y.A., Sadeh M.E., Bergtraum M.P., Tsujino A., Ohno K., Shen X.M.,
RA Brengman J., Edwardson S., Matoth I., Engel A.G.;
RT "Three novel COLQ mutations and variation of phenotypic expressivity due to
RT G240X.";
RL Neurology 58:603-609(2002).
RN [8]
RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA Hillman R.T., Green R.E., Brenner S.E.;
RT "An unappreciated role for RNA surveillance.";
RL Genome Biol. 5:R8.1-R8.16(2004).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 53-67 IN COMPLEX WITH ACHE.
RX PubMed=15526038; DOI=10.1038/sj.emboj.7600425;
RA Dvir H., Harel M., Bon S., Liu W.-Q., Vidal M., Garbay C., Sussman J.L.,
RA Massoulie J., Silman I.;
RT "The synaptic acetylcholinesterase tetramer assembles around a polyproline
RT II helix.";
RL EMBO J. 23:4394-4405(2004).
RN [10]
RP VARIANTS CMS5 GLN-59; GLU-342; GLN-410 AND TYR-444.
RC TISSUE=Blood, and Muscle;
RX PubMed=10665486;
RX DOI=10.1002/1531-8249(200002)47:2<162::aid-ana5>3.0.co;2-q;
RA Ohno K., Engel A.G., Brengman J.M., Shen X.-M., Heidenreich F., Vincent A.,
RA Milone M., Tan E., Demirci M., Walsh P., Nakano S., Akiguchi I.;
RT "The spectrum of mutations causing end-plate acetylcholinesterase
RT deficiency.";
RL Ann. Neurol. 47:162-170(2000).
RN [11]
RP VARIANT CMS5 THR-337.
RX PubMed=24938146; DOI=10.1016/j.pediatrneurol.2014.03.012;
RA Matlik H.N., Milhem R.M., Saadeldin I.Y., Al-Jaibeji H.S., Al-Gazali L.,
RA Ali B.R.;
RT "Clinical and molecular analysis of a novel COLQ missense mutation causing
RT congenital myasthenic syndrome in a Syrian family.";
RL Pediatr. Neurol. 51:165-169(2014).
CC -!- FUNCTION: Anchors the catalytic subunits of asymmetric AChE to the
CC synaptic basal lamina.
CC -!- SUBUNIT: Homotrimer. Component of the asymmetric form of AChE, a
CC disulfide-bonded oligomer composed of the collagenic subunits (Q) and a
CC variable number of asymmetric catalytic subunits (T). The N-terminal of
CC a collagenic subunit (Q) associates with the C-terminal of a catalytic
CC subunit (T). {ECO:0000269|PubMed:15526038}.
CC -!- INTERACTION:
CC Q9Y215; P22303: ACHE; NbExp=2; IntAct=EBI-1637847, EBI-1637793;
CC Q9Y215; Q96EQ0: SGTB; NbExp=3; IntAct=EBI-1637847, EBI-744081;
CC -!- SUBCELLULAR LOCATION: Synapse.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=I;
CC IsoId=Q9Y215-1; Sequence=Displayed;
CC Name=II;
CC IsoId=Q9Y215-2; Sequence=VSP_001175;
CC Name=III;
CC IsoId=Q9Y215-3; Sequence=VSP_001177;
CC Name=IV;
CC IsoId=Q9Y215-4; Sequence=VSP_001176;
CC Name=V;
CC IsoId=Q9Y215-5; Sequence=VSP_001178;
CC Name=VI;
CC IsoId=Q9Y215-6; Sequence=VSP_001179, VSP_001183;
CC Name=VII;
CC IsoId=Q9Y215-7; Sequence=VSP_001180, VSP_001182;
CC Name=VIII;
CC IsoId=Q9Y215-8; Sequence=VSP_001181, VSP_001184;
CC -!- TISSUE SPECIFICITY: Found at the end plate of skeletal muscle.
CC -!- DOMAIN: The proline-rich attachment domain (PRAD) binds the AChE
CC catalytic subunits.
CC -!- PTM: The triple-helical tail is stabilized by disulfide bonds at each
CC end.
CC -!- DISEASE: Myasthenic syndrome, congenital, 5 (CMS5) [MIM:603034]: A form
CC of congenital myasthenic syndrome, a group of disorders characterized
CC by failure of neuromuscular transmission, including pre-synaptic,
CC synaptic, and post-synaptic disorders that are not of autoimmune
CC origin. Clinical features are easy fatigability and muscle weakness
CC affecting the axial and limb muscles (with hypotonia in early-onset
CC forms), the ocular muscles (leading to ptosis and ophthalmoplegia), and
CC the facial and bulbar musculature (affecting sucking and swallowing,
CC and leading to dysphonia). The symptoms fluctuate and worsen with
CC physical effort. CMS5 inheritance is autosomal recessive.
CC {ECO:0000269|PubMed:10665486, ECO:0000269|PubMed:11865139,
CC ECO:0000269|PubMed:24938146, ECO:0000269|PubMed:9758617}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: [Isoform VII]: May be produced at very low levels due to
CC a premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the COLQ family. {ECO:0000305}.
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DR EMBL; AJ225895; CAA12648.1; -; mRNA.
DR EMBL; AF057036; AAC39927.1; -; mRNA.
DR EMBL; AF229126; AAF43195.1; -; Genomic_DNA.
DR EMBL; AF229117; AAF43195.1; JOINED; Genomic_DNA.
DR EMBL; AF229118; AAF43195.1; JOINED; Genomic_DNA.
DR EMBL; AF229119; AAF43195.1; JOINED; Genomic_DNA.
DR EMBL; AF229120; AAF43195.1; JOINED; Genomic_DNA.
DR EMBL; AF229121; AAF43195.1; JOINED; Genomic_DNA.
DR EMBL; AF229122; AAF43195.1; JOINED; Genomic_DNA.
DR EMBL; AF229123; AAF43195.1; JOINED; Genomic_DNA.
DR EMBL; AF229124; AAF43195.1; JOINED; Genomic_DNA.
DR EMBL; AF229125; AAF43195.1; JOINED; Genomic_DNA.
DR EMBL; AF229126; AAF43196.1; -; Genomic_DNA.
DR EMBL; AF229118; AAF43196.1; JOINED; Genomic_DNA.
DR EMBL; AF229119; AAF43196.1; JOINED; Genomic_DNA.
DR EMBL; AF229120; AAF43196.1; JOINED; Genomic_DNA.
DR EMBL; AF229121; AAF43196.1; JOINED; Genomic_DNA.
DR EMBL; AF229122; AAF43196.1; JOINED; Genomic_DNA.
DR EMBL; AF229123; AAF43196.1; JOINED; Genomic_DNA.
DR EMBL; AF229124; AAF43196.1; JOINED; Genomic_DNA.
DR EMBL; AF229125; AAF43196.1; JOINED; Genomic_DNA.
DR EMBL; AF229126; AAF43197.1; -; Genomic_DNA.
DR EMBL; AF229117; AAF43197.1; JOINED; Genomic_DNA.
DR EMBL; AF229118; AAF43197.1; JOINED; Genomic_DNA.
DR EMBL; AF229119; AAF43197.1; JOINED; Genomic_DNA.
DR EMBL; AF229120; AAF43197.1; JOINED; Genomic_DNA.
DR EMBL; AF229121; AAF43197.1; JOINED; Genomic_DNA.
DR EMBL; AF229122; AAF43197.1; JOINED; Genomic_DNA.
DR EMBL; AF229123; AAF43197.1; JOINED; Genomic_DNA.
DR EMBL; AF229124; AAF43197.1; JOINED; Genomic_DNA.
DR EMBL; AF229125; AAF43197.1; JOINED; Genomic_DNA.
DR EMBL; AF229126; AAF43198.1; -; Genomic_DNA.
DR EMBL; AF229117; AAF43198.1; JOINED; Genomic_DNA.
DR EMBL; AF229118; AAF43198.1; JOINED; Genomic_DNA.
DR EMBL; AF229119; AAF43198.1; JOINED; Genomic_DNA.
DR EMBL; AF229120; AAF43198.1; JOINED; Genomic_DNA.
DR EMBL; AF229121; AAF43198.1; JOINED; Genomic_DNA.
DR EMBL; AF229122; AAF43198.1; JOINED; Genomic_DNA.
DR EMBL; AF229123; AAF43198.1; JOINED; Genomic_DNA.
DR EMBL; AF229124; AAF43198.1; JOINED; Genomic_DNA.
DR EMBL; AF229125; AAF43198.1; JOINED; Genomic_DNA.
DR EMBL; AF229126; AAF43199.1; -; Genomic_DNA.
DR EMBL; AF229117; AAF43199.1; JOINED; Genomic_DNA.
DR EMBL; AF229118; AAF43199.1; JOINED; Genomic_DNA.
DR EMBL; AF229119; AAF43199.1; JOINED; Genomic_DNA.
DR EMBL; AF229120; AAF43199.1; JOINED; Genomic_DNA.
DR EMBL; AF229121; AAF43199.1; JOINED; Genomic_DNA.
DR EMBL; AF229122; AAF43199.1; JOINED; Genomic_DNA.
DR EMBL; AF229123; AAF43199.1; JOINED; Genomic_DNA.
DR EMBL; AF229124; AAF43199.1; JOINED; Genomic_DNA.
DR EMBL; AF229125; AAF43199.1; JOINED; Genomic_DNA.
DR EMBL; AF229122; AAF43200.1; -; Genomic_DNA.
DR EMBL; AF229117; AAF43200.1; JOINED; Genomic_DNA.
DR EMBL; AF229118; AAF43200.1; JOINED; Genomic_DNA.
DR EMBL; AF229119; AAF43200.1; JOINED; Genomic_DNA.
DR EMBL; AF229120; AAF43200.1; JOINED; Genomic_DNA.
DR EMBL; AF229121; AAF43200.1; JOINED; Genomic_DNA.
DR EMBL; AF229124; AAF43201.1; -; Genomic_DNA.
DR EMBL; AF229117; AAF43201.1; JOINED; Genomic_DNA.
DR EMBL; AF229118; AAF43201.1; JOINED; Genomic_DNA.
DR EMBL; AF229119; AAF43201.1; JOINED; Genomic_DNA.
DR EMBL; AF229120; AAF43201.1; JOINED; Genomic_DNA.
DR EMBL; AF229121; AAF43201.1; JOINED; Genomic_DNA.
DR EMBL; AF229122; AAF43201.1; JOINED; Genomic_DNA.
DR EMBL; AF229126; AAF43202.1; -; Genomic_DNA.
DR EMBL; AF229117; AAF43202.1; JOINED; Genomic_DNA.
DR EMBL; AF229118; AAF43202.1; JOINED; Genomic_DNA.
DR EMBL; AF229119; AAF43202.1; JOINED; Genomic_DNA.
DR EMBL; AF229120; AAF43202.1; JOINED; Genomic_DNA.
DR EMBL; AF229121; AAF43202.1; JOINED; Genomic_DNA.
DR EMBL; AF229122; AAF43202.1; JOINED; Genomic_DNA.
DR EMBL; AY150334; AAO06814.1; -; mRNA.
DR EMBL; AY150336; AAO06816.1; -; mRNA.
DR EMBL; AY150337; AAO06817.1; -; mRNA.
DR EMBL; AY150338; AAO06818.1; -; mRNA.
DR EMBL; AY150339; AAO06819.1; -; mRNA.
DR EMBL; AK128401; BAG54671.1; -; mRNA.
DR EMBL; CH471055; EAW64250.1; -; Genomic_DNA.
DR EMBL; BC074828; AAH74828.1; -; mRNA.
DR EMBL; BC074829; AAH74829.1; -; mRNA.
DR CCDS; CCDS33709.1; -. [Q9Y215-1]
DR CCDS; CCDS43057.1; -. [Q9Y215-3]
DR CCDS; CCDS46768.1; -. [Q9Y215-2]
DR RefSeq; NP_005668.2; NM_005677.3. [Q9Y215-1]
DR RefSeq; NP_536799.1; NM_080538.2. [Q9Y215-2]
DR RefSeq; NP_536800.2; NM_080539.3. [Q9Y215-3]
DR PDB; 1VZJ; X-ray; 2.35 A; I/J=53-67.
DR PDBsum; 1VZJ; -.
DR AlphaFoldDB; Q9Y215; -.
DR SMR; Q9Y215; -.
DR BioGRID; 113897; 29.
DR IntAct; Q9Y215; 18.
DR STRING; 9606.ENSP00000373298; -.
DR iPTMnet; Q9Y215; -.
DR PhosphoSitePlus; Q9Y215; -.
DR BioMuta; COLQ; -.
DR DMDM; 116241309; -.
DR MassIVE; Q9Y215; -.
DR PaxDb; Q9Y215; -.
DR PeptideAtlas; Q9Y215; -.
DR PRIDE; Q9Y215; -.
DR ProteomicsDB; 85588; -. [Q9Y215-6]
DR Antibodypedia; 11101; 151 antibodies from 23 providers.
DR DNASU; 8292; -.
DR Ensembl; ENST00000383781.8; ENSP00000373291.3; ENSG00000206561.14. [Q9Y215-2]
DR Ensembl; ENST00000383786.9; ENSP00000373296.3; ENSG00000206561.14. [Q9Y215-3]
DR Ensembl; ENST00000383788.10; ENSP00000373298.3; ENSG00000206561.14. [Q9Y215-1]
DR Ensembl; ENST00000681097.1; ENSP00000505397.1; ENSG00000206561.14. [Q9Y215-7]
DR GeneID; 8292; -.
DR KEGG; hsa:8292; -.
DR MANE-Select; ENST00000383788.10; ENSP00000373298.3; NM_005677.4; NP_005668.2.
DR UCSC; uc003bzv.4; human. [Q9Y215-1]
DR CTD; 8292; -.
DR DisGeNET; 8292; -.
DR GeneCards; COLQ; -.
DR GeneReviews; COLQ; -.
DR HGNC; HGNC:2226; COLQ.
DR HPA; ENSG00000206561; Tissue enhanced (heart).
DR MalaCards; COLQ; -.
DR MIM; 603033; gene.
DR MIM; 603034; phenotype.
DR neXtProt; NX_Q9Y215; -.
DR OpenTargets; ENSG00000206561; -.
DR Orphanet; 98915; Synaptic congenital myasthenic syndromes.
DR PharmGKB; PA26743; -.
DR VEuPathDB; HostDB:ENSG00000206561; -.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000157248; -.
DR HOGENOM; CLU_650464_0_0_1; -.
DR InParanoid; Q9Y215; -.
DR OMA; GHLKCTP; -.
DR OrthoDB; 1156383at2759; -.
DR PhylomeDB; Q9Y215; -.
DR TreeFam; TF331890; -.
DR PathwayCommons; Q9Y215; -.
DR SignaLink; Q9Y215; -.
DR BioGRID-ORCS; 8292; 9 hits in 1068 CRISPR screens.
DR ChiTaRS; COLQ; human.
DR EvolutionaryTrace; Q9Y215; -.
DR GeneWiki; COLQ; -.
DR GenomeRNAi; 8292; -.
DR Pharos; Q9Y215; Tbio.
DR PRO; PR:Q9Y215; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9Y215; protein.
DR Bgee; ENSG00000206561; Expressed in right uterine tube and 105 other tissues.
DR ExpressionAtlas; Q9Y215; baseline and differential.
DR Genevisible; Q9Y215; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005604; C:basement membrane; TAS:ProtInc.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0043083; C:synaptic cleft; IEA:GOC.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0008201; F:heparin binding; IBA:GO_Central.
DR GO; GO:0001507; P:acetylcholine catabolic process in synaptic cleft; TAS:ProtInc.
DR GO; GO:0090150; P:establishment of protein localization to membrane; IEA:Ensembl.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0008582; P:regulation of synaptic assembly at neuromuscular junction; IEA:Ensembl.
DR GO; GO:0071340; P:skeletal muscle acetylcholine-gated channel clustering; IEA:Ensembl.
DR InterPro; IPR011936; Myxo_disulph_rpt.
DR TIGRFAMs; TIGR02232; myxo_disulf_rpt; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Collagen;
KW Congenital myasthenic syndrome; Disease variant; Disulfide bond;
KW Neurotransmitter degradation; Reference proteome; Repeat; Signal; Synapse.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..455
FT /note="Acetylcholinesterase collagenic tail peptide"
FT /id="PRO_0000005854"
FT DOMAIN 96..269
FT /note="Collagen-like 1"
FT DOMAIN 277..291
FT /note="Collagen-like 2"
FT REGION 51..67
FT /note="PRAD"
FT REGION 90..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 130..133
FT /note="Heparan sulfate proteoglycan binding"
FT /evidence="ECO:0000255"
FT REGION 235..238
FT /note="Heparan sulfate proteoglycan binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 133..150
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..273
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 51
FT /note="Interchain (with T subunit)"
FT /evidence="ECO:0000255"
FT DISULFID 52
FT /note="Interchain (with T subunit)"
FT /evidence="ECO:0000255"
FT DISULFID 93
FT /note="Interchain"
FT /evidence="ECO:0000255"
FT DISULFID 291
FT /note="Interchain"
FT /evidence="ECO:0000255"
FT DISULFID 293
FT /note="Interchain"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..35
FT /note="MVVLNPMTLGIYLQLFFLSIVSQPTFINSVLPISA -> MTGSSFSLAHLLI
FT ISGLLCYSAGCL (in isoform II)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_001175"
FT VAR_SEQ 73..76
FT /note="Missing (in isoform IV)"
FT /evidence="ECO:0000305"
FT /id="VSP_001176"
FT VAR_SEQ 74..107
FT /note="Missing (in isoform III)"
FT /evidence="ECO:0000305"
FT /id="VSP_001177"
FT VAR_SEQ 124..132
FT /note="Missing (in isoform V)"
FT /evidence="ECO:0000305"
FT /id="VSP_001178"
FT VAR_SEQ 240..291
FT /note="GQKGDSGVMGPPGKPGPSGQPGRPGPPGPPPAGQLIMGPKGERGFPGPPGRC
FT -> SSRTPCTLPRRPPVPCGQGSRSPVTVVAGNESQACLLPRFEEDYISSGTERG (in
FT isoform VI)"
FT /evidence="ECO:0000305"
FT /id="VSP_001179"
FT VAR_SEQ 272..281
FT /note="GQLIMGPKGE -> DFCGQQPGGA (in isoform VII)"
FT /evidence="ECO:0000305"
FT /id="VSP_001180"
FT VAR_SEQ 273..329
FT /note="QLIMGPKGERGFPGPPGRCLCGPTMNVNNPSYGESVYGPSSPRVPVIFVVNN
FT QEELE -> HMETCNAPSTATSTPRPAATSPEGREEKVGCAPQNWQQLLHCHQTGHVLA
FT PSPPTFV (in isoform VIII)"
FT /evidence="ECO:0000305"
FT /id="VSP_001181"
FT VAR_SEQ 282..455
FT /note="Missing (in isoform VII)"
FT /evidence="ECO:0000305"
FT /id="VSP_001182"
FT VAR_SEQ 292..455
FT /note="Missing (in isoform VI)"
FT /evidence="ECO:0000305"
FT /id="VSP_001183"
FT VAR_SEQ 330..455
FT /note="Missing (in isoform VIII)"
FT /evidence="ECO:0000305"
FT /id="VSP_001184"
FT VARIANT 59
FT /note="P -> Q (in CMS5; abrogates binding to T subunit)"
FT /evidence="ECO:0000269|PubMed:10665486"
FT /id="VAR_010133"
FT VARIANT 312
FT /note="S -> G (in dbSNP:rs6782980)"
FT /id="VAR_048809"
FT VARIANT 337
FT /note="I -> T (in CMS5; dbSNP:rs1057521153)"
FT /evidence="ECO:0000269|PubMed:24938146"
FT /id="VAR_071710"
FT VARIANT 342
FT /note="D -> E (in CMS5; impairs anchoring to the basal
FT lamina; dbSNP:rs758554049)"
FT /evidence="ECO:0000269|PubMed:10665486"
FT /id="VAR_010134"
FT VARIANT 410
FT /note="R -> Q (in CMS5; dbSNP:rs1025361623)"
FT /evidence="ECO:0000269|PubMed:10665486"
FT /id="VAR_010135"
FT VARIANT 430
FT /note="Y -> S (in CMS5; dbSNP:rs121908923)"
FT /evidence="ECO:0000269|PubMed:9758617"
FT /id="VAR_010136"
FT VARIANT 444
FT /note="C -> Y (in CMS5)"
FT /evidence="ECO:0000269|PubMed:10665486"
FT /id="VAR_010137"
FT CONFLICT 370
FT /note="D -> N (in Ref. 3; AAO06818)"
FT /evidence="ECO:0000305"
FT CONFLICT 399
FT /note="R -> RD (in Ref. 1; CAA12648 and 3; AAO06814/
FT AAO06816/AAO06817/AAO06818/AAO06819)"
FT /evidence="ECO:0000305"
FT CONFLICT 400
FT /note="C -> Y (in Ref. 3; AAO06816)"
FT /evidence="ECO:0000305"
FT CONFLICT 404
FT /note="Y -> D (in Ref. 3; AAO06817)"
FT /evidence="ECO:0000305"
FT CONFLICT 423
FT /note="G -> V (in Ref. 3; AAO06819)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 455 AA; 47766 MW; A95D3E5D5ECDBE55 CRC64;
MVVLNPMTLG IYLQLFFLSI VSQPTFINSV LPISAALPSL DQKKRGGHKA CCLLTPPPPP
LFPPPFFRGG RSPLLSPDMK NLMLELETSQ SPCMQGSLGS PGPPGPQGPP GLPGKTGPKG
EKGELGRPGR KGRPGPPGVP GMPGPIGWPG PEGPRGEKGD LGMMGLPGSR GPMGSKGYPG
SRGEKGSRGE KGDLGPKGEK GFPGFPGMLG QKGEMGPKGE PGIAGHRGPT GRPGKRGKQG
QKGDSGVMGP PGKPGPSGQP GRPGPPGPPP AGQLIMGPKG ERGFPGPPGR CLCGPTMNVN
NPSYGESVYG PSSPRVPVIF VVNNQEELER LNTQNAIAFR RDQRSLYFKD SLGWLPIQLT
PFYPVDYTAD QHGTCGDGLL QPGEECDDGN SDVGDDCIRC HRAYCGDGHR HEGVEDCDGS
DFGYLTCETY LPGSYGDLQC TQYCYIDSTP CRYFT
