COLQ_MOUSE
ID COLQ_MOUSE Reviewed; 457 AA.
AC O35348; Q08EK8;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 138.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 37-273.
RC STRAIN=129/SvJ;
RX PubMed=9278446; DOI=10.1074/jbc.272.36.22840;
RA Krejci E., Thomine S., Boschetti N., Legay C., Sketelj J., Massoulie J.;
RT "The mammalian gene of acetylcholinesterase-associated collagen.";
RL J. Biol. Chem. 272:22840-22847(1997).
CC -!- FUNCTION: Anchors the catalytic subunits of asymmetric AChE to the
CC synaptic basal lamina. {ECO:0000250}.
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) (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Synapse {ECO:0000250}.
CC -!- DOMAIN: The proline-rich attachment domain (PRAD) binds the AChE
CC catalytic subunits. {ECO:0000250}.
CC -!- PTM: The triple-helical tail is stabilized by disulfide bonds at each
CC end. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the COLQ family. {ECO:0000305}.
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DR EMBL; BC107386; AAI07387.1; -; mRNA.
DR EMBL; AH005576; AAB72195.1; -; Genomic_DNA.
DR CCDS; CCDS36856.2; -.
DR RefSeq; NP_034067.2; NM_009937.2.
DR AlphaFoldDB; O35348; -.
DR SMR; O35348; -.
DR STRING; 10090.ENSMUSP00000107658; -.
DR PhosphoSitePlus; O35348; -.
DR MaxQB; O35348; -.
DR PaxDb; O35348; -.
DR PRIDE; O35348; -.
DR ProteomicsDB; 285245; -.
DR Antibodypedia; 11101; 151 antibodies from 23 providers.
DR Ensembl; ENSMUST00000112027; ENSMUSP00000107658; ENSMUSG00000057606.
DR GeneID; 382864; -.
DR KEGG; mmu:382864; -.
DR UCSC; uc007sxv.2; mouse.
DR CTD; 8292; -.
DR MGI; MGI:1338761; Colq.
DR VEuPathDB; HostDB:ENSMUSG00000057606; -.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000157248; -.
DR HOGENOM; CLU_650464_0_0_1; -.
DR InParanoid; O35348; -.
DR OMA; GHLKCTP; -.
DR OrthoDB; 1156383at2759; -.
DR PhylomeDB; O35348; -.
DR TreeFam; TF331890; -.
DR BioGRID-ORCS; 382864; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Colq; mouse.
DR PRO; PR:O35348; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; O35348; protein.
DR Bgee; ENSMUSG00000057606; Expressed in thymus and 60 other tissues.
DR ExpressionAtlas; O35348; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
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; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0008201; F:heparin binding; ISO:MGI.
DR GO; GO:0090150; P:establishment of protein localization to membrane; IMP:MGI.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0042135; P:neurotransmitter catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0008582; P:regulation of synaptic assembly at neuromuscular junction; IMP:MGI.
DR GO; GO:0071340; P:skeletal muscle acetylcholine-gated channel clustering; IDA:MGI.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR011936; Myxo_disulph_rpt.
DR Pfam; PF01391; Collagen; 2.
DR TIGRFAMs; TIGR02232; myxo_disulf_rpt; 1.
PE 2: Evidence at transcript level;
KW Collagen; Disulfide bond; Neurotransmitter degradation; Reference proteome;
KW Repeat; Signal; Synapse.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..457
FT /note="Acetylcholinesterase collagenic tail peptide"
FT /id="PRO_0000059415"
FT DOMAIN 95..154
FT /note="Collagen-like 1"
FT DOMAIN 158..271
FT /note="Collagen-like 2"
FT REGION 51..67
FT /note="PRAD"
FT /evidence="ECO:0000250"
FT REGION 89..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..132
FT /note="Heparan sulfate proteoglycan binding"
FT /evidence="ECO:0000255"
FT REGION 234..237
FT /note="Heparan sulfate proteoglycan binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 96..112
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..149
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..272
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 92
FT /note="Interchain"
FT /evidence="ECO:0000255"
FT DISULFID 293
FT /note="Interchain"
FT /evidence="ECO:0000255"
FT DISULFID 295
FT /note="Interchain"
FT /evidence="ECO:0000255"
FT CONFLICT 105
FT /note="Missing (in Ref. 2; AAB72195)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="P -> H (in Ref. 2; AAB72195)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="P -> A (in Ref. 2; AAB72195)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 457 AA; 47684 MW; 461E93C3DB0162B2 CRC64;
MVVLNPMTLG IYLQLFFCSI VSQPTFINSV VPISAALPGL DQKKRGSHKA CCLLMPPPPP
LFPPPFFRGS RSPLLSPDMK NLLELEASPS PCIQGSLGSP GPPGPQGPPG LPGKTGPKGE
KGDLGRPGRK GRPGPPGVPG MPGPVGWPGP EGPRGEKGDL GMMGLPGSRG PMGSKGFPGS
RGEKGSRGER GDLGPKGEKG FPGFPGMLGQ KGEMGPKGES GLAGHRGPTG RPGKRGKQGQ
KGDSGIMGPP GKPGPSGQPG RQGPPGPPGP PSAGQLVMGL KGERGFPGPP GRCLCGPPVN
VNNPSYGDSM YGRGSPRVPA IFVVNNQEEL ERLNTQNAIA FRRDQRSLYF KDSLGWLPIQ
LTPFYPVGYT VKQPGTCGDG VLQPGEECDD GNPDVSDGCI DCHRAYCGDG YRHQGVEDCD
GSDFGYLTCE TYLPGSYGDL RCTQYCSIDS TPCRYFT
