COLQ_RAT
ID COLQ_RAT Reviewed; 458 AA.
AC O35167;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 123.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Wistar; TISSUE=Soleus muscle;
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).
CC -!- SUBCELLULAR LOCATION: Synapse {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=O35167-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=O35167-2; Sequence=VSP_001185, VSP_001186;
CC -!- TISSUE SPECIFICITY: Expressed in skeletal muscle, heart, brain, as well
CC as in lung, spleen, testis, but not liver. The short isoform represents
CC about 5% of the transcripts in the soleus muscle and about 15% in the
CC heart ventricle.
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.
CC -!- SIMILARITY: Belongs to the COLQ family. {ECO:0000305}.
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DR EMBL; AF007583; AAB81717.1; -; mRNA.
DR RefSeq; NP_062147.1; NM_019274.2. [O35167-1]
DR AlphaFoldDB; O35167; -.
DR STRING; 10116.ENSRNOP00000026550; -.
DR GeneID; 29755; -.
DR KEGG; rno:29755; -.
DR UCSC; RGD:2377; rat. [O35167-1]
DR CTD; 8292; -.
DR RGD; 2377; Colq.
DR eggNOG; KOG3544; Eukaryota.
DR InParanoid; O35167; -.
DR OrthoDB; 1156383at2759; -.
DR PhylomeDB; O35167; -.
DR PRO; PR:O35167; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005604; C:basement membrane; TAS:RGD.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
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; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IEA:GOC.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0008201; F:heparin binding; IDA:RGD.
DR GO; GO:0005198; F:structural molecule activity; TAS:RGD.
DR GO; GO:0090150; P:establishment of protein localization to membrane; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0071340; P:skeletal muscle acetylcholine-gated channel clustering; ISO:RGD.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR011936; Myxo_disulph_rpt.
DR Pfam; PF01391; Collagen; 1.
DR TIGRFAMs; TIGR02232; myxo_disulf_rpt; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Collagen; Disulfide bond;
KW Neurotransmitter degradation; Reference proteome; Repeat; Signal; Synapse.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..458
FT /note="Acetylcholinesterase collagenic tail peptide"
FT /id="PRO_0000005855"
FT DOMAIN 95..271
FT /note="Collagen-like 1"
FT DOMAIN 279..293
FT /note="Collagen-like 2"
FT REGION 51..67
FT /note="PRAD"
FT REGION 89..291
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 VAR_SEQ 74..81
FT /note="LLSPDMKN -> VSTPDLGE (in isoform Short)"
FT /evidence="ECO:0000305"
FT /id="VSP_001185"
FT VAR_SEQ 82..458
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000305"
FT /id="VSP_001186"
SQ SEQUENCE 458 AA; 47912 MW; 9A650767AF9F8C8E CRC64;
MAVLNPMTLG IYLQLFFCSI VSQPTFINSV LPISAALPGL DQKKRGNHKA CCLLMPPPPP
LFPPPFFRGS RSPLLSPDMK NLLELEASPS PCMQGSLGSP GPPGPQGPPG LPGKAGPKGE
KGDLGRPGRK GRPGPPGVPG EPGPVGWPGP EGPRGEKGDV GMMGLPGSRG PMGSKGFPGS
RGEKGSRGER GDLGPKGEKG FPGFPGMLGQ KGEMGPKGES GIAGHRGPTG RPGKRGKQGQ
KGDSGIMGPP GKPGPSGQPG RQGPPGPPGP PSAGQLVMGL KGERGFPGPP GRCLCGPPAN
VNNPSYGDPM YGRGSPRVPA IFVVNNQEEL EKLNTQNAIA FRRDQRSLYF KDSLGWLPIQ
LTPFYPVGLH HKAAWHLCGD GVLQPGEECD DGNPDVSDGC IDCHRAYCGD GYRHRGVEDC
DGSDFGYLKC ETYLPGSYGE LRCTQYCSID STPCRYFT
