ID   COLQ_TORMA              Reviewed;         471 AA.
AC   Q03637;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Acetylcholinesterase collagenic tail peptide;
DE   AltName: Full=AChE Q subunit;
DE   Flags: Precursor;
OS   Torpedo marmorata (Marbled electric ray).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Elasmobranchii; Batoidea; Torpediniformes; Torpedinidae; Torpedo.
OX   NCBI_TaxID=7788;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Electric organ;
RX   PubMed=1840520; DOI=10.1002/j.1460-2075.1991.tb08070.x;
RA   Krejci E., Coussen F., Duval N., Chatel J.-M., Legay C., Puype M.,
RA   Vanderkerckhove J., Cartaud J., Bon S., Massoulie J.;
RT   "Primary structure of a collagenic tail peptide of Torpedo
RT   acetylcholinesterase: co-expression with catalytic subunit induces the
RT   production of collagen-tailed forms in transfected cells.";
RL   EMBO J. 10:1285-1293(1991).
RN   [2]
RP   SUBUNITS INTERACTION.
RC   TISSUE=Electric organ;
RX   PubMed=1380451; DOI=10.1002/j.1460-2075.1992.tb05403.x;
RA   Duval N., Krejci E., Grassi J., Coussen F., Massoulie J., Bon S.;
RT   "Molecular architecture of acetylcholinesterase collagen-tailed forms;
RT   construction of a glycolipid-tailed tetramer.";
RL   EMBO J. 11:3255-3261(1992).
RN   [3]
RP   IDENTIFICATION OF PRO-RICH ATTACHMENT DOMAIN.
RX   PubMed=9006950; DOI=10.1074/jbc.272.5.3016;
RA   Bon S., Coussen F., Massoulie J.;
RT   "Quaternary associations of acetylcholinesterase. II. The polyproline
RT   attachment domain of the collagen tail.";
RL   J. Biol. Chem. 272:3016-3021(1997).
RN   [4]
RP   3D-STRUCTURE MODELING OF COLLAGEN-LIKE DOMAIN.
RX   PubMed=10679527; DOI=10.1093/protein/13.1.27;
RA   Deprez P., Inestrosa N.C.;
RT   "Molecular modeling of the collagen-like tail of asymmetric
RT   acetylcholinesterase.";
RL   Protein Eng. 13:27-34(2000).
CC   -!- FUNCTION: Anchors the catalytic subunits of asymmetric AChE to the
CC       synaptic basal lamina.
CC   -!- SUBUNIT: The asymmetric form of AChE is a disulfide-bonded oligomer
CC       composed of a collagenic subunit (Q) and a variable number of
CC       asymmetric (T) catalytic subunits. The N-terminal of the collagenic
CC       subunit (Q) associates with the C-terminal of the catalytic subunit
CC       (T). {ECO:0000269|PubMed:1380451}.
CC   -!- SUBCELLULAR LOCATION: Synapse.
CC   -!- TISSUE SPECIFICITY: Expressed in electric organs but not in muscle.
CC   -!- DOMAIN: The proline-rich attachment domain (PRAD) binds the AChE
CC       catalytic subunits.
CC   -!- SIMILARITY: Belongs to the COLQ family. {ECO:0000305}.
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DR   EMBL; X59359; CAA42009.1; -; mRNA.
DR   PIR; S15035; S15035.
DR   AlphaFoldDB; Q03637; -.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR   GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR   GO; GO:0042135; P:neurotransmitter catabolic process; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Collagen; Direct protein sequencing; Disulfide bond;
KW   Neurotransmitter degradation; Repeat; Signal; Synapse.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..471
FT                   /note="Acetylcholinesterase collagenic tail peptide"
FT                   /id="PRO_0000005856"
FT   DOMAIN          118..282
FT                   /note="Collagen-like 1"
FT   DOMAIN          293..307
FT                   /note="Collagen-like 2"
FT   REPEAT          388..413
FT                   /note="1"
FT   REPEAT          420..443
FT                   /note="2"
FT   REGION          70..86
FT                   /note="PRAD"
FT   REGION          140..205
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          237..267
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          388..443
FT                   /note="2 X 26 AA approximate repeats"
FT   DISULFID        70
FT                   /note="Interchain (with T subunit)"
FT                   /evidence="ECO:0000255"
FT   DISULFID        71
FT                   /note="Interchain (with T subunit)"
FT                   /evidence="ECO:0000255"
FT   DISULFID        111
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255"
FT   DISULFID        115
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255"
FT   DISULFID        307
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255"
FT   DISULFID        309
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   471 AA;  49545 MW;  B0137A393758D539 CRC64;
     MLGILLQKAT ATLASGLNSS RAGMFPIALG LLLQLFFDHA LAESTFLDKA FSLQAALLPM
     EHKKRSVNKC CLLTPPPPPM FPPPFFTETN ILQEVDLNNL PLEIKPTEPS CKITCIIGPP
     GPSGPQGPQG IQGIMGPKGE IGEIGRPGRK GRPGVRGPRG MPGSPCSPGP IGPRGEKGDI
     GLTGLPGARG PMGPKGLTGQ KGEKGIIGEK GQQGIKGEMG VMGLPGMLGQ KGEMGPKGVS
     GAPGHRGPVG RPGKRGKTGL KGDIGPPGIM GPSGPPGPSG LPVMSGSGHL MVGPKGERGL
     PGPVGRCDCN LPQTVVNPSY NKFPTLINPP QVPAIFVVDS EDELEKLNTE NALAFRKDQK
     SLYYRDTVGW LPIQIAPIQQ MRQNPTGFCG DEIVQVENGE ECDDGNRIVT DSCINCKQAY
     CGDGYLQSGL EECDGKDFGY HTCKSYLPGS YGELKCTSYC YIDSTGCRYF T