CP9A_CONTE
ID CP9A_CONTE Reviewed; 88 AA.
AC Q9GU58;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=Conotoxin tx9a {ECO:0000303|PubMed:10677206};
DE AltName: Full=Spasmodic peptide {ECO:0000303|PubMed:10677206};
DE Flags: Precursor;
OS Conus textile (Cloth-of-gold cone).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Cylinder.
OX NCBI_TaxID=6494;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 61-87,
RP GAMMA-CARBOXYGLUTAMATION AT GLU-68 AND GLU-73, AMIDATION AT ASN-87, MASS
RP SPECTROMETRY, BIOASSAY, AND FUNCTION.
RC TISSUE=Venom;
RX PubMed=10677206; DOI=10.1021/bi9923712;
RA Lirazan M.B., Hooper D., Corpuz G.P., Ramilo C.A., Bandyopadhyay P.,
RA Cruz L.J., Olivera B.M.;
RT "The spasmodic peptide defines a new conotoxin superfamily.";
RL Biochemistry 39:1583-1588(2000).
RN [2]
RP PROTEIN SEQUENCE OF 61-87, SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND
RP AMIDATION AT ASN-87.
RC TISSUE=Venom;
RX PubMed=19380747; DOI=10.1073/pnas.0900745106;
RA Ueberheide B.M., Fenyo D., Alewood P.F., Chait B.T.;
RT "Rapid sensitive analysis of cysteine rich peptide venom components.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:6910-6915(2009).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY, POSITION IN VENOM
RP DUCT, GAMMA-CARBOXYGLUTAMATION AT GLU-68 AND GLU-73, AND AMIDATION AT
RP ASN-87.
RC TISSUE=Venom;
RX PubMed=23031820; DOI=10.1016/j.toxicon.2012.09.013;
RA Dobson R., Collodoro M., Gilles N., Turtoi A., De Pauw E., Quinton L.;
RT "Secretion and maturation of conotoxins in the venom ducts of Conus
RT textile.";
RL Toxicon 60:1370-1379(2012).
CC -!- FUNCTION: Neurotoxin. In vivo, intracranial injection into mice of 10
CC pmol/g of the peptide induces running in circles and hyperactivity. At
CC higher doses (50 pmol/g), the mice exhibit running and climbing
CC symptoms for close to one hour. Between 130 and 150 pmol/g,
CC characteristic 'spasmodic' symptomatology is elicited. A hand clap
CC would make mice jump high and start running rapidly. When exposed to a
CC loud hand clap, or if the cage cover were dropped, the mice lose motor
CC control and exhibit seizure-like symptoms from which they eventually
CC recover. At the highest doses tested (over 250 pmol/g), after the
CC characteristic spasmodic symptomatology, lethality occurs. Injection of
CC a similar dose range intramuscularly into Siamese fighting fish
CC elicited no unusual symptomatology. {ECO:0000269|PubMed:10677206}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19380747}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct. All different gamma-
CC carboxyalted forms are mostly present in part 2, part 3 and part 4 of
CC the venom duct. They are also found in part 1 (proximal part near the
CC venom bulb) and part 5, but in lower quantity.
CC {ECO:0000305|PubMed:19380747, ECO:0000305|PubMed:23031820}.
CC -!- DOMAIN: The cysteine framework is IX (C-C-C-C-C-C). {ECO:0000305}.
CC -!- PTM: Exists in 4 different forms, depending on gamma-
CC carboxyglutamations. Tx9a-EE does not contain gamma-carboxyglutamate,
CC tx9a-E/gamma has one gamma-carboxyglutamate at position 73, tx9a-
CC gamma/E has one gamma-carboxyglutamate at position 68, and tx9a-
CC agmma/gamma has two gamma-carboxyglutamates at positions 68 and 73.
CC {ECO:0000269|PubMed:23031820}.
CC -!- MASS SPECTROMETRY: Mass=2955.0; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10677206};
CC -!- MASS SPECTROMETRY: Mass=2866.021; Mass_error=0.01; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:19380747};
CC -!- SIMILARITY: Belongs to the conotoxin P superfamily. {ECO:0000305}.
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DR EMBL; AF193510; AAG28406.1; -; mRNA.
DR AlphaFoldDB; Q9GU58; -.
DR SMR; Q9GU58; -.
DR ConoServer; 608; TxIXA precursor.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR InterPro; IPR010012; Toxin_11.
DR Pfam; PF07473; Toxin_11; 1.
PE 1: Evidence at protein level;
KW Amidation; Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Gamma-carboxyglutamic acid; Neurotoxin; Secreted; Signal;
KW Toxin.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT PROPEP 28..58
FT /evidence="ECO:0000305"
FT /id="PRO_0000035011"
FT PEPTIDE 61..87
FT /note="Conotoxin tx9a"
FT /evidence="ECO:0000269|PubMed:10677206,
FT ECO:0000269|PubMed:19380747"
FT /id="PRO_0000035012"
FT MOD_RES 68
FT /note="4-carboxyglutamate; partial"
FT /evidence="ECO:0000269|PubMed:10677206,
FT ECO:0000269|PubMed:23031820"
FT MOD_RES 73
FT /note="4-carboxyglutamate; partial"
FT /evidence="ECO:0000269|PubMed:10677206,
FT ECO:0000269|PubMed:23031820"
FT MOD_RES 87
FT /note="Asparagine amide"
FT /evidence="ECO:0000269|PubMed:10677206,
FT ECO:0000269|PubMed:19380747, ECO:0000269|PubMed:23031820"
FT DISULFID 62..76
FT /evidence="ECO:0000250|UniProtKB:Q9GU57"
FT DISULFID 66..78
FT /evidence="ECO:0000250|UniProtKB:Q9GU57"
FT DISULFID 72..83
FT /evidence="ECO:0000250|UniProtKB:Q9GU57"
SQ SEQUENCE 88 AA; 9773 MW; 6C502E42A6C89E87 CRC64;
MHLSLARSAV LMLLLLFALG NFVVVQSGQI TRDVDNGQLT DNRRNLQSKW KPVSLYMSRR
GCNNSCQEHS DCESHCICTF RGCGAVNG
