CONOT_CONTU
ID CONOT_CONTU Reviewed; 9 AA.
AC P0DL76;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2017, sequence version 1.
DT 07-OCT-2020, entry version 11.
DE RecName: Full=Conopressin-T {ECO:0000303|PubMed:18174156};
DE Short=Con-T {ECO:0000303|PubMed:18174156};
OS Conus tulipa (Fish-hunting cone snail) (Tulip cone).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Gastridium.
OX NCBI_TaxID=6495;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LEU-7,
RP STRUCTURE BY NMR, DISULFIDE BOND, AMIDATION AT VAL-9, MASS SPECTROMETRY,
RP AND SYNTHESIS.
RC TISSUE=Venom;
RX PubMed=18174156; DOI=10.1074/jbc.m706477200;
RA Dutertre S., Croker D., Daly N.L., Andersson A., Muttenthaler M.,
RA Lumsden N.G., Craik D.J., Alewood P.F., Guillon G., Lewis R.J.;
RT "Conopressin-T from Conus tulipa reveals an antagonist switch in
RT vasopressin-like peptides.";
RL J. Biol. Chem. 283:7100-7108(2008).
CC -!- FUNCTION: Interacts with high affinity with oxytocin receptor (OXTR)
CC (Ki=108 nM) and vasopressin V1a receptor (V1aR/AVPR1A) (Ki=319 nM).
CC Acts as a partial agonist on OXTR (Kact=37 nM, 22% of oxytocin maximum
CC activity at 10 uM), and as a full antagonist on V1aR (Kinact=329 nM).
CC {ECO:0000269|PubMed:18174156}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18174156}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC {ECO:0000305|PubMed:18174156}.
CC -!- DOMAIN: The cysteine framework is C-C. {ECO:0000305}.
CC -!- MASS SPECTROMETRY: Mass=1107.54; Method=Electrospray; Note=Monoisotopic
CC mass.; Evidence={ECO:0000269|PubMed:18174156};
CC -!- MISCELLANEOUS: Does not show binding with vasopressin V1b and V2
CC receptors (up to 10 uM). Shows a weak agonist activity on V1bR/AVPR1B
CC (9% at 10 uM). {ECO:0000269|PubMed:18174156}.
CC -!- SIMILARITY: Belongs to the vasopressin/oxytocin family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Biological Magnetic Resonance Data Bank;
CC URL="http://www.bmrb.wisc.edu/data_library/summary/index.php?bmrbId=20007";
CC -!- WEB RESOURCE: Name=Biological Magnetic Resonance Data Bank; Note=L7P
CC mutant;
CC URL="http://www.bmrb.wisc.edu/data_library/summary/index.php?bmrbId=20008";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Amidation; Direct protein sequencing; Disulfide bond;
KW G-protein coupled receptor impairing toxin; Secreted; Toxin.
FT PEPTIDE 1..9
FT /note="Conopressin-T"
FT /evidence="ECO:0000269|PubMed:18174156"
FT /id="PRO_0000442232"
FT SITE 9
FT /note="Important residue for antagonist activity on
FT V1aR/AVPR1A (a Gly in this position produces agonist
FT activity)"
FT /evidence="ECO:0000269|PubMed:18174156"
FT MOD_RES 9
FT /note="Valine amide"
FT /evidence="ECO:0000269|PubMed:18174156"
FT DISULFID 1..6
FT /evidence="ECO:0000269|PubMed:18174156"
FT MUTAGEN 7
FT /note="L->P: 8-fold increase in affinity for V1aR/AVPR1A,
FT no change in affinity for V1b and oxytocin receptors (OXTR)
FT and gain of affinity for V2R (Ki=1.8 uM)."
FT /evidence="ECO:0000269|PubMed:18174156"
SQ SEQUENCE 9 AA; 1111 MW; 0D5B072EB456D04B CRC64;
CYIQNCLRV