ID   CSST1_CONBE             Reviewed;          69 AA.
AC   A0A142C197;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   08-JUN-2016, sequence version 1.
DT   03-AUG-2022, entry version 7.
DE   RecName: Full=Consomatin Be1 {ECO:0000303|PubMed:35383850};
DE            Short=ConSST Be1 {ECO:0000305};
DE   AltName: Full=Somatostatin-related peptide {ECO:0000303|PubMed:35383850};
DE            Short=SSRP {ECO:0000303|PubMed:35383850};
DE   Flags: Precursor;
OS   Conus betulinus (Beech cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Dendroconus.
OX   NCBI_TaxID=89764;
RN   [1] {ECO:0000312|EMBL:AMP44598.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Ruan Z., Peng C., Shi Q., Yao G., Gao B.-M.;
RT   "High throughput identification of novel conotoxins from the Chinese
RT   tubular cone snail Conus betulinus by multitranscriptome sequencing.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom duct;
RX   PubMed=35383850; DOI=10.1093/molbev/msac075;
RA   Koch T.L., Ramiro I.B.L., Florez-Salcedo P., Engholm E., Jensen K.J.,
RA   Chase K., Olivera B.M., Bjoern-Yoshimoto W.E., Safavi-Hemami H.;
RT   "Reconstructing the origins of the somatostatin and allatostatin-C
RT   signaling systems using the accelerated evolution of biodiverse cone snail
RT   venoms.";
RL   Mol. Biol. Evol. 0:0-0(2022).
CC   -!- FUNCTION: Moderately activates human somatostatin receptors (SSTR) with
CC       a preferential activation of SSTR1 and SSTR4. In vivo, does not cause
CC       behavioral changes in mice within a few minutes of intracranial
CC       injection, but causes a progressive loss of movement thereafter. Four
CC       to five hours after injection, mice recover, even with the highest dose
CC       tested. Shows antinociception and antihyperalgesia activities in two
CC       mouse models of acute pain, most probably by acting outside the central
CC       nervous system. {ECO:0000250|UniProtKB:P0DQT5}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:35383850}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:35383850}.
CC   -!- DOMAIN: The cysteine framework is C-C. {ECO:0000305}.
CC   -!- MISCELLANEOUS: This peptide is an evolutionarily optimized stable
CC       analog of somatostatin. In addition, it adopts nearly identical
CC       conformations as in the somatostatin drug analog Octreotide. As this
CC       drug, it contains a D-Trp at the same position, whose synthesis is a
CC       common strategy used for enhancing the metabolic stability of compounds
CC       in drug design. {ECO:0000250|UniProtKB:P0DQT5}.
CC   -!- MISCELLANEOUS: Consomatins evolved by gene duplication of a
CC       'Somatostatin and related peptides (SSRP)' gene expressed in the snail
CC       neuroendocrine system. {ECO:0000269|PubMed:35383850}.
CC   -!- MISCELLANEOUS: Does not activate any of the other 313 GPCRs tested.
CC       Shows little or no activating activity at the SSTR2, SSTR3 and SSTR5.
CC       {ECO:0000250|UniProtKB:P0DQT5}.
CC   -!- SIMILARITY: Belongs to the conotoxin C superfamily. Consomatin family.
CC       {ECO:0000305}.
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DR   EMBL; KU317638; AMP44598.1; -; mRNA.
PE   3: Inferred from homology;
KW   D-amino acid; Disulfide bond; G-protein coupled receptor impairing toxin;
KW   Gamma-carboxyglutamic acid; Hydroxylation; Secreted; Signal; Toxin.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..57
FT                   /evidence="ECO:0000305|PubMed:35383850"
FT                   /id="PRO_0000456120"
FT   PEPTIDE         58..69
FT                   /note="Consomatin Be1"
FT                   /id="PRO_5007493520"
FT   MOD_RES         58
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P0DQT5"
FT   MOD_RES         64
FT                   /note="D-tryptophan"
FT                   /evidence="ECO:0000250|UniProtKB:P0DQT5"
FT   MOD_RES         68
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         69
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:P0DQT5"
FT   DISULFID        62..67
FT                   /evidence="ECO:0000250|UniProtKB:P0DQT5"
SQ   SEQUENCE   69 AA;  7909 MW;  750AEB60EAF6BF55 CRC64;
     MEMAYWVMVM MMVWITAPLS EGGKLNDVIR ALAPDDVTPQ FILRSLISRR RSDSDVREVP
     VCSWKICPP