ID   CSST1_CONMA             Reviewed;          74 AA.
AC   A0A679PF76;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   17-JUN-2020, sequence version 1.
DT   03-AUG-2022, entry version 4.
DE   RecName: Full=Consomatin Ma1 {ECO:0000303|PubMed:35383850};
DE            Short=ConSST Ma1 {ECO:0000305};
DE   AltName: Full=Somatostatin-related peptide {ECO:0000303|PubMed:35383850};
DE            Short=SSRP {ECO:0000303|PubMed:35383850};
DE   Flags: Precursor;
OS   Conus magus (Magical cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Pionoconus.
OX   NCBI_TaxID=6492;
RN   [1] {ECO:0000312|EMBL:DAC80550.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=31569823; DOI=10.3390/md17100553;
RA   Pardos-Blas J.R., Irisarri I., Abalde S., Tenorio M.J., Zardoya R.;
RT   "Conotoxin diversity in the venom gland transcriptome of the Magician's
RT   Cone, Pionoconus magus.";
RL   Mar. Drugs 17:E553-E553(2019).
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:31569823}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:31569823}.
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}.
CC   -!- CAUTION: The name 'Consomatin Ma1' has also been given to a peptide
CC       from Conus maioensis. As a consequence, we have suggested to rename the
CC       peptide from Conus maioensis 'Consomatin Mao1'. {ECO:0000305}.
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DR   EMBL; BK011202; DAC80550.1; -; mRNA.
PE   3: Inferred from homology;
KW   D-amino acid; Disulfide bond; G-protein coupled receptor impairing toxin;
KW   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_0000456134"
FT   PEPTIDE         52..73
FT                   /note="Consomatin Ma1"
FT                   /evidence="ECO:0000305|PubMed:35383850"
FT                   /id="PRO_5025673322"
FT   MOD_RES         65
FT                   /note="D-tryptophan"
FT                   /evidence="ECO:0000250|UniProtKB:P0DQT5"
FT   MOD_RES         69
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         70
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         72
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000305"
FT   DISULFID        63..68
FT                   /evidence="ECO:0000250|UniProtKB:P0DQT5"
SQ   SEQUENCE   74 AA;  8254 MW;  EBD7BDB242063E3B CRC64;
     MQTAYWVMVM MMVWITAPLS EGGKLNGEIR GLVSHILIPQ HTLRSLTSRD RSDNGGSSGA
     QICIWKVCPP SPWR