CSST1_CONLV
ID CSST1_CONLV Reviewed; 81 AA.
AC A0A0K8TUE2;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 11-NOV-2015, sequence version 1.
DT 03-AUG-2022, entry version 7.
DE RecName: Full=Consomatin Le1 {ECO:0000305};
DE Short=ConSST Le1 {ECO:0000305};
DE AltName: Full=Somatostatin-related peptide {ECO:0000305};
DE Short=SSRP {ECO:0000305};
DE Flags: Precursor;
OS Conus lenavati (Cone snail).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Splinoconus.
OX NCBI_TaxID=1519839;
RN [1] {ECO:0000312|EMBL:JAI17883.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom duct;
RA Syromyatnikov M.Y., Popov V.N.;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:P0DQT5}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct. {ECO:0000305|Ref.1}.
CC -!- DOMAIN: The cysteine framework is C-C. {ECO:0000305|Ref.1}.
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:0000250|UniProtKB:P0DQT5}.
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; GCVH01000010; JAI17883.1; -; Transcribed_RNA.
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:0000250|UniProtKB:P0DQT5"
FT /id="PRO_0000456110"
FT PEPTIDE 58..70
FT /note="Consomatin Le1"
FT /evidence="ECO:0000250|UniProtKB:P0DQT5"
FT /id="PRO_5005520531"
FT PROPEP 71..81
FT /evidence="ECO:0000250|UniProtKB:P0DQT5"
FT /id="PRO_0000456111"
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 69
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P0DQT5"
FT DISULFID 62..67
FT /evidence="ECO:0000250|UniProtKB:P0DQT5"
SQ SEQUENCE 81 AA; 9461 MW; 85B1F87F71960599 CRC64;
MQTAYWVMVM MMVWITAPLS EGGKPNDVIR GLVPDDLTPQ LILRSLISRR RSDKDVREGY
KCVWKTCMPA LWRRHDLKGK D