ID   CG2RB_CONMI             Reviewed;          68 AA.
AC   A0A0E3SVB8;
DT   18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT   24-JUN-2015, sequence version 1.
DT   25-MAY-2022, entry version 10.
DE   RecName: Full=Conotoxin phi-MiXXVIIB {ECO:0000305};
DE   AltName: Full=Conopeptide Mi046 {ECO:0000303|PubMed:24043424};
DE   AltName: Full=Mi27.2 {ECO:0000305};
DE   Flags: Precursor;
OS   Conus miles (Soldier cone) (Mile cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Rhizoconus.
OX   NCBI_TaxID=69564;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, AND
RP   HYDROXYLATION AT PRO-44.
RC   TISSUE=Venom duct;
RX   PubMed=24043424; DOI=10.1074/mcp.m113.030353;
RA   Jin A.H., Dutertre S., Kaas Q., Lavergne V., Kubala P., Lewis R.J.,
RA   Alewood P.F.;
RT   "Transcriptomic messiness in the venom duct of Conus miles contributes to
RT   conotoxin diversity.";
RL   Mol. Cell. Proteomics 12:3824-3833(2013).
CC   -!- FUNCTION: This peptide promotes cell proliferation (EC(50)=17.85 uM)
CC       and inhibits apoptosis (EC(50)=2.2 uM).
CC       {ECO:0000250|UniProtKB:A0A0E3SVE7}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:24043424}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:24043424}.
CC   -!- DOMAIN: Displays a mini-granulin fold, a structure composed of two
CC       short, stacked beta-hairpins connected by two parallel disulfide bonds.
CC       This newly described fold is derived from the same cysteine
CC       connectivity as knottins (ICK fold). The name 'mini-granulin fold'
CC       comes from the structural homology with the N-terminal region of the
CC       human granulin. {ECO:0000250|UniProtKB:A0A0E3SVE7}.
CC   -!- DOMAIN: The cysteine framework is XXVII (C-C-C-CC-C-C). {ECO:0000305}.
CC   -!- MISCELLANEOUS: This peptide does not show activities on voltage-gated
CC       sodium (Nav) and calcium (Cav) channels as well as on nicotinic
CC       acetylcholine receptors (nAChRs) (at concentrations up to 100 uM).
CC       {ECO:0000250|UniProtKB:A0A0E3SVE7}.
CC   -!- SIMILARITY: Belongs to the conotoxin G2 superfamily. 1 family.
CC       {ECO:0000305}.
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DR   EMBL; KP216861; AKB91384.1; -; mRNA.
DR   AlphaFoldDB; A0A0E3SVB8; -.
DR   SMR; A0A0E3SVB8; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
PE   1: Evidence at protein level;
KW   Disulfide bond; Hydroxylation; Secreted; Signal.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000305|PubMed:24043424"
FT   PROPEP          30..35
FT                   /evidence="ECO:0000305|PubMed:24043424"
FT                   /id="PRO_0000444690"
FT   CHAIN           36..68
FT                   /note="Conotoxin phi-MiXXVIIB"
FT                   /evidence="ECO:0000305|PubMed:24043424"
FT                   /id="PRO_5002412104"
FT   MOD_RES         44
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000305|PubMed:24043424"
FT   DISULFID        38..49
FT                   /evidence="ECO:0000250|UniProtKB:A0A0E3SVE7"
FT   DISULFID        42..51
FT                   /evidence="ECO:0000250|UniProtKB:A0A0E3SVE7"
FT   DISULFID        45..56
FT                   /evidence="ECO:0000250|UniProtKB:A0A0E3SVE7"
FT   DISULFID        50..61
FT                   /evidence="ECO:0000250|UniProtKB:A0A0E3SVE7"
SQ   SEQUENCE   68 AA;  7342 MW;  81093AA9EB649251 CRC64;
     MRFFFLLLTV ALFLTSITGD DAERMLGMKE GGYVREDCGS DCAPCGGECC CEPNSCIDGT
     CHHESSPN