CG2RA_CONMI
ID CG2RA_CONMI Reviewed; 68 AA.
AC A0A0E3SVE7;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 24-JUN-2015, sequence version 1.
DT 25-MAY-2022, entry version 14.
DE RecName: Full=Conotoxin phi-MiXXVIIA {ECO:0000303|PubMed:28984021};
DE AltName: Full=Conopeptide Mi045 {ECO:0000303|PubMed:24043424};
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], AND IDENTIFICATION BY MASS SPECTROMETRY.
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).
RN [2]
RP STRUCTURE BY NMR OF 36-68, FUNCTION, SYNTHESIS OF 36-68, AND DISULFIDE
RP BOND.
RX PubMed=28984021; DOI=10.1002/anie.201708927;
RA Jin A.H., Dekan Z., Smout M.J., Wilson D., Dutertre S., Vetter I.,
RA Lewis R.J., Loukas A., Daly N.L., Alewood P.F.;
RT "Conotoxin Phi-MiXXVIIA from the superfamily G2 employs a novel cysteine
RT framework that mimics granulin and displays anti-apoptotic activity.";
RL Angew. Chem. Int. Ed. 56:14973-14976(2017).
CC -!- FUNCTION: This peptide promotes cell proliferation (EC(50)=17.85 uM)
CC and inhibits apoptosis (EC(50)=2.2 uM). {ECO:0000269|PubMed:28984021}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28984021}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC {ECO:0000305|PubMed:28984021}.
CC -!- DOMAIN: The cysteine framework is XXVII (C-C-C-CCC-C-C). {ECO:0000305}.
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:0000305|PubMed:28984021}.
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:0000269|PubMed:28984021}.
CC -!- SIMILARITY: Belongs to the conotoxin G2 superfamily. 1 family.
CC {ECO:0000305}.
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DR EMBL; KP216860; AKB91383.1; -; mRNA.
DR PDB; 6PPC; NMR; -; A=36-68.
DR PDBsum; 6PPC; -.
DR AlphaFoldDB; A0A0E3SVE7; -.
DR BMRB; A0A0E3SVE7; -.
DR SMR; A0A0E3SVE7; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; 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_0000444689"
FT CHAIN 36..68
FT /note="Conotoxin phi-MiXXVIIA"
FT /evidence="ECO:0000305|PubMed:24043424"
FT /id="PRO_5002412259"
FT DISULFID 38..49
FT /evidence="ECO:0000269|PubMed:28984021,
FT ECO:0007744|PDB:6PPC"
FT DISULFID 42..51
FT /evidence="ECO:0000269|PubMed:28984021,
FT ECO:0007744|PDB:6PPC"
FT DISULFID 45..56
FT /evidence="ECO:0000269|PubMed:28984021,
FT ECO:0007744|PDB:6PPC"
FT DISULFID 50..61
FT /evidence="ECO:0000269|PubMed:28984021,
FT ECO:0007744|PDB:6PPC"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:6PPC"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:6PPC"
SQ SEQUENCE 68 AA; 7402 MW; 8105FA65EB649251 CRC64;
MRFFFLLLTV ALFLTSITGD DAERMLGMKE GGYVREDCGS DCMPCGGECC CEPNSCIDGT
CHHESSPN
