ID   COMA_CONMR              Reviewed;          71 AA.
AC   B2KPN7;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   25-MAY-2022, entry version 36.
DE   RecName: Full=Conomarphin {ECO:0000303|PubMed:18355315};
DE   AltName: Full=Marmophine;
DE   Flags: Precursor;
OS   Conus marmoreus (Marble cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Conus.
OX   NCBI_TaxID=42752;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 55-69
RP   (D-PHE13-CONOMARPHIN), SYNTHESIS OF 55-69 (L-PHE13-CONOMARPHIN),
RP   HYDROXYLATION AT PRO-64, D-AMINO ACID AT PHE-67, SUBCELLULAR LOCATION, AND
RP   STRUCTURE BY NMR OF 55-69.
RC   TISSUE=Venom, and Venom duct;
RX   PubMed=18355315; DOI=10.1111/j.1742-4658.2008.06352.x;
RA   Han Y., Huang F., Jiang H., Liu L., Wang Q., Wang Y., Shao X., Chi C.,
RA   Du W., Wang C.;
RT   "Purification and structural characterization of a D-amino acid-containing
RT   conopeptide, conomarphin, from Conus marmoreus.";
RL   FEBS J. 275:1976-1987(2008).
RN   [2]
RP   STRUCTURE BY NMR OF 55-69 OF HYP-64 VARIANT.
RX   PubMed=19375441; DOI=10.1016/j.toxicon.2009.03.033;
RA   Huang F., Du W.;
RT   "Solution structure of Hyp10Pro variant of conomarphin, a cysteine-free and
RT   d-amino-acid containing conopeptide.";
RL   Toxicon 54:153-160(2009).
CC   -!- FUNCTION: May act as a neurotoxin.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18355315}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:18355315}.
CC   -!- PTM: The D-phenylalanine is essential to the structural conformation.
CC       {ECO:0000269|PubMed:18355315}.
CC   -!- PTM: Since conomarphin is a cysteine-free peptide, hydroxyproline plays
CC       a critical role in maintaining a restricted conformation of the
CC       peptide.
CC   -!- MISCELLANEOUS: The mature peptide does not contain cysteine residues.
CC       {ECO:0000305}.
CC   -!- MISCELLANEOUS: The amino acid sequence of conomarphin is identical to
CC       that of C.imperialis Im-conomarphin (AC P0CH39). Their nucleotide
CC       sequences are not identical. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the conotoxin M superfamily. {ECO:0000305}.
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DR   EMBL; EU048276; ABW16858.1; -; mRNA.
DR   PDB; 2JQB; NMR; -; A=55-69.
DR   PDB; 2JQC; NMR; -; A=55-69.
DR   PDB; 2YYF; NMR; -; A=55-69.
DR   PDBsum; 2JQB; -.
DR   PDBsum; 2JQC; -.
DR   PDBsum; 2YYF; -.
DR   AlphaFoldDB; B2KPN7; -.
DR   BMRB; B2KPN7; -.
DR   SMR; B2KPN7; -.
DR   ConoServer; 2783; conomarphin-Mr1 precursor.
DR   EvolutionaryTrace; B2KPN7; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR004214; Conotoxin.
DR   Pfam; PF02950; Conotoxin; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cleavage on pair of basic residues; D-amino acid;
KW   Direct protein sequencing; Hydroxylation; Neurotoxin; Secreted; Signal;
KW   Toxin.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..54
FT                   /evidence="ECO:0000269|PubMed:18355315"
FT                   /id="PRO_0000366051"
FT   PEPTIDE         55..69
FT                   /note="Conomarphin"
FT                   /evidence="ECO:0000269|PubMed:18355315"
FT                   /id="PRO_5000346506"
FT   PROPEP          70..71
FT                   /evidence="ECO:0000269|PubMed:18355315"
FT                   /id="PRO_0000366052"
FT   REGION          27..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         64
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:18355315"
FT   MOD_RES         67
FT                   /note="D-phenylalanine"
FT                   /evidence="ECO:0000269|PubMed:18355315"
FT   STRAND          61..63
FT                   /evidence="ECO:0007829|PDB:2YYF"
FT   HELIX           66..68
FT                   /evidence="ECO:0007829|PDB:2JQB"
SQ   SEQUENCE   71 AA;  8325 MW;  190447838FFA04C3 CRC64;
     MMSKLGVLLC IFLVLFPMAT LQLDGDQTAD RHADQRGQDL TEQQRNSKRV LKKRDWEYHA
     HPKPNSFWTL V