ID   SCR1B_MONCP             Reviewed;          81 AA.
AC   C0H694;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 17.
DE   RecName: Full=Small cysteine-rich protein 1 2 {ECO:0000305|PubMed:19283069};
DE            Short=Mcap-SCRiP1b {ECO:0000303|PubMed:19283069};
DE            Short=SCRiP1b {ECO:0000303|PubMed:19283069};
DE   Flags: Precursor;
OS   Montipora capitata (Rice coral).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Scleractinia;
OC   Astrocoeniina; Acroporidae; Montipora.
OX   NCBI_TaxID=46704;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=19283069; DOI=10.1371/journal.pone.0004865;
RA   Sunagawa S., DeSalvo M.K., Voolstra C.R., Reyes-Bermudez A., Medina M.;
RT   "Identification and gene expression analysis of a taxonomically restricted
RT   cysteine-rich protein family in reef-building corals.";
RL   PLoS ONE 4:E4865-E4865(2009).
CC   -!- FUNCTION: Induces neurotoxic symptoms on zebrafish (By similarity). Has
CC       also been claimed to be implied in calcification, but tests on homolog
CC       proteins suggest that proteins of this family have a neurotoxic
CC       function and not a calcification function (PubMed:19283069).
CC       {ECO:0000250|UniProtKB:C0H691, ECO:0000250|UniProtKB:C0H692,
CC       ECO:0000305|PubMed:19283069}.
CC   -!- SUBCELLULAR LOCATION: Secreted. Nematocyst {ECO:0000305}.
CC   -!- PTM: The basic myotoxic domain of rattlesnake crotamine toxins (with 6
CC       Cys residues) has been detected in this protein. However, this protein
CC       contains 2 additional Cys at the C-terminal region. Hence, this protein
CC       may contain 4 disulfide bonds instead of the 3 suggested by the
CC       myotoxin domain. {ECO:0000305}.
CC   -!- MISCELLANEOUS: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ third party annotation (TPA) entry.
CC   -!- SIMILARITY: Belongs to the Cnidaria small cysteine-rich protein (SCRiP)
CC       family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BK006538; DAA06486.1; -; mRNA.
DR   AlphaFoldDB; C0H694; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042151; C:nematocyst; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   PROSITE; PS51345; MYOTOXINS_2; 1.
PE   3: Inferred from homology;
KW   Cleavage on pair of basic residues; Disulfide bond; Nematocyst; Neurotoxin;
KW   Secreted; Signal; Toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..39
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000434279"
FT   CHAIN           42..81
FT                   /note="Small cysteine-rich protein 1 2"
FT                   /id="PRO_0000434280"
SQ   SEQUENCE   81 AA;  8892 MW;  FE8AD47506158E98 CRC64;
     MGVNFNICLL LLLVATISSQ PLKATEKDDS TDENPFGIYR RGSQCAVYGG RCIPTSVRCP
     PNTFQCDLSG CSWSERCCCH L