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CM3L_CONRE
ID   CM3L_CONRE              Reviewed;          19 AA.
AC   P0DQO8;
DT   10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2021, sequence version 1.
DT   25-MAY-2022, entry version 3.
DE   RecName: Full=Conotoxin reg3l {ECO:0000303|PubMed:29283511};
OS   Conus regius (Crown cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Stephanoconus.
OX   NCBI_TaxID=101314;
RN   [1]
RP   PROTEIN SEQUENCE, MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=29283511; DOI=10.1111/febs.14372;
RA   Franco A., Dovell S., Moller C., Grandal M., Clark E., Mari F.;
RT   "Structural plasticity of Mini-M conotoxins: expression of all mini-M
RT   subtypes by Conus regius.";
RL   FEBS J. 285:887-902(2017).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29283511}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:29283511}.
CC   -!- DOMAIN: The cysteine framework is III (CC-C-C-CC). Classified in the M-
CC       1 branch, since 1 residue stands between the fourth and the fifth
CC       cysteine residues. {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=1981.6; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:29283511};
CC   -!- MISCELLANEOUS: The precursor sequence of reg3l described in Franco et
CC       al., 2017 corresponds to the precursor of conotoxin reg12l (AC
CC       A0A2I6EDL5). {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the conotoxin M superfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0DQO8; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Cleavage on pair of basic residues; Direct protein sequencing;
KW   Disulfide bond; Secreted; Toxin.
FT   PEPTIDE         1..19
FT                   /note="Conotoxin reg3l"
FT                   /evidence="ECO:0000269|PubMed:29283511"
FT                   /id="PRO_0000452027"
FT   DISULFID        2..16
FT                   /evidence="ECO:0000250|UniProtKB:Q5EHP3"
FT   DISULFID        3..14
FT                   /evidence="ECO:0000250|UniProtKB:Q5EHP3"
FT   DISULFID        8..17
FT                   /evidence="ECO:0000250|UniProtKB:Q5EHP3"
SQ   SEQUENCE   19 AA;  1988 MW;  4AD9747F9FB0F6AB CRC64;
     RCCPMPGCFA GPFCPCCPV
 
 
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