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O164_CONCL
ID   O164_CONCL              Reviewed;          64 AA.
AC   D5KR58;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 1.
DT   23-FEB-2022, entry version 21.
DE   RecName: Full=Conotoxin cal6.4a {ECO:0000303|PubMed:21172372};
DE   AltName: Full=Conotoxin cal6.4c {ECO:0000303|PubMed:21172372};
DE   Flags: Precursor;
OS   Californiconus californicus (California cone) (Conus californicus).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Californiconus.
OX   NCBI_TaxID=1736779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 42-64, HYDROXYLATION AT
RP   PRO-49, BROMINATION AT TRP-44, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom, and Venom duct;
RX   PubMed=21172372; DOI=10.1016/j.toxicon.2010.12.008;
RA   Elliger C.A., Richmond T.A., Lebaric Z.N., Pierce N.T., Sweedler J.V.,
RA   Gilly W.F.;
RT   "Diversity of conotoxin types from Conus californicus reflects a diversity
RT   of prey types and a novel evolutionary history.";
RL   Toxicon 57:311-322(2011).
CC   -!- FUNCTION: Probable neurotoxin with unknown target. Possibly targets ion
CC       channels. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21172372}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC       {ECO:0000305|PubMed:21172372}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin. {ECO:0000250}.
CC   -!- DOMAIN: The cysteine framework is VI/VII (C-C-CC-C-C).
CC   -!- PTM: Five different peptides have been sequenced after total venom
CC       examination by HPLC-MS. cal6.4a-4c are identical in length but are
CC       differentially hydroxylated and brominated.
CC       {ECO:0000269|PubMed:21172372}.
CC   -!- SIMILARITY: Belongs to the conotoxin O1 superfamily. {ECO:0000305}.
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DR   EMBL; GU591494; ADD97802.1; -; mRNA.
DR   ConoServer; 4057; Cal6.4 precursor.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0099106; F:ion channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Bromination; Direct protein sequencing; Disulfide bond; Hydroxylation;
KW   Ion channel impairing toxin; Knottin; Neurotoxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..64
FT                   /evidence="ECO:0000305|PubMed:21172372"
FT                   /id="PRO_5000585094"
FT   PEPTIDE         42..64
FT                   /note="Conotoxin cal6.4a"
FT                   /evidence="ECO:0000269|PubMed:21172372"
FT                   /id="PRO_5000585095"
FT   MOD_RES         44
FT                   /note="6'-bromotryptophan; in form cal6.4c"
FT                   /evidence="ECO:0000269|PubMed:21172372"
FT   MOD_RES         49
FT                   /note="4-hydroxyproline; in form cal6.4b, and form cal6.4c"
FT                   /evidence="ECO:0000269|PubMed:21172372"
FT   DISULFID        43..53
FT                   /evidence="ECO:0000250"
FT   DISULFID        46..58
FT                   /evidence="ECO:0000250"
FT   DISULFID        52..62
FT                   /evidence="ECO:0000250"
FT   VARIANT         64
FT                   /note="R -> S (in cal6.4b and cal6.4c)"
SQ   SEQUENCE   64 AA;  7111 MW;  DC8024A2345840E4 CRC64;
     MKLTCVLIVA VLILTACQFT AADDMEYPKW LRGLSTDXSE RGCWLCLGPN ACCRGSVCHD
     YCPR
 
 
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