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3SA1_NAJOX
ID   3SA1_NAJOX              Reviewed;          60 AA.
AC   P01451;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=Cytotoxin 1;
DE   AltName: Full=Cytotoxin I;
DE            Short=CTI;
OS   Naja oxiana (Central Asian cobra) (Oxus cobra).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
OX   NCBI_TaxID=8657;
RN   [1]
RP   PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RA   Grishin E.V., Sukhikh A.P., Adamovich T.B., Ovchinnikov Y.A.;
RT   "Isolation, properties and sequence determination of the two cytotoxins
RT   from the venom of the Middle-Asian cobra Naja Naja oxiana.";
RL   Bioorg. Khim. 2:1018-1034(1976).
RN   [2]
RP   STRUCTURE BY NMR, AND DISULFIDE BONDS.
RX   PubMed=15584897; DOI=10.1042/bj20041814;
RA   Dubovskii P.V., Lesovoy D.M., Dubinnyi M.A., Konshina A.G., Utkin Y.N.,
RA   Efremov R.G., Arseniev A.S.;
RT   "Interaction of three-finger toxins with phospholipid membranes: comparison
RT   of S- and P-type cytotoxins.";
RL   Biochem. J. 387:807-815(2005).
CC   -!- FUNCTION: This three-finger cytotoxin is a basic protein that interacts
CC       and penetrates into the cell membrane, with the tips of all the three
CC       loops. Cytotoxins which have a 'Pro-30' (P-type) interacts with
CC       membrane stronger that those which have a Ser-28 (S-type). CTI
CC       interacts with membrane weaker than CTII.
CC   -!- SUBUNIT: Monomer in solution; Homodimer and oligomer in the presence of
CC       negatively charged lipids forming a pore with a size ranging between 20
CC       and 30 Angstroms. {ECO:0000250|UniProtKB:P60301}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.1}. Target cell
CC       membrane {ECO:0000250|UniProtKB:P60301}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC   -!- MISCELLANEOUS: Is classified as a S-type cytotoxin, since a serine
CC       residue stands at position 27 (Ser-29 in standard classification).
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the snake three-finger toxin family. Short-chain
CC       subfamily. Type IA cytotoxin sub-subfamily. {ECO:0000305}.
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DR   PIR; A01716; H3NJ1R.
DR   PDB; 1RL5; NMR; -; A=1-60.
DR   PDB; 1ZAD; NMR; -; A=1-60.
DR   PDB; 5NPN; NMR; -; A=1-60.
DR   PDB; 5NQ4; NMR; -; A=1-60.
DR   PDB; 5T8A; NMR; -; A=1-60.
DR   PDBsum; 1RL5; -.
DR   PDBsum; 1ZAD; -.
DR   PDBsum; 5NPN; -.
DR   PDBsum; 5NQ4; -.
DR   PDBsum; 5T8A; -.
DR   AlphaFoldDB; P01451; -.
DR   BMRB; P01451; -.
DR   SMR; P01451; -.
DR   EvolutionaryTrace; P01451; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   CDD; cd00206; snake_toxin; 1.
DR   Gene3D; 2.10.60.10; -; 1.
DR   InterPro; IPR003572; Cytotoxin_Cobra.
DR   InterPro; IPR003571; Snake_3FTx.
DR   InterPro; IPR045860; Snake_toxin-like_sf.
DR   InterPro; IPR018354; Snake_toxin_con_site.
DR   PRINTS; PR00282; CYTOTOXIN.
DR   SUPFAM; SSF57302; SSF57302; 1.
DR   PROSITE; PS00272; SNAKE_TOXIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cardiotoxin; Cytolysis; Direct protein sequencing;
KW   Disulfide bond; Membrane; Secreted; Target cell membrane; Target membrane;
KW   Toxin.
FT   CHAIN           1..60
FT                   /note="Cytotoxin 1"
FT                   /evidence="ECO:0000269|Ref.1"
FT                   /id="PRO_0000093516"
FT   DISULFID        3..21
FT                   /evidence="ECO:0000269|PubMed:15584897,
FT                   ECO:0000312|PDB:1RL5, ECO:0000312|PDB:1ZAD,
FT                   ECO:0000312|PDB:5NPN, ECO:0000312|PDB:5NQ4,
FT                   ECO:0000312|PDB:5T8A"
FT   DISULFID        14..38
FT                   /evidence="ECO:0000269|PubMed:15584897,
FT                   ECO:0000312|PDB:1RL5, ECO:0000312|PDB:1ZAD,
FT                   ECO:0000312|PDB:5NPN, ECO:0000312|PDB:5NQ4,
FT                   ECO:0000312|PDB:5T8A"
FT   DISULFID        42..53
FT                   /evidence="ECO:0000269|PubMed:15584897,
FT                   ECO:0000312|PDB:1RL5, ECO:0000312|PDB:1ZAD,
FT                   ECO:0000312|PDB:5NPN, ECO:0000312|PDB:5NQ4,
FT                   ECO:0000312|PDB:5T8A"
FT   DISULFID        54..59
FT                   /evidence="ECO:0000269|PubMed:15584897,
FT                   ECO:0000312|PDB:1RL5, ECO:0000312|PDB:1ZAD,
FT                   ECO:0000312|PDB:5NPN, ECO:0000312|PDB:5NQ4,
FT                   ECO:0000312|PDB:5T8A"
FT   STRAND          2..4
FT                   /evidence="ECO:0007829|PDB:1RL5"
FT   STRAND          11..13
FT                   /evidence="ECO:0007829|PDB:1RL5"
FT   STRAND          20..29
FT                   /evidence="ECO:0007829|PDB:1RL5"
FT   STRAND          34..41
FT                   /evidence="ECO:0007829|PDB:1RL5"
FT   STRAND          47..54
FT                   /evidence="ECO:0007829|PDB:1RL5"
SQ   SEQUENCE   60 AA;  6821 MW;  C0E8AE8AC6A86F11 CRC64;
     LKCNKLVPIA YKTCPEGKNL CYKMFMMSDL TIPVKRGCID VCPKNSLLVK YVCCNTDRCN
 
 
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