ID   DIS_DABPA               Reviewed;          41 AA.
AC   P0C6E2;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 41.
DE   RecName: Full=Disintegrin viperistatin;
OS   Daboia palaestinae (Palestine viper) (Vipera palaestinae).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Daboia.
OX   NCBI_TaxID=1170828;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SYNTHESIS OF 19-29, MUTAGENESIS OF ARG-24, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=15556632; DOI=10.1016/j.febslet.2004.10.050;
RA   Kisiel D.G., Calvete J.J., Katzhendler J., Fertala A., Lazarovici P.,
RA   Marcinkiewicz C.;
RT   "Structural determinants of the selectivity of KTS-disintegrins for the
RT   alpha1beta1 integrin.";
RL   FEBS Lett. 577:478-482(2004).
RN   [2]
RP   FUNCTION.
RX   PubMed=19502781; DOI=10.4161/cbt.8.15.8999;
RA   Staniszewska I., Walsh E.M., Rothman V.L., Gaathon A., Tuszynski G.P.,
RA   Calvete J.J., Lazarovici P., Marcinkiewicz C.;
RT   "Effect of VP12 and viperistatin on inhibition of collagen-receptor-
RT   dependent melanoma metastasis.";
RL   Cancer Biol. Ther. 8:1507-1516(2009).
CC   -!- FUNCTION: Potent and highly selective inhibitor of alpha-1/beta-1
CC       (ITGA1/ITGB1) integrin binding to collagen I and IV. Is about 25-fold
CC       more potent than obtustatin inhibiting the binding of this integrin to
CC       collagen IV. {ECO:0000269|PubMed:15556632,
CC       ECO:0000269|PubMed:19502781}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MASS SPECTROMETRY: Mass=4454.5; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:15556632};
CC   -!- SIMILARITY: Belongs to the disintegrin family. Short disintegrin
CC       subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0C6E2; -.
DR   SMR; P0C6E2; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   Gene3D; 4.10.70.10; -; 1.
DR   InterPro; IPR001762; Disintegrin_dom.
DR   InterPro; IPR036436; Disintegrin_dom_sf.
DR   PRINTS; PR00289; DISINTEGRIN.
DR   SUPFAM; SSF57552; SSF57552; 1.
PE   1: Evidence at protein level;
KW   Cell adhesion impairing toxin; Direct protein sequencing; Disulfide bond;
KW   Secreted; Toxin.
FT   CHAIN           1..41
FT                   /note="Disintegrin viperistatin"
FT                   /id="PRO_0000321884"
FT   DOMAIN          1..41
FT                   /note="Disintegrin"
FT   MOTIF           21..23
FT                   /note="Cell attachment site; atypical (KTS)"
FT   DISULFID        1..10
FT                   /evidence="ECO:0000250"
FT   DISULFID        6..29
FT                   /evidence="ECO:0000250"
FT   DISULFID        7..34
FT                   /evidence="ECO:0000250"
FT   DISULFID        19..36
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         24
FT                   /note="R->L: Decrease in inhibitory activity towards alpha-
FT                   1/beta-1 integrin."
FT                   /evidence="ECO:0000269|PubMed:15556632"
SQ   SEQUENCE   41 AA;  4461 MW;  AC9720CBDE8DD536 CRC64;
     CTTGPCCRQC KLKPAGTTCW KTSRTSHYCT GKSCDCPVYQ G