KUNPM_ORNKA
ID KUNPM_ORNKA Reviewed; 82 AA.
AC Q8MVZ2;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Savignygrin (-) {ECO:0000303|PubMed:11932256, ECO:0000303|PubMed:12593588};
DE AltName: Full=Platelet aggregation inhibitor {ECO:0000303|PubMed:11932256};
DE Short=PAI {ECO:0000303|PubMed:11932256};
DE Flags: Precursor;
OS Ornithodoros kalahariensis (Tick).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Ixodida; Ixodoidea; Argasidae; Ornithodoros.
OX NCBI_TaxID=1580572;
RN [1] {ECO:0000312|EMBL:AAM54048.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 22-42, FUNCTION, MASS
RP SPECTROMETRY, AND 3D-STRUCTURE MODELING.
RC TISSUE=Salivary gland;
RX PubMed=11932256; DOI=10.1074/jbc.m112060200;
RA Mans B.J., Louw A.I., Neitz A.W.;
RT "Savignygrin, a platelet aggregation inhibitor from the soft tick
RT Ornithodoros savignyi, presents the RGD integrin recognition motif on the
RT Kunitz-BPTI fold.";
RL J. Biol. Chem. 277:21371-21378(2002).
RN [2]
RP FUNCTION.
RX PubMed=12593588; DOI=10.1023/a:1021613001297;
RA Mans B.J., Louw A.I., Neitz A.W.;
RT "Disaggregation of aggregated platelets by savignygrin, a alphaIIbeta3
RT antagonist from Ornithodoros savignyi.";
RL Exp. Appl. Acarol. 27:231-239(2002).
RN [3]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC TISSUE=Salivary gland;
RX PubMed=15285144; DOI=10.1023/b:appa.0000030012.47964.b3;
RA Mans B.J., Venter J.D., Coons L.B., Louw A.I., Neitz A.W.;
RT "A reassessment of argasid tick salivary gland ultrastructure from an
RT immuno-cytochemical perspective.";
RL Exp. Appl. Acarol. 33:119-129(2004).
RN [4]
RP FUNCTION, AND 3D-STRUCTURE MODELING IN COMPLEX WITH INTEGRIN ITGA2B/ITGB3.
RC TISSUE=Salivary gland;
RX PubMed=15147758; DOI=10.1016/j.ibmb.2004.03.005;
RA Mans B.J., Neitz A.W.;
RT "The mechanism of alphaIIbbeta3 antagonism by savignygrin and its
RT implications for the evolution of anti-hemostatic strategies in soft
RT ticks.";
RL Insect Biochem. Mol. Biol. 34:573-584(2004).
CC -!- FUNCTION: Tick salivary platelet aggregation inhibitor that plays an
CC important part in the anti-hemostatic strategy of ticks
CC (PubMed:11932256). Inhibits platelet aggregation induced by ADP
CC (IC(50)=130 nM), collagen, the thrombin receptor-activating peptide,
CC and epinephrine, although platelets are activated and their shape
CC changed (PubMed:11932256). Binding to platelets is similar for resting
CC and activated platelets (Kd=50-70 nM) (PubMed:15147758). Acts by
CC specifically binding to platelet membrane glycoprotein IIb-IIIa
CC (ITGA2B/ITGB3) in a divalent metal ion dependent manner (Probable)
CC (PubMed:15147758). In contrast to many disintegrins which only
CC interacts with the beta-3 subunit, this protein interacts with the two
CC subunits (alpha-IIb and beta-3) (Probable). Also causes disaggregation
CC of aggregated platelets without influencing the activated spherical
CC shape associated with aggregated platelets and causes a decrease in the
CC number of pseudopodia on the activated platelet surface
CC (PubMed:12593588). Does not show any inhibitory activity for the
CC different serine proteases tested (PubMed:11932256).
CC {ECO:0000269|PubMed:11932256, ECO:0000269|PubMed:12593588,
CC ECO:0000269|PubMed:15147758, ECO:0000305|PubMed:11932256,
CC ECO:0000305|PubMed:12593588, ECO:0000305|PubMed:15147758}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle
CC {ECO:0000269|PubMed:15285144}. Secreted {ECO:0000305|PubMed:11932256,
CC ECO:0000305|PubMed:15285144}. Note=Before secretion, is localized to
CC dense core granule type 'a' and to granule type 'b', but not to
CC granules 'c' or 'd'. {ECO:0000269|PubMed:15285144}.
CC -!- TISSUE SPECIFICITY: Expressed in salivary glands.
CC {ECO:0000269|PubMed:15285144}.
CC -!- MASS SPECTROMETRY: Mass=6808.84; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:11932256};
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DR EMBL; AF452886; AAM54048.1; -; mRNA.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR Gene3D; 4.10.410.10; -; 1.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR SUPFAM; SSF57362; SSF57362; 1.
PE 1: Evidence at protein level;
KW Cell adhesion impairing toxin; Cytoplasmic vesicle;
KW Direct protein sequencing; Disulfide bond; Hemostasis impairing toxin;
KW Platelet aggregation inhibiting toxin; Secreted; Signal; Toxin.
FT SIGNAL 1..21
FT /evidence="ECO:0000305|PubMed:11932256"
FT CHAIN 22..82
FT /note="Savignygrin (-)"
FT /evidence="ECO:0000305|PubMed:11932256"
FT /id="PRO_5004314105"
FT MOTIF 35..37
FT /note="Cell attachment site"
FT /evidence="ECO:0000269|PubMed:11932256"
FT DISULFID 26..79
FT /evidence="ECO:0000305|PubMed:11932256"
FT DISULFID 34..59
FT /evidence="ECO:0000305|PubMed:11932256"
FT DISULFID 53..75
FT /evidence="ECO:0000305|PubMed:11932256"
SQ SEQUENCE 82 AA; 9043 MW; 063DE4767C73344D CRC64;
MQANIFVFAF LLLSVAVAAY GYQPECLEPS LYGCRGDEDA TFGWTFDRED GGCRQGSYCT
RFGQPKNYFR SEGDCKKACG GA