KUNP2_ARGMO
ID KUNP2_ARGMO Reviewed; 107 AA.
AC Q09JW3;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 27.
DE RecName: Full=Monogrin 2 {ECO:0000303|PubMed:18070663};
DE Short=MG2 {ECO:0000303|PubMed:18070663};
DE AltName: Full=Monogrin 1B {ECO:0000312|EMBL:ABI52650.1};
DE AltName: Full=Platelet aggregation inhibitor {ECO:0000303|PubMed:18070663};
DE Short=PAI {ECO:0000305};
DE Flags: Precursor;
GN ORFNames=AM-30B {ECO:0000303|PubMed:18070663, ECO:0000303|PubMed:18070664};
OS Argas monolakensis (Mono lake bird tick).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Ixodida; Ixodoidea; Argasidae; Argas.
OX NCBI_TaxID=34602;
RN [1] {ECO:0000312|EMBL:ABI52650.1}
RP NUCLEOTIDE SEQUENCE [MRNA], MASS SPECTROMETRY, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Salivary gland;
RX PubMed=18070663; DOI=10.1016/j.ibmb.2007.09.002;
RA Mans B.J., Andersen J.F., Schwan T.G., Ribeiro J.M.;
RT "Characterization of anti-hemostatic factors in the argasid, Argas
RT monolakensis: implications for the evolution of blood-feeding in the soft
RT tick family.";
RL Insect Biochem. Mol. Biol. 38:22-41(2008).
RN [2] {ECO:0000312|EMBL:ABI52650.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Salivary gland;
RX PubMed=18070664; DOI=10.1016/j.ibmb.2007.09.003;
RA Mans B.J., Andersen J.F., Francischetti I.M., Valenzuela J.G., Schwan T.G.,
RA Pham V.M., Garfield M.K., Hammer C.H., Ribeiro J.M.C.;
RT "Comparative sialomics between hard and soft ticks: implications for the
RT evolution of blood-feeding behavior.";
RL Insect Biochem. Mol. Biol. 38:42-58(2008).
CC -!- FUNCTION: Tick salivary platelet aggregation inhibitor that plays an
CC important part in the anti-hemostatic strategy of ticks. Inhibits
CC platelet aggregation induced by ADP (IC(50)~150 nM), collagen, and
CC platelet activating factor (PAF) (PubMed:18070663). Acts by binding to
CC platelet membrane glycoprotein IIb-IIIa (ITGA2B/ITGB3) in a metal ion
CC dependent manner (PubMed:18070663). Does not inhibit aggregation
CC induced by ristocecin, an agonist that aggregates platelets
CC independently from the glycoprotein IIb-IIIa (ITGA2B/ITGB3). In
CC contrast to other tick platelet aggregation inhibitors, this protein
CC does not protect ITGA2B/ITGB3 from dissociation under SDS condition,
CC suggesting it may dissocate much faster than its orthologs
CC (PubMed:18070663). {ECO:0000269|PubMed:18070663}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle
CC {ECO:0000250|UniProtKB:Q8MVZ2}. Secreted {ECO:0000305|PubMed:18070663}.
CC -!- TISSUE SPECIFICITY: Expressed in salivary glands.
CC {ECO:0000305|PubMed:18070663, ECO:0000305|PubMed:18070664}.
CC -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:18070663}.
CC -!- MASS SPECTROMETRY: Mass=9940.0; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:18070663};
CC -!- MISCELLANEOUS: The monogrins comprise about 4% of the total salivary
CC gland protein. {ECO:0000269|PubMed:18070663}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ886733; ABI52650.1; -; 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 Cytoplasmic vesicle; Disulfide bond; Hemostasis impairing toxin;
KW Platelet aggregation inhibiting toxin; Protease inhibitor; Secreted;
KW Serine protease inhibitor; Signal; Toxin.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..107
FT /note="Monogrin 2"
FT /evidence="ECO:0000305|PubMed:18070663"
FT /id="PRO_5004167643"
FT DOMAIN 29..82
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT MOTIF 37..39
FT /note="Cell attachment site"
FT /evidence="ECO:0000305|PubMed:18070663"
FT DISULFID 28..82
FT /evidence="ECO:0000305|PubMed:18070663"
FT DISULFID 36..62
FT /evidence="ECO:0000305|PubMed:18070663"
FT DISULFID 55..78
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031,
FT ECO:0000305|PubMed:18070663"
SQ SEQUENCE 107 AA; 11970 MW; 46CA69E4EDA30267 CRC64;
MEGKVLLCFA LLLPFTVAQA AKGDTRRCGY LMMQRCRGDT TETKAWGFNY EEKKCQKETV
ICGTGGAPRN AFETKKDCDA LCKGYSGPQY SMQEMLQHIR DNAKKTG