ID MOUB_ORNMO Reviewed; 171 AA. AC Q04669; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1994, sequence version 1. DT 14-DEC-2022, entry version 54. DE RecName: Full=Moubatin {ECO:0000303|PubMed:8449906, ECO:0000303|PubMed:8449907}; DE AltName: Full=Lipocalin {ECO:0000303|PubMed:18694828}; DE AltName: Full=Platelet aggregation inhibitor {ECO:0000303|PubMed:8449907}; DE Short=PAI {ECO:0000305}; DE Flags: Precursor; OS Ornithodoros moubata (Soft tick) (Argasid tick). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari; OC Parasitiformes; Ixodida; Ixodoidea; Argasidae; Ornithodorinae; OC Ornithodoros. OX NCBI_TaxID=6938; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, AND RP RECOMBINANT EXPRESSION. RX PubMed=8449907; DOI=10.1016/s0021-9258(18)53342-1; RA Keller P.M., Waxman L., Arnold B.A., Schultz L.D., Condra C., RA Connolly T.M.; RT "Cloning of the cDNA and expression of moubatin, an inhibitor of platelet RT aggregation."; RL J. Biol. Chem. 268:5450-5456(1993). RN [2] RP FUNCTION. RX PubMed=8449906; DOI=10.1016/s0021-9258(18)53341-x; RA Waxman L., Connolly T.M.; RT "Isolation of an inhibitor selective for collagen-stimulated platelet RT aggregation from the soft tick Ornithodoros moubata."; RL J. Biol. Chem. 268:5445-5449(1993). RN [3] RP FUNCTION, AND RECOMBINANT EXPRESSION. RX PubMed=18694828; DOI=10.1016/j.ibmb.2008.06.007; RA Mans B.J., Ribeiro J.M.; RT "Function, mechanism and evolution of the moubatin-clade of soft tick RT lipocalins."; RL Insect Biochem. Mol. Biol. 38:841-852(2008). CC -!- FUNCTION: Tick salivary platelet aggregation inhibitor that plays an CC important part in the anti-hemostatic strategy of ticks. Acts by CC scavenging thromboxane A2 (TXA2), a potent inducer of platelet CC aggregation and blood vessel constriction (PubMed:8449906, CC PubMed:18694828). As a consequence, is a specific inhibitor of CC collagen-induced platelet aggregation (PubMed:8449907, PubMed:8449906). CC In addition, it also acts as a potent inhibitor of TXA2-mediated CC vasoconstriction (PubMed:18694828). Has also been found to bind CC leukotriene B4 (LTB4) (which also derives from arachidonic acid, as CC TXA2) with affinities in the nanomolar range (PubMed:18694828). It does CC not interact with complement protein C5 (PubMed:18694828). CC {ECO:0000269|PubMed:18694828, ECO:0000269|PubMed:8449906, CC ECO:0000269|PubMed:8449907}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:18694828}. CC -!- TISSUE SPECIFICITY: Expressed in salivary glands. CC {ECO:0000305|PubMed:18694828}. CC -!- PTM: The N-terminus is blocked. {ECO:0000305|PubMed:8449906}. CC -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family. CC {ECO:0000305}. CC -!- CAUTION: There are 10 AA differences between the cDNA deduced sequence CC and the determined protein sequence. These differences are not CC indicated in the paper. {ECO:0000305|PubMed:8449907}. 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; L04129; AAA29432.1; -; mRNA. DR PIR; A46618; A46618. DR AlphaFoldDB; Q04669; -. DR SMR; Q04669; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW. DR Gene3D; 2.40.128.20; -; 1. DR InterPro; IPR012674; Calycin. PE 1: Evidence at protein level; KW Direct protein sequencing; Disulfide bond; Hemostasis impairing toxin; KW Platelet aggregation inhibiting toxin; Secreted; Signal; Toxin. FT SIGNAL 1..15 FT /evidence="ECO:0000255" FT CHAIN 16..171 FT /note="Moubatin" FT /evidence="ECO:0000305|PubMed:8449907" FT /id="PRO_0000021732" FT DISULFID 23..144 FT /evidence="ECO:0000250|UniProtKB:Q5YD59" FT DISULFID 55..166 FT /evidence="ECO:0000250|UniProtKB:Q5YD59" FT DISULFID 118..145 FT /evidence="ECO:0000250|UniProtKB:Q5YD59" FT CONFLICT 54 FT /note="D -> DE (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" SQ SEQUENCE 171 AA; 18824 MW; 79EC7B7E460FA74B CRC64; MMLVLTTLIF SFSASIAYAQ SGCSVSDPLD ALKAFKDGAG TFLLQKSTDP QARDCLKGTP NGNRDGNTLP VTMTYKDDSK WVSLNWMFTL EGANIVATLE GKRKQRGELV YDVQSHDCHI TKLSSGVYQQ WQSNGSADDK DIKCCDEKFK ELTSGIDYTK PQEKGCETSA K //