ID A0A443S9G3_9ACAR Unreviewed; 196 AA.
AC A0A443S9G3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Astacin-like metallopeptidase 10 protein {ECO:0000313|EMBL:RWS24206.1};
GN ORFNames=B4U80_06976 {ECO:0000313|EMBL:RWS24206.1};
OS Leptotrombidium deliense.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Trombidiformes; Prostigmata; Anystina; Parasitengona;
OC Trombiculoidea; Trombiculidae; Leptotrombidium.
OX NCBI_TaxID=299467 {ECO:0000313|EMBL:RWS24206.1, ECO:0000313|Proteomes:UP000288716};
RN [1] {ECO:0000313|EMBL:RWS24206.1, ECO:0000313|Proteomes:UP000288716}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UoL-UT {ECO:0000313|EMBL:RWS24206.1};
RA Dong X., Chaisiri K., Xia D., Armstrong S.D., Fang Y., Donnelly M.J.,
RA Kadowaki T., McGarry J.W., Darby A.C., Makepeace B.L.;
RT "Genomes of trombidid mites reveal novel predicted allergens and laterally-
RT transferred genes associated with secondary metabolism.";
RL Gigascience 0:0-0(2018).
CC -!- FUNCTION: Zinc metalloprotease. Provoques deadhesion of endothelial
CC cells from cell cultures, and also degradation of fibronectin,
CC fibrinogen and gelatin in vitro. Its role in the venom is not fully
CC understood but it might act as a spreading factor that facilitates
CC diffusion of other venom toxins. Alternatively, it might be involved in
CC the proteolytic processing of other venom toxins or it might play a
CC role in extra-oral digestion of prey. {ECO:0000256|ARBA:ARBA00025529}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01211}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RWS24206.1}.
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DR EMBL; NCKV01005215; RWS24206.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A443S9G3; -.
DR STRING; 299467.A0A443S9G3; -.
DR EnsemblMetazoa; LDEU007837-RA; LDEU007837-PA; LDEU007837.
DR VEuPathDB; VectorBase:LDEU007837; -.
DR Proteomes; UP000288716; Unassembled WGS sequence.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 2.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001506; Peptidase_M12A.
DR InterPro; IPR006026; Peptidase_Metallo.
DR PANTHER; PTHR10127; DISCOIDIN, CUB, EGF, LAMININ , AND ZINC METALLOPROTEASE DOMAIN CONTAINING; 1.
DR PANTHER; PTHR10127:SF850; METALLOENDOPEPTIDASE; 1.
DR Pfam; PF01400; Astacin; 1.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS51864; ASTACIN; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Reference proteome {ECO:0000313|Proteomes:UP000288716};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..196
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019239367"
FT DOMAIN 57..144
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
SQ SEQUENCE 196 AA; 22190 MW; 943822E042443061 CRC64;
MYSRKVFILA VIPLVFVTVL SAPIEESSEN DDIYRSALEN PDLFGGDIVL PESNNKFGLR
SSYYRWPKNT IPYAISSDRM NLKQQIEKAM RHIEDKTCIR FVPHTTETDS IYIYNGPGCF
SYMGRQGGKQ ALSLGSGCEP FGTISIMLYD SKSFSKNGKN TMTAKDSRIS LNPVWMKKYL
SDSDILSINK MYNCDV
//
