ID A0A132AI26_SARSC Unreviewed; 882 AA.
AC A0A132AI26;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU361183};
GN ORFNames=QR98_0092040 {ECO:0000313|EMBL:KPM10644.1};
OS Sarcoptes scabiei (Itch mite) (Acarus scabiei).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Sarcoptiformes; Astigmata; Psoroptidia; Sarcoptoidea;
OC Sarcoptidae; Sarcoptinae; Sarcoptes.
OX NCBI_TaxID=52283 {ECO:0000313|EMBL:KPM10644.1, ECO:0000313|Proteomes:UP000616769};
RN [1] {ECO:0000313|EMBL:KPM10644.1, ECO:0000313|Proteomes:UP000616769}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Arlian Lab {ECO:0000313|EMBL:KPM10644.1};
RX PubMed=26555130; DOI=10.1186/s13071-015-1198-2;
RA Rider S.D.Jr., Morgan M.S., Arlian L.G.;
RT "Draft genome of the scabies mite.";
RL Parasit. Vectors 8:585-585(2015).
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PROSITE-ProRule:PRU01211,
CC ECO:0000256|RuleBase:RU361183};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PROSITE-
CC ProRule:PRU01211, ECO:0000256|RuleBase:RU361183};
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:PRU00076}.
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:KPM10644.1}.
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DR EMBL; JXLN01015550; KPM10644.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A132AI26; -.
DR VEuPathDB; VectorBase:SSCA004402; -.
DR OMA; RTVQTIN; -.
DR OrthoDB; 3107710at2759; -.
DR Proteomes; UP000616769; Unassembled WGS sequence.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00041; CUB; 5.
DR CDD; cd00054; EGF_CA; 2.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 5.
DR InterPro; IPR015446; BMP_1/tolloid-like.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001506; Peptidase_M12A.
DR InterPro; IPR006026; Peptidase_Metallo.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR PANTHER; PTHR24255; COMPLEMENT COMPONENT 1, S SUBCOMPONENT-RELATED; 1.
DR PANTHER; PTHR24255:SF34; CUB AND SUSHI DOMAIN-CONTAINING PROTEIN 3 ISOFORM X1; 1.
DR Pfam; PF01400; Astacin; 1.
DR Pfam; PF00431; CUB; 5.
DR Pfam; PF14670; FXa_inhibition; 2.
DR PIRSF; PIRSF001199; BMP_1/tolloid-like; 1.
DR PRINTS; PR00480; ASTACIN.
DR SMART; SM00042; CUB; 5.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 5.
DR PROSITE; PS51864; ASTACIN; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 2.
DR PROSITE; PS01180; CUB; 5.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01187; EGF_CA; 2.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU01211};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001199-2, ECO:0000256|PROSITE-
KW ProRule:PRU01211};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049, ECO:0000256|PROSITE-
KW ProRule:PRU01211};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR001199-2}.
FT ACT_SITE 61
FT /evidence="ECO:0000256|PIRSR:PIRSR001199-1,
FT ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001199-2,
FT ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001199-2,
FT ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001199-2,
FT ECO:0000256|PROSITE-ProRule:PRU01211"
FT DISULFID 30..52
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT DISULFID 32..33
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
SQ SEQUENCE 882 AA; 100466 MW; F42941A82DF1F3B5 CRC64;
MKHWENYTCV KFVERTIEHP NYIIFTERPC GCCSYVGKRG NGPQAISIGK NCDKFGIVVH
ELGHVVGFWH EHTRPDRDEN VQIVTENIMP GIEYNFNKLT EDEVNSLGIK YDFDSIMHYS
RNTFSKSISL DTILPKDDPA NTVRPEIGQR LRLSQGDIAQ TKLLYRCPKC GHTIQNTNGM
ISSPNYPQSS PPAEGEYCEW RITGTHGERI IINITDIDIY ETNNCENGYL EIRDGYWFKS
PLIGKYCGQG EIQTAMMSKG HRLLISYMAT PNQHNHRGFN MTYEVICGGD IVAEQGYLQS
PNYPEEYRSN KECVWRITVP EGFQVALKFQ SFEIENHDNC AYDYLEIRDG KSEDSTILGK
FCGNKIPNEI RGSSNYLFVK FISDSSVNKA GFSATFIKEI NECLGSNHGC EQECINTFGG
YHCECRIGYE LHSDRKKCEN ACGGIIESSN GTISSPSFPD LYPPNKNCIW EIVAEEGFRI
LLNFTFFDLE GNNQDCEYDK LDVKSKVNNH YSTHGLFCGS RLPPIITSQG HNIRLEFSSD
NSVQRGGFNL HYFTDRDECA INNGGCQHIC RNTIGSYVCE CNSGYVLHEN KHTCKEGSCS
YQITSSNAEI ISPQYPDGYP SKKDCTWFFL ATLGHRVKLV FEDFDLEPQQ ECSYDYVIIY
DGITTNKSVL GRFCGSKSPH PIISTTNKVL MKFKTDASVQ KKGFKAHYYT VCGGRLFAKN
SIEHLYSHFK FGDANYEKKE DCDWHIVTNI GMKIYLKFIT FELEHEANCS YDFVEIFDGD
DDNSPSLGKF CGNQMPTDMI SSSESILIRF RTDDSIHNKG FTLIYSAVET IENELINAID
SNKSIEKSIR KTQQSFLNEK NNNYLSKYLS INEDQQDDFL LP
//
