ID A0A1B0GNY2_PHLPP Unreviewed; 707 AA.
AC A0A1B0GNY2;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=ADAM10 endopeptidase {ECO:0000256|ARBA:ARBA00012332};
DE EC=3.4.24.81 {ECO:0000256|ARBA:ARBA00012332};
OS Phlebotomus papatasi (Sandfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Psychodoidea; Psychodidae;
OC Phlebotomus; Phlebotomus.
OX NCBI_TaxID=29031 {ECO:0000313|EnsemblMetazoa:PPAI006275-PA, ECO:0000313|Proteomes:UP000092462};
RN [1] {ECO:0000313|Proteomes:UP000092462}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Israel {ECO:0000313|Proteomes:UP000092462};
RA Fulton L., Warren W., Minx P., Wilson R., Clifton S., Abrudan J.,
RA Ramalho-Ortigao M., Lawyer P., Kamhawi S., Rowton E., Lehane M., Bates P.,
RA Valenzeula J., Dillon R., Lobo N., Collins F., McDowell M.A.;
RT "Phlebotomus papatasi, whole genome shotgun sequencing project.";
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:PPAI006275-PA}
RP IDENTIFICATION.
RC STRAIN=Israel {ECO:0000313|EnsemblMetazoa:PPAI006275-PA};
RG EnsemblMetazoa;
RL Submitted (AUG-2022) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endopeptidase of broad specificity.; EC=3.4.24.81;
CC Evidence={ECO:0000256|ARBA:ARBA00001809};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
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DR EMBL; AJVK01005589; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJVK01005590; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A1B0GNY2; -.
DR EnsemblMetazoa; PPAI006275-RA; PPAI006275-PA; PPAI006275.
DR VEuPathDB; VectorBase:PPAI006275; -.
DR OrthoDB; 5395001at2759; -.
DR Proteomes; UP000092462; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 4.10.70.10; Disintegrin domain; 1.
DR InterPro; IPR049038; ADAM10_Cys-rich.
DR InterPro; IPR001762; Disintegrin_dom.
DR InterPro; IPR036436; Disintegrin_dom_sf.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR PANTHER; PTHR45702; ADAM10/ADAM17 METALLOPEPTIDASE FAMILY MEMBER; 1.
DR PANTHER; PTHR45702:SF2; KUZBANIAN, ISOFORM A; 1.
DR Pfam; PF21299; ADAM10_Cys-rich; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF13574; Reprolysin_2; 1.
DR SMART; SM00050; DISIN; 1.
DR SUPFAM; SSF57552; Blood coagulation inhibitor (disintegrin); 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50214; DISINTEGRIN_2; 1.
PE 4: Predicted;
KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022989};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT ACT_SITE 444
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 443
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 447
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 453
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ SEQUENCE 707 AA; 79586 MW; 2C26BEB9BA8B18CE CRC64;
MNFIDIFFLF YLFFFAGRRL NEYISHYETL SYDTKHVHAS HNRAKRSVTK DPYVYLRFDA
HGENFHIRLK RDVTTFSDNL VIDGSDGPVA VDTSHIYQGE LLNVPKSHVF GSVIDGIFEG
RILTGRESYY VENAKHYFPN STHRDESGFH SVIYKESHVS DPYDDIRQGH GGGCGITDEI
SSWMDSIQNA AVDDETPAVP SAKIPAVEKP RESAQEEDSY WPPHRKYSKE ANWRAESNVE
DEKSHHEEAH ERVRRATRPR EENRNTCSLY IQTDPLIWRH IREGIADRAV NPKIKHDRSR
RQEIDEKTRE EILSLIAHHV TAVNYIYRNT KFDGRVEHRN IRFEVQRIKI DDDSACSESY
NGESNPFCME NIDVDFTGGT LGLAWVASAS GASGGICEKY KTYTETVGGL YQSTKRSLNT
GIITFVNYNS RVPPKVSQLT LAHEIGHNFG SPHDYPQECR PGGLHGNYIM FASATSGDRP
NNSKFSTCSI RNISNVLDAI EDTKKRNCFL ASEGAFCGNK IVESGEECDC GFNDEECQDR
CCYPRQIGER DLSLNATARG CTRRARTQCS PSQGPCCQSE TCSFMPAHLG VKCKEETECS
WSSMCNGTTP ECPEPKPRDD KTKCNNGTQL CIAGECSGSI CLLWNMTECF LTSSIIPNID
KRKLCELACQ NGNDTGTCRS TSEFAQLFGL PDGGINLRPG SPCDNFQ
//
