ID T1L1V0_TETUR Unreviewed; 980 AA.
AC T1L1V0;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=ADAM10 endopeptidase {ECO:0000256|ARBA:ARBA00012332};
DE EC=3.4.24.81 {ECO:0000256|ARBA:ARBA00012332};
GN Name=107369529 {ECO:0000313|EnsemblMetazoa:tetur32g00930.1};
OS Tetranychus urticae (Two-spotted spider mite).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Trombidiformes; Prostigmata; Eleutherengona; Raphignathae;
OC Tetranychoidea; Tetranychidae; Tetranychus.
OX NCBI_TaxID=32264 {ECO:0000313|EnsemblMetazoa:tetur32g00930.1, ECO:0000313|Proteomes:UP000015104};
RN [1] {ECO:0000313|Proteomes:UP000015104}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=London {ECO:0000313|Proteomes:UP000015104};
RA Rombauts S.;
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:tetur32g00930.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) 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; CAEY01000921; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015792978.1; XM_015937492.1.
DR AlphaFoldDB; T1L1V0; -.
DR STRING; 32264.T1L1V0; -.
DR EnsemblMetazoa; tetur32g00930.1; tetur32g00930.1; tetur32g00930.
DR GeneID; 107369529; -.
DR KEGG; tut:107369529; -.
DR eggNOG; KOG3658; Eukaryota.
DR HOGENOM; CLU_004602_0_1_1; -.
DR OrthoDB; 5395001at2759; -.
DR Proteomes; UP000015104; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; IPR011489; EMI_domain.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR PANTHER; PTHR45702; ADAM10/ADAM17 METALLOPEPTIDASE FAMILY MEMBER; 1.
DR PANTHER; PTHR45702:SF3; KUZBANIAN-LIKE, ISOFORM A; 1.
DR Pfam; PF21299; ADAM10_Cys-rich; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF07546; EMI; 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.
DR PROSITE; PS51041; EMI; 1.
PE 4: Predicted;
KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Reference proteome {ECO:0000313|Proteomes:UP000015104};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..980
FT /note="ADAM10 endopeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004592036"
FT TRANSMEM 868..889
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 27..102
FT /note="EMI"
FT /evidence="ECO:0000259|PROSITE:PS51041"
FT DOMAIN 412..632
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 647..743
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT REGION 333..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 576
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 575
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 579
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 585
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ SEQUENCE 980 AA; 110258 MW; 9FCA67BE3B755881 CRC64;
MDYFKCFCTR QLLLLFVRNF LVVCLQGPHV CSKTKDINQP VNISSTIQID QQSYTWCLQF
PPICLQNRTS YQKVVKTKWE TKKITINVCC DGFKEIDDQC YPVESNEFIL PYEPVSYDRD
YLLEQRRSHR SKRSAPTNVI KDNLGSMDSF FNSIWSQSHS QSTENYILIN FTAYNRLFDL
KLTLDNTLFS PETLFESTRR GKFHYDTSNA LIGALSDVND SHVEGVITND GLFDGFIRTK
AEEFYIEPAS RYSNLNSSQF HTIIYRVPDA LLLTFNSSKC FNSTSSPSSS SLPLPGNSCL
PSVLKSITLD VGDSSNYTKL EEISNQTNYN RLRRDIGNSH SSSPSSVDQS SPSSLPSSSS
PSNLKLKQTY WRDFDSLNYE GDTEAYGIRA VQRAHWPEER PERHFVIDPK KTTCMLYLQA
DHLFYEKLGS EEACIETMTR HVQKVNNIYR STDFNQDGKS DNISFLIKRI KVHTTEALKD
PVYRYKGTYG VEKYLELFSE EDYDAFCLAY MFTYRDFEGG TLGLAWTGDL KNAGGVCEKN
GHYRGSLKSL NTGIVTLLNY GKHVPPIVSH VTLAHEIGHN FGSPHDPENE GSCTPGGEDG
NYIMFARATS GDKRNNNHFS PCSLKSINAV LNTKARSSKG CFQEPQESIC GNEVVEPGEE
CDCGWAEDCT ESCCFPMQSN PPKNEIPCRL RPNVICSPSQ GPCCAHDCRL TVGNKCRDDN
GCRTASYCNG QGPSCPPSTF VPNKTVCNQE SVCFMGECTG SICIAYGLES CQCKRKFDEP
DTKLCELCCR FPGDDATCKS SFEWNTAPLD VPDLYSKPGT PCNNYNGYCD IFQQCREVDP
SGPLATLRRF LLSNESMASL KRWLNEQWIC VIILCIMALL IVFLLVKVFE KRNYELPKSE
LFEANCLDIS SSASSAVSVF ARHRHNSSSS SASSSRPAMV RNHGNLVRTS LAFGHQLSYH
QNDHNEFHCH PLGLTGNGWV
//
