ID A0A3B0JZI9_DROGU Unreviewed; 769 AA.
AC A0A3B0JZI9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Blast:ADAM 17-like protease {ECO:0000313|EMBL:SPP80930.1};
GN ORFNames=DGUA_6G005892 {ECO:0000313|EMBL:SPP80930.1};
OS Drosophila guanche (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7266 {ECO:0000313|EMBL:SPP80930.1, ECO:0000313|Proteomes:UP000268350};
RN [1] {ECO:0000313|Proteomes:UP000268350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Alioto T., Alioto T.;
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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; OUUW01000005; SPP80930.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B0JZI9; -.
DR STRING; 7266.A0A3B0JZI9; -.
DR OMA; NINKVMR; -.
DR Proteomes; UP000268350; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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:UniProtKB-KW.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR CDD; cd14246; ADAM17_MPD; 1.
DR CDD; cd04270; ZnMc_TACE_like; 1.
DR Gene3D; 4.10.70.30; -; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 4.10.70.10; Disintegrin domain; 1.
DR InterPro; IPR034025; ADAM10_ADAM17.
DR InterPro; IPR032029; ADAM17_MPD.
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:SF6; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 17; 1.
DR Pfam; PF16698; ADAM17_MPD; 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 Hydrolase {ECO:0000313|EMBL:SPP80930.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Protease {ECO:0000313|EMBL:SPP80930.1};
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..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..769
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017319776"
FT TRANSMEM 700..722
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 260..504
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 505..596
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT REGION 230..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 437
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 436
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 440
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 446
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ SEQUENCE 769 AA; 87466 MW; 3F7BB6EA68730DFA CRC64;
MASLSIHTLV TLTTTAEARD PKKSIMQKNI NCGRKMFTKC ISCCGFTIIY VFFACLLIEN
CVALHRTLRH YELFHKDDVL HRVVKRGIIK HSRNPFNTIK EVEFTTLGKN FRLILHPHRE
VLHSKFRAYA VDADGNETVV HMDHDSFYTG RVFGELESSV RAHIEDGTMT MSIHLPDETY
HIEPSWRHLP AAKKDTMVAY KSSDVKLHKN EQGATPKTCG YIKEGLELES KDKDDDTVDN
EIHAREKRQS DQYEYTPTKT RCPLLLVADY RFFQEMGGGN TKTTINYLIS LIDRVHKIYN
DTVWQDRSDQ EGFKGMGFVI KKIVVHSEPT RLRGGEAHYN MIREKWDVRN LLEVFSREYS
HKDFCLAHLF TDLKFEGGIL GLAYVGSPRR NSVGGICTPE YFKNGYTLYL NSGLSSSRNH
YGQRVITREA DLVTAHEFGH NWGSEHDPDI PECSPSASQG GSFLMYTYSV SGYDVNNKKF
SPCSLRSIRK VLQAKSGRCF SEPEESFCGN LRVEGDEQCD AGLLGTEDND SCCDKNCKLR
RNQGAMCSDK NSPCCQNCQF MASGMKCREA QYATCEQEAR CTGAHAECPK SPAMADGTIC
QERGQCRNGK CVPYCETQGL QSCMCDIIAD ACKRCCRMSI NETCFPVEPP DVLPDGTPCI
TGFCNKGVCE KTIQDVVERF WDIIEEINVA KTLRFLKDNI VMAVVLVTSV FWIPISCVIS
YFDRKKLRHE MKLIDWSQKL DLIHPSDERR RVIHIRVPRQ KISVARACN
//
