ID A0A0P7USU2_SCLFO Unreviewed; 724 AA.
AC A0A0P7USU2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=ADAM10 endopeptidase {ECO:0000256|ARBA:ARBA00012332};
DE EC=3.4.24.81 {ECO:0000256|ARBA:ARBA00012332};
GN ORFNames=Z043_116551 {ECO:0000313|EMBL:KPP65056.1};
OS Scleropages formosus (Asian bonytongue) (Osteoglossum formosum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Osteoglossidae; Scleropages.
OX NCBI_TaxID=113540 {ECO:0000313|EMBL:KPP65056.1, ECO:0000313|Proteomes:UP000034805};
RN [1] {ECO:0000313|EMBL:KPP65056.1, ECO:0000313|Proteomes:UP000034805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Aro1 {ECO:0000313|EMBL:KPP65056.1};
RA Tan M.H., Gan H.M., Croft L.J., Austin C.M.;
RT "The genome of the Asian arowana (Scleropages formosus).";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:KPP65056.1}.
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DR EMBL; JARO02006583; KPP65056.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7USU2; -.
DR STRING; 113540.ENSSFOP00015012676; -.
DR Proteomes; UP000034805; 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:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
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:SF1; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 10 ISOFORM X1; 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 Integrin {ECO:0000313|EMBL:KPP65056.1};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Reference proteome {ECO:0000313|Proteomes:UP000034805};
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 DOMAIN 263..489
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 490..582
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 421
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 420
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 424
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 430
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ SEQUENCE 724 AA; 80588 MW; 772C4AEAB3E05241 CRC64;
MARHGRDSRD TWGGYDKRGL HPRDGRDWDS GRKMDGDRPW QSGDRGMPGQ GHMGRGGMPS
RGGYMQGGAS QGLSGALNRQ NQMMQGSGMQ GALVAICPFI RHYEELSYDR EAVHQQHERF
RREILPRSHV VMLDFKAFYR TFRLRLKRDT TEFSDNFKIH IRNVSRVADL SHIYSGHLEG
EEGSSCYGSI IEGQFDGFIQ TENGTYYIEP LDRYSTRPSS NHSIIYHGDD IVHIRILATN
ILVMVNDGEP VSRSKRTVDY SKTTCYLYLH VDYLYFKKFG SAEAVIAQIG SYMNAVNYIY
SKVDFDGIRL INFKVKFLNI SSVEDPSSLL SQAFIGPEKL LSLFSEENWD DYCLSYLLTN
RDFSGVLGLA WNGMQGNLGG ICSKVMIVNG GKMTRNTGLI TLQKYGDQLT PRHIQLTLAH
ELGHSLGAPH DVGSNCGDQG STGDKGRYLM FPYATTMIRE NNDKFSPCSI KHISSLLKVK
KDDCFVVSDQ PICGNFIVEE GEECDIGHNE SDPCCYSANE PRTIQCRLKH GKICSPSQGM
CCSPSCLFKP YGITCEDESE CRFASQCSGT AAACPTPGPK PNMTTCSLET RVCFAGECVQ
SLCVKYGLES CDCLSESMTE KCHMCCQQPG EPNTCASTMS SVLSQFFQGK RLALVAGTPC
SDKQGYCDKF HACRLLDADG PIARLKNAFL HLDGFDDLSE WMKVSGRACV YCAACSFVAY
RSDI
//
