ID A0A0N0BES5_9HYME Unreviewed; 1623 AA.
AC A0A0N0BES5;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=ADAM10 endopeptidase {ECO:0000256|ARBA:ARBA00012332};
DE EC=3.4.24.81 {ECO:0000256|ARBA:ARBA00012332};
GN ORFNames=WN51_01432 {ECO:0000313|EMBL:KOX72334.1};
OS Melipona quadrifasciata.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Melipona.
OX NCBI_TaxID=166423 {ECO:0000313|EMBL:KOX72334.1, ECO:0000313|Proteomes:UP000053105};
RN [1] {ECO:0000313|EMBL:KOX72334.1, ECO:0000313|Proteomes:UP000053105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0111107301 {ECO:0000313|EMBL:KOX72334.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KOX72334.1};
RA Pan H., Kapheim K.;
RT "The genome of Melipona quadrifasciata.";
RL Submitted (JUL-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 -!- 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; KQ435821; KOX72334.1; -; Genomic_DNA.
DR STRING; 166423.A0A0N0BES5; -.
DR OrthoDB; 5395001at2759; -.
DR Proteomes; UP000053105; 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:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd04270; ZnMc_TACE_like; 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; 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:SF3; KUZBANIAN-LIKE, 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 Integrin {ECO:0000313|EMBL:KOX72334.1};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Reference proteome {ECO:0000313|Proteomes:UP000053105};
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 727..945
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 959..1055
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT REGION 154..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1223..1394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..192
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..666
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1247..1262
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1288..1314
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1339..1359
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1365..1390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 891
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 890
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 894
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 900
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ SEQUENCE 1623 AA; 181125 MW; 014A86E1EF285CB9 CRC64;
MILSYIEVVL KGGNLEGTKG SPCAVWLSGG RENEQDIVVC EASVASLGYS GGGLVGESGP
GNSRDFFDTS TSNRIIEKNR LVVILISNNV WKSSLDSFNT CQRSMTHWEI ERERPIFAFK
EIRSTEKLQN LGIAPLVIAG PENVEPMRAT TLAVDEGGEE EEEEEEEEEE EEEEEEEEEE
EEEEEEEAKE EKGEEDEGGK DRGGQNGAQR AAIFFRKMEN VTQRSHLLES TNRMTKADDL
PFIGQKHFKR DYFVTTTPYT EDQYQDQLEE FIYILFTLYI QKIQIRKVET NLKTHVDKRY
KPHVQHEYAF KYMERGGNYA NYHVIVLVEL TGLFWIKQWT LRLIRDEGLF SKDATFESTN
GPIDFDSSHS YVGTVLDIPK TKNSLGGNVR AVVDKQKFKA ICDNSLPRLI SGAAADGSDS
LPQTPVIVTK PAIRLVRQPI LPSGVPQHSA CLTSKIGRRS TLGAQPLAAC ASRVFETHLQ
NKRNGILGLS YPDYSDWRYL LAFAVHRIPT QQQKYTCRHC GLLSLCKFAV LYSQAVTSNF
IFRHIGAATL LRSRAIEDEN AMVQGIVTED GLFDGTVVTG FEEYYIEPTN RYLNKEEDTS
PPYHSIAYRA SDVLTPRRSL PCASHHLHQS ASHDSTEREG DEGQIKFKKK RKDEKRGERG
KHGYANDSRT LYEPLLGERR ALYSKENGAR VLTTERDKSA ARMETVSDAD RIARHLHKRA
TVDPRKTTCM LYLQADHQFF ARYGTEEACI EVMTRHVQRV NSIYKHTDFN QDGRPDNISF
MIKRVKVHSE DALRDPNYRF PGNYGVEKYL ELFSEEDYDA FCLAYMFTYR DFEMGTLGLA
WTGDLKNAGG VCEKNGHYRG SMKSLNTGIV TLLNYGKHVP PAVSHVTLAH EIGHNFGSPH
DPEQCTPGGE DGNFIMFARA TSGDKRNNNR FSPCSLSAIN PVLNSKARSP KGCFTEPQVS
LCGNGVIEEG EECDCGWEED CRDSCCFPQR RYPPPGETPC TLTPGSICSP SQGPCCTAEC
NLRFGDKCRD DNGCRDASFC DGRSPYCPPS INKPNKTICN REFVCFMGEC TGSICLAYGL
ESCQCIPGPN DPSTKACELC CRLPGENQPC LSSFDWNSPP YDIPDMFSKP GTPCNDYNGY
CDVFQKCREV DPSGPLATLR KLLLSDESLA TFRRWIIDHW YAAALIILAA VSLLVASMRL
LGKRPDLKLK SVTIIHSSTT ETVRLPPEGT EGVTVHPPAV RAKLPLSRKV REKRRHRKHK
DSHGNGDKSG KDPSKKKKQS QTKRTSATNE DLPRKRSADA MVQESKRKKS FPSRDKQNTN
GNSSNADNEK RKRKKQHKKE VIDYSAIQAE KETEPNADPK SKVRSWLLAS SQCRPETGRG
NATGLPKSKS TPVGLTGAGA RLPATRQQQV ALRRPTESKE AKITANSGAR KERAKLQVVY
KPPFRFSVKL RKSDKVAQVP AVAANATHAT GRPKLPRTGV LLRTAKKKDR VRIGRARQIA
PTGIGNSAGD LPEPANSDLH TLKLVCPYEV SLKINNCRQL DYFLSALAIV NPTYYSDGSY
SPAIPNRGVK PAGLFAFPVD NCIASQVITT SNVRCLFVLN GFQFGALCDS VTKTTAVTAS
TLV
//
