ID V3ZLC7_LOTGI Unreviewed; 735 AA.
AC V3ZLC7;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=ADAM10 endopeptidase {ECO:0000256|ARBA:ARBA00012332};
DE EC=3.4.24.81 {ECO:0000256|ARBA:ARBA00012332};
GN ORFNames=LOTGIDRAFT_235956 {ECO:0000313|EMBL:ESO85097.1};
OS Lottia gigantea (Giant owl limpet).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Patellogastropoda; Lottioidea; Lottiidae; Lottia.
OX NCBI_TaxID=225164 {ECO:0000313|EMBL:ESO85097.1, ECO:0000313|Proteomes:UP000030746};
RN [1] {ECO:0000313|EMBL:ESO85097.1, ECO:0000313|Proteomes:UP000030746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23254933; DOI=10.1038/nature11696;
RA Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT "Insights into bilaterian evolution from three spiralian genomes.";
RL Nature 493:526-531(2013).
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; KB203331; ESO85097.1; -; Genomic_DNA.
DR RefSeq; XP_009064238.1; XM_009065990.1.
DR AlphaFoldDB; V3ZLC7; -.
DR STRING; 225164.V3ZLC7; -.
DR MEROPS; M12.322; -.
DR EnsemblMetazoa; LotgiT235956; LotgiP235956; LotgiG235956.
DR GeneID; 20250010; -.
DR KEGG; lgi:LOTGIDRAFT_235956; -.
DR CTD; 20250010; -.
DR HOGENOM; CLU_004602_0_1_1; -.
DR OMA; FTNRDFA; -.
DR OrthoDB; 5395001at2759; -.
DR Proteomes; UP000030746; 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; 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; PF13574; Reprolysin_2; 1.
DR SMART; SM00050; DISIN; 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|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Reference proteome {ECO:0000313|Proteomes:UP000030746};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
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 TRANSMEM 652..674
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 235..457
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 471..552
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT REGION 683..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..735
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 401
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 400
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 404
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 410
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ SEQUENCE 735 AA; 83259 MW; 6391D2B5AB7B048C CRC64;
MTEEEFYRRR RRMCETFIDT VLTSRTNICI VVLHLKQGRG LNDDISYYEP LSYYTDDVLH
DHNRAKRDLF HTVRLNINAF GRSFNIRLKP NKGVLSDDIE VSTSNEDYHY DGSGIYKGYI
ANEDHSIVHG IINSQGHFDG KIWTPFDQFI IGPSLKYYEN EQPFHSIIYR LSDITFNQTN
IDNKSIRDLL KFKARLNVQD MSVVSDNHNT RHINHNIQYF HQHTRRRRAV LQPKTTCELY
VKADNYFYNA HGNSPDLVIN EIVQFVQTIN TIFSPIDFDR DGSNDNIKFT IKKIKLYTNA
SDPDYARYVG NMDVVKFLES HSEENYDDYC LSYILTHRDF GEGVLGLAWT ASQDENQVGG
VCEKYKVVNG KSQSLNTGIV TTLNYGQTVP SLVSHLTLAH EIGHNMGSDH DPDNVTCTPS
GTGGNYIMYP KATSGKQTNN QFFSTCSINY MSPIITSRGT GLNGCFTADS GSICGNKVID
EGEECDCGWE DECQEYCCNA RGGSGTPCTL KSNATCSTSA NYNAECPEPQ SLPNKTVCDG
SRVCMNGECT GSICLAYDYE PCQCSPTEGV NWKDEVLCAV CCIVNEKCTS SFEVSFMPNL
TMVPGSPCYD NEGYCDVFSR CREVDPSGFY NDLSKWLISS SKEIESWIST NWWAAALIAL
GLVIILGLFV KFCSKSPSKV RREKWEEHQR QRQTQDGFRM QQPQQRRLGS STNRVAPVFT
TRESRGGQIQ QYRNT
//
