ID A0A1S3JI21_LINUN Unreviewed; 583 AA.
AC A0A1S3JI21;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 7-like isoform X1 {ECO:0000313|RefSeq:XP_013410065.1};
GN Name=LOC106173472 {ECO:0000313|RefSeq:XP_013410065.1};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013410065.1};
RN [1] {ECO:0000313|RefSeq:XP_013410065.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013410065.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
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DR RefSeq; XP_013410065.1; XM_013554611.1.
DR AlphaFoldDB; A0A1S3JI21; -.
DR EnsemblMetazoa; XM_013554611.1; XP_013410065.1; LOC106173472.
DR GeneID; 106173472; -.
DR KEGG; lak:106173472; -.
DR InParanoid; A0A1S3JI21; -.
DR OrthoDB; 2969287at2759; -.
DR Proteomes; UP000085678; Unplaced.
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 Gene3D; 3.40.1620.60; -; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR InterPro; IPR006586; ADAM_Cys-rich.
DR InterPro; IPR041645; ADAMTS_CR_2.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR PANTHER; PTHR13723; ADAMTS A DISINTEGRIN AND METALLOPROTEASE WITH THROMBOSPONDIN MOTIFS PROTEASE; 1.
DR Pfam; PF17771; ADAMTS_CR_2; 1.
DR Pfam; PF13582; Reprolysin_3; 1.
DR SMART; SM00608; ACR; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00023049};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000085678};
KW Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..583
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010324464"
FT DOMAIN 243..464
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT REGION 180..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..230
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 412
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 411
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 415
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 421
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ SEQUENCE 583 AA; 65781 MW; A51AA3A329B7FB00 CRC64;
MKLGSILPTL LLRSCISCLD AAHIDWTPDE GLDFQLVTVR ELPQAAVRGR VERGLDENLA
TRRYQFDAYS KHFDLRLHRN SRIDINSIPV YYVADDGSIL KKEEESEDDF VLYQDKGSNA
AVGMSVVADK EKLEGFVVDG DTMYELRHVA DDNYHVVRKK IESINAVDGR GFIDTDTEVR
HFGGTKEGNA QERRSAKTIS LPEPPLLRTK RHGKKTKKTK TKKNKKSPKA KGSPRFSGNH
IDACVELLIL SDDSMWDFYM ARNDQNVDKT EWELKRLYAQ TTNMLDLTFQ RIEDPDLNIH
VVLSAYVIVT NSSQAPGFGR YTFPGEPERL DRVLVDGYET YDYWREFLQK SYNSFPKHDH
GMAFTRRDIT SRTPEKPYLL GLANVGAICN GAGSTSLVED SGLLSYLTAA HELGHSLGAL
HDVTPACQGY LMAASVFELN VTTLFQLYKF SSCSIEKFKE TLTNACCLAD GGQYENEKEY
KHLTKKLHGD QYDADEQCQL VFGNESKACT PIESPEFCHF LLCNTTTTCH NQLNPMDGTF
CGKGKWCIEG DCVSKRAPLP SHYTQRRGAS GEPTSWCSEV RRK
//