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Database: UniProt
Entry: A0A1S3JI21_LINUN
LinkDB: A0A1S3JI21_LINUN
Original site: A0A1S3JI21_LINUN 
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
//
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