ID A0A1S3J9F7_LINUN Unreviewed; 410 AA.
AC A0A1S3J9F7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=A disintegrin and metalloproteinase with thrombospondin motifs adt-1 {ECO:0000313|RefSeq:XP_013406504.1};
GN Name=LOC106170979 {ECO:0000313|RefSeq:XP_013406504.1};
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_013406504.1};
RN [1] {ECO:0000313|RefSeq:XP_013406504.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013406504.1};
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_013406504.1; XM_013551050.1.
DR AlphaFoldDB; A0A1S3J9F7; -.
DR EnsemblMetazoa; XM_013551050.1; XP_013406504.1; LOC106170979.
DR GeneID; 106170979; -.
DR KEGG; lak:106170979; -.
DR InParanoid; A0A1S3J9F7; -.
DR OrthoDB; 2940912at2759; -.
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:InterPro.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR PANTHER; PTHR11905:SF243; SOL NARAE, ISOFORM C; 1.
DR Pfam; PF13688; Reprolysin_5; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Reference proteome {ECO:0000313|Proteomes:UP000085678};
KW Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..410
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010310101"
FT DOMAIN 215..410
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT ACT_SITE 353
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 352
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 356
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 362
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ SEQUENCE 410 AA; 45317 MW; 5B818FE95C030CBF CRC64;
MASPPKTLTL CFTACILSSV VVAAQVAIQQ LTRTELQEIF GVQDHSKVPD YSLTEIHEYQ
TRGASNHDGR LRMSMKVGGR LLRLHLSRND DLVQNTLVTK LSVNDDGQTI EENVTGKDDV
DGELSQLYED PVHSAAFTIQ RDASGLLLDG SVGDYVVRTL PDHVTSNSSL RHVVYRQPDV
RFVSDEYYPP DENTSANITQ PRGLHKRQVK VPAIVYAEVT LIVAHSVIRN KGSEANAKKY
VLNYWNSVSS NYKSYKMSPD IRFKIKEFIM CSSPTAAMCN GIDQSGSLGD VLQRMVDYLK
PRKKYDIAVA HNCANGWNRG DGMGAVAKAC DPWAVGVVSD DCSQRFTKLH LHETGHILGS
PHDGDSGMPC DRSAYLMTPN GYSTSHLPSP CTRAKWSAYW SSSKGACMHM
//
