ID   A0A0V1MYM8_9BILA        Unreviewed;       884 AA.
AC   A0A0V1MYM8;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 12 {ECO:0000313|EMBL:KRZ76684.1};
GN   Name=Adamts12 {ECO:0000313|EMBL:KRZ76684.1};
GN   ORFNames=T10_626 {ECO:0000313|EMBL:KRZ76684.1};
OS   Trichinella papuae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ76684.1, ECO:0000313|Proteomes:UP000054843};
RN   [1] {ECO:0000313|EMBL:KRZ76684.1, ECO:0000313|Proteomes:UP000054843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ76684.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRZ76684.1}.
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DR   EMBL; JYDO01000026; KRZ76684.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1MYM8; -.
DR   Proteomes; UP000054843; Unassembled WGS sequence.
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   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:SF251; PEPTIDASE M12B DOMAIN-CONTAINING PROTEIN; 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   Integrin {ECO:0000313|EMBL:KRZ76684.1};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054843};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT   DOMAIN          252..449
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000259|PROSITE:PS50215"
FT   ACT_SITE        404
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         403
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         407
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         413
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ   SEQUENCE   884 AA;  98857 MW;  E8A1DE0088DF497E CRC64;
     MSLKKKHFSI LFIATDENSY PNPPNHFYDD FNIEELRETF GVSNHEKIPD HEIVKPELQA
     TGNQSEPPWI MRIHFGNRTH QLHLNTVDLE NLFSPQLLTV ERYNNRTLLN VGSSFAPLCR
     NHYRTIQTDH VHGALSLCEG MLASYPSLFI QFCAKGSLLL NDGLYTLLPL PKRKNDHLVR
     LKRMAPTNKF EQFHVIYKRQ TTAGSFFYPS ATFCGVDTSF ERTMRDDPTK MKKHHNNWNA
     PAGGTQFHHD RLVMELAIFI DNELWLRYSR KYGDQAEDKL KDFIYTVFHH VQILYQQPSI
     EPLIEFSIVR YEIFKTQPKA LKGTKHNHGS ALSYLNAFCK FQYYLGARKR WDFALLFSGY
     DIHRPPSDRT ISGIARLYGV CDPLNSCLLA EGVDFSSAYI AAHEIGHGLG MLHDEPTCSS
     DYIMSGSLGA GKVQWSSCSV QSLNNYIRKL ELWTDSGQNG HRWNVPVVNV HLYHQDWVYY
     HQHVAVLIHL RKMAAMFVQE AIFCEVNGTN ADSISFRFFG DSMPEGSPCG EGHYCINGKC
     LMKILLQPQQ QHTNGPLGVN GQNAASLVVA VQNHEAEPVG KVPPLAGLGQ EHAIVDVLSA
     NVSVLMTKLN NALTHHAVSG MHGHFGLHVQ SAAVRAHARE HVPALIHPAK DQIEKLLDAT
     YVLVNLMAFG IVGLNGHHVQ SVAVLVFDNE IVSVQPETVM ASHTCQNNAN CPVAQSGVRG
     DNGQSVVRRV ELDNELDNAT GLAHAWVRTL SPKHVNLATG GQNGAHGLCV PVLVAKVYDV
     VIVLALVLFI PAREISKFSK YATKKTAPML IWVMLRQHCP RNLPPVCTLS ATNGASGVIA
     WDAVVQAFEK GFAYVKDITA VRRSLQNLNI VNCCHATQYS TLDH
//