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Database: UniProt
Entry: A0A4C1YAF4_EUMVA
LinkDB: A0A4C1YAF4_EUMVA
Original site: A0A4C1YAF4_EUMVA 
ID   A0A4C1YAF4_EUMVA        Unreviewed;       512 AA.
AC   A0A4C1YAF4;
DT   03-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   03-JUL-2019, sequence version 1.
DT   02-APR-2025, entry version 25.
DE   SubName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 8 {ECO:0000313|EMBL:GBP71609.1};
GN   Name=ADAMTS8 {ECO:0000313|EMBL:GBP71609.1};
GN   ORFNames=EVAR_10822_1 {ECO:0000313|EMBL:GBP71609.1};
OS   Eumeta variegata (Bagworm moth) (Eumeta japonica).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Tineoidea;
OC   Psychidae; Oiketicinae; Eumeta.
OX   NCBI_TaxID=151549 {ECO:0000313|EMBL:GBP71609.1, ECO:0000313|Proteomes:UP000299102};
RN   [1] {ECO:0000313|EMBL:GBP71609.1, ECO:0000313|Proteomes:UP000299102}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=31044173; DOI=.1038/s42003-019-0412-8;
RA   Kono N., Nakamura H., Ohtoshi R., Tomita M., Numata K., Arakawa K.;
RT   "The bagworm genome reveals a unique fibroin gene that provides high
RT   tensile strength.";
RL   Commun. Biol. 2:148-148(2019).
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:GBP71609.1}.
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DR   EMBL; BGZK01001114; GBP71609.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4C1YAF4; -.
DR   STRING; 151549.A0A4C1YAF4; -.
DR   OrthoDB; 9936463at2759; -.
DR   Proteomes; UP000299102; 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:0006509; P:membrane protein ectodomain proteolysis; IEA:TreeGrafter.
DR   Gene3D; 3.40.1620.60; -; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   InterPro; IPR041645; ADAMTS_CR_2.
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:SF249; SOL NARAE, ISOFORM C; 1.
DR   Pfam; PF17771; ADAMTS_CR_2; 1.
DR   Pfam; PF13582; Reprolysin_3; 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   Integrin {ECO:0000313|EMBL:GBP71609.1};
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:UP000299102};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT   DOMAIN          45..187
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000259|PROSITE:PS50215"
FT   ACT_SITE        117
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         116
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         120
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         126
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ   SEQUENCE   512 AA;  57638 MW;  ADCA9E7552E13C9C CRC64;
     MDDNTYANNE RGVGRDATPY LERNRVGRDA IDSAAALTDM GKYLFRERRL PVYDIAVAIT
     KYDMCRRRKG GRCTKGTAGF AYVGGACVVN KRLEKVNSVA IIEDTGGFSG IIVAAHEVGH
     LLGAVHDGSP PPSYLGGPGA EKCRWEDGFI MSDLRHTEKG FRWSPCSVQS FHHFLNGDTA
     TCLYNSPHED DSLPRVLPGR LLTLDAQCRK DRGTSACFKD ERVCAQLFCF DSASGYCVAY
     RPAAEGSPCG DGQYCINGQC ITEHENIIPD YSQHTPSYVR PDTSPFYGNI TSYAETTPVI
     PNTSNYQRNF FSEYSRSTAS WNSYTKTTPS STHTPYKYNF YSTTRSPFFN YQKSTNPTTY
     PPSINKYSIT STRSPYNFKD FFTRSQDSTK RGYSEVIKST TKSPANDKGF RSFYKFGTYF
     SQPKSNDNSI RPDANSQQVQ IEPAKLQPPL VERARRALKT ANAGMARERE FHRQIVRYKA
     AMVYELSAAI LFQHEYKCSE LMHSRENKIH GF
//
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