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
//