ID A0A0B2VUR5_TOXCA Unreviewed; 724 AA.
AC A0A0B2VUR5;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Disintegrin and metalloproteinase domain-containing protein 28 {ECO:0000313|EMBL:KHN85154.1};
GN Name=Adam28 {ECO:0000313|EMBL:KHN85154.1};
GN ORFNames=Tcan_04262 {ECO:0000313|EMBL:KHN85154.1};
OS Toxocara canis (Canine roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Toxocaridae; Toxocara.
OX NCBI_TaxID=6265 {ECO:0000313|EMBL:KHN85154.1, ECO:0000313|Proteomes:UP000031036};
RN [1] {ECO:0000313|EMBL:KHN85154.1, ECO:0000313|Proteomes:UP000031036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PN_DK_2014 {ECO:0000313|EMBL:KHN85154.1};
RA Zhu X.-Q., Korhonen P.K., Cai H., Young N.D., Nejsum P.,
RA von Samson-Himmelstjerna G., Boag P.R., Tan P., Li Q., Min J., Yang Y.,
RA Wang X., Fang X., Hall R.S., Hofmann A., Sternberg P.W., Jex A.R.,
RA Gasser R.B.;
RT "Genetic blueprint of the zoonotic pathogen Toxocara canis.";
RL Submitted (NOV-2014) 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:KHN85154.1}.
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DR EMBL; JPKZ01000852; KHN85154.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B2VUR5; -.
DR STRING; 6265.A0A0B2VUR5; -.
DR Proteomes; UP000031036; 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 Gene3D; 4.10.70.10; Disintegrin domain; 1.
DR InterPro; IPR036436; Disintegrin_dom_sf.
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; PEPTIDASE M12B DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
PE 4: Predicted;
KW Integrin {ECO:0000313|EMBL:KHN85154.1};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Reference proteome {ECO:0000313|Proteomes:UP000031036};
KW Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..724
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002096346"
FT DOMAIN 71..294
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT REGION 437..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 630..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 675..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..651
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..709
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 194
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 193
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 203
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ SEQUENCE 724 AA; 79995 MW; 2DFD9C7DB9BAFEED CRC64;
MPLISLAAFI AALFSFVIFI PICAGKNADS TTPYIVHDEV RSTKPTNQHG TITLMAGVPD
WKGVNTDGRI RYIETLLIAD SGVSKYYNRD MKKLRRAVIT LMQALDLYVY QIGVRMIVVD
VIEMSAHNVT LEHFANYRSE RFTQLPEHDL AILISSAYEG GIAYVNGICS RSAVGIIGFF
ADAPMEYASI FFHELAHLLG LSHDASAECS CNNIRIDEGC LKIDGFDNDC SVQALVEKLP
DHICIQSPPA SMPKNALPVC GNQIVEQHEE CDCGPERFCK SLICNPVTCT RTISDLQLLT
VLTGITTAIS LSVYCIRKWR KPKKQQAFAH ANIGVARKVW DTPTFTPLVS SLSDSQAPIW
NPSTFSEDSC TFNTPTTSPM KLLDPPLTST PNRHSFLPPL LPRLATYANI SPAKSAENIL
QAGIPPFVMS IPRTTQTLGR QPRRPAMRHQ SQSPLLTHSP LHPPSSTTEP FEAKHTFNCV
SRRTVPHSHE SNREHSAKMN LASRRLVFST DSSQEISALS TTSMEHDSPQ TLLDECIQLP
KTPEKERQHQ ELIAALSQCL LAEECILNNK ICPSSSPARL YPLLPIEQHA TVSSASNRLY
DTPTSSDQAI SLVAAKCDND SDDHLVKLSF TREPSRRDSS TSKHCRRSRS FVEKPTTSNG
VLNVDEKSFE ILRNRRLPSS SGHVDNCVTN GRPKVPPPPP PPPPHASEPR PQTEFEAALR
ATEP
//
