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Database: UniProt
Entry: A0A0V1NZZ4_9BILA
LinkDB: A0A0V1NZZ4_9BILA
Original site: A0A0V1NZZ4_9BILA 
ID   A0A0V1NZZ4_9BILA        Unreviewed;       667 AA.
AC   A0A0V1NZZ4;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Disintegrin and metalloproteinase domain-containing protein 10 {ECO:0000313|EMBL:KRZ89615.1};
GN   Name=Adam10 {ECO:0000313|EMBL:KRZ89615.1};
GN   ORFNames=T08_3949 {ECO:0000313|EMBL:KRZ89615.1};
OS   Trichinella sp. T8.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ89615.1, ECO:0000313|Proteomes:UP000054924};
RN   [1] {ECO:0000313|EMBL:KRZ89615.1, ECO:0000313|Proteomes:UP000054924}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS272 {ECO:0000313|EMBL:KRZ89615.1};
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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:KRZ89615.1}.
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DR   EMBL; JYDM01000067; KRZ89615.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1NZZ4; -.
DR   Proteomes; UP000054924; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; IPR001762; Disintegrin_dom.
DR   InterPro; IPR036436; Disintegrin_dom_sf.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   PANTHER; PTHR45702; ADAM10/ADAM17 METALLOPEPTIDASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR45702:SF2; KUZBANIAN, ISOFORM A; 1.
DR   Pfam; PF00200; Disintegrin; 1.
DR   Pfam; PF13574; Reprolysin_2; 1.
DR   SMART; SM00050; DISIN; 1.
DR   SUPFAM; SSF57552; Blood coagulation inhibitor (disintegrin); 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
DR   PROSITE; PS50214; DISINTEGRIN_2; 1.
PE   4: Predicted;
KW   Integrin {ECO:0000313|EMBL:KRZ89615.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054924};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT   TRANSMEM        21..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          282..522
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000259|PROSITE:PS50215"
FT   DOMAIN          547..648
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000259|PROSITE:PS50214"
FT   ACT_SITE        467
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         466
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         470
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         476
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ   SEQUENCE   667 AA;  75168 MW;  EAC475C8FE4546A2 CRC64;
     MSTLFTPSSH CHQHLNGFFK CFITMLTNVL TFVVFHLCLA LSVSGQSPLK FLRRFEKLDY
     DSSSVSSAHA RFKRSIDSRS DPFPITISLK YLDKTFKLKL KPDSSSFSSS HAFDENGKKK
     NVDLSFLFDG QVEGESNSYV YGSLIDGVFD GHIHIKDNVY HVEKIVKYDV NQLKPAYHSI
     IYSDDDIKFE KLRVKRHVDS SASSSCGLHG RVRRTMQRFQ RSAVVEEPQL FTYGSGHQWT
     GASRNADEAM QPWRKYVEKV HRDDEELSDR WKRSADGLYD VRTCTLYMQA DQKLWEFVYN
     HEGQRNSERT RNEILSLFNS HIKAVNTIYE GTNFNGIKGI NFVVQRTTIF DNNTCPSIVT
     PDSGNPFCEE NVDVSNFLNL NSIKNHSDFC LAYALTYRDF VGGTLGLAWV ASPQPSEHTS
     GGICEIYKPY SEGSRRVRRS LNTGIITLVN YHNRVPPKVS QLTLAHEIGH NFGSPHDYPP
     FCQPGLPDGN YIMFASATSG DKVNNNKFSI CSVNNISSVL HEVLRQNPNM PRLGSSAKRN
     CFKRRETSFC GNALVEDGEE CDCGFNQQEC RQRGDSCCYP RTHGGEAKGC TRVEGVQCSP
     SEGVCCNKSC QFITSSAHFL CRQATECSTD QYCKGNQPGC PLPDAKPNGT RCQDNTKVCN
     RGVMQFL
//
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