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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//