ID U3IZJ3_ANAPP Unreviewed; 870 AA.
AC U3IZJ3;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 2.
DT 24-JAN-2024, entry version 66.
DE SubName: Full=ADAM metallopeptidase domain 8 {ECO:0000313|Ensembl:ENSAPLP00000012670.2};
GN Name=ADAM8 {ECO:0000313|Ensembl:ENSAPLP00000012670.2};
OS Anas platyrhynchos platyrhynchos (Northern mallard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8840 {ECO:0000313|Ensembl:ENSAPLP00000012670.2, ECO:0000313|Proteomes:UP000016666};
RN [1] {ECO:0000313|Ensembl:ENSAPLP00000012670.2, ECO:0000313|Proteomes:UP000016666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hou Z.-C., Zhou Z.-K., Zhu F., Hou S.-S.;
RT "A new Pekin duck reference genome.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPLP00000012670.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR AlphaFoldDB; U3IZJ3; -.
DR STRING; 8840.ENSAPLP00000012670; -.
DR Ensembl; ENSAPLT00000013413.2; ENSAPLP00000012670.2; ENSAPLG00000012822.2.
DR GeneTree; ENSGT00940000158585; -.
DR HOGENOM; CLU_012714_7_1_1; -.
DR OMA; HGQDHCL; -.
DR Proteomes; UP000016666; Chromosome 6.
DR GO; GO:0071133; C:alpha9-beta1 integrin-ADAM8 complex; IEA:Ensembl.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0032127; C:dense core granule membrane; IEA:Ensembl.
DR GO; GO:0032010; C:phagolysosome; IEA:Ensembl.
DR GO; GO:0002102; C:podosome; IEA:Ensembl.
DR GO; GO:0042581; C:specific granule; IEA:Ensembl.
DR GO; GO:0070820; C:tertiary granule; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR GO; GO:0050839; F:cell adhesion molecule binding; IEA:Ensembl.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
DR GO; GO:0007249; P:canonical NF-kappaB signal transduction; IEA:Ensembl.
DR GO; GO:0000902; P:cell morphogenesis; IEA:Ensembl.
DR GO; GO:0098609; P:cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
DR GO; GO:0002523; P:leukocyte migration involved in inflammatory response; IEA:Ensembl.
DR GO; GO:0048247; P:lymphocyte chemotaxis; IEA:Ensembl.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0002675; P:positive regulation of acute inflammatory response; IEA:Ensembl.
DR GO; GO:0045780; P:positive regulation of bone resorption; IEA:Ensembl.
DR GO; GO:2000418; P:positive regulation of eosinophil migration; IEA:Ensembl.
DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IEA:Ensembl.
DR GO; GO:2000415; P:positive regulation of fibronectin-dependent thymocyte migration; IEA:Ensembl.
DR GO; GO:0045089; P:positive regulation of innate immune response; IEA:Ensembl.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
DR GO; GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; IEA:Ensembl.
DR GO; GO:2000391; P:positive regulation of neutrophil extravasation; IEA:Ensembl.
DR GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl.
DR GO; GO:0033089; P:positive regulation of T cell differentiation in thymus; IEA:Ensembl.
DR GO; GO:0070245; P:positive regulation of thymocyte apoptotic process; IEA:Ensembl.
DR GO; GO:1901394; P:positive regulation of transforming growth factor beta1 activation; IEA:Ensembl.
DR GO; GO:2000309; P:positive regulation of tumor necrosis factor (ligand) superfamily member 11 production; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 4.10.70.10; Disintegrin domain; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR InterPro; IPR006586; ADAM_Cys-rich.
DR InterPro; IPR018358; Disintegrin_CS.
DR InterPro; IPR001762; Disintegrin_dom.
DR InterPro; IPR036436; Disintegrin_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR034027; Reprolysin_adamalysin.
DR PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR PANTHER; PTHR11905:SF20; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 8; 1.
DR Pfam; PF08516; ADAM_CR; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR PRINTS; PR00289; DISINTEGRIN.
DR SMART; SM00608; ACR; 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; PS00427; DISINTEGRIN_1; 1.
DR PROSITE; PS50214; DISINTEGRIN_2; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Reference proteome {ECO:0000313|Proteomes:UP000016666};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..870
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5021230476"
FT TRANSMEM 688..711
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 211..411
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 419..505
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 643..675
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 721..758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 770..842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..758
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 346
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 345
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 349
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 355
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 477..497
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 647..657
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 665..674
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 870 AA; 95803 MW; CD2ABB3A44A5FCA0 CRC64;
MVPTLVLRLL GLLLLLLLGH GVSSGPEEEL AHVEQYEMVM PRRVLEPRGK RDLSASPSTY
PDHVLYSIQA EGRDYLLHLE KNRELLGQHY TETHYLADGT EITEKPDVQD HCFYQGHVVG
YTDSAASIST CGGLSGFFHV NETTFLLKPL EEDKAGWHAV YRAAHLRTKR GACQEAGATR
SMHLEYDHDP KIAAPMKLYH WKSAQLRKGP RYVELVLVVD NEEFRKYKDL HRVQNRMKEI
VNHVDKLYQP LGLRVALIGL EVWSNRDKIT VSRNAEVTLE NFLRWRETEL LKRKQHDNAQ
LITGVDFYDT TVGLAKKLAM CTRDSGGVNQ DHSMDPIGAA STMAHEMGHN LGMSHDEDIA
GCHCPVIKDQ GGCVMAAKIS LTYPRLFSSC SEQDMWQFLK DPRTSCLLNV PQADELYGEP
VCGNRFVERG EQCDCGRPEE CFDRCCNATT CQLREGAECA QGDCCQDCKV KAAGTMCRAS
KNDCDLPEHC TGLSSECPED VFQENGIPCQ SGNGYCYNGA CPTHAEQCRV LWGAAARVAP
DECFKQNSRQ DLKLHCLTES GKRPCSPKDV KCGTLLCVSD TTSPVLGSGF FTLSFGQFKC
KAALDSNDGN EMVANLRLVP TGTKCGEEMV CYAGRCQNLL VYGKKNCSAK CNSHGVCNHK
RMCHCEPGWA PPYCQHKVLE LTPGSSSMVL AAVLSVLALS SILLGGGVVL LRGRGMRYFQ
KGPLPHRTSS RTTTGLTNPV FQEGNRLQPP SSQLSHRDIS SPKLLSTTMA PRSTQPLVPS
RPVPQVPSQH PEGLKSLPSC PQERPKPPRK PLPALKRKEP CGVVAGAASP SPPVPPTKPP
TLLSQPCTSL VLPQLDIPPK AALKPTAARR
//
