ID   ADAM8_MOUSE             Reviewed;         826 AA.
AC   Q05910;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 3.
DT   24-JAN-2024, entry version 189.
DE   RecName: Full=Disintegrin and metalloproteinase domain-containing protein 8;
DE            Short=ADAM 8;
DE            EC=3.4.24.-;
DE   AltName: Full=Cell surface antigen MS2;
DE   AltName: Full=Macrophage cysteine-rich glycoprotein;
DE   AltName: CD_antigen=CD156a;
DE   Flags: Precursor;
GN   Name=Adam8; Synonyms=Ms2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ICR;
RA   Yamamoto S., Yoshiyama K., Setoguchi M., Matsuura K., Higuchi Y.,
RA   Akizuki S.;
RL   Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BALB/cJ; TISSUE=Liver;
RX   PubMed=9218457; DOI=10.1074/jbc.272.29.18209;
RA   Kataoka M., Yoshiyama K., Matsuura K., Hijiya N., Higuchi Y., Yamamoto S.;
RT   "Structure of the murine CD156 gene, characterization of its promoter, and
RT   chromosomal location.";
RL   J. Biol. Chem. 272:18209-18215(1997).
RN   [3]
RP   PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ICR;
RX   PubMed=1982220; DOI=10.1093/intimm/2.6.585;
RA   Yoshida S., Setoguchi M., Higuchi Y., Akizuki S., Yamamoto S.;
RT   "Molecular cloning of cDNA encoding MS2 antigen, a novel cell surface
RT   antigen strongly expressed in murine monocytic lineage.";
RL   Int. Immunol. 2:585-591(1990).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Possible involvement in extravasation of leukocytes.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P78325};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P78325};
CC   -!- SUBUNIT: Interacts with FST3. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC   -!- TISSUE SPECIFICITY: Macrophages.
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DR   EMBL; D10911; BAA21771.1; -; Genomic_DNA.
DR   EMBL; X13335; CAA31712.1; -; mRNA.
DR   CCDS; CCDS21959.1; -.
DR   RefSeq; NP_031429.1; NM_007403.3.
DR   AlphaFoldDB; Q05910; -.
DR   SMR; Q05910; -.
DR   BioGRID; 197972; 9.
DR   IntAct; Q05910; 1.
DR   STRING; 10090.ENSMUSP00000101684; -.
DR   MEROPS; M12.208; -.
DR   GlyCosmos; Q05910; 4 sites, No reported glycans.
DR   GlyGen; Q05910; 4 sites.
DR   iPTMnet; Q05910; -.
DR   PhosphoSitePlus; Q05910; -.
DR   EPD; Q05910; -.
DR   PaxDb; 10090-ENSMUSP00000101684; -.
DR   PeptideAtlas; Q05910; -.
DR   ProteomicsDB; 285616; -.
DR   Antibodypedia; 19390; 482 antibodies from 39 providers.
DR   DNASU; 11501; -.
DR   Ensembl; ENSMUST00000106069.9; ENSMUSP00000101684.3; ENSMUSG00000025473.17.
DR   GeneID; 11501; -.
DR   KEGG; mmu:11501; -.
DR   UCSC; uc009kgj.2; mouse.
DR   AGR; MGI:107825; -.
DR   CTD; 101; -.
DR   MGI; MGI:107825; Adam8.
DR   VEuPathDB; HostDB:ENSMUSG00000025473; -.
DR   eggNOG; KOG3607; Eukaryota.
DR   GeneTree; ENSGT00940000158585; -.
DR   InParanoid; Q05910; -.
DR   OMA; HGQDHCL; -.
DR   OrthoDB; 5406290at2759; -.
DR   PhylomeDB; Q05910; -.
DR   TreeFam; TF314733; -.
DR   Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   BioGRID-ORCS; 11501; 1 hit in 63 CRISPR screens.
DR   ChiTaRS; Adam8; mouse.
DR   PRO; PR:Q05910; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; Q05910; Protein.
DR   Bgee; ENSMUSG00000025473; Expressed in granulocyte and 161 other cell types or tissues.
DR   ExpressionAtlas; Q05910; baseline and differential.
DR   GO; GO:0071133; C:alpha9-beta1 integrin-ADAM8 complex; IDA:BHF-UCL.
DR   GO; GO:0009986; C:cell surface; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; ISS:BHF-UCL.
DR   GO; GO:0032127; C:dense core granule membrane; ISS:BHF-UCL.
DR   GO; GO:0032010; C:phagolysosome; ISS:BHF-UCL.
DR   GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR   GO; GO:0002102; C:podosome; ISS:BHF-UCL.
DR   GO; GO:0042581; C:specific granule; ISS:BHF-UCL.
DR   GO; GO:0070820; C:tertiary granule; ISS:BHF-UCL.
DR   GO; GO:0005509; F:calcium ion binding; IDA:BHF-UCL.
DR   GO; GO:0050839; F:cell adhesion molecule binding; IPI:BHF-UCL.
DR   GO; GO:0005178; F:integrin binding; TAS:BHF-UCL.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR   GO; GO:0008237; F:metallopeptidase activity; IDA:BHF-UCL.
DR   GO; GO:0008270; F:zinc ion binding; IDA:BHF-UCL.
DR   GO; GO:0001525; P:angiogenesis; IDA:BHF-UCL.
DR   GO; GO:0043534; P:blood vessel endothelial cell migration; NAS:BHF-UCL.
DR   GO; GO:0007249; P:canonical NF-kappaB signal transduction; IDA:BHF-UCL.
DR   GO; GO:0000902; P:cell morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0098609; P:cell-cell adhesion; IDA:MGI.
DR   GO; GO:0007160; P:cell-matrix adhesion; TAS:BHF-UCL.
DR   GO; GO:0071456; P:cellular response to hypoxia; ISS:BHF-UCL.
DR   GO; GO:0006954; P:inflammatory response; ISO:MGI.
DR   GO; GO:0002523; P:leukocyte migration involved in inflammatory response; IMP:BHF-UCL.
DR   GO; GO:0048247; P:lymphocyte chemotaxis; IDA:BHF-UCL.
DR   GO; GO:0061025; P:membrane fusion; TAS:BHF-UCL.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; IDA:BHF-UCL.
DR   GO; GO:2000399; P:negative regulation of thymocyte aggregation; NAS:BHF-UCL.
DR   GO; GO:0072675; P:osteoclast fusion; TAS:BHF-UCL.
DR   GO; GO:0002675; P:positive regulation of acute inflammatory response; IMP:BHF-UCL.
DR   GO; GO:0045780; P:positive regulation of bone resorption; IDA:BHF-UCL.
DR   GO; GO:0045785; P:positive regulation of cell adhesion; IDA:BHF-UCL.
DR   GO; GO:0002693; P:positive regulation of cellular extravasation; IMP:BHF-UCL.
DR   GO; GO:2000418; P:positive regulation of eosinophil migration; IMP:BHF-UCL.
DR   GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IMP:UniProtKB.
DR   GO; GO:2000415; P:positive regulation of fibronectin-dependent thymocyte migration; IMP:BHF-UCL.
DR   GO; GO:0050729; P:positive regulation of inflammatory response; IDA:BHF-UCL.
DR   GO; GO:0045089; P:positive regulation of innate immune response; IDA:BHF-UCL.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:BHF-UCL.
DR   GO; GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; IDA:BHF-UCL.
DR   GO; GO:2000391; P:positive regulation of neutrophil extravasation; ISO:MGI.
DR   GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IDA:BHF-UCL.
DR   GO; GO:0033089; P:positive regulation of T cell differentiation in thymus; IDA:BHF-UCL.
DR   GO; GO:2000406; P:positive regulation of T cell migration; IMP:BHF-UCL.
DR   GO; GO:0070245; P:positive regulation of thymocyte apoptotic process; IMP:BHF-UCL.
DR   GO; GO:1901394; P:positive regulation of transforming growth factor beta1 activation; IMP:UniProtKB.
DR   GO; GO:2000309; P:positive regulation of tumor necrosis factor (ligand) superfamily member 11 production; IMP:BHF-UCL.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   GO; GO:0022407; P:regulation of cell-cell adhesion; ISS:BHF-UCL.
DR   GO; GO:0045670; P:regulation of osteoclast differentiation; NAS:BHF-UCL.
DR   GO; GO:0048729; P:tissue morphogenesis; TAS:BHF-UCL.
DR   CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR   Gene3D; 3.40.1620.60; -; 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; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
DR   Genevisible; Q05910; MM.
PE   1: Evidence at protein level;
KW   Disulfide bond; EGF-like domain; Glycoprotein; Hydrolase; Membrane;
KW   Metal-binding; Metalloprotease; Protease; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix; Zinc.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..826
FT                   /note="Disintegrin and metalloproteinase domain-containing
FT                   protein 8"
FT                   /id="PRO_0000029061"
FT   TOPO_DOM        17..658
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        659..683
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        684..826
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          196..395
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   DOMAIN          403..489
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DOMAIN          611..643
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   REGION          701..826
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        736..800
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        330
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT                   ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         329
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P78325"
FT   BINDING         333
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P78325"
FT   BINDING         339
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P78325"
FT   CARBOHYD        89
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        260
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        431
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        614
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        305..390
FT                   /evidence="ECO:0000250"
FT   DISULFID        346..374
FT                   /evidence="ECO:0000250"
FT   DISULFID        348..357
FT                   /evidence="ECO:0000250"
FT   DISULFID        430..452
FT                   /evidence="ECO:0000250|UniProtKB:Q10741"
FT   DISULFID        443..449
FT                   /evidence="ECO:0000250|UniProtKB:Q10741"
FT   DISULFID        461..481
FT                   /evidence="ECO:0000250|UniProtKB:Q10741"
FT   DISULFID        468..498
FT                   /evidence="ECO:0000250|UniProtKB:Q10741"
FT   DISULFID        493..503
FT                   /evidence="ECO:0000250|UniProtKB:Q10741"
FT   DISULFID        563..615
FT                   /evidence="ECO:0000250|UniProtKB:Q10741"
FT   DISULFID        615..625
FT                   /evidence="ECO:0000250"
FT   DISULFID        619..631
FT                   /evidence="ECO:0000250"
FT   DISULFID        633..642
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   826 AA;  90046 MW;  3142CC81DBBADFB9 CRC64;
     MLGLWLLSVL WTPAVAPGPP LPHVKQYEVV WPRRLAASRS RRALPSHWGQ YPESLSYALG
     TSGHVFTLHL RKNRDLLGSS YTETYSAANG SEVTEQLQEQ DHCLYQGHVE GYEGSAASIS
     TCAGLRGFFR VGSTVHLIEP LDADEEGQHA MYQAKHLQQK AGTCGVKDTN LNDLGPRALE
     IYRAQPRNWL IPRETRYVEL YVVADSQEFQ KLGSREAVRQ RVLEVVNHVD KLYQELSFRV
     VLVGLEIWNK DKFYISRYAN VTLENFLSWR EQNLQGQHPH DNVQLITGVD FIGSTVGLAK
     VSALCSRHSG AVNQDHSKNS IGVASTMAHE LGHNLGMSHD EDIPGCYCPE PREGGGCIMT
     ESIGSKFPRI FSRCSKIDLE SFVTKPQTGC LTNVPDVNRF VGGPVCGNLF VEHGEQCDCG
     TPQDCQNPCC NATTCQLVKG AECASGTCCH ECKVKPAGEV CRLSKDKCDL EEFCDGRKPT
     CPEDAFQQNG TPCPGGYCFD GSCPTLAQQC RDLWGPGARV AADSCYTFSI PPGCNGRMYS
     GRINRCGALY CEGGQKPLER SFCTFSSNHG VCHALGTGSN IDTFELVLQG TKCEEGKVCM
     DGSCQDLRVY RSENCSAKCN NHGVCNHKRE CHCHKGWAPP NCVQRLADVS DEQAASTSLP
     VSVVVVLVIL VAAMVIVAGI VIYRKAPRQI QRRSVAPKPI SGLSNPLFYT RDSSLPAKNR
     PPDPSETVST NQPPRPIVKP KRPPPAPPGA VSSSPLPVPV YAPKIPNQFR PDPPTKPLPE
     LKPKQVKPTF APPTPPVKPG TGGTVPGATQ GAGEPKVALK VPIQKR
//