ADAM8_MOUSE
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 03-AUG-2022, entry version 181.
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; 8.
DR IntAct; Q05910; 1.
DR STRING; 10090.ENSMUSP00000101684; -.
DR MEROPS; M12.208; -.
DR GlyGen; Q05910; 4 sites.
DR iPTMnet; Q05910; -.
DR PhosphoSitePlus; Q05910; -.
DR EPD; Q05910; -.
DR PaxDb; Q05910; -.
DR PeptideAtlas; Q05910; -.
DR PRIDE; Q05910; -.
DR ProteomicsDB; 285616; -.
DR Antibodypedia; 19390; 434 antibodies from 39 providers.
DR DNASU; 11501; -.
DR Ensembl; ENSMUST00000106069; ENSMUSP00000101684; ENSMUSG00000025473.
DR GeneID; 11501; -.
DR KEGG; mmu:11501; -.
DR UCSC; uc009kgj.2; mouse.
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; 162519at2759; -.
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 60 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 158 other tissues.
DR ExpressionAtlas; Q05910; baseline and differential.
DR Genevisible; Q05910; MM.
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:0005887; C:integral component of plasma 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; IEA:InterPro.
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: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: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:0043406; P:positive regulation of MAP kinase activity; 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:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:BHF-UCL.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; 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:2000309; P:positive regulation of tumor necrosis factor (ligand) superfamily member 11 production; IMP:BHF-UCL.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; 3.40.390.10; -; 1.
DR Gene3D; 4.10.70.10; -; 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 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; SSF57552; 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.
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
