ADA11_MOUSE
ID ADA11_MOUSE Reviewed; 773 AA.
AC Q9R1V4; A2AUA8;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Disintegrin and metalloproteinase domain-containing protein 11;
DE Short=ADAM 11;
DE AltName: Full=Metalloproteinase-like, disintegrin-like, and cysteine-rich protein;
DE Short=MDC;
DE Flags: Precursor;
GN Name=Adam11; Synonyms=Mdc;
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 [MRNA].
RC TISSUE=Brain;
RX PubMed=10433968; DOI=10.1016/s0378-1119(99)00253-x;
RA Sagane K., Yamazaki K., Mizui Y., Tanaka I.;
RT "Cloning and chromosomal mapping of mouse ADAM11, ADAM22 and ADAM23.";
RL Gene 236:79-86(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP INTERACTION WITH LGI1 AND LGI4.
RX PubMed=18974846; DOI=10.7150/ijbs.4.387;
RA Sagane K., Ishihama Y., Sugimoto H.;
RT "LGI1 and LGI4 bind to ADAM22, ADAM23 and ADAM11.";
RL Int. J. Biol. Sci. 4:387-396(2008).
CC -!- FUNCTION: Probable ligand for integrin in the brain. This is a non
CC catalytic metalloprotease-like protein.
CC -!- SUBUNIT: Can bind to LGI1 and LGI4.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Highly expressed in the brain. Weakly detected in
CC the heart, liver and testis.
CC -!- DOMAIN: A conserved motif [AVN[ED]CD] within the disintegrin-like
CC domain could be involved in the binding to the integrin receptor.
CC -!- PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}.
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DR EMBL; AB009676; BAA83384.1; -; mRNA.
DR EMBL; AL929067; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS25503.1; -.
DR RefSeq; NP_033743.2; NM_009613.3.
DR AlphaFoldDB; Q9R1V4; -.
DR SMR; Q9R1V4; -.
DR BioGRID; 197961; 9.
DR STRING; 10090.ENSMUSP00000069466; -.
DR MEROPS; M12.976; -.
DR GlyGen; Q9R1V4; 4 sites.
DR iPTMnet; Q9R1V4; -.
DR PhosphoSitePlus; Q9R1V4; -.
DR MaxQB; Q9R1V4; -.
DR PaxDb; Q9R1V4; -.
DR PRIDE; Q9R1V4; -.
DR ProteomicsDB; 285755; -.
DR ABCD; Q9R1V4; 1 sequenced antibody.
DR Antibodypedia; 29870; 139 antibodies from 24 providers.
DR DNASU; 11488; -.
DR Ensembl; ENSMUST00000103081; ENSMUSP00000099370; ENSMUSG00000020926.
DR GeneID; 11488; -.
DR KEGG; mmu:11488; -.
DR UCSC; uc007lsi.2; mouse.
DR CTD; 4185; -.
DR MGI; MGI:1098667; Adam11.
DR VEuPathDB; HostDB:ENSMUSG00000020926; -.
DR eggNOG; KOG3607; Eukaryota.
DR GeneTree; ENSGT00940000159790; -.
DR HOGENOM; CLU_012714_5_2_1; -.
DR InParanoid; Q9R1V4; -.
DR OMA; LWLGCIM; -.
DR OrthoDB; 162519at2759; -.
DR Reactome; R-MMU-5682910; LGI-ADAM interactions.
DR BioGRID-ORCS; 11488; 2 hits in 73 CRISPR screens.
DR PRO; PR:Q9R1V4; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9R1V4; protein.
DR Bgee; ENSMUSG00000020926; Expressed in cerebellar cortex and 202 other tissues.
DR ExpressionAtlas; Q9R1V4; baseline and differential.
DR Genevisible; Q9R1V4; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
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; IPR013111; EGF_extracell.
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; PF07974; EGF_2; 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; PS50026; EGF_3; 1.
PE 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Disulfide bond; EGF-like domain;
KW Glycoprotein; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..229
FT /evidence="ECO:0000250"
FT /id="PRO_0000029076"
FT CHAIN 230..773
FT /note="Disintegrin and metalloproteinase domain-containing
FT protein 11"
FT /id="PRO_0000029077"
FT TOPO_DOM 230..738
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 739..759
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 760..773
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 243..442
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 448..535
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DOMAIN 681..713
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 36..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 609
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 677
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 353..437
FT /evidence="ECO:0000250"
FT DISULFID 396..421
FT /evidence="ECO:0000250"
FT DISULFID 398..405
FT /evidence="ECO:0000250"
FT DISULFID 507..527
FT /evidence="ECO:0000250"
FT DISULFID 681..696
FT /evidence="ECO:0000250"
FT DISULFID 690..702
FT /evidence="ECO:0000250"
FT DISULFID 704..713
FT /evidence="ECO:0000250"
FT CONFLICT 181
FT /note="W -> R (in Ref. 1; BAA83384)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="A -> T (in Ref. 1; BAA83384)"
FT /evidence="ECO:0000305"
FT CONFLICT 340
FT /note="Q -> K (in Ref. 1; BAA83384)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 773 AA; 84134 MW; F3F0131ECDA58D72 CRC64;
MRRLRRWAIA ALLLLPLLPP PGLGALGPRG ALHWRSSAHV GSPESPEGSE VTEPSRLVRQ
SSGGEVRKPQ LDTRVRQDPP RGTPVHLAQV SFVIPAFDSN FTLDLELNHH LLSSQYVERH
FSREGTRQHS TGAGDHCYYH GKLRGNPQSF AALSTCQGLH GVFSDGNLTY IVEPKEIAGP
WGPPQGPLPH LIYRTPLLPA PLGCREPGCL FAVPAQSALP NWPKLRRKRQ VRRGHPTVHS
ETKYVELIVI NDHQLFEQMR QSVVLTSNFA KSVVNLADVI YKEQLNTRIV LVAMETWADG
DKIQVQDDLL ETLARLMVYR REGLPEPSDA THLFSGRTFQ STSSGAAYVG GICSLSRGGG
VNEYGNMGAM AVTLAQTLGQ NLGMMWNKHR SSAGDCKCPD IWLGCIMEDT GFYLPRKFSR
CSIDEYNQFL QEGGGSCLFN KPLKLLDPPE CGNGFVEAGE ECDCGSVQEC SRAGGNCCKK
CTLTHDAMCS DGLCCRRCKY EPRGVSCREA VNECDIAETC TGDSSQCPPN LHKLDGYYCD
HEQGRCYGGR CKTRDRQCQA LWGHAAADRF CYEKLNVEGT ERGNCGRKGS GWVQCSKQDV
LCGFLLCVNI SGAPRLGDLG GDISSVTFYH QGKELDCRGG HVQLADGSDL SYVEDGTACG
PNMLCLDHRC LPASAFNFST CPGSGERRIC SHHGVCSNEG KCICQPDWTG KDCSIHNPLP
TSPPTGETER YKGPSGTNII IGSIAGAVLV AAIVLGGTGW GFKNIRRGRS GGA
