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Database: UniProt
Entry: Q9R1V4
LinkDB: Q9R1V4
Original site: Q9R1V4 
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   13-FEB-2019, entry version 146.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the 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
CC       protein.
CC   -!- TISSUE SPECIFICITY: Highly expressed in the brain. Weakly detected
CC       in 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.
CC       {ECO:0000250}.
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   UniGene; Mm.89854; -.
DR   ProteinModelPortal; Q9R1V4; -.
DR   SMR; Q9R1V4; -.
DR   IntAct; Q9R1V4; 1.
DR   STRING; 10090.ENSMUSP00000069466; -.
DR   MEROPS; M12.976; -.
DR   iPTMnet; Q9R1V4; -.
DR   PhosphoSitePlus; Q9R1V4; -.
DR   MaxQB; Q9R1V4; -.
DR   PaxDb; Q9R1V4; -.
DR   PRIDE; Q9R1V4; -.
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   eggNOG; KOG3607; Eukaryota.
DR   eggNOG; ENOG410XX2M; LUCA.
DR   GeneTree; ENSGT00940000159790; -.
DR   HOGENOM; HOG000231962; -.
DR   HOVERGEN; HBG050456; -.
DR   InParanoid; Q9R1V4; -.
DR   KO; K16067; -.
DR   OMA; DNMGAMA; -.
DR   OrthoDB; 162519at2759; -.
DR   Reactome; R-MMU-5682910; LGI-ADAM interactions.
DR   PRO; PR:Q9R1V4; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   Bgee; ENSMUSG00000020926; Expressed in 219 organ(s), highest expression level in cerebellum.
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   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; IPR013032; EGF-like_CS.
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; Complete proteome; Disulfide bond;
KW   EGF-like domain; Glycoprotein; Membrane; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     24       {ECO:0000255}.
FT   PROPEP       25    229       {ECO:0000250}.
FT                                /FTId=PRO_0000029076.
FT   CHAIN       230    773       Disintegrin and metalloproteinase domain-
FT                                containing protein 11.
FT                                /FTId=PRO_0000029077.
FT   TOPO_DOM    230    738       Extracellular. {ECO:0000255}.
FT   TRANSMEM    739    759       Helical. {ECO:0000255}.
FT   TOPO_DOM    760    773       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      243    442       Peptidase M12B. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00276}.
FT   DOMAIN      448    535       Disintegrin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00068}.
FT   DOMAIN      681    713       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   COMPBIAS    536    680       Cys-rich.
FT   CARBOHYD    100    100       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    167    167       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    609    609       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    677    677       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    353    437       {ECO:0000250}.
FT   DISULFID    396    421       {ECO:0000250}.
FT   DISULFID    398    405       {ECO:0000250}.
FT   DISULFID    507    527       {ECO:0000250}.
FT   DISULFID    681    696       {ECO:0000250}.
FT   DISULFID    690    702       {ECO:0000250}.
FT   DISULFID    704    713       {ECO:0000250}.
FT   CONFLICT    181    181       W -> R (in Ref. 1; BAA83384).
FT                                {ECO:0000305}.
FT   CONFLICT    218    218       A -> T (in Ref. 1; BAA83384).
FT                                {ECO:0000305}.
FT   CONFLICT    340    340       Q -> K (in Ref. 1; BAA83384).
FT                                {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
//
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