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Q9R1V4 (ADA11_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Disintegrin and metalloproteinase domain-containing protein 11

Short name=ADAM 11
Alternative name(s):
Metalloproteinase-like, disintegrin-like, and cysteine-rich protein
Short name=MDC
Gene names
Name:Adam11
Synonyms:Mdc
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length773 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Probable ligand for integrin in the brain. This is a non catalytic metalloprotease-like protein.

Subunit structure

Can bind to LGI1 and LGI4.

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

Highly expressed in the brain. Weakly detected in the heart, liver and testis.

Domain

A conserved motif [AVN[ED]CD] within the disintegrin-like domain could be involved in the binding to the integrin receptor.

Post-translational modification

The precursor is cleaved by a furin endopeptidase By similarity.

Sequence similarities

Contains 1 disintegrin domain.

Contains 1 EGF-like domain.

Contains 1 peptidase M12B domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Propeptide25 – 229205 By similarity
PRO_0000029076
Chain230 – 773544Disintegrin and metalloproteinase domain-containing protein 11
PRO_0000029077

Regions

Topological domain230 – 738509Extracellular Potential
Transmembrane739 – 75921Helical; Potential
Topological domain760 – 77314Cytoplasmic Potential
Domain243 – 442200Peptidase M12B
Domain448 – 53588Disintegrin
Domain681 – 71333EGF-like
Compositional bias536 – 680145Cys-rich

Amino acid modifications

Glycosylation1001N-linked (GlcNAc...) Potential
Glycosylation1671N-linked (GlcNAc...) Potential
Glycosylation6091N-linked (GlcNAc...) Potential
Glycosylation6771N-linked (GlcNAc...) Potential
Disulfide bond353 ↔ 437 By similarity
Disulfide bond396 ↔ 421 By similarity
Disulfide bond398 ↔ 405 By similarity
Disulfide bond507 ↔ 527 By similarity
Disulfide bond681 ↔ 696 By similarity
Disulfide bond690 ↔ 702 By similarity
Disulfide bond704 ↔ 713 By similarity

Experimental info

Sequence conflict1811W → R in BAA83384. Ref.1
Sequence conflict2181A → T in BAA83384. Ref.1
Sequence conflict3401Q → K in BAA83384. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9R1V4 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: F3F0131ECDA58D72

FASTA77384,134
        10         20         30         40         50         60 
MRRLRRWAIA ALLLLPLLPP PGLGALGPRG ALHWRSSAHV GSPESPEGSE VTEPSRLVRQ 

        70         80         90        100        110        120 
SSGGEVRKPQ LDTRVRQDPP RGTPVHLAQV SFVIPAFDSN FTLDLELNHH LLSSQYVERH 

       130        140        150        160        170        180 
FSREGTRQHS TGAGDHCYYH GKLRGNPQSF AALSTCQGLH GVFSDGNLTY IVEPKEIAGP 

       190        200        210        220        230        240 
WGPPQGPLPH LIYRTPLLPA PLGCREPGCL FAVPAQSALP NWPKLRRKRQ VRRGHPTVHS 

       250        260        270        280        290        300 
ETKYVELIVI NDHQLFEQMR QSVVLTSNFA KSVVNLADVI YKEQLNTRIV LVAMETWADG 

       310        320        330        340        350        360 
DKIQVQDDLL ETLARLMVYR REGLPEPSDA THLFSGRTFQ STSSGAAYVG GICSLSRGGG 

       370        380        390        400        410        420 
VNEYGNMGAM AVTLAQTLGQ NLGMMWNKHR SSAGDCKCPD IWLGCIMEDT GFYLPRKFSR 

       430        440        450        460        470        480 
CSIDEYNQFL QEGGGSCLFN KPLKLLDPPE CGNGFVEAGE ECDCGSVQEC SRAGGNCCKK 

       490        500        510        520        530        540 
CTLTHDAMCS DGLCCRRCKY EPRGVSCREA VNECDIAETC TGDSSQCPPN LHKLDGYYCD 

       550        560        570        580        590        600 
HEQGRCYGGR CKTRDRQCQA LWGHAAADRF CYEKLNVEGT ERGNCGRKGS GWVQCSKQDV 

       610        620        630        640        650        660 
LCGFLLCVNI SGAPRLGDLG GDISSVTFYH QGKELDCRGG HVQLADGSDL SYVEDGTACG 

       670        680        690        700        710        720 
PNMLCLDHRC LPASAFNFST CPGSGERRIC SHHGVCSNEG KCICQPDWTG KDCSIHNPLP 

       730        740        750        760        770 
TSPPTGETER YKGPSGTNII IGSIAGAVLV AAIVLGGTGW GFKNIRRGRS GGA 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and chromosomal mapping of mouse ADAM11, ADAM22 and ADAM23."
Sagane K., Yamazaki K., Mizui Y., Tanaka I.
Gene 236:79-86(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"LGI1 and LGI4 bind to ADAM22, ADAM23 and ADAM11."
Sagane K., Ishihama Y., Sugimoto H.
Int. J. Biol. Sci. 4:387-396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LGI1 AND LGI4.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB009676 mRNA. Translation: BAA83384.1.
AL929067 Genomic DNA. Translation: CAM27995.1.
RefSeqNP_033743.2. NM_009613.2.
UniGeneMm.89854.

3D structure databases

ProteinModelPortalQ9R1V4.
SMRQ9R1V4. Positions 238-718.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9R1V4. 1 interaction.

Protein family/group databases

MEROPSM12.976.

PTM databases

PhosphoSiteQ9R1V4.

Proteomic databases

PaxDbQ9R1V4.
PRIDEQ9R1V4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000103081; ENSMUSP00000099370; ENSMUSG00000020926.
GeneID11488.
KEGGmmu:11488.
UCSCuc007lsi.2. mouse.

Organism-specific databases

CTD4185.
MGIMGI:1098667. Adam11.

Phylogenomic databases

eggNOGNOG256419.
GeneTreeENSGT00680000099751.
HOGENOMHOG000231962.
HOVERGENHBG050456.
KOK16067.
OrthoDBEOG7B31M6.

Gene expression databases

ArrayExpressQ9R1V4.
BgeeQ9R1V4.
CleanExMM_ADAM11.
GenevestigatorQ9R1V4.

Family and domain databases

Gene3D3.40.390.10. 1 hit.
4.10.70.10. 1 hit.
InterProIPR006586. ADAM_Cys-rich.
IPR001762. Blood-coag_inhib_Disintegrin.
IPR018358. Disintegrin_CS.
IPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR002870. Peptidase_M12B_N.
[Graphical view]
PfamPF08516. ADAM_CR. 1 hit.
PF00200. Disintegrin. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
[Graphical view]
PRINTSPR00289. DISINTEGRIN.
SMARTSM00608. ACR. 1 hit.
SM00050. DISIN. 1 hit.
SM00181. EGF. 1 hit.
[Graphical view]
SUPFAMSSF57552. SSF57552. 1 hit.
PROSITEPS50215. ADAM_MEPRO. 1 hit.
PS00427. DISINTEGRIN_1. 1 hit.
PS50214. DISINTEGRIN_2. 1 hit.
PS00022. EGF_1. 1 hit.
PS50026. EGF_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio278852.
PROQ9R1V4.
SOURCESearch...

Entry information

Entry nameADA11_MOUSE
AccessionPrimary (citable) accession number: Q9R1V4
Secondary accession number(s): A2AUA8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: July 27, 2011
Last modified: February 19, 2014
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot