ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q10743


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name ADA10_RAT
Primary accession number Q10743
Secondary accession numbers None
Integrated into Swiss-Prot on February 28, 2003
Sequence was last modified on November 1, 1996 (Sequence version 1)
Annotations were last modified on    June 10, 2008 (Entry version 69)
Name and origin of the protein
Protein name ADAM 10 [Precursor] [Fragment]
Synonyms EC 3.4.24.81
A disintegrin and metalloproteinase domain 10
Mammalian disintegrin-metalloprotease
Kuzbanian protein homolog
CD156c antigen
Gene name
Name: Adam10
Synonyms: Madm
From
Rattus norvegicus (Rat) [TaxID: 10116] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Rattus.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley;
TISSUE=Brain;
PubMed=8694785 [NCBI, ExPASy, EBI, Israel, Japan]
Howard L., Mitchell S., Lu X., Griffiths S., Glynn P.;
"Molecular cloning of MADM: a catalytically active mammalian disintegrin-metalloprotease expressed in various cell types.";
Biochem. J. 317:45-50(1996).
Comments
  • FUNCTION: Cleaves the membrane-bound precursor of TNF-alpha to its mature soluble form. Responsible for the proteolytic release of several other cell-surface proteins, including heparin-binding epidermal growth-like factor, ephrin-A2 and for constitutive and regulated alpha-secretase cleavage of amyloid precursor protein (APP). Contributes to the normal cleavage of the cellular prion protein. Involved in the cleavage of the adhesion molecule L1 at the cell surface and in released membrane vesicles, suggesting a vesicle-based protease activity. Controls also the proteolytic processing of Notch (By similarity).
  • CATALYTIC ACTIVITY: Endopeptidase of broad specificity.
  • COFACTOR: Binds 1 zinc ion (By similarity).
  • SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
  • TISSUE SPECIFICITY: Expressed in brain, kidney, lung, spleen, ovary and testis.
  • PTM: The precursor is cleaved by a furin endopeptidase (By similarity).
  • SIMILARITY: Contains 1 disintegrin domain.
  • SIMILARITY: Contains 1 peptidase M12B domain [view classification].
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Z48444; CAA88359.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S52477; S52477.
UniGene Rn.42924
3D structure databases
HSSP P18619; 1FVL. [HSSP ENTRY / PDB]
SMR Q10743; 292-442.
ModBase Q10743.
Protein family/group databases
MEROPS M12.210; -.
Organism-specific databases
RGD 2032; Adam10.
GeneLynx Adam10; Rattus norvegicus.
Gene expression databases
ArrayExpress Q10743; -.
GermOnline ENSRNOG00000015038; Rattus norvegicus.
Ontologies
GO
GO:0009986; Cellular component: cell surface (inferred from sequence or structural similarity from UniProtKB).
GO:0005798; Cellular component: Golgi-associated vesicle (inferred from sequence or structural similarity from UniProtKB).
GO:0005634; Cellular component: nucleus (inferred from sequence or structural similarity from UniProtKB).
GO:0008237; Molecular function: metallopeptidase activity (inferred from sequence or structural similarity from UniProtKB).
GO:0042803; Molecular function: protein homodimerization activity (inferred from sequence or structural similarity from UniProtKB).
GO:0019901; Molecular function: protein kinase binding (inferred from sequence or structural similarity from UniProtKB).
GO:0001701; Biological process: in utero embryonic development (inferred from sequence or structural similarity from UniProtKB).
GO:0006509; Biological process: membrane protein ectodomain proteolysis (inferred from sequence or structural similarity from UniProtKB).
GO:0007162; Biological process: negative regulation of cell adhesion (inferred from sequence or structural similarity from UniProtKB).
GO:0007219; Biological process: Notch signaling pathway (inferred from sequence or structural similarity from UniProtKB).
GO:0006468; Biological process: protein amino acid phosphorylation (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR001762; Blood-coag_inhib_Disintegrin.
IPR001818; Pept_M10A_M12B.
IPR006025; Pept_M_Zn_BS.
IPR001590; Peptidase_M12B.
Graphical view of domain structure.
Gene3D G3DSA:4.10.70.10; Blood-coag_inhib_Disintegrin; 1.
Pfam PF00200; Disintegrin; 1.
PF01421; Reprolysin; 1.
Pfam graphical view of domain structure.
ProDom PD000664; Disintegrin; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00050; DISIN; 1.
SMART graphical view of domain structure.
PROSITE PS50215; ADAM_MEPRO; 1.
PS00546; CYSTEINE_SWITCH; FALSE_NEG.
PS00427; DISINTEGRIN_1; FALSE_NEG.
PS50214; DISINTEGRIN_2; 1.
PS00142; ZINC_PROTEASE; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q10743.
Genome annotation databases
Ensembl ENSRNOG00000015038; Rattus norvegicus. [Contig view]
Phylogenomic databases
HOVERGEN Q10743; -.
Other
ProtoNet Q10743.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cleavage on pair of basic residues; Glycoprotein; Hydrolase; Membrane; Metal-binding; Metalloprotease; Notch signaling pathway; Protease; SH3-binding; Transmembrane; Zinc; Zymogen.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
PROPEP   <1     9  >9     Potential. PRO_0000029070
CHAIN   10   544  535     ADAM 10. PRO_0000029071
TOPO_DOM   10   468  459     Extracellular (Potential). 
TRANSMEM   469   492  24     Potential. 
TOPO_DOM   493   544  52     Cytoplasmic (Potential). 
DOMAIN   16   252  237     Peptidase M12B. 
DOMAIN   253   347  95     Disintegrin. 
MOTIF   504   511  8     SH3-binding (Potential). 
MOTIF   518   524  7     SH3-binding (Potential). 
COMPBIAS   347   468  122     Cys-rich. 
ACT_SITE   180   180        By similarity. 
METAL   179   179        Zinc (catalytic) (By similarity). 
METAL   183   183        Zinc (catalytic) (By similarity). 
METAL   189   189        Zinc (catalytic) (By similarity). 
CARBOHYD   63    63        N-linked (GlcNAc...) (Potential). 
CARBOHYD   74    74        N-linked (GlcNAc...) (Potential). 
CARBOHYD   235   235        N-linked (GlcNAc...) (Potential). 
CARBOHYD   347   347        N-linked (GlcNAc...) (Potential). 
DISULFID   18   109        By similarity. 
DISULFID   140   247        By similarity. 
DISULFID   195   231        By similarity. 
DISULFID   299   307        By similarity. 
DISULFID   320   339        By similarity. 
DISULFID   326   358        By similarity. 
DISULFID   351   363        By similarity. 
DISULFID   368   394        By similarity. 
DISULFID   376   403        By similarity. 
DISULFID   378   393        By similarity. 
NON_TER   1     1         
Sequence information
Length: 544 AA [This is the length of the partial sequence of the unprocessed precursor] Molecular weight: 60445 Da [This is the MW of the partial sequence of the unprocessed precursor] CRC64: F75E0E8D6C88A7DD [This is a checksum on the sequence]
        10         20         30         40         50         60 
GPELLRKKRT TLPERNTCQL YIQTDHLFFK SYGTREAVIA QISSHVKAID AIYQTTDFSG 

        70         80         90        100        110        120 
IRNISFMVKR IRINTTSDEK DPTNPFRFPN IGVEKFLELN SEQNHDDYCL AYVFTDRDFD 

       130        140        150        160        170        180 
DGVLGLAWVG APSGSSGGIC EKSKLYSDGK KKSLNTGIIT VQNYGSHVPP KVSHITFAHE 

       190        200        210        220        230        240 
VGHNFGSPHD SGTECTPGES KNLGQKENGN YIMYARATSG DKLNNNKFSL CSIRNISQVL 

       250        260        270        280        290        300 
EKKRNNCFVE SGQPICGNGM VEQGEECDCG YSDQCKDECC FDANQPEGKK CKLKPGKQCS 

       310        320        330        340        350        360 
PSQGPCCTAQ CAFKSKSEKC RDDSDCAKEG ICNGFTALCP ASDPKPNFTD CNRHTQVCIN 

       370        380        390        400        410        420 
GQCAGSICEK YDLEECTCAS SDGKDDKELC HVCCMKKMAP STCASTGSLQ WNKQFTGRTI 

       430        440        450        460        470        480 
TLQPGSPCND FRGYCDVFMR CRLVDADGPL ARLKKAIFSP QLYENIAEWI VAHWWAVLLM 

       490        500        510        520        530        540 
GIALIMLMAG FIKICSVHTP SSNPKLPPPK PLPGTLKRRR PPQPIQQPQR QRPRESYQMG 


HMRR 

Q10743 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!