Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10090-00758
Entry Name
UniProt Accession
Theoretical PI
8.27
Molecular Weight
83968.11
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Disintegrin and metalloproteinase domain-containing protein 10
Protein Synonyms/Alias
ADAM 10; 3.4.24.81; Kuzbanian protein homolog; Mammalian disintegrin-metalloprotease; CD156c;
Gene Name
Adam10
Gene Synonyms/Alias
Kuz; Madm;
Created Date
28-FEB-2003
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
511
Canonical
CSPSQGPCCTAQCAF
[1]
S-Palmitoylation
598
Canonical
DKELCHVCCMKKMAP
[1]
S-Palmitoylation
Organism
Mus musculus (Mouse)
NCBI Taxa ID
10090
Reference
[1] Predicted from GPS-Lipid
Functional Description
Cleaves the membrane-bound precursor of TNF-alpha to its mature soluble form. Responsible for the proteolytical release of soluble JAM3 from endothelial cells surface (By similarity). 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) at '687- Lys-|-Leu-688'. 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. Responsible for the FasL ectodomain shedding and for the generation of the remnant ADAM10- processed FasL (FasL APL) transmembrane form. Also cleaves the ectodomain of the integral membrane proteins CORIN and ITM2B. May regulate the EFNA5-EPHA3 signaling (By similarity).
Sequence Annotation
Topological domain: 20 673 Extracellular.
Transmembrane: 674 694 Helical.
Topological domain: 695 749 Cytoplasmic.
Domain: 221 457 Peptidase M12B.
Domain: 458 552 Disintegrin.
Motif: 171 178 Cysteine switch.
Motif: 709 716 SH3-binding.
Motif: 723 729 SH3-binding.
Active site: 385 385
Metal binding site: 173 173 Zinc; in inhibited form.
Metal binding site: 384 384 Zinc; catalytic.
Metal binding site: 388 388 Zinc; catalytic.
Metal binding site: 394 394 Zinc; catalytic.
Protein Length
749 AA.
Protein Sequence
(Canonical)
MVLPTVLILL LSWAAGLGGQ YGNPLNKYIR HYEGLSYNVD SLHQKHQRAK RAVSHEDQFL  60
LLDFHAHGRQ FNLRMKRDTS LFSDEFKVET SNKVLDYDTS HIYTGHIYGE EGSFSHGSVI  120
DGRFEGFIKT RGGTFYIEPA ERYIKDRILP FHSVIYHEDD INYPHKYGPQ GGCADHSVFE  180
RMRKYQMTGV EEGARAHPEK HAASSGPELL RKKRTTLAER NTCQLYIQTD HLFFKYYGTR  240
EAVIAQISSH VKAIDTIYQT TDFSGIRNIS FMVKRIRINT TSDEKDPTNP FRFPNIGVEK  300
FLELNSEQNH DDYCLAYVFT DRDFDDGVLG LAWVGAPSGS SGGICEKSKL YSDGKKKSLN  360
TGIITVQNYG SHVPPKVSHI TFAHEVGHNF GSPHDSGTEC TPGESKNLGQ KENGNYIMYA  420
RATSGDKLNN NKFSLCSIRN ISQVLEKKRN NCFVESGQPI CGNGMVEQGE ECDCGYSDQC  480
KDDCCFDANQ PEGKKCKLKP GKQCSPSQGP CCTAQCAFKS KSEKCRDDSD CAKEGICNGF  540
TALCPASDPK PNFTDCNRHT QVCINGQCAG SICEKYDLEE CTCASSDGKD DKELCHVCCM  600
KKMAPSTCAS TGSLQWSKQF SGRTITLQPG SPCNDFRGYC DVFMRCRLVD ADGPLARLKK  660
AIFSPQLYEN IAEWIVAHWW AVLLMGIALI MLMAGFIKIC SVHTPSSNPK LPPPKPLPGT  720
LKRRRPPQPI QQPPRQRPRE SYQMGHMRR                                    749
FASTA
(Canonical)
>LipidDB-10090-00758|O35598
MVLPTVLILLLSWAAGLGGQYGNPLNKYIRHYEGLSYNVDSLHQKHQRAKRAVSHEDQFL
LLDFHAHGRQFNLRMKRDTSLFSDEFKVETSNKVLDYDTSHIYTGHIYGEEGSFSHGSVI
DGRFEGFIKTRGGTFYIEPAERYIKDRILPFHSVIYHEDDINYPHKYGPQGGCADHSVFE
RMRKYQMTGVEEGARAHPEKHAASSGPELLRKKRTTLAERNTCQLYIQTDHLFFKYYGTR
EAVIAQISSHVKAIDTIYQTTDFSGIRNISFMVKRIRINTTSDEKDPTNPFRFPNIGVEK
FLELNSEQNHDDYCLAYVFTDRDFDDGVLGLAWVGAPSGSSGGICEKSKLYSDGKKKSLN
TGIITVQNYGSHVPPKVSHITFAHEVGHNFGSPHDSGTECTPGESKNLGQKENGNYIMYA
RATSGDKLNNNKFSLCSIRNISQVLEKKRNNCFVESGQPICGNGMVEQGEECDCGYSDQC
KDDCCFDANQPEGKKCKLKPGKQCSPSQGPCCTAQCAFKSKSEKCRDDSDCAKEGICNGF
TALCPASDPKPNFTDCNRHTQVCINGQCAGSICEKYDLEECTCASSDGKDDKELCHVCCM
KKMAPSTCASTGSLQWSKQFSGRTITLQPGSPCNDFRGYCDVFMRCRLVDADGPLARLKK
AIFSPQLYENIAEWIVAHWWAVLLMGIALIMLMAGFIKICSVHTPSSNPKLPPPKPLPGT
LKRRRPPQPIQQPPRQRPRESYQMGHMRR
Gene Ontology
GO:0009986; C:cell surface; ISS:UniProtKB
GO:0005737; C:cytoplasm; IDA:UniProtKB
GO:0070062; C:extracellular vesicular exosome; IEA:Ensembl
GO:0005794; C:Golgi apparatus; ISS:UniProtKB
GO:0005798; C:Golgi-associated vesicle; ISS:UniProtKB
GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW
GO:0005634; C:nucleus; IDA:UniProtKB
GO:0097038; C:perinuclear endoplasmic reticulum; IEA:Ensembl
GO:0005886; C:plasma membrane; TAS:Reactome
GO:0014069; C:postsynaptic density; IDA:MGI
GO:0097197; C:tetraspanin-enriched microdomain; IEA:Ensembl
GO:0004175; F:endopeptidase activity; IDA:MGI
GO:0004222; F:metalloendopeptidase activity; ISS:UniProtKB
GO:0008237; F:metallopeptidase activity; IMP:UniProtKB
GO:0042803; F:protein homodimerization activity; IPI:UniProtKB
GO:0019901; F:protein kinase binding; IDA:UniProtKB
GO:0042169; F:SH2 domain binding; NAS:UniProtKB
GO:0008270; F:zinc ion binding; IEA:InterPro
GO:0051089; P:constitutive protein ectodomain proteolysis; IEA:Ensembl
GO:0001701; P:in utero embryonic development; IMP:UniProtKB
GO:0006509; P:membrane protein ectodomain proteolysis; ISS:UniProtKB
GO:0042117; P:monocyte activation; IEA:Ensembl
GO:0007162; P:negative regulation of cell adhesion; ISS:UniProtKB
GO:0007220; P:Notch receptor processing; NAS:UniProtKB
GO:0007219; P:Notch signaling pathway; IMP:UniProtKB
GO:0006913; P:nucleocytoplasmic transport; NAS:UniProtKB
GO:0051088; P:PMA-inducible membrane protein ectodomain proteolysis; IEA:Ensembl
GO:0030307; P:positive regulation of cell growth; IEA:Ensembl
GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl
GO:0010820; P:positive regulation of T cell chemotaxis; IEA:Ensembl
GO:0006468; P:protein phosphorylation; IDA:UniProtKB
GO:0034612; P:response to tumor necrosis factor; IEA:Ensembl
Interpro
InterPro; IPR027053; ADAM_10
InterPro; IPR001762; Blood-coag_inhib_Disintegrin
InterPro; IPR024079; MetalloPept_cat_dom
InterPro; IPR001590; Peptidase_M12B
InterPro; IPR002870; Peptidase_M12B_N
Pfam
Pfam; PF00200; Disintegrin;
Pfam; PF01562; Pep_M12B_propep;
SMART
SMART; SM00050; DISIN;
PROSITE
PROSITE; PS50215; ADAM_MEPRO;
PROSITE; PS50214; DISINTEGRIN_2;
PROSITE; PS00142; ZINC_PROTEASE;
PRINTS