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Reviewed, UniProtKB/Swiss-Prot Q8JIY1 (ADA10_XENLA)

Last modified October 13, 2009. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Disintegrin and metalloproteinase domain-containing protein 10
      Short name=ADAM 10
    EC=3.4.24.81
Alternative name(s):
    Kuzbanian protein homolog
      Short name=xKuz
Gene names
Name: adam10
Synonyms: kuz
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Mesobatrachia › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

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Protein attributes

Sequence length749 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

Controls the proteolytic processing of Notch and mediates lateral inhibition during neurogenesis By similarity.

Catalytic activity

Endopeptidase of broad specificity.

Cofactor

Binds 1 zinc ion By similarity.

Subcellular location

Membrane; Single-pass type I membrane protein.

Developmental stage

Expressed maternally throughout the embryo and then becomes restricted to a pan-neural expression pattern.

Domain

The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.

Post-translational modification

The precursor is cleaved by a furin endopeptidase By similarity.

Sequence similarities

Contains 1 disintegrin domain.

Contains 1 peptidase M12B domain.

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Ontologies

Keywords
   Biological processNotch signaling pathway
   Cellular componentMembrane
   DomainSH3-binding
Signal
Transmembrane
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
Zymogen
Gene Ontology (GO)
   Biological processNotch signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

membrane protein ectodomain proteolysis

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell adhesion

Inferred from sequence or structural similarity. Source: UniProtKB

protein amino acid phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular componentGolgi-associated vesicle

Inferred from sequence or structural similarity. Source: UniProtKB

cell surface

Inferred from sequence or structural similarity. Source: UniProtKB

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular functionSH3 domain binding

Inferred from electronic annotation. Source: UniProtKB-KW

metalloendopeptidase activity

Inferred from electronic annotation. Source: InterPro

protein homodimerization activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein kinase binding

Inferred from sequence or structural similarity. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Propeptide19 – 213195 By similarity
PRO_0000029072
Chain214 – 749536Disintegrin and metalloproteinase domain-containing protein 10
PRO_0000029073

Regions

Topological domain19 – 673655Extracellular Potential
Transmembrane674 – 69421 Potential
Topological domain695 – 74955Cytoplasmic Potential
Domain220 – 457238Peptidase M12B
Domain458 – 55295Disintegrin
Motif170 – 1778Cysteine switch By similarity
Motif709 – 7168SH3-binding Potential
Motif723 – 7297SH3-binding Potential
Compositional bias555 – 673119Cys-rich

Sites

Active site3851 By similarity
Metal binding1721Zinc; in inhibited form By similarity
Metal binding3841Zinc; catalytic
Metal binding3881Zinc; catalytic
Metal binding3941Zinc; catalytic

Amino acid modifications

Glycosylation2681N-linked (GlcNAc...) Potential
Glycosylation2791N-linked (GlcNAc...) Potential
Glycosylation4401N-linked (GlcNAc...) Potential
Glycosylation5521N-linked (GlcNAc...) Potential
Disulfide bond222 ↔ 314 By similarity
Disulfide bond345 ↔ 452 By similarity
Disulfide bond400 ↔ 436 By similarity
Disulfide bond504 ↔ 512 By similarity
Disulfide bond525 ↔ 544 By similarity
Disulfide bond531 ↔ 563 By similarity
Disulfide bond556 ↔ 568 By similarity
Disulfide bond573 ↔ 599 By similarity
Disulfide bond581 ↔ 608 By similarity
Disulfide bond583 ↔ 598 By similarity

Experimental info

Sequence conflict5151D → G in AAC60248. Ref.2
Sequence conflict5221S → G in AAC60248. Ref.2
Sequence conflict6041K → I in AAC60248. Ref.2
Sequence conflict6151A → V in AAC60248. Ref.2

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Sequences

Sequence LengthMass (Da)Tools
Q8JIY1-1 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: FC7A2FEEE7016A6A

FASTA74984,068
        10         20         30         40         50         60 
MGLLRLVFLL SWAASAGGLY GNPLNKYIRH YEGLSYNVDS LHQKHQRAKR AVSQEDQFVH 

        70         80         90        100        110        120 
LDFQAHGRQF NLRMKKDTSL FSPDFKLEVG GETVNYDTSH IYTGQLFGEQ GTLSHGSVVD 

       130        140        150        160        170        180 
GKSKGLLKPL KAHSYVEPSE RFFKDQAVPF HSVMYHEDDI KYPHKYGSEG GCADSSVFKR 

       190        200        210        220        230        240 
MKEYQMSVQE EPEKHDHKED HEDSGPVILR KKRAAQAEKN TCQLFIQTDH LFYKRYGETR 

       250        260        270        280        290        300 
EAVIAQISSH VKAIDTIYQS TDFSGIRNIS FMVKRIRINV TSDEKDPTNP FRFPNIGVEK 

       310        320        330        340        350        360 
FLELNSEQNH DDYCLAYVFT DRDFDDGVLG LAWVGAPSGS SGGICERNKL YSDGKKKSLN 

       370        380        390        400        410        420 
TGIITVQNYG SHVPPKVSHI TFAHEVGHNF GSPHDSGNEC TPGEAKNLGF KENGNFIMYA 

       430        440        450        460        470        480 
RTTSGDKLNN NKFSICSVRN ISQVLDKKEN SCFVESGQPI CGNGLVEPGE QCDCGYSDQC 

       490        500        510        520        530        540 
KDECCYDANQ PENLKCTLKP GKQCSPSQGP CCTTDCTFKR ASENCREESD CAKMGTCNGN 

       550        560        570        580        590        600 
SAQCPPSEPR ENLTECNRAT QVCIKGQCSG SICERYDLEE CTCGSTDEKD DKELCHVCCM 

       610        620        630        640        650        660 
EKMKPHTCAS TGSEAWKAYF KGKTITLQPG SPCNEFKGYC DVFMRCRLVD ADGPLARLKK 

       670        680        690        700        710        720 
AIFNPELYEN IAEWIVAHWW AVLLMGIALI MLMAGFIKIC SVHTPSSNPK LPPPKPLPGT 

       730        740 
LKRRRPPQTT QQPSRQRPRE NYQMGHMRH

« Hide

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References

[1]"The cysteine-rich domain regulates ADAM protease function in vivo."
Smith K.M., Gaultier A., Cousin H., Alfandari D., White J.M., DeSimone D.W.
J. Cell Biol. 159:893-902(2002) [PubMed: 12460986] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Kuzbanian controls proteolytic processing of Notch and mediates lateral inhibition during Drosophila and vertebrate neurogenesis."
Pan D., Rubin G.M.
Cell 90:271-280(1997) [PubMed: 9244301] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 476-637, FUNCTION.

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Cross-references

Sequence databases

AF508151 mRNA. Translation: AAM34686.1.
AF011380 mRNA. Translation: AAC60248.1.
RefSeqNP_001083912.1.
UniGeneXl.51047

3D structure databases

HSSPHSSP built from PDB template 1FVL based on UniProtKB P18619.
SMRQ8JIY1. Positions 494-647.
ModBaseSearch...

Protein family/group databases

MEROPSM12.210.

Genome annotation databases

GeneID399187.
KEGGxla:399187.

Organism-specific databases

CTD399187.
XenbaseXB-FEAT-945387. adam10.

Phylogenomic databases

HOVERGENQ8JIY1.

Enzyme and pathway databases

BRENDA3.4.24.81. 648.

Family and domain databases

InterProIPR001762. Blood-coag_inhib_Disintegrin.
IPR018358. Disintegrin_CS.
IPR001818. Pept_M10A_M12B.
IPR006025. Pept_M_Zn_BS.
IPR001590. Peptidase_M12B.
[Graphical view]
Gene3DG3DSA:4.10.70.10. Blood-coag_inhib_Disintegrin. 1 hit.
PfamPF00200. Disintegrin. 1 hit.
PF01421. Reprolysin. 1 hit.
[Graphical view]
ProDomPD000664. Disintegrin. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00050. DISIN. 1 hit.
[Graphical view]
PROSITEPS50215. ADAM_MEPRO. 1 hit.
PS00546. CYSTEINE_SWITCH. False negative.
PS00427. DISINTEGRIN_1. False negative.
PS50214. DISINTEGRIN_2. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameADA10_XENLA
AccessionPrimary (citable) accession number: Q8JIY1
Secondary accession number(s): O42568
Entry history
Integrated into UniProtKB/Swiss-Prot: February 28, 2003
Last sequence update: October 1, 2002
Last modified: October 13, 2009
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectXenopus annotation project

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Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents