Reviewed, UniProtKB/Swiss-Prot Q8JIY1 (ADA10_XENLA)

Names and origin

Protein names

Recommended 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

Organism

Xenopus laevis (African clawed frog)

Taxonomic identifier

8355 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Mesobatrachia › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Protein attributes

Sequence length	749 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Controls the proteolytic processing of Notch and mediates lateral inhibition during neurogenesis By similarity. Ref.2
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.

Ontologies

Keywords
Biological process	Notch signaling pathway
Cellular component	Membrane
Domain	SH3-binding Signal Transmembrane
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Zymogen
Gene Ontology (GO)
Biological process	Notch 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 component	Golgi-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 function	SH3 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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 18	18	Potential
	Propeptide	19 – 213	195	By similarity		PRO_0000029072
	Chain	214 – 749	536	Disintegrin and metalloproteinase domain-containing protein 10		PRO_0000029073
Regions
	Topological domain	19 – 673	655	Extracellular Potential
	Transmembrane	674 – 694	21	Potential
	Topological domain	695 – 749	55	Cytoplasmic Potential
	Domain	220 – 457	238	Peptidase M12B
	Domain	458 – 552	95	Disintegrin
	Motif	170 – 177	8	Cysteine switch By similarity
	Motif	709 – 716	8	SH3-binding Potential
	Motif	723 – 729	7	SH3-binding Potential
	Compositional bias	555 – 673	119	Cys-rich
Sites
	Active site	385	1	By similarity
	Metal binding	172	1	Zinc; in inhibited form By similarity
	Metal binding	384	1	Zinc; catalytic
	Metal binding	388	1	Zinc; catalytic
	Metal binding	394	1	Zinc; catalytic
Amino acid modifications
	Glycosylation	268	1	N-linked (GlcNAc...) Potential
	Glycosylation	279	1	N-linked (GlcNAc...) Potential
	Glycosylation	440	1	N-linked (GlcNAc...) Potential
	Glycosylation	552	1	N-linked (GlcNAc...) Potential
	Disulfide bond	222 ↔ 314		By similarity
	Disulfide bond	345 ↔ 452		By similarity
	Disulfide bond	400 ↔ 436		By similarity
	Disulfide bond	504 ↔ 512		By similarity
	Disulfide bond	525 ↔ 544		By similarity
	Disulfide bond	531 ↔ 563		By similarity
	Disulfide bond	556 ↔ 568		By similarity
	Disulfide bond	573 ↔ 599		By similarity
	Disulfide bond	581 ↔ 608		By similarity
	Disulfide bond	583 ↔ 598		By similarity
Experimental info
	Sequence conflict	515	1	D → G in AAC60248. Ref.2
	Sequence conflict	522	1	S → G in AAC60248. Ref.2
	Sequence conflict	604	1	K → I in AAC60248. Ref.2
	Sequence conflict	615	1	A → V in AAC60248. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q8JIY1-1 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: FC7A2FEEE7016A6A	FASTA	749	84,068
	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

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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF508151 mRNA. Translation: AAM34686.1. AF011380 mRNA. Translation: AAC60248.1.
RefSeq	NP_001083912.1.
UniGene	Xl.51047
3D structure databases
SMR	Q8JIY1. Positions 207-570, 484-647.
ModBase	Search...
Protein family/group databases
MEROPS	M12.210.
Genome annotation databases
GeneID	399187.
KEGG	xla:399187.
Organism-specific databases
CTD	399187.
Xenbase	XB-FEAT-945387. adam10.
Phylogenomic databases
HOVERGEN	Q8JIY1.
Enzyme and pathway databases
BRENDA	3.4.24.81. 648.
Family and domain databases
InterPro	IPR001762. Blood-coag_inhib_Disintegrin. IPR001590. Peptidase_M12B. IPR002870. Peptidase_M12B_N. [Graphical view]
Gene3D	G3DSA:4.10.70.10. Blood-coag_inhib_Disintegrin. 1 hit.
Pfam	PF00200. Disintegrin. 1 hit. PF01562. Pep_M12B_propep. 1 hit. PF01421. Reprolysin. 1 hit. [Graphical view]
SMART	SM00050. DISIN. 1 hit. [Graphical view]
PROSITE	PS50215. 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]
ProtoNet	Search...

Entry information

Entry name

ADA10_XENLA

Accession

Primary (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:	January 19, 2010
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Xenopus annotation project