Disintegrin and metalloproteinase domain-containing protein 10 precursor

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Q10743 (ADA10_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 106. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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
Mammalian disintegrin-metalloprotease
CD_antigen=CD156c

Gene names

Name:	Adam10
Synonyms:	Madm

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	544 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	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. 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. 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.
Catalytic activity	Endopeptidase of broad specificity.
Cofactor	Binds 1 zinc ion By similarity.
Subunit structure	Forms a ternary EFNA5-EPHA3-ADAM10 complex mediating EFNA5 extracellular domain shedding by ADAM10 which regulates the EFNA5-EPHA3 complex internalization and function. Interacts with EPHA2, the cleavage occurs in trans, with ADAM10 and its substrate being on the membranes of opposing cells By similarity.
Subcellular location	Membrane; Single-pass type I membrane protein.
Tissue specificity	Expressed in brain, kidney, lung, spleen, ovary and testis.
Domain	The Cys-rich region C-terminal to the disintegrin domain functions as a substrate-recognition module, it recognizes the EFNA5-EPHA3 Complex but not the individual proteins By similarity.
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 Transmembrane Transmembrane helix
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Zymogen
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Notch signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB in utero embryonic development 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 phosphorylation Inferred from sequence or structural similarity. Source: UniProtKB regulation of osteoclast differentiation Non-traceable author statement PubMed 10423016. Source: RGD
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-KW membrane Inferred from direct assay PubMed 10423016. Source: RGD nucleus Inferred from sequence or structural similarity. Source: UniProtKB trans-Golgi network Inferred from direct assay PubMed 10423016. Source: RGD
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW metalloendopeptidase activity Inferred from direct assay PubMed 10423016. Source: RGD protein homodimerization activity Inferred from sequence or structural similarity. Source: UniProtKB protein kinase binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Propeptide

‹1 – 9

›9

Potential

PRO_0000029070

Chain

10 – 544

535

Disintegrin and metalloproteinase domain-containing protein 10

PRO_0000029071

Regions

Topological domain

10 – 468

459

Extracellular Potential

Transmembrane

469 – 492

Helical; Potential

Topological domain

493 – 544

Cytoplasmic Potential

Domain

16 – 252

237

Peptidase M12B

Domain

253 – 347

Disintegrin

Motif

504 – 511

SH3-binding Potential

Motif

518 – 524

SH3-binding Potential

Compositional bias

347 – 468

122

Cys-rich

Sites

Active site

180

By similarity

Metal binding

179

Zinc; catalytic By similarity

Metal binding

183

Zinc; catalytic By similarity

Metal binding

189

Zinc; catalytic By similarity

Amino acid modifications

Glycosylation

N-linked (GlcNAc...) Potential

Glycosylation

N-linked (GlcNAc...) Potential

Glycosylation

235

N-linked (GlcNAc...) Potential

Glycosylation

347

N-linked (GlcNAc...) Potential

Disulfide bond

18 ↔ 109

By similarity

Disulfide bond

140 ↔ 247

By similarity

Disulfide bond

195 ↔ 231

By similarity

Disulfide bond

280 ↔ 311

By similarity

Disulfide bond

299 ↔ 307

By similarity

Disulfide bond

320 ↔ 339

By similarity

Disulfide bond

326 ↔ 358

By similarity

Disulfide bond

351 ↔ 363

By similarity

Disulfide bond

368 ↔ 394

By similarity

Disulfide bond

376 ↔ 403

By similarity

Disulfide bond

378 ↔ 393

By similarity

Disulfide bond

390 ↔ 435

By similarity

Disulfide bond

428 ↔ 441

By similarity

Experimental info

Non-terminal residue

Sequences

Sequence

Length

Mass (Da)

Tools

Q10743 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: F75E0E8D6C88A7DD
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FASTA

544

60,445

        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

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References

[1]	"Molecular cloning of MADM: a catalytically active mammalian disintegrin-metalloprotease expressed in various cell types." Howard L., Mitchell S., Lu X., Griffiths S., Glynn P. Biochem. J. 317:45-50(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley. Tissue: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z48444 mRNA. Translation: CAA88359.1.
IPI	IPI01016310.
PIR	S52477.
UniGene	Rn.42924.
3D structure databases
ProteinModelPortal	Q10743.
SMR	Q10743. Positions 292-442.
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000021066.
Protein family/group databases
MEROPS	M12.210.
Proteomic databases
PaxDb	Q10743.
PRIDE	Q10743.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
UCSC	RGD:2032. rat.
Organism-specific databases
RGD	2032. Adam10.
Phylogenomic databases
eggNOG	NOG271989.
HOVERGEN	HBG050455.
InParanoid	Q10743.
Gene expression databases
Genevestigator	Q10743.
GermOnline	ENSRNOG00000015038. Rattus norvegicus.
Family and domain databases
Gene3D	3.40.390.10. 1 hit. 4.10.70.10. 1 hit.
InterPro	IPR027053. ADAM_10. IPR001762. Blood-coag_inhib_Disintegrin. IPR024079. MetalloPept_cat_dom. IPR001590. Peptidase_M12B. [Graphical view]
PANTHER	PTHR11905:SF4. PTHR11905:SF4. 1 hit.
Pfam	PF00200. Disintegrin. 1 hit. [Graphical view]
SMART	SM00050. DISIN. 1 hit. [Graphical view]
SUPFAM	SSF57552. Disintegrin. 1 hit.
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_RAT

Accession

Primary (citable) accession number: Q10743

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 28, 2003
Last sequence update:	November 1, 1996
Last modified:	April 3, 2013
This is version 106 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

Recent format changes

Overview of recent format changes

Recent format changes (XML)

Overview of recent format changes in the XML format

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents