ADAM 10 precursor - Rattus norvegicus (Rat)

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Reviewed, UniProtKB/Swiss-Prot Q10743 (ADA10_RAT)

Last modified September 2, 2008. Version 71. History...

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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 names

Recommended name:
    ADAM 10
    EC=3.4.24.81
Alternative name(s):
    A disintegrin and metalloproteinase domain 10
    Mammalian disintegrin-metalloprotease
    Kuzbanian protein homolog
    CD_antigen=CD156c

Gene names

Name:	Adam10
Synonyms:	Madm

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

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

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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.

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General annotation (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.
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 process	Notch signaling pathway
Cellular component	Membrane
Domain	SH3-binding Transmembrane
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Cleavage on pair of basic residues Glycoprotein Zymogen
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 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 nucleus Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	metallopeptidase activity Inferred from sequence or structural similarity. Source: UniProtKB 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...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Molecule processing

Propeptide

‹1 – 9

›9

Potential

Chain

10 – 544

535

ADAM 10

Regions

Topological domain

10 – 468

459

Extracellular Potential

Transmembrane

469 – 492

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

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

Experimental info

Non-terminal residue

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Sequences

Sequence

Length

Mass (Da)

Tools

Q10743-1 [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: 8694785] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Brain.

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Cross-references

Sequence databases
	Z48444 mRNA. Translation: CAA88359.1.
PIR	S52477.
UniGene	Rn.42924
3D structure databases
HSSP	HSSP built from PDB template 1FVL based on UniProtKB P18619.
SMR	Q10743. Positions 292-442.
ModBase	Search...
Protein family/group databases
MEROPS	M12.210.
Genome annotation databases
Ensembl	ENSRNOG00000015038. Rattus norvegicus. [Contig view]
Organism-specific databases
RGD	2032. Adam10.
Phylogenomic databases
HOVERGEN	Q10743.
Gene expression databases
ArrayExpress	Q10743.
GermOnline	ENSRNOG00000015038. Rattus norvegicus.
Family and domain databases
InterPro	IPR001762. Blood-coag_inhib_Disintegrin. IPR001818. Pept_M10A_M12B. IPR006025. Pept_M_Zn_BS. IPR001590. Peptidase_M12B. [Graphical view]
Gene3D	G3DSA:4.10.70.10. Blood-coag_inhib_Disintegrin. 1 hit.
Pfam	PF00200. Disintegrin. 1 hit. PF01421. Reprolysin. 1 hit. [Graphical view]
ProDom	PD000664. Disintegrin. 1 hit. [Graphical view] [Entries sharing at least one domain]
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]
BLOCKS	Search...
Other Resources
ProtoNet	Search...

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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:	September 2, 2008
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Recent format changes

Overview of recent format changes

Recent format changes (XML)

Overview of recent format changes in the XML format

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Keywords

Gene Ontology (GO)

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents