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Q9JLN6 (ADA28_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Disintegrin and metalloproteinase domain-containing protein 28

Short name=ADAM 28
EC=3.4.24.-
Alternative name(s):
Thymic epithelial cell-ADAM
Short name=TECADAM
Gene names
Name:Adam28
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length793 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May play a role in organogenesis and organ-specific functions such as thymic T-cell development.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

Strong expression in thymic epithelial cells and developmentally related tissues including the trachea, thyroid, lung and stomach, but not in lymphocytes. Expressed at high levels also in epididymis. In contrast with human is not expressed in immature or mature lymphocyte populations of thymocytes, lymph node, spleen, and bone marrow. Ref.2

Developmental stage

The expression patterns in adult and day 15.5 embryos are similar.

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

Pro-domain removal and maturation may be, at least in part, autocatalytic.

Sequence similarities

Contains 1 disintegrin domain.

Contains 1 EGF-like domain.

Contains 1 peptidase M12B domain.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: Q9JLN6-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9JLN6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     769-793: Missing.
Isoform 3 (identifier: Q9JLN6-3)

The sequence of this isoform differs from the canonical sequence as follows:
     769-771: TGR → DPN
     775-793: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Propeptide21 – 195175 By similarity
PRO_0000029132
Chain196 – 793598Disintegrin and metalloproteinase domain-containing protein 28
PRO_0000029133

Regions

Topological domain196 – 668473Extracellular Potential
Transmembrane669 – 68921Helical; Potential
Topological domain690 – 793104Cytoplasmic Potential
Domain206 – 402197Peptidase M12B
Domain410 – 49687Disintegrin
Domain628 – 66033EGF-like
Motif169 – 1768Cysteine switch By similarity
Compositional bias497 – 631135Cys-rich
Compositional bias760 – 7656Poly-Pro

Sites

Active site3431 By similarity
Metal binding1711Zinc; in inhibited form By similarity
Metal binding3421Zinc; catalytic By similarity
Metal binding3461Zinc; catalytic By similarity
Metal binding3521Zinc; catalytic By similarity

Amino acid modifications

Glycosylation911N-linked (GlcNAc...) Potential
Glycosylation2721N-linked (GlcNAc...) Potential
Glycosylation2771N-linked (GlcNAc...) Potential
Glycosylation5311N-linked (GlcNAc...) Potential
Glycosylation5511N-linked (GlcNAc...) Potential
Glycosylation6051N-linked (GlcNAc...) Potential
Glycosylation6311N-linked (GlcNAc...) Potential
Disulfide bond317 ↔ 397 By similarity
Disulfide bond357 ↔ 381 By similarity
Disulfide bond359 ↔ 364 By similarity
Disulfide bond468 ↔ 488 By similarity
Disulfide bond632 ↔ 642 By similarity
Disulfide bond636 ↔ 648 By similarity
Disulfide bond650 ↔ 659 By similarity

Natural variations

Alternative sequence769 – 79325Missing in isoform 2.
VSP_005488
Alternative sequence769 – 7713TGR → DPN in isoform 3.
VSP_005489
Alternative sequence775 – 79319Missing in isoform 3.
VSP_005490

Experimental info

Mutagenesis3431E → A: Abolishes prodomain removal. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 12, 2003. Version 3.
Checksum: 7715E71456D4403B

FASTA79388,671
        10         20         30         40         50         60 
MQQWSLLVVS FLLSPVPVSA IKELPKAKKY EVVYPIRLHP LRKRETQEPE PKETFETELR 

        70         80         90        100        110        120 
YKMTVNGKVA VLYLKKNNKL LAPDYSETYY NSSGNKVTTS PQIMDSCYYQ GHIVNEKVSA 

       130        140        150        160        170        180 
ASISTCQGLR GYISQGDEKY FIEPLSSENL DEQAHALFKD DSNEDQEKSN CGVDDALWLQ 

       190        200        210        220        230        240 
GLHQDVALPA TRLIKLNDGM VQEPKKYIEY YVVLDNGEFK KYNKNLAEIR KIVLEMANYI 

       250        260        270        280        290        300 
NMLYNKLDAH VALVGVEIWT DGDKIKITPD ANTTLENFSK WRGNDLLKRK HHDIAQLISS 

       310        320        330        340        350        360 
TDFSGSTVGL AFMSSMCSPY HSVGIVQDHS NYHLRVAGTM AHEMGHNLGM IHDYLSCKCP 

       370        380        390        400        410        420 
SEVCVMEQSL RFHMPTDFSS CSRVNYKQFL EEKLSHCLFN SPLPSDIIST PVCGNQLLEM 

       430        440        450        460        470        480 
NEDCDCGTPK ECTNKCCDAR TCKIKAGFQC ALGECCEKCQ LKKPGVVCRA AKDECDLPEV 

       490        500        510        520        530        540 
CDGKSSHCPG DRFRVNGSPC QNGHGYCLKG KCPTLQQQCM DMWGPGTKVA NTSCYKQNEG 

       550        560        570        580        590        600 
GTKYGYCHVE NGTHMPCKAK DAMCGKLFCE GGSGDLPWKG LTISFLTCKL FDPEDTSQGV 

       610        620        630        640        650        660 
DMVANGTKCG TNKVCINAEC VDMEKTYKSA NCSSKCKGHA VCDHELQCQC KEGWAPPDCE 

       670        680        690        700        710        720 
NSATVFHFSI VVGVLFPLAV IFVVVAIVIQ RQSARRKQRR VQRLPSTKDA KLHNQKCRPQ 

       730        740        750        760        770        780 
KVKDVQPQEM SQMKKLHVSD LPSEEPEPPP DVLITKPNFP PPPIPVSLTG RAKVPFVKTP 

       790 
HPFSQQIGRV YLK 

« Hide

Isoform 2 [UniParc].

Checksum: 6786AB68FD631A36
Show »

FASTA76885,833
Isoform 3 [UniParc].

Checksum: 93C42E7C92A20786
Show »

FASTA77486,458

References

« Hide 'large scale' references
[1]"Cloning and characterization of ADAM28: evidence for autocatalytic pro-domain removal and for cell surface localization of mature ADAM28."
Howard L., Maciewicz R.A., Blobel C.P.
Biochem. J. 348:21-27(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), CHARACTERIZATION, MUTAGENESIS OF GLU-343.
Tissue: Lung.
[2]"An ADAM family member with expression in thymic epithelial cells and related tissues."
Haidl I.D., Huber G., Eichmann K.
Gene 283:163-170(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), TISSUE SPECIFICITY.
Tissue: Thymus.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Olfactory epithelium.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF153350 mRNA. Translation: AAF71993.1.
AF163290 mRNA. Translation: AAM21935.1.
AF163291 mRNA. Translation: AAM21936.1.
AF163292 mRNA. Translation: AAM21937.1.
BC058782 mRNA. Translation: AAH58782.1.
RefSeqNP_001041640.1. NM_001048175.2.
NP_034212.1. NM_010082.2.
NP_899222.1. NM_183366.3.
UniGeneMm.117450.

3D structure databases

ProteinModelPortalQ9JLN6.
SMRQ9JLN6. Positions 201-665.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSM12.020.

PTM databases

PhosphoSiteQ9JLN6.

Proteomic databases

PaxDbQ9JLN6.
PRIDEQ9JLN6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000022642; ENSMUSP00000022642; ENSMUSG00000014725. [Q9JLN6-1]
ENSMUST00000111072; ENSMUSP00000106701; ENSMUSG00000014725. [Q9JLN6-3]
GeneID13522.
KEGGmmu:13522.
UCSCuc007ult.1. mouse. [Q9JLN6-3]
uc007ulv.1. mouse. [Q9JLN6-1]

Organism-specific databases

CTD10863.
MGIMGI:105988. Adam28.

Phylogenomic databases

eggNOGNOG277164.
GeneTreeENSGT00740000114848.
HOGENOMHOG000230883.
HOVERGENHBG006978.
InParanoidQ9JLN6.
KOK08614.
OMATSPQIMD.
OrthoDBEOG7PGDQ7.
PhylomeDBQ9JLN6.
TreeFamTF314733.

Gene expression databases

ArrayExpressQ9JLN6.
BgeeQ9JLN6.
CleanExMM_ADAM28.
GenevestigatorQ9JLN6.

Family and domain databases

Gene3D3.40.390.10. 1 hit.
4.10.70.10. 1 hit.
InterProIPR006586. ADAM_Cys-rich.
IPR001762. Blood-coag_inhib_Disintegrin.
IPR018358. Disintegrin_CS.
IPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR002870. Peptidase_M12B_N.
[Graphical view]
PfamPF08516. ADAM_CR. 1 hit.
PF00200. Disintegrin. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
[Graphical view]
PRINTSPR00289. DISINTEGRIN.
SMARTSM00608. ACR. 1 hit.
SM00050. DISIN. 1 hit.
SM00181. EGF. 1 hit.
[Graphical view]
SUPFAMSSF57552. SSF57552. 1 hit.
PROSITEPS50215. ADAM_MEPRO. 1 hit.
PS00427. DISINTEGRIN_1. 1 hit.
PS50214. DISINTEGRIN_2. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio284092.
PMAP-CutDBQ9JLN6.
PROQ9JLN6.
SOURCESearch...

Entry information

Entry nameADA28_MOUSE
AccessionPrimary (citable) accession number: Q9JLN6
Secondary accession number(s): Q5D070, Q8K5D2, Q8K5D3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: February 12, 2003
Last modified: April 16, 2014
This is version 120 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot