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Q8BNJ2 (ATS4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 96. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
A disintegrin and metalloproteinase with thrombospondin motifs 4

Short name=ADAM-TS 4
Short name=ADAM-TS4
Short name=ADAMTS-4
EC=3.4.24.82
Alternative name(s):
Aggrecanase-1
Gene names
Name:Adamts4
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length833 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Cleaves aggrecan, a cartilage proteoglycan, and may be involved in its turnover. May play an important role in the destruction of aggrecan in arthritic diseases. Cleaves aggrecan at the '392-Glu-|-Ala-393' site By similarity.

Catalytic activity

Glutamyl endopeptidase; bonds cleaved include 370-Thr-Glu-Gly-Glu-|-Ala-Arg-Gly-Ser-377 in the interglobular domain of mammalian aggrecan.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subunit structure

Interacts with SRPX2 By similarity.

Subcellular location

Secretedextracellular spaceextracellular matrix By similarity.

Domain

The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix By similarity.

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.

Glycosylated. Can be O-fucosylated by POFUT2 on a serine or a threonine residue found within the consensus sequence C1-X(2)-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are the first and second cysteine residue of the repeat, respectively. Fucosylated repeats can then be further glycosylated by the addition of a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL. Fucosylation mediates the efficient secretion of ADAMTS family members. Also can be C-glycosylated with one or two mannose molecules on tryptophan residues within the consensus sequence W-X-X-W of the TPRs, and N-glycosylated. These other glycosylations can also facilitate secretion By similarity.

Sequence similarities

Contains 1 disintegrin domain.

Contains 1 peptidase M12B domain.

Contains 1 TSP type-1 domain.

Sequence caution

The sequence BAC38944.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4949 Potential
Propeptide50 – 208159 By similarity
PRO_0000029166
Chain209 – 833625A disintegrin and metalloproteinase with thrombospondin motifs 4
PRO_0000029167

Regions

Domain214 – 424211Peptidase M12B
Domain433 – 51583Disintegrin
Domain516 – 57156TSP type-1
Region682 – 833152Spacer
Motif188 – 1958Cysteine switch By similarity

Sites

Active site3581 By similarity
Metal binding1901Zinc; in inhibited form By similarity
Metal binding3571Zinc; catalytic By similarity
Metal binding3611Zinc; catalytic By similarity
Metal binding3671Zinc; catalytic By similarity

Amino acid modifications

Glycosylation631N-linked (GlcNAc...) Potential
Glycosylation2991N-linked (GlcNAc...) Potential
Disulfide bond289 ↔ 341 By similarity
Disulfide bond318 ↔ 323 By similarity
Disulfide bond335 ↔ 419 By similarity
Disulfide bond373 ↔ 403 By similarity
Disulfide bond445 ↔ 468 By similarity
Disulfide bond456 ↔ 478 By similarity
Disulfide bond463 ↔ 497 By similarity
Disulfide bond491 ↔ 502 By similarity
Disulfide bond528 ↔ 565 By similarity
Disulfide bond532 ↔ 570 By similarity
Disulfide bond543 ↔ 555 By similarity

Experimental info

Sequence conflict181Q → R in AAH27773. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q8BNJ2 [UniParc].

Last modified May 10, 2005. Version 2.
Checksum: 6512B9ED2617F3A4

FASTA83390,070
        10         20         30         40         50         60 
MSQMGLHPRR GLTGHWLQRF QPCLPLHTVQ WRRLLLLAFL LSLAWPASPL PREEEIVFPE 

        70         80         90        100        110        120 
KLNGSSILPG SGVPARLLYR LPAFGEMLLL ELEQDPGVQV EGLTVQYLGQ APEMLGGAEP 

       130        140        150        160        170        180 
GTYLTGTING DPESVASLHW DGGALLGVLQ YRGAELHLQP LEGGALNSAG GPGAHILRRK 

       190        200        210        220        230        240 
SPASSQGPMC TVKAPSGSPS PISRRTKRFA SLSRFVETLV VADDKMAAFH GTGLKRYLLT 

       250        260        270        280        290        300 
VMAAAAKAFK HPSIRNPVNL VVTRLVILGS GQEGPQVGPS AAQTLRSFCT WQRGLNTPND 

       310        320        330        340        350        360 
SDPDHFDTAI LFTRQDLCGV STCDTLGMAD VGTVCDPARS CAIVEDDGLQ SAFTAAHELG 

       370        380        390        400        410        420 
HVFNMLHDNS KPCTNLNGQG GSSRHVMAPV MAHVDPEEPW SPCSARFITD FLDNGYGHCL 

       430        440        450        460        470        480 
LDKPEAPLHL PATFPGKDYD ADRQCQLTFG PDSSHCPQLP PPCAALWCSG HLNGHAMCQT 

       490        500        510        520        530        540 
KHSPWADGTP CGSSQACMGG RCLHVDQLKD FNVPQAGGWG PWGPWGDCSR TCGGGVQFSS 

       550        560        570        580        590        600 
RDCTRPVPRN GGKYCEGRRT RFRSCNTENC PHGSALTFRE EQCAAYNHRT DLFKSFPGPM 

       610        620        630        640        650        660 
DWVPRYTGVA PRDQCKLTCQ ARALGYYYVL EPRVADGTPC SPDTSSVCVQ GRCIHAGCDR 

       670        680        690        700        710        720 
IIGSKKKFDK CMVCGGDGSR CSKQSGSFKK FRYGYSDVVT IPAGATHILV RQQGGSGLKS 

       730        740        750        760        770        780 
IYLALKLSDG SYALNGEYTL MPSPTDVVLP GAVSLRYSGA TAASETLSGH GPLAQPLTLQ 

       790        800        810        820        830 
VLVAGNPQNA RLRYSFFVPR PVPSTPRPPP QDWLQRRAEI LKILRKRPWA GRK 

« Hide

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
[2]"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].
Strain: FVB/N.
Tissue: Mammary tumor.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK083534 mRNA. Translation: BAC38944.1. Different initiation.
BC027773 mRNA. Translation: AAH27773.1.
RefSeqNP_766433.1. NM_172845.2.
UniGeneMm.491147.

3D structure databases

ProteinModelPortalQ8BNJ2.
SMRQ8BNJ2. Positions 210-801.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSM12.221.

PTM databases

PhosphoSiteQ8BNJ2.

Proteomic databases

PaxDbQ8BNJ2.
PRIDEQ8BNJ2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000111315; ENSMUSP00000106947; ENSMUSG00000006403.
GeneID240913.
KEGGmmu:240913.

Organism-specific databases

CTD9507.
MGIMGI:1339949. Adamts4.

Phylogenomic databases

eggNOGNOG271890.
GeneTreeENSGT00650000092972.
HOGENOMHOG000004799.
HOVERGENHBG004313.
InParanoidQ8BNJ2.
KOK07764.
OrthoDBEOG7WDN1M.

Gene expression databases

ArrayExpressQ8BNJ2.
BgeeQ8BNJ2.
GenevestigatorQ8BNJ2.

Family and domain databases

Gene3D3.40.390.10. 1 hit.
InterProIPR010294. ADAM_spacer1.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR013273. Peptidase_M12B_ADAM-TS.
IPR002870. Peptidase_M12B_N.
IPR000884. Thrombospondin_1_rpt.
[Graphical view]
PfamPF05986. ADAM_spacer1. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 1 hit.
[Graphical view]
PRINTSPR01857. ADAMTSFAMILY.
SMARTSM00209. TSP1. 1 hit.
[Graphical view]
SUPFAMSSF82895. SSF82895. 1 hit.
PROSITEPS50215. ADAM_MEPRO. 1 hit.
PS50092. TSP1. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio384802.
PROQ8BNJ2.
SOURCESearch...

Entry information

Entry nameATS4_MOUSE
AccessionPrimary (citable) accession number: Q8BNJ2
Secondary accession number(s): Q8K384
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: May 10, 2005
Last modified: April 16, 2014
This is version 96 of the entry and version 2 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