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Q5RFQ8

- ATS4_PONAB

UniProt

Q5RFQ8 - ATS4_PONAB

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Protein

A disintegrin and metalloproteinase with thrombospondin motifs 4

Gene
ADAMTS4
Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at transcript leveli

Functioni

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.

Catalytic activityi

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

Cofactori

Binds 1 zinc ion per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi194 – 1941Zinc; in inhibited form By similarity
Metal bindingi361 – 3611Zinc; catalytic By similarity
Active sitei362 – 3621 By similarity
Metal bindingi365 – 3651Zinc; catalytic By similarity
Metal bindingi371 – 3711Zinc; catalytic By similarity

GO - Molecular functioni

  1. metalloendopeptidase activity Source: InterPro
  2. zinc ion binding Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM12.221.

Names & Taxonomyi

Protein namesi
Recommended name:
A disintegrin and metalloproteinase with thrombospondin motifs 4 (EC:3.4.24.82)
Short name:
ADAM-TS 4
Short name:
ADAM-TS4
Short name:
ADAMTS-4
Alternative name(s):
Aggrecanase-1
Gene namesi
Name:ADAMTS4
OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic identifieri9601 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
ProteomesiUP000001595: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. proteinaceous extracellular matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 5151 Reviewed predictionAdd
BLAST
Propeptidei52 – 212161 By similarityPRO_0000239803Add
BLAST
Chaini213 – 837625A disintegrin and metalloproteinase with thrombospondin motifs 4PRO_0000239804Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi68 – 681N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi293 ↔ 345 By similarity
Disulfide bondi322 ↔ 327 By similarity
Disulfide bondi339 ↔ 423 By similarity
Disulfide bondi377 ↔ 407 By similarity
Disulfide bondi449 ↔ 472 By similarity
Disulfide bondi460 ↔ 482 By similarity
Disulfide bondi467 ↔ 501 By similarity
Disulfide bondi495 ↔ 506 By similarity
Disulfide bondi532 ↔ 569 By similarity
Disulfide bondi536 ↔ 574 By similarity
Disulfide bondi547 ↔ 559 By similarity

Post-translational modificationi

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.

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Zymogen

Interactioni

Subunit structurei

Interacts with SRPX2 By similarity.

Structurei

3D structure databases

ProteinModelPortaliQ5RFQ8.
SMRiQ5RFQ8. Positions 215-507.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini218 – 428211Peptidase M12BAdd
BLAST
Domaini437 – 51983DisintegrinAdd
BLAST
Domaini520 – 57556TSP type-1Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni686 – 837152Spacer By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi192 – 1998Cysteine switch By similarity

Domaini

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

Sequence similaritiesi

Contains 1 disintegrin domain.
Contains 1 TSP type-1 domain.

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG004313.
InParanoidiQ5RFQ8.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR010294. ADAM_spacer1.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR013273. Peptidase_M12B_ADAM-TS.
IPR002870. Peptidase_M12B_N.
IPR000884. Thrombospondin_1_rpt.
[Graphical view]
PfamiPF05986. ADAM_spacer1. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 1 hit.
[Graphical view]
PRINTSiPR01857. ADAMTSFAMILY.
SMARTiSM00209. TSP1. 1 hit.
[Graphical view]
SUPFAMiSSF82895. SSF82895. 1 hit.
PROSITEiPS50215. ADAM_MEPRO. 1 hit.
PS50092. TSP1. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q5RFQ8-1 [UniParc]FASTAAdd to Basket

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MSQTGSHPGR GLAGRWLWGA QPCLLLPIVP LSWLVWLLLL LLASLLPSAR    50
LASPLPREEE IVFPEKLNGS VLPGSGAPAR LLCRLQAFGE TLLLELEHDS 100
GVQVEGLTVQ YLGQAPELLG GAEPGTYLTG TINGEPESVA SLHWDGGALL 150
GVLQYRGAEL HLQPLEGGTP NSAGGPGAHI LRRKSPASGQ GPMCNVKAPL 200
GSPSPRPRRA KRFASLSRFV ETLVVADDKM AAFHGAGLKR YLLTVMAAAA 250
KAFKHPSIRN PVSLVVTRLV ILGSGEEGPQ VGPSAAQTLR SFCAWQRGLN 300
TPEDSDPDHF DTAILFTRQD LCGVSTCDTL GMADVGTVCD PARSCAIVED 350
DGLQSAYTAA HELGHVFNML HDNSKPCISL NGPLSTSRHV MAPVMAHVDP 400
EEPWSPCSAR FITDFLDNGY GHCLLDKPEA PLHLPVTFPG KDYDADRQCQ 450
LTFGPDSRHC PQLPPPCAAL WCSGHLNGHA MCQTKHSPWA DGTPCGPAQA 500
CMGGRCLHMD QLQDFNIPQA GGWGPWGPWG DCSRTCGGGV QFSSRDCTRP 550
VPRNGGKYCE GRRTRFRSCN TEDCPTGSVL TFREEQCAAY NHCTDLFKSF 600
PGPMDWVPRY TGVAPQDQCK LTCQARALGY YYVLEPRVVD GTPCSPDSSS 650
VCVQGRCIHA GCDRIIGSKK KFDKCMVCGG DGSGCSKQSG SFRKFRYGYN 700
NVVTIPTGAT HILVRQQGNP GHRSIYLALK LPDGSYALNG EYTLMPSPTD 750
VVLPGAISLR YSGATAASET LSGHGPLAQP LTLQVLVAGN PQDARLRYSF 800
FVPRPTPSTP HPTPQDWLHR RAQILEILRR RPWVGRK 837
Length:837
Mass (Da):90,262
Last modified:December 21, 2004 - v1
Checksum:i08F5E69F65CF6B4C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR857094 mRNA. Translation: CAH89399.1.
UniGeneiPab.12192.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR857094 mRNA. Translation: CAH89399.1 .
UniGenei Pab.12192.

3D structure databases

ProteinModelPortali Q5RFQ8.
SMRi Q5RFQ8. Positions 215-507.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi M12.221.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG004313.
InParanoidi Q5RFQ8.

Family and domain databases

Gene3Di 3.40.390.10. 1 hit.
InterProi IPR010294. ADAM_spacer1.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR013273. Peptidase_M12B_ADAM-TS.
IPR002870. Peptidase_M12B_N.
IPR000884. Thrombospondin_1_rpt.
[Graphical view ]
Pfami PF05986. ADAM_spacer1. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 1 hit.
[Graphical view ]
PRINTSi PR01857. ADAMTSFAMILY.
SMARTi SM00209. TSP1. 1 hit.
[Graphical view ]
SUPFAMi SSF82895. SSF82895. 1 hit.
PROSITEi PS50215. ADAM_MEPRO. 1 hit.
PS50092. TSP1. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. The German cDNA consortium
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney.

Entry informationi

Entry nameiATS4_PONAB
AccessioniPrimary (citable) accession number: Q5RFQ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: December 21, 2004
Last modified: May 14, 2014
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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