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A disintegrin and metalloproteinase with thrombospondin motifs 4 (ADAM-TS 4) (ADAM-TS4) (ADAMTS-4) (EC 3.4.24.82) (Aggrecanase-1)

 ATS4_PONAB              Reviewed;         837 AA.
Q5RFQ8;
13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
21-DEC-2004, sequence version 1.
20-JUN-2018, entry version 74.
RecName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 4;
Short=ADAM-TS 4;
Short=ADAM-TS4;
Short=ADAMTS-4;
EC=3.4.24.82;
AltName: Full=Aggrecanase-1;
Flags: Precursor;
Name=ADAMTS4;
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Pongo.
NCBI_TaxID=9601;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
The German cDNA consortium;
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
-!- 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.
-!- 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:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000250|UniProtKB:O75173};
Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:O75173};
-!- SUBUNIT: Interacts with SRPX2. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix {ECO:0000250}.
-!- DOMAIN: The spacer domain and the TSP type-1 domains are important
for a tight interaction with the extracellular matrix.
-!- 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.
-!- PTM: The precursor is cleaved by a furin endopeptidase.
{ECO:0000250}.
-!- PTM: 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). {ECO:0000250}.
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EMBL; CR857094; CAH89399.1; -; mRNA.
UniGene; Pab.12192; -.
ProteinModelPortal; Q5RFQ8; -.
SMR; Q5RFQ8; -.
STRING; 9601.ENSPPYP00000000708; -.
MEROPS; M12.221; -.
PRIDE; Q5RFQ8; -.
eggNOG; KOG3538; Eukaryota.
eggNOG; ENOG410XPKZ; LUCA.
HOVERGEN; HBG004313; -.
InParanoid; Q5RFQ8; -.
Proteomes; UP000001595; Unplaced.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
Gene3D; 2.20.100.10; -; 1.
Gene3D; 3.40.390.10; -; 1.
InterPro; IPR006586; ADAM_Cys-rich.
InterPro; IPR010294; ADAM_spacer1.
InterPro; IPR024079; MetalloPept_cat_dom_sf.
InterPro; IPR001590; Peptidase_M12B.
InterPro; IPR002870; Peptidase_M12B_N.
InterPro; IPR000884; TSP1_rpt.
InterPro; IPR036383; TSP1_rpt_sf.
Pfam; PF05986; ADAM_spacer1; 1.
Pfam; PF01562; Pep_M12B_propep; 1.
Pfam; PF01421; Reprolysin; 1.
Pfam; PF00090; TSP_1; 1.
SMART; SM00608; ACR; 1.
SMART; SM00209; TSP1; 1.
SUPFAM; SSF82895; SSF82895; 1.
PROSITE; PS50215; ADAM_MEPRO; 1.
PROSITE; PS50092; TSP1; 1.
PROSITE; PS00142; ZINC_PROTEASE; 1.
2: Evidence at transcript level;
Cleavage on pair of basic residues; Complete proteome; Disulfide bond;
Extracellular matrix; Glycoprotein; Hydrolase; Metal-binding;
Metalloprotease; Protease; Reference proteome; Secreted; Signal; Zinc;
Zymogen.
SIGNAL 1 51 {ECO:0000255}.
PROPEP 52 212 {ECO:0000250}.
/FTId=PRO_0000239803.
CHAIN 213 837 A disintegrin and metalloproteinase with
thrombospondin motifs 4.
/FTId=PRO_0000239804.
DOMAIN 218 428 Peptidase M12B. {ECO:0000255|PROSITE-
ProRule:PRU00276}.
DOMAIN 437 519 Disintegrin.
DOMAIN 520 575 TSP type-1. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
REGION 686 837 Spacer. {ECO:0000250}.
MOTIF 192 199 Cysteine switch. {ECO:0000250}.
ACT_SITE 362 362 {ECO:0000255|PROSITE-ProRule:PRU00276,
ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 194 194 Zinc; in inhibited form. {ECO:0000250}.
METAL 361 361 Zinc; catalytic.
{ECO:0000250|UniProtKB:O75173}.
METAL 365 365 Zinc; catalytic.
{ECO:0000250|UniProtKB:O75173}.
METAL 371 371 Zinc; catalytic.
{ECO:0000250|UniProtKB:O75173}.
CARBOHYD 68 68 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 293 345 {ECO:0000250|UniProtKB:O75173}.
DISULFID 322 327 {ECO:0000250|UniProtKB:O75173}.
DISULFID 339 423 {ECO:0000250|UniProtKB:O75173}.
DISULFID 377 407 {ECO:0000250|UniProtKB:O75173}.
DISULFID 449 472 {ECO:0000250|UniProtKB:O75173}.
DISULFID 460 482 {ECO:0000250|UniProtKB:O75173}.
DISULFID 467 501 {ECO:0000250|UniProtKB:O75173}.
DISULFID 495 506 {ECO:0000250|UniProtKB:O75173}.
DISULFID 532 569 {ECO:0000250}.
DISULFID 536 574 {ECO:0000250}.
DISULFID 547 559 {ECO:0000250}.
SEQUENCE 837 AA; 90262 MW; 08F5E69F65CF6B4C CRC64;
MSQTGSHPGR GLAGRWLWGA QPCLLLPIVP LSWLVWLLLL LLASLLPSAR LASPLPREEE
IVFPEKLNGS VLPGSGAPAR LLCRLQAFGE TLLLELEHDS GVQVEGLTVQ YLGQAPELLG
GAEPGTYLTG TINGEPESVA SLHWDGGALL GVLQYRGAEL HLQPLEGGTP NSAGGPGAHI
LRRKSPASGQ GPMCNVKAPL GSPSPRPRRA KRFASLSRFV ETLVVADDKM AAFHGAGLKR
YLLTVMAAAA KAFKHPSIRN PVSLVVTRLV ILGSGEEGPQ VGPSAAQTLR SFCAWQRGLN
TPEDSDPDHF DTAILFTRQD LCGVSTCDTL GMADVGTVCD PARSCAIVED DGLQSAYTAA
HELGHVFNML HDNSKPCISL NGPLSTSRHV MAPVMAHVDP EEPWSPCSAR FITDFLDNGY
GHCLLDKPEA PLHLPVTFPG KDYDADRQCQ LTFGPDSRHC PQLPPPCAAL WCSGHLNGHA
MCQTKHSPWA DGTPCGPAQA CMGGRCLHMD QLQDFNIPQA GGWGPWGPWG DCSRTCGGGV
QFSSRDCTRP VPRNGGKYCE GRRTRFRSCN TEDCPTGSVL TFREEQCAAY NHCTDLFKSF
PGPMDWVPRY TGVAPQDQCK LTCQARALGY YYVLEPRVVD GTPCSPDSSS VCVQGRCIHA
GCDRIIGSKK KFDKCMVCGG DGSGCSKQSG SFRKFRYGYN NVVTIPTGAT HILVRQQGNP
GHRSIYLALK LPDGSYALNG EYTLMPSPTD VVLPGAISLR YSGATAASET LSGHGPLAQP
LTLQVLVAGN PQDARLRYSF FVPRPTPSTP HPTPQDWLHR RAQILEILRR RPWVGRK


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