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Reviewed, UniProtKB/Swiss-Prot Q9P2N4 (ATS9_HUMAN)

Last modified September 2, 2008. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    A disintegrin and metalloproteinase with thrombospondin motifs 9
      Short name=ADAMTS-9
      Short name=ADAM-TS 9
      Short name=ADAM-TS9
    EC=3.4.24.-
Gene names
Name: ADAMTS9
Synonyms: KIAA1312
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1935 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Cleaves the large aggregating proteoglycans, aggrecan and versican.

Catalytic activity

Cleaves aggrecan at the 1838-Glu-|-Ala-1839 site and versican at the 1428-Glu-|-Ala-1429 site.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subcellular location

Secretedextracellular spaceextracellular matrixBy similarity.

Tissue specificity

Highly expressed in all fetal tissues. Expressed in a number of adult tissues with highest expression in heart, placenta and skeletal muscle.

Domain

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

The ancillary domains, including the TSRs domain, are required for specific extracellular localization and for its versicanase and aggrecanase activities.

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.

Sequence similarities

Contains 1 disintegrin domain.

Contains 1 GON domain.

Contains 1 peptidase M12B domain.

Contains 15 TSP type-1 domains.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9P2N4-3)

Also known as: ADAMTS-9B;

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: Q9P2N4-1)

Also known as: Long;

The sequence of this isoform differs from the canonical sequence as follows:
     1624-1629: CSVTCG → VPSWEL
     1630-1935: Missing.
Notes: May result from the retention of an intron in the cDNA leading to a prematurate stop codon.
Isoform 3 (identifier: Q9P2N4-2)

Also known as: Short;

The sequence of this isoform differs from the canonical sequence as follows:
     1064-1072: CLVTCGKGH → VRWEGCYFP
     1073-1935: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Signal peptide1 – 1818 Potential
Propeptide19 – 287269
Chain288 – 19351648A disintegrin and metalloproteinase with thrombospondin motifs 9

Regions

Domain293 – 499207Peptidase M12B
Domain509 – 58779Disintegrin
Domain588 – 64356TSP type-1 1
Domain878 – 93659TSP type-1 2
Domain939 – 99759TSP type-1 3
Domain998 – 104952TSP type-1 4
Domain1052 – 110958TSP type-1 5
Domain1110 – 116657TSP type-1 6
Domain1182 – 124059TSP type-1 7
Domain1241 – 129656TSP type-1 8
Domain1328 – 137952TSP type-1 9
Domain1382 – 144059TSP type-1 10
Domain1441 – 149454TSP type-1 11
Domain1497 – 155559TSP type-1 12
Domain1556 – 161156TSP type-1 13
Domain1612 – 167665TSP type-1 14
Domain1677 – 173458TSP type-1 15
Domain1735 – 1935201GON
Region753 – 877125Spacer
Motif221 – 2288Cysteine switch By similarity
Compositional bias88 – 969Poly-Ser
Compositional bias644 – 752109Cys-rich

Sites

Active site4351 By similarity
Metal binding2231Zinc; in inhibited form By similarity
Metal binding4341Zinc; catalytic By similarity
Metal binding4381Zinc; catalytic By similarity
Metal binding4441Zinc; catalytic By similarity

Amino acid modifications

Glycosylation1121N-linked (GlcNAc...) Potential
Glycosylation1351N-linked (GlcNAc...) Potential
Glycosylation2711N-linked (GlcNAc...) Potential
Glycosylation7491N-linked (GlcNAc...) Potential
Glycosylation8401N-linked (GlcNAc...) Potential
Glycosylation12131N-linked (GlcNAc...) Potential
Glycosylation12671N-linked (GlcNAc...) Potential
Glycosylation17881N-linked (GlcNAc...) Potential
Glycosylation18061N-linked (GlcNAc...) Potential
Disulfide bond412 ↔ 494 By similarity
Disulfide bond450 ↔ 478 By similarity
Disulfide bond600 ↔ 637 By similarity
Disulfide bond604 ↔ 642 By similarity
Disulfide bond615 ↔ 627 By similarity
Disulfide bond890 ↔ 931 By similarity
Disulfide bond894 ↔ 935 By similarity
Disulfide bond904 ↔ 918 By similarity
Disulfide bond1250 ↔ 1290 By similarity
Disulfide bond1254 ↔ 1295 By similarity
Disulfide bond1265 ↔ 1278 By similarity
Disulfide bond1624 ↔ 1670 By similarity
Disulfide bond1628 ↔ 1675 By similarity
Disulfide bond1639 ↔ 1659 By similarity

Natural variations

Alternative sequence1064 – 10729CLVTCGKGH → VRWEGCYFP in isoform 3.
Alternative sequence1073 – 1935863Missing in isoform 3.
Alternative sequence1624 – 16296CSVTCG → VPSWEL in isoform 2.
Alternative sequence1630 – 1935306Missing in isoform 2.

Experimental info

Sequence conflict461S → G in AAF89106. Ref.1
Sequence conflict961P → S in AAF89106. Ref.1
Sequence conflict1821D → G in AAO15765. Ref.2
Sequence conflict3671F → L in AAF89106. Ref.1
Sequence conflict11171V → G in BAA92550. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (ADAMTS-9B) [UniParc].

Last modified June 16, 2003. Version 3.
Checksum: FD3D51E88300A3C6

FASTA1,935216,557
        10         20         30         40         50         60 
MQFVSWATLL TLLVRDLAEM GSPDAAAAVR KDRLHPRQVK LLETLSEYEI VSPIRVNALG 

        70         80         90        100        110        120 
EPFPTNVHFK RTRRSINSAT DPWPAFASSS SSSTSPQAHY RLSAFGQQFL FNLTANAGFI 

       130        140        150        160        170        180 
APLFTVTLLG TPGVNQTKFY SEEEAELKHC FYKGYVNTNS EHTAVISLCS GMLGTFRSHD 

       190        200        210        220        230        240 
GDYFIEPLQS MDEQEDEEEQ NKPHIIYRRS APQREPSTGR HACDTSEHKN RHSKDKKKTR 

       250        260        270        280        290        300 
ARKWGERINL AGDVAALNSG LATEAFSAYG NKTDNTREKR THRRTKRFLS YPRFVEVLVV 

       310        320        330        340        350        360 
ADNRMVSYHG ENLQHYILTL MSIVASIYKD PSIGNLINIV IVNLIVIHNE QDGPSISFNA 

       370        380        390        400        410        420 
QTTLKNFCQW QHSKNSPGGI HHDTAVLLTR QDICRAHDKC DTLGLAELGT ICDPYRSCSI 

       430        440        450        460        470        480 
SEDSGLSTAF TIAHELGHVF NMPHDDNNKC KEEGVKSPQH VMAPTLNFYT NPWMWSKCSR 

       490        500        510        520        530        540 
KYITEFLDTG YGECLLNEPE SRPYPLPVQL PGILYNVNKQ CELIFGPGSQ VCPYMMQCRR 

       550        560        570        580        590        600 
LWCNNVNGVH KGCRTQHTPW ADGTECEPGK HCKYGFCVPK EMDVPVTDGS WGSWSPFGTC 

       610        620        630        640        650        660 
SRTCGGGIKT AIRECNRPEP KNGGKYCVGR RMKFKSCNTE PCLKQKRDFR DEQCAHFDGK 

       670        680        690        700        710        720 
HFNINGLLPN VRWVPKYSGI LMKDRCKLFC RVAGNTAYYQ LRDRVIDGTP CGQDTNDICV 

       730        740        750        760        770        780 
QGLCRQAGCD HVLNSKARRD KCGVCGGDNS SCKTVAGTFN TVHYGYNTVV RIPAGATNID 

       790        800        810        820        830        840 
VRQHSFSGET DDDNYLALSS SKGEFLLNGN FVVTMAKREI RIGNAVVEYS GSETAVERIN 

       850        860        870        880        890        900 
STDRIEQELL LQVLSVGKLY NPDVRYSFNI PIEDKPQQFY WNSHGPWQAC SKPCQGERKR 

       910        920        930        940        950        960 
KLVCTRESDQ LTVSDQRCDR LPQPGHITEP CGTDCDLRWH VASRSECSAQ CGLGYRTLDI 

       970        980        990       1000       1010       1020 
YCAKYSRLDG KTEKVDDGFC SSHPKPSNRE KCSGECNTGG WRYSAWTECS KSCDGGTQRR 

      1030       1040       1050       1060       1070       1080 
RAICVNTRND VLDDSKCTHQ EKVTIQRCSE FPCPQWKSGD WSECLVTCGK GHKHRQVWCQ 

      1090       1100       1110       1120       1130       1140 
FGEDRLNDRM CDPETKPTSM QTCQQPECAS WQAGPWVQCS VTCGQGYQLR AVKCIIGTYM 

      1150       1160       1170       1180       1190       1200 
SVVDDNDCNA ATRPTDTQDC ELPSCHPPPA APETRRSTYS APRTQWRFGS WTPCSATCGK 

      1210       1220       1230       1240       1250       1260 
GTRMRYVSCR DENGSVADES ACATLPRPVA KEECSVTPCG QWKALDWSSC SVTCGQGRAT 

      1270       1280       1290       1300       1310       1320 
RQVMCVNYSD HVIDRSECDQ DYIPETDQDC SMSPCPQRTP DSGLAQHPFQ NEDYRPRSAS 

      1330       1340       1350       1360       1370       1380 
PSRTHVLGGN QWRTGPWGAC SSTCAGGSQR RVVVCQDENG YTANDCVERI KPDEQRACES 

      1390       1400       1410       1420       1430       1440 
GPCPQWAYGN WGECTKLCGG GIRTRLVVCQ RSNGERFPDL SCEILDKPPD REQCNTHACP 

      1450       1460       1470       1480       1490       1500 
HDAAWSTGPW SSCSVSCGRG HKQRNVYCMA KDGSHLESDY CKHLAKPHGH RKCRGGRCPK 

      1510       1520       1530       1540       1550       1560 
WKAGAWSQCS VSCGRGVQQR HVGCQIGTHK IARETECNPY TRPESERDCQ GPRCPLYTWR 

      1570       1580       1590       1600       1610       1620 
AEEWQECTKT CGEGSRYRKV VCVDDNKNEV HGARCDVSKR PVDRESCSLQ PCEYVWITGE 

      1630       1640       1650       1660       1670       1680 
WSECSVTCGK GYKQRLVSCS EIYTGKENYE YSYQTTINCP GTQPPSVHPC YLRECPVSAT 

      1690       1700       1710       1720       1730       1740 
WRVGNWGSCS VSCGVGVMQR SVQCLTNEDQ PSHLCHTDLK PEERKTCRNV YNCELPQNCK 

      1750       1760       1770       1780       1790       1800 
EVKRLKGASE DGEYFLMIRG KLLKIFCAGM HSDHPKEYVT LVHGDSENFS EVYGHRLHNP 

      1810       1820       1830       1840       1850       1860 
TECPYNGSRR DDCQCRKDYT AAGFSSFQKI RIDLTSMQII TTDLQFARTS EGHPVPFATA 

      1870       1880       1890       1900       1910       1920 
GDCYSAAKCP QGRFSINLYG TGLSLTESAR WISQGNYAVS DIKKSPDGTR VVGKCGGYCG 

      1930 
KCTPSSGTGL EVRVL 

« Hide

Isoform 2 (Long) [UniParc].

Checksum: 5227DFD03ED67249
Show »

1,629182,732
Isoform 3 (Short) [UniParc].

Checksum: 8B9E86DFA0B1300A
Show »

1,072120,727

References

« Hide 'large scale' references
[1]"ADAMTS 9, a novel member of the ADAM-TS/Metallospondin gene family."
Clark M.E., Kelner G.S., Turbeville L.A., Boyer A., Arden K.A., Maki R.A.
Genomics 67:343-350(2000) [PubMed: 10936055] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Tissue: Fetus.
[2]"Characterization of ADAMTS-9 and ADAMTS-20 as a distinct ADAMTS subfamily related to Caenorhabditis elegans GON-1."
Somerville R.P., Longpre J.-M., Jungers K.A., Engle J.M., Ross M., Evanko S., Wight T.N., Leduc R., Apte S.S.
J. Biol. Chem. 278:9503-9513(2003) [PubMed: 12514189] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
[3]"Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
DNA Res. 7:65-73(2000) [PubMed: 10718198] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 159-1935 (ISOFORM 2).
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

AF261918 mRNA. Translation: AAF89106.1.
AF488803 mRNA. Translation: AAO15765.1.
AB037733 mRNA. Translation: BAA92550.1.