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Q9UKP4 (ATS7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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 7

Short name=ADAM-TS 7
Short name=ADAM-TS7
Short name=ADAMTS-7
EC=3.4.24.-
Alternative name(s):
COMPase
Gene names
Name:ADAMTS7
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1686 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Metalloprotease that may play a role in the degradation of COMP. Ref.1

Cofactor

Binds 1 zinc ion per subunit By similarity. Ref.1

Subunit structure

Interacts with COMP. Ref.1

Subcellular location

Secretedextracellular spaceextracellular matrix By similarity. Note: Also found associated with the external cell surface By similarity.

Tissue specificity

Expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Detected in meniscus, bone, tendon, cartilage, synovium, fat and ligaments. Ref.1 Ref.4

Induction

Up-regulated in articular cartilage and synovium from arthritis patients. Ref.1

Domain

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.

Post-translational modification

N-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. N- and C-glycosylations can also facilitate secretion. O-glycosylated proteoglycan. Contains chondroitin sulfate. Ref.4

May be cleaved by a furin endopeptidase By similarity. The precursor is sequentially processed. Ref.4

Sequence similarities

Contains 1 disintegrin domain.

Contains 1 peptidase M12B domain.

Contains 1 PLAC domain.

Contains 8 TSP type-1 domains.

Biophysicochemical properties

pH dependence:

Optimum pH is between 7.5 and 9.5.

Sequence caution

The sequence AAD56358.1 differs from that shown. Reason: Probable cloning artifact.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Potential
Propeptide28 – 236209
PRO_0000029176
Chain237 – 16861450A disintegrin and metalloproteinase with thrombospondin motifs 7
PRO_0000029177

Regions

Domain242 – 452211Peptidase M12B
Domain462 – 53776Disintegrin
Domain538 – 59356TSP type-1 1
Domain821 – 88060TSP type-1 2
Domain881 – 94060TSP type-1 3
Domain942 – 99554TSP type-1 4
Domain1411 – 145949TSP type-1 5
Domain1462 – 152261TSP type-1 6
Domain1523 – 156745TSP type-1 7
Domain1569 – 162961TSP type-1 8
Domain1632 – 167241PLAC
Region698 – 809112Spacer
Motif202 – 2098Cysteine switch By similarity
Compositional bias595 – 697103Cys-rich

Sites

Active site3891 By similarity
Metal binding2041Zinc; in inhibited form By similarity
Metal binding3881Zinc; catalytic By similarity
Metal binding3921Zinc; catalytic By similarity
Metal binding3981Zinc; catalytic By similarity

Amino acid modifications

Glycosylation941N-linked (GlcNAc...) Potential
Glycosylation6931N-linked (GlcNAc...) Potential
Glycosylation7781N-linked (GlcNAc...) Potential
Disulfide bond318 ↔ 372 By similarity
Disulfide bond347 ↔ 354 By similarity
Disulfide bond366 ↔ 447 By similarity
Disulfide bond405 ↔ 431 By similarity
Disulfide bond474 ↔ 497 By similarity
Disulfide bond485 ↔ 503 By similarity
Disulfide bond492 ↔ 522 By similarity
Disulfide bond516 ↔ 527 By similarity
Disulfide bond550 ↔ 587 By similarity
Disulfide bond554 ↔ 592 By similarity
Disulfide bond565 ↔ 577 By similarity

Natural variations

Natural variant2141S → P.
Corresponds to variant rs3825807 [ dbSNP | Ensembl ].
VAR_046112
Natural variant3071T → M. Ref.2
Corresponds to variant rs2127898 [ dbSNP | Ensembl ].
VAR_046113
Natural variant13191T → A. Ref.1
Corresponds to variant rs11630236 [ dbSNP | Ensembl ].
VAR_046114
Natural variant14141G → S. Ref.1
Corresponds to variant rs2929155 [ dbSNP | Ensembl ].
VAR_046115
Natural variant15831G → A. Ref.1
Corresponds to variant rs7495616 [ dbSNP | Ensembl ].
VAR_046116

Experimental info

Sequence conflict6421E → K in AAD56358. Ref.1
Sequence conflict11011H → R in AAQ94616. Ref.2
Sequence conflict13641S → T in AAQ94616. Ref.2
Sequence conflict14791G → D in AAQ94616. Ref.2
Sequence conflict15111P → H in AAQ94616. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9UKP4 [UniParc].

Last modified September 2, 2008. Version 2.
Checksum: AB38264B8E8DB740

FASTA1,686184,095
        10         20         30         40         50         60 
MPGGPSPRSP APLLRPLLLL LCALAPGAPG PAPGRATEGR AALDIVHPVR VDAGGSFLSY 

        70         80         90        100        110        120 
ELWPRALRKR DVSVRRDAPA FYELQYRGRE LRFNLTANQH LLAPGFVSET RRRGGLGRAH 

       130        140        150        160        170        180 
IRAHTPACHL LGEVQDPELE GGLAAISACD GLKGVFQLSN EDYFIEPLDS APARPGHAQP 

       190        200        210        220        230        240 
HVVYKRQAPE RLAQRGDSSA PSTCGVQVYP ELESRRERWE QRQQWRRPRL RRLHQRSVSK 

       250        260        270        280        290        300 
EKWVETLVVA DAKMVEYHGQ PQVESYVLTI MNMVAGLFHD PSIGNPIHIT IVRLVLLEDE 

       310        320        330        340        350        360 
EEDLKITHHA DNTLKSFCKW QKSINMKGDA HPLHHDTAIL LTRKDLCAAM NRPCETLGLS 

       370        380        390        400        410        420 
HVAGMCQPHR SCSINEDTGL PLAFTVAHEL GHSFGIQHDG SGNDCEPVGK RPFIMSPQLL 

       430        440        450        460        470        480 
YDAAPLTWSR CSRQYITRFL DRGWGLCLDD PPAKDIIDFP SVPPGVLYDV SHQCRLQYGA 

       490        500        510        520        530        540 
YSAFCEDMDN VCHTLWCSVG TTCHSKLDAA VDGTRCGENK WCLSGECVPV GFRPEAVDGG 

       550        560        570        580        590        600 
WSGWSAWSIC SRSCGMGVQS AERQCTQPTP KYKGRYCVGE RKRFRLCNLQ ACPAGRPSFR 

       610        620        630        640        650        660 
HVQCSHFDAM LYKGQLHTWV PVVNDVNPCE LHCRPANEYF AEKLRDAVVD GTPCYQVRAS 

       670        680        690        700        710        720 
RDLCINGICK NVGCDFEIDS GAMEDRCGVC HGNGSTCHTV SGTFEEAEGL GYVDVGLIPA 

       730        740        750        760        770        780 
GAREIRIQEV AEAANFLALR SEDPEKYFLN GGWTIQWNGD YQVAGTTFTY ARRGNWENLT 

       790        800        810        820        830        840 
SPGPTKEPVW IQLLFQESNP GVHYEYTIHR EAGGHDEVPP PVFSWHYGPW TKCTVTCGRG 

       850        860        870        880        890        900 
VQRQNVYCLE RQAGPVDEEH CDPLGRPDDQ QRKCSEQPCP ARWWAGEWQL CSSSCGPGGL 

       910        920        930        940        950        960 
SRRAVLCIRS VGLDEQSALE PPACEHLPRP PTETPCNRHV PCPATWAVGN WSQCSVTCGE 

       970        980        990       1000       1010       1020 
GTQRRNVLCT NDTGVPCDEA QQPASEVTCS LPLCRWPLGT LGPEGSGSGS SSHELFNEAD 

      1030       1040       1050       1060       1070       1080 
FIPHHLAPRP SPASSPKPGT MGNAIEEEAP ELDLPGPVFV DDFYYDYNFI NFHEDLSYGP 

      1090       1100       1110       1120       1130       1140 
SEEPDLDLAG TGDRTPPPHS HPAAPSTGSP VPATEPPAAK EEGVLGPWSP SPWPSQAGRS 

      1150       1160       1170       1180       1190       1200 
PPPPSEQTPG NPLINFLPEE DTPIGAPDLG LPSLSWPRVS TDGLQTPATP ESQNDFPVGK 

      1210       1220       1230       1240       1250       1260 
DSQSQLPPPW RDRTNEVFKD DEEPKGRGAP HLPPRPSSTL PPLSPVGSTH SSPSPDVAEL 

      1270       1280       1290       1300       1310       1320 
WTGGTVAWEP ALEGGLGPVD SELWPTVGVA SLLPPPIAPL PEMKVRDSSL EPGTPSFPTP 

      1330       1340       1350       1360       1370       1380 
GPGSWDLQTV AVWGTFLPTT LTGLGHMPEP ALNPGPKGQP ESLSPEVPLS SRLLSTPAWD 

      1390       1400       1410       1420       1430       1440 
SPANSHRVPE TQPLAPSLAE AGPPADPLVV RNAGWQAGNW SECSTTCGLG AVWRPVRCSS 

      1450       1460       1470       1480       1490       1500 
GRDEDCAPAG RPQPARRCHL RPCATWHSGN WSKCSRSCGG GSSVRDVQCV DTRDLRPLRP 

      1510       1520       1530       1540       1550       1560 
FHCQPGPAKP PAHRPCGAQP CLSWYTSSWR ECSEACGGGE QQRLVTCPEP GLCEEALRPN 

      1570       1580       1590       1600       1610       1620 
TTRPCNTHPC TQWVVGPWGQ CSGPCGGGVQ RRLVKCVNTQ TGLPEEDSDQ CGHEAWPESS 

      1630       1640       1650       1660       1670       1680 
RPCGTEDCEP VEPPRCERDR LSFGFCETLR LLGRCQLPTI RTQCCRSCSP PSHGAPSRGH 


QRVARR 

« Hide

References

« Hide 'large scale' references
[1]"ADAMTS-7: a metalloproteinase that directly binds to and degrades cartilage oligomeric matrix protein."
Liu C.-J., Kong W., Ilalov K., Yu S., Xu K., Prazak L., Fajardo M., Sehgal B., Di Cesare P.E.
FASEB J. 20:988-990(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, COFACTOR, PH DEPENDENCE, INTERACTION WITH COMP, INDUCTION, TISSUE SPECIFICITY, VARIANTS ALA-1319; SER-1414 AND ALA-1583.
[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], VARIANT MET-307.
Tissue: Ovary.
[3]"ADAM-TS5, ADAM-TS6, and ADAM-TS7, novel members of a new family of zinc metalloproteases."
Hurskainen T.L., Hirohata S., Seldin M.F., Apte S.S.
J. Biol. Chem. 274:25555-25563(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA].
[4]"ADAMTS7B, the full-length product of the ADAMTS7 gene, is a chondroitin sulfate proteoglycan containing a mucin domain."
Somerville R.P.T., Longpre J.-M., Apel E.D., Lewis R.M., Wang L.W., Sanes J.R., Leduc R., Apte S.S.
J. Biol. Chem. 279:35159-35175(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 237-243, IDENTIFICATION, GLYCOSYLATION, PROTEOLYTIC PROCESSING, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY327122 mRNA. Translation: AAQ94616.1.
BC061631 mRNA. Translation: AAH61631.1.
AF140675 mRNA. Translation: AAD56358.1. Sequence problems.
RefSeqNP_055087.2. NM_014272.3.
UniGeneHs.16441.

3D structure databases

ProteinModelPortalQ9UKP4.
SMRQ9UKP4. Positions 239-811, 826-1021, 1408-1628.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9UKP4. 3 interactions.
STRING9606.ENSP00000373472.

Protein family/group databases

MEROPSM12.231.

PTM databases

PhosphoSiteQ9UKP4.

Polymorphism databases

DMDM205371741.

Proteomic databases

PaxDbQ9UKP4.
PRIDEQ9UKP4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000388820; ENSP00000373472; ENSG00000136378.
GeneID11173.
KEGGhsa:11173.
UCSCuc002bej.4. human.

Organism-specific databases

CTD11173.
GeneCardsGC15M079051.
H-InvDBHIX0012467.
HGNCHGNC:223. ADAMTS7.
HPAHPA034581.
MIM605009. gene.
neXtProtNX_Q9UKP4.
PharmGKBPA24551.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG237764.
HOGENOMHOG000015092.
HOVERGENHBG050620.
KOK08622.
OMAKGKYCVG.
OrthoDBEOG7V765X.
PhylomeDBQ9UKP4.
TreeFamTF313537.

Gene expression databases

BgeeQ9UKP4.
CleanExHS_ADAMTS7.
GenevestigatorQ9UKP4.

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.
IPR010909. PLAC.
IPR000884. Thrombospondin_1_rpt.
[Graphical view]
PfamPF05986. ADAM_spacer1. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 7 hits.
[Graphical view]
PRINTSPR01857. ADAMTSFAMILY.
SMARTSM00209. TSP1. 8 hits.
[Graphical view]
SUPFAMSSF82895. SSF82895. 8 hits.
PROSITEPS50215. ADAM_MEPRO. 1 hit.
PS50900. PLAC. 1 hit.
PS50092. TSP1. 7 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi11173.
NextBio42517.
PROQ9UKP4.
SOURCESearch...

Entry information

Entry nameATS7_HUMAN
AccessionPrimary (citable) accession number: Q9UKP4
Secondary accession number(s): Q14F51, Q6P7J9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: September 2, 2008
Last modified: April 16, 2014
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM