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Q9UKP4

- ATS7_HUMAN

UniProt

Q9UKP4 - ATS7_HUMAN

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Protein

A disintegrin and metalloproteinase with thrombospondin motifs 7

Gene

ADAMTS7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

pH dependencei

Optimum pH is between 7.5 and 9.5.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi204 – 2041Zinc; in inhibited formBy similarity
Metal bindingi388 – 3881Zinc; catalyticBy similarity
Active sitei389 – 3891PROSITE-ProRule annotation
Metal bindingi392 – 3921Zinc; catalyticBy similarity
Metal bindingi398 – 3981Zinc; catalyticBy similarity

GO - Molecular functioni

  1. metalloendopeptidase activity Source: BHF-UCL
  2. metallopeptidase activity Source: ProtInc
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. cellular response to BMP stimulus Source: BHF-UCL
  2. cellular response to interleukin-1 Source: BHF-UCL
  3. cellular response to tumor necrosis factor Source: BHF-UCL
  4. negative regulation of chondrocyte differentiation Source: BHF-UCL
  5. proteolysis involved in cellular protein catabolic process Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_200626. O-glycosylation of TSR domain-containing proteins.

Protein family/group databases

MEROPSiM12.231.

Names & Taxonomyi

Protein namesi
Recommended name:
A disintegrin and metalloproteinase with thrombospondin motifs 7 (EC:3.4.24.-)
Short name:
ADAM-TS 7
Short name:
ADAM-TS7
Short name:
ADAMTS-7
Alternative name(s):
COMPase
Gene namesi
Name:ADAMTS7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:223. ADAMTS7.

Subcellular locationi

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

GO - Cellular componenti

  1. cell surface Source: Ensembl
  2. proteinaceous extracellular matrix Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24551.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727Sequence AnalysisAdd
BLAST
Propeptidei28 – 2362091 PublicationPRO_0000029176Add
BLAST
Chaini237 – 16861450A disintegrin and metalloproteinase with thrombospondin motifs 7PRO_0000029177Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi94 – 941N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi318 ↔ 372By similarity
Disulfide bondi347 ↔ 354By similarity
Disulfide bondi366 ↔ 447By similarity
Disulfide bondi405 ↔ 431By similarity
Disulfide bondi474 ↔ 497By similarity
Disulfide bondi485 ↔ 503By similarity
Disulfide bondi492 ↔ 522By similarity
Disulfide bondi516 ↔ 527By similarity
Disulfide bondi550 ↔ 587By similarity
Disulfide bondi554 ↔ 592By similarity
Disulfide bondi565 ↔ 577By similarity
Glycosylationi693 – 6931N-linked (GlcNAc...)Sequence Analysis
Glycosylationi778 – 7781N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

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.1 Publication
May be cleaved by a furin endopeptidase (By similarity). The precursor is sequentially processed.By similarity1 Publication

Keywords - PTMi

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

Proteomic databases

PaxDbiQ9UKP4.
PRIDEiQ9UKP4.

PTM databases

PhosphoSiteiQ9UKP4.

Expressioni

Tissue specificityi

Expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Detected in meniscus, bone, tendon, cartilage, synovium, fat and ligaments.2 Publications

Inductioni

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

Gene expression databases

BgeeiQ9UKP4.
CleanExiHS_ADAMTS7.
GenevestigatoriQ9UKP4.

Organism-specific databases

HPAiHPA034581.

Interactioni

Subunit structurei

Interacts with COMP.1 Publication

Protein-protein interaction databases

IntActiQ9UKP4. 3 interactions.
STRINGi9606.ENSP00000373472.

Structurei

3D structure databases

ProteinModelPortaliQ9UKP4.
SMRiQ9UKP4. Positions 239-713.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini242 – 452211Peptidase M12BPROSITE-ProRule annotationAdd
BLAST
Domaini462 – 53776DisintegrinAdd
BLAST
Domaini538 – 59356TSP type-1 1PROSITE-ProRule annotationAdd
BLAST
Domaini821 – 88060TSP type-1 2PROSITE-ProRule annotationAdd
BLAST
Domaini881 – 94060TSP type-1 3PROSITE-ProRule annotationAdd
BLAST
Domaini942 – 99554TSP type-1 4PROSITE-ProRule annotationAdd
BLAST
Domaini1411 – 145949TSP type-1 5PROSITE-ProRule annotationAdd
BLAST
Domaini1462 – 152261TSP type-1 6PROSITE-ProRule annotationAdd
BLAST
Domaini1523 – 156745TSP type-1 7PROSITE-ProRule annotationAdd
BLAST
Domaini1569 – 162961TSP type-1 8PROSITE-ProRule annotationAdd
BLAST
Domaini1632 – 167241PLACPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni698 – 809112SpacerAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi202 – 2098Cysteine switchBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi595 – 697103Cys-richAdd
BLAST

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.Curated
Contains 1 peptidase M12B domain.PROSITE-ProRule annotation
Contains 1 PLAC domain.PROSITE-ProRule annotation
Contains 8 TSP type-1 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG237764.
GeneTreeiENSGT00760000118885.
HOGENOMiHOG000015092.
HOVERGENiHBG050620.
InParanoidiQ9UKP4.
KOiK08622.
OMAiKGKYCVG.
OrthoDBiEOG7V765X.
PhylomeDBiQ9UKP4.
TreeFamiTF313537.

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.
IPR010909. PLAC.
IPR000884. Thrombospondin_1_rpt.
[Graphical view]
PfamiPF05986. ADAM_spacer1. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 7 hits.
[Graphical view]
PRINTSiPR01857. ADAMTSFAMILY.
SMARTiSM00209. TSP1. 8 hits.
[Graphical view]
SUPFAMiSSF82895. SSF82895. 8 hits.
PROSITEiPS50215. ADAM_MEPRO. 1 hit.
PS50900. PLAC. 1 hit.
PS50092. TSP1. 7 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9UKP4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPGGPSPRSP APLLRPLLLL LCALAPGAPG PAPGRATEGR AALDIVHPVR
60 70 80 90 100
VDAGGSFLSY ELWPRALRKR DVSVRRDAPA FYELQYRGRE LRFNLTANQH
110 120 130 140 150
LLAPGFVSET RRRGGLGRAH IRAHTPACHL LGEVQDPELE GGLAAISACD
160 170 180 190 200
GLKGVFQLSN EDYFIEPLDS APARPGHAQP HVVYKRQAPE RLAQRGDSSA
210 220 230 240 250
PSTCGVQVYP ELESRRERWE QRQQWRRPRL RRLHQRSVSK EKWVETLVVA
260 270 280 290 300
DAKMVEYHGQ PQVESYVLTI MNMVAGLFHD PSIGNPIHIT IVRLVLLEDE
310 320 330 340 350
EEDLKITHHA DNTLKSFCKW QKSINMKGDA HPLHHDTAIL LTRKDLCAAM
360 370 380 390 400
NRPCETLGLS HVAGMCQPHR SCSINEDTGL PLAFTVAHEL GHSFGIQHDG
410 420 430 440 450
SGNDCEPVGK RPFIMSPQLL YDAAPLTWSR CSRQYITRFL DRGWGLCLDD
460 470 480 490 500
PPAKDIIDFP SVPPGVLYDV SHQCRLQYGA YSAFCEDMDN VCHTLWCSVG
510 520 530 540 550
TTCHSKLDAA VDGTRCGENK WCLSGECVPV GFRPEAVDGG WSGWSAWSIC
560 570 580 590 600
SRSCGMGVQS AERQCTQPTP KYKGRYCVGE RKRFRLCNLQ ACPAGRPSFR
610 620 630 640 650
HVQCSHFDAM LYKGQLHTWV PVVNDVNPCE LHCRPANEYF AEKLRDAVVD
660 670 680 690 700
GTPCYQVRAS RDLCINGICK NVGCDFEIDS GAMEDRCGVC HGNGSTCHTV
710 720 730 740 750
SGTFEEAEGL GYVDVGLIPA GAREIRIQEV AEAANFLALR SEDPEKYFLN
760 770 780 790 800
GGWTIQWNGD YQVAGTTFTY ARRGNWENLT SPGPTKEPVW IQLLFQESNP
810 820 830 840 850
GVHYEYTIHR EAGGHDEVPP PVFSWHYGPW TKCTVTCGRG VQRQNVYCLE
860 870 880 890 900
RQAGPVDEEH CDPLGRPDDQ QRKCSEQPCP ARWWAGEWQL CSSSCGPGGL
910 920 930 940 950
SRRAVLCIRS VGLDEQSALE PPACEHLPRP PTETPCNRHV PCPATWAVGN
960 970 980 990 1000
WSQCSVTCGE GTQRRNVLCT NDTGVPCDEA QQPASEVTCS LPLCRWPLGT
1010 1020 1030 1040 1050
LGPEGSGSGS SSHELFNEAD FIPHHLAPRP SPASSPKPGT MGNAIEEEAP
1060 1070 1080 1090 1100
ELDLPGPVFV DDFYYDYNFI NFHEDLSYGP SEEPDLDLAG TGDRTPPPHS
1110 1120 1130 1140 1150
HPAAPSTGSP VPATEPPAAK EEGVLGPWSP SPWPSQAGRS PPPPSEQTPG
1160 1170 1180 1190 1200
NPLINFLPEE DTPIGAPDLG LPSLSWPRVS TDGLQTPATP ESQNDFPVGK
1210 1220 1230 1240 1250
DSQSQLPPPW RDRTNEVFKD DEEPKGRGAP HLPPRPSSTL PPLSPVGSTH
1260 1270 1280 1290 1300
SSPSPDVAEL WTGGTVAWEP ALEGGLGPVD SELWPTVGVA SLLPPPIAPL
1310 1320 1330 1340 1350
PEMKVRDSSL EPGTPSFPTP GPGSWDLQTV AVWGTFLPTT LTGLGHMPEP
1360 1370 1380 1390 1400
ALNPGPKGQP ESLSPEVPLS SRLLSTPAWD SPANSHRVPE TQPLAPSLAE
1410 1420 1430 1440 1450
AGPPADPLVV RNAGWQAGNW SECSTTCGLG AVWRPVRCSS GRDEDCAPAG
1460 1470 1480 1490 1500
RPQPARRCHL RPCATWHSGN WSKCSRSCGG GSSVRDVQCV DTRDLRPLRP
1510 1520 1530 1540 1550
FHCQPGPAKP PAHRPCGAQP CLSWYTSSWR ECSEACGGGE QQRLVTCPEP
1560 1570 1580 1590 1600
GLCEEALRPN TTRPCNTHPC TQWVVGPWGQ CSGPCGGGVQ RRLVKCVNTQ
1610 1620 1630 1640 1650
TGLPEEDSDQ CGHEAWPESS RPCGTEDCEP VEPPRCERDR LSFGFCETLR
1660 1670 1680
LLGRCQLPTI RTQCCRSCSP PSHGAPSRGH QRVARR
Length:1,686
Mass (Da):184,095
Last modified:September 2, 2008 - v2
Checksum:iAB38264B8E8DB740
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti642 – 6421E → K in AAD56358. (PubMed:16585064)Curated
Sequence conflicti1101 – 11011H → R in AAQ94616. (PubMed:15489334)Curated
Sequence conflicti1364 – 13641S → T in AAQ94616. (PubMed:15489334)Curated
Sequence conflicti1479 – 14791G → D in AAQ94616. (PubMed:15489334)Curated
Sequence conflicti1511 – 15111P → H in AAQ94616. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti214 – 2141S → P.
Corresponds to variant rs3825807 [ dbSNP | Ensembl ].
VAR_046112
Natural varianti307 – 3071T → M.1 Publication
Corresponds to variant rs2127898 [ dbSNP | Ensembl ].
VAR_046113
Natural varianti1319 – 13191T → A.1 Publication
Corresponds to variant rs11630236 [ dbSNP | Ensembl ].
VAR_046114
Natural varianti1414 – 14141G → S.1 Publication
Corresponds to variant rs2929155 [ dbSNP | Ensembl ].
VAR_046115
Natural varianti1583 – 15831G → A.1 Publication
Corresponds to variant rs7495616 [ dbSNP | Ensembl ].
VAR_046116

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY327122 mRNA. Translation: AAQ94616.1.
BC061631 mRNA. Translation: AAH61631.1.
AF140675 mRNA. Translation: AAD56358.1. Sequence problems.
CCDSiCCDS32303.1.
RefSeqiNP_055087.2. NM_014272.3.
UniGeneiHs.16441.

Genome annotation databases

EnsembliENST00000388820; ENSP00000373472; ENSG00000136378.
GeneIDi11173.
KEGGihsa:11173.
UCSCiuc002bej.4. human.

Polymorphism databases

DMDMi205371741.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY327122 mRNA. Translation: AAQ94616.1 .
BC061631 mRNA. Translation: AAH61631.1 .
AF140675 mRNA. Translation: AAD56358.1 . Sequence problems.
CCDSi CCDS32303.1.
RefSeqi NP_055087.2. NM_014272.3.
UniGenei Hs.16441.

3D structure databases

ProteinModelPortali Q9UKP4.
SMRi Q9UKP4. Positions 239-713.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9UKP4. 3 interactions.
STRINGi 9606.ENSP00000373472.

Protein family/group databases

MEROPSi M12.231.

PTM databases

PhosphoSitei Q9UKP4.

Polymorphism databases

DMDMi 205371741.

Proteomic databases

PaxDbi Q9UKP4.
PRIDEi Q9UKP4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000388820 ; ENSP00000373472 ; ENSG00000136378 .
GeneIDi 11173.
KEGGi hsa:11173.
UCSCi uc002bej.4. human.

Organism-specific databases

CTDi 11173.
GeneCardsi GC15M079051.
H-InvDB HIX0012467.
HGNCi HGNC:223. ADAMTS7.
HPAi HPA034581.
MIMi 605009. gene.
neXtProti NX_Q9UKP4.
PharmGKBi PA24551.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG237764.
GeneTreei ENSGT00760000118885.
HOGENOMi HOG000015092.
HOVERGENi HBG050620.
InParanoidi Q9UKP4.
KOi K08622.
OMAi KGKYCVG.
OrthoDBi EOG7V765X.
PhylomeDBi Q9UKP4.
TreeFami TF313537.

Enzyme and pathway databases

Reactomei REACT_200626. O-glycosylation of TSR domain-containing proteins.

Miscellaneous databases

GenomeRNAii 11173.
NextBioi 42517.
PROi Q9UKP4.
SOURCEi Search...

Gene expression databases

Bgeei Q9UKP4.
CleanExi HS_ADAMTS7.
Genevestigatori Q9UKP4.

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.
IPR010909. PLAC.
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. 7 hits.
[Graphical view ]
PRINTSi PR01857. ADAMTSFAMILY.
SMARTi SM00209. TSP1. 8 hits.
[Graphical view ]
SUPFAMi SSF82895. SSF82895. 8 hits.
PROSITEi PS50215. ADAM_MEPRO. 1 hit.
PS50900. PLAC. 1 hit.
PS50092. TSP1. 7 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiATS7_HUMAN
AccessioniPrimary (citable) accession number: Q9UKP4
Secondary accession number(s): Q14F51, Q6P7J9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: September 2, 2008
Last modified: November 26, 2014
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Peptidase families
    Classification of peptidase families and list of entries
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3