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Protein

A disintegrin and metalloproteinase with thrombospondin motifs 7

Gene

Adamts7

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi194 – 1941Zinc; in inhibited formBy similarity
Metal bindingi372 – 3721Zinc; catalyticBy similarity
Active sitei373 – 3731PROSITE-ProRule annotation
Metal bindingi376 – 3761Zinc; catalyticBy similarity
Metal bindingi382 – 3821Zinc; catalyticBy similarity

GO - Molecular functioni

  • metalloendopeptidase activity Source: MGI
  • metallopeptidase activity Source: MGI
  • zinc ion binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-5173214. O-glycosylation of TSR domain-containing proteins.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1347346. Adamts7.

Subcellular locationi

GO - Cellular componenti

  • cell surface Source: MGI
  • 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 – 2020Sequence analysisAdd
BLAST
Propeptidei21 – 2202001 PublicationPRO_0000348234Add
BLAST
Chaini221 – 16571437A disintegrin and metalloproteinase with thrombospondin motifs 7PRO_0000348235Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi84 – 841N-linked (GlcNAc...)Sequence analysis
Disulfide bondi302 ↔ 356By similarity
Disulfide bondi331 ↔ 338By similarity
Disulfide bondi350 ↔ 432By similarity
Disulfide bondi389 ↔ 416By similarity
Disulfide bondi459 ↔ 482By similarity
Disulfide bondi470 ↔ 488By similarity
Disulfide bondi477 ↔ 507By similarity
Disulfide bondi501 ↔ 512By similarity
Disulfide bondi535 ↔ 572By similarity
Disulfide bondi539 ↔ 577By similarity
Disulfide bondi550 ↔ 562By similarity
Glycosylationi622 – 6221N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

May be cleaved by a furin endopeptidase (By similarity). The precursor is sequentially processed.By similarity1 Publication
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 (By similarity). O-glycosylated proteoglycan. Contains chondroitin sulfate.By similarity1 Publication

Keywords - PTMi

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

Proteomic databases

PaxDbiQ68SA9.
PRIDEiQ68SA9.

PTM databases

iPTMnetiQ68SA9.
PhosphoSiteiQ68SA9.

Expressioni

Gene expression databases

BgeeiENSMUSG00000032363.
ExpressionAtlasiQ68SA9. baseline and differential.
GenevisibleiQ68SA9. MM.

Interactioni

Subunit structurei

Interacts with COMP.By similarity

Protein-protein interaction databases

IntActiQ68SA9. 1 interaction.
STRINGi10090.ENSMUSP00000108683.

Structurei

3D structure databases

ProteinModelPortaliQ68SA9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini226 – 437212Peptidase M12BPROSITE-ProRule annotationAdd
BLAST
Domaini447 – 52276DisintegrinAdd
BLAST
Domaini523 – 57856TSP type-1 1PROSITE-ProRule annotationAdd
BLAST
Domaini804 – 86360TSP type-1 2PROSITE-ProRule annotationAdd
BLAST
Domaini864 – 92360TSP type-1 3PROSITE-ProRule annotationAdd
BLAST
Domaini925 – 97854TSP type-1 4PROSITE-ProRule annotationAdd
BLAST
Domaini1366 – 141449TSP type-1 5PROSITE-ProRule annotationAdd
BLAST
Domaini1417 – 147761TSP type-1 6PROSITE-ProRule annotationAdd
BLAST
Domaini1479 – 152244TSP type-1 7PROSITE-ProRule annotationAdd
BLAST
Domaini1524 – 158461TSP type-1 8PROSITE-ProRule annotationAdd
BLAST
Domaini1587 – 162741PLACPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni683 – 794112SpacerAdd
BLAST

Motif

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

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi580 – 682103Cys-richAdd
BLAST
Compositional biasi1078 – 1364287Pro-richAdd
BLAST

Domaini

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

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

eggNOGiKOG3538. Eukaryota.
ENOG410XPKZ. LUCA.
GeneTreeiENSGT00760000118880.
HOGENOMiHOG000015092.
HOVERGENiHBG050620.
InParanoidiQ68SA9.
OMAiQCCRSCP.
OrthoDBiEOG091G14M8.
TreeFamiTF313537.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR006586. ADAM_Cys-rich.
IPR010294. ADAM_spacer1.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR013273. Peptidase_M12B_ADAM-TS.
IPR002870. Peptidase_M12B_N.
IPR010909. PLAC.
IPR000884. TSP1_rpt.
[Graphical view]
PfamiPF05986. ADAM_spacer1. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 8 hits.
[Graphical view]
PRINTSiPR01857. ADAMTSFAMILY.
SMARTiSM00608. ACR. 1 hit.
SM00209. TSP1. 8 hits.
[Graphical view]
SUPFAMiSSF82895. SSF82895. 8 hits.
PROSITEiPS50215. ADAM_MEPRO. 1 hit.
PS50900. PLAC. 1 hit.
PS50092. TSP1. 6 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q68SA9-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MHRGPSLLLI LCALASRVLG PASGLVTEGR AGLDIVHPVR VDAGGSFLSY
60 70 80 90 100
ELWPRVLRKR DVSTTQASSA FYQLQYQGRE LLFNLTTNPY LMAPGFVSEI
110 120 130 140 150
RRHSTLGHAH IQTSVPTCHL LGDVQDPELE GGFAAISACD GLRGVFQLSN
160 170 180 190 200
EDYFIEPLDG VSAQPGHAQP HVVYKHQGSR KQAQQGDSRP SGTCGMQVPP
210 220 230 240 250
DLEQQREHWE QQQQKRRQQR SVSKEKWVET LVVADSKMVE YHGQPQVESY
260 270 280 290 300
VLTIMNMVAG LFHDPSIGNP IHISIVRLII LEDEEKDLKI THHAEETLKN
310 320 330 340 350
FCRWQKNINI KGDDHPQHHD TAILLTRKDL CASMNQPCET LGLSHVSGLC
360 370 380 390 400
HPQLSCSVSE DTGMPLAFTV AHELGHSFGI QHDGTGNDCE SIGKRPFIMS
410 420 430 440 450
PQLLYDRGIP LTWSRCSREY ITRFLDRGWG LCLDDRPSKD VIALPSVLPG
460 470 480 490 500
VLYDVNHQCR LQYGSHSAYC EDMDDVCHTL WCSVGTTCHS KLDAAVDGTS
510 520 530 540 550
CGKNKWCLKG ECVPEGFQPE AVDGGWSGWS AWSDCSRSCG VGVRSSERQC
560 570 580 590 600
TQPVPKNRGK YCVGERKRSQ LCNLPACPPD RPSFRHTQCS QFDGMLYKGK
610 620 630 640 650
LHKWVPVPND DNPCELHCRP SNSSNTEKLR DAVVDGTPCY QSRISRDICL
660 670 680 690 700
NGICKNVGCD FVIDSGAEED RCGVCRGDGS TCQTVSRTFK ETEGQGYVDI
710 720 730 740 750
GLIPAGAREI LIEEVAEAAN FLALRSEDPD KYFLNGGWTI QWNGDYRVAG
760 770 780 790 800
TTFTYARKGN WENLTSPGPT SEPVWIQLLF QEKNPGVHYQ YTIQRDSHDQ
810 820 830 840 850
VRPPEFSWHY GPWSKCTVTC GTGVQRQSLY CMERQAGVVA EEYCNTLNRP
860 870 880 890 900
DERQRKCSEE PCPPRWWAGE WQPCSRSCGP EGLSRRAVFC IRSMGLDEQR
910 920 930 940 950
ALELSACEHL PRPLAETPCN RHVICPSTWG VGNWSQCSVT CGAGIRQRSV
960 970 980 990 1000
LCINNTDVPC DEAERPITET FCFLQPCQYP MYIVDTGASG SGSSSPELFN
1010 1020 1030 1040 1050
EVDFIPNQLA PRPSPASSPK PVSISNAIDE EELDPPGPVF VDDFYYDYNF
1060 1070 1080 1090 1100
INFHEDLSYG SFEEPHPDLV DNGGWTAPPH IRPTESPSDT PVPTAGALGA
1110 1120 1130 1140 1150
EAEDIQGSWS PSPLLSEASY SPPGLEQTSI NPLANFLTEE DTPMGAPELG
1160 1170 1180 1190 1200
FPSLPWPPAS VDDMMTPVGP GNPDELLVKE DEQSPPSTPW SDRNKLSTDG
1210 1220 1230 1240 1250
NPLGHTSPAL PQSPIPTQPS PPSISPTQAS PSPDVVEVST GWNAAWDPVL
1260 1270 1280 1290 1300
EADLKPGHGE LPSTVEVASP PLLPMATVPG IWGRDSPLEP GTPTFSSPEL
1310 1320 1330 1340 1350
SSQHLKTLTM PGTLLLTVPT DLRSPGPSGQ PQTPNLEGTQ SPGLLPTPAR
1360 1370 1380 1390 1400
ETQTNSSKDP EVQPLQPSLE EDGDPADPLP ARNASWQVGN WSQCSTTCGL
1410 1420 1430 1440 1450
GAIWRLVSCS SGNDEDCTLA SRPQPARHCH LRPCAAWRTG NWSKCSRNCG
1460 1470 1480 1490 1500
GGSSTRDVQC VDTRDLRPLR PFHCQPGPTK PPNRQLCGTQ PCLPWYTSSW
1510 1520 1530 1540 1550
RECSEACGGG EQQRLVTCPE PGLCEESLRP NNSRPCNTHP CTQWVVGPWG
1560 1570 1580 1590 1600
QCSAPCGGGV QRRLVRCVNT QTGLAEEDSD LCSHEAWPES SRPCATEDCE
1610 1620 1630 1640 1650
LVEPPRCERD RLSFNFCETL RLLGRCQLPT IRAQCCRSCP PLSRGVPSRG

HQRVARR
Length:1,657
Mass (Da):182,313
Last modified:July 27, 2011 - v3
Checksum:i2B05A3B6567617FD
GO
Isoform 2 (identifier: Q68SA9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     936-977: Missing.

Show »
Length:1,615
Mass (Da):177,712
Checksum:i0F7E9D2D303C12E2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti600 – 6001K → N in AAT36307 (PubMed:15192113).Curated
Sequence conflicti1124 – 11241G → V in AAT36307 (PubMed:15192113).Curated
Sequence conflicti1124 – 11241G → V in AAI41174 (PubMed:15489334).Curated
Sequence conflicti1244 – 12441A → V in AAT36307 (PubMed:15192113).Curated
Sequence conflicti1244 – 12441A → V in AAI41174 (PubMed:15489334).Curated
Sequence conflicti1312 – 133322GTLLL…GQPQT → VAGPMV in AAT36307 (PubMed:15192113).CuratedAdd
BLAST

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei936 – 97742Missing in isoform 2. 1 PublicationVSP_035113Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY551090 mRNA. Translation: AAT36307.1.
AC140392 Genomic DNA. No translation available.
AC151735 Genomic DNA. No translation available.
BC141173 mRNA. Translation: AAI41174.1.
CCDSiCCDS40724.1. [Q68SA9-2]
UniGeneiMm.102141.

Genome annotation databases

EnsembliENSMUST00000113059; ENSMUSP00000108682; ENSMUSG00000032363. [Q68SA9-1]
ENSMUST00000113060; ENSMUSP00000108683; ENSMUSG00000032363. [Q68SA9-2]
UCSCiuc009raa.1. mouse. [Q68SA9-1]
uc009rab.1. mouse. [Q68SA9-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY551090 mRNA. Translation: AAT36307.1.
AC140392 Genomic DNA. No translation available.
AC151735 Genomic DNA. No translation available.
BC141173 mRNA. Translation: AAI41174.1.
CCDSiCCDS40724.1. [Q68SA9-2]
UniGeneiMm.102141.

3D structure databases

ProteinModelPortaliQ68SA9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ68SA9. 1 interaction.
STRINGi10090.ENSMUSP00000108683.

PTM databases

iPTMnetiQ68SA9.
PhosphoSiteiQ68SA9.

Proteomic databases

PaxDbiQ68SA9.
PRIDEiQ68SA9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000113059; ENSMUSP00000108682; ENSMUSG00000032363. [Q68SA9-1]
ENSMUST00000113060; ENSMUSP00000108683; ENSMUSG00000032363. [Q68SA9-2]
UCSCiuc009raa.1. mouse. [Q68SA9-1]
uc009rab.1. mouse. [Q68SA9-2]

Organism-specific databases

CTDi11173.
MGIiMGI:1347346. Adamts7.

Phylogenomic databases

eggNOGiKOG3538. Eukaryota.
ENOG410XPKZ. LUCA.
GeneTreeiENSGT00760000118880.
HOGENOMiHOG000015092.
HOVERGENiHBG050620.
InParanoidiQ68SA9.
OMAiQCCRSCP.
OrthoDBiEOG091G14M8.
TreeFamiTF313537.

Enzyme and pathway databases

ReactomeiR-MMU-5173214. O-glycosylation of TSR domain-containing proteins.

Miscellaneous databases

PROiQ68SA9.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000032363.
ExpressionAtlasiQ68SA9. baseline and differential.
GenevisibleiQ68SA9. MM.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR006586. ADAM_Cys-rich.
IPR010294. ADAM_spacer1.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR013273. Peptidase_M12B_ADAM-TS.
IPR002870. Peptidase_M12B_N.
IPR010909. PLAC.
IPR000884. TSP1_rpt.
[Graphical view]
PfamiPF05986. ADAM_spacer1. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 8 hits.
[Graphical view]
PRINTSiPR01857. ADAMTSFAMILY.
SMARTiSM00608. ACR. 1 hit.
SM00209. TSP1. 8 hits.
[Graphical view]
SUPFAMiSSF82895. SSF82895. 8 hits.
PROSITEiPS50215. ADAM_MEPRO. 1 hit.
PS50900. PLAC. 1 hit.
PS50092. TSP1. 6 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiATS7_MOUSE
AccessioniPrimary (citable) accession number: Q68SA9
Secondary accession number(s): B2RUI8, E9QMY0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: July 27, 2011
Last modified: September 7, 2016
This is version 97 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.