Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

A disintegrin and metalloproteinase with thrombospondin motifs 7

Gene

Adamts7

Organism
Rattus norvegicus (Rat)
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.By similarity

Cofactori

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi191 – 1911Zinc; in inhibited formBy similarity
Metal bindingi369 – 3691Zinc; catalyticBy similarity
Active sitei370 – 3701PROSITE-ProRule annotation
Metal bindingi373 – 3731Zinc; catalyticBy similarity
Metal bindingi379 – 3791Zinc; catalyticBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding

Enzyme and pathway databases

ReactomeiR-RNO-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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 8

Organism-specific databases

RGDi1306713. Adamts7.

Subcellular locationi

GO - Cellular componenti

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 – 217197By similarityPRO_0000348236Add
BLAST
Chaini218 – 15951378A disintegrin and metalloproteinase with thrombospondin motifs 7PRO_0000348237Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi84 – 841N-linked (GlcNAc...)Sequence analysis
Glycosylationi105 – 1051N-linked (GlcNAc...)Sequence analysis
Disulfide bondi299 ↔ 353By similarity
Disulfide bondi328 ↔ 335By similarity
Disulfide bondi347 ↔ 429By similarity
Disulfide bondi386 ↔ 413By similarity
Disulfide bondi456 ↔ 479By similarity
Disulfide bondi467 ↔ 485By similarity
Disulfide bondi474 ↔ 504By similarity
Disulfide bondi498 ↔ 509By similarity
Disulfide bondi532 ↔ 569By similarity
Disulfide bondi536 ↔ 574By similarity
Disulfide bondi547 ↔ 559By similarity
Glycosylationi619 – 6191N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

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

Keywords - PTMi

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

Proteomic databases

PaxDbiQ1EHB3.
PRIDEiQ1EHB3.

PTM databases

PhosphoSiteiQ1EHB3.

Expressioni

Tissue specificityi

Detected in liver, ovary, kidney, testicle, lung and embryo.1 Publication

Gene expression databases

GenevisibleiQ1EHB3. RN.

Interactioni

Subunit structurei

Interacts with COMP.1 Publication

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000060069.

Structurei

3D structure databases

ProteinModelPortaliQ1EHB3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini223 – 434212Peptidase M12BPROSITE-ProRule annotationAdd
BLAST
Domaini444 – 51976DisintegrinAdd
BLAST
Domaini520 – 57556TSP type-1 1PROSITE-ProRule annotationAdd
BLAST
Domaini801 – 86060TSP type-1 2PROSITE-ProRule annotationAdd
BLAST
Domaini861 – 91757TSP type-1 3PROSITE-ProRule annotationAdd
BLAST
Domaini922 – 97554TSP type-1 4PROSITE-ProRule annotationAdd
BLAST
Domaini1320 – 136849TSP type-1 5PROSITE-ProRule annotationAdd
BLAST
Domaini1371 – 143161TSP type-1 6PROSITE-ProRule annotationAdd
BLAST
Domaini1433 – 147644TSP type-1 7PROSITE-ProRule annotationAdd
BLAST
Domaini1478 – 153861TSP type-1 8PROSITE-ProRule annotationAdd
BLAST
Domaini1541 – 158141PLACPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni680 – 791112SpacerAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi189 – 1968Cysteine switchBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi577 – 679103Cys-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.
InParanoidiQ1EHB3.
KOiK08622.
OMAiQCCRSCP.
OrthoDBiEOG7V765X.
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. TSP1_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]

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: Q1EHB3-1) [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
MHRGLNLLLI LCALAPHVLG PASGLPTEGR AGLDIVHPVR VDAGGSFLSY
60 70 80 90 100
ELWPRVLRKR DVSAAQASSA FYQLQYQGRE LLFNLTTNPY LLAPGFVSEI
110 120 130 140 150
RRRSNLSNVH IQTSVPTCHL LGDVQDPELE GGFAAISACD GLRGVFQLSN
160 170 180 190 200
EDYFIEPLDE VPAQPGHAQP HMVYKHKRSG QQDDSRTSGT CGVQGSPELK
210 220 230 240 250
HQREHWEQRQ QKRRQQRSIS KEKWVETLVV ADSKMVEYHG QPQVESYVLT
260 270 280 290 300
IMNMVAGLYH DPSIGNPIHI TVVRLIILED EEKDLKITHH ADDTLKNFCR
310 320 330 340 350
WQKNVNMKGD DHPQHHDTAI LLTRKDLCAT MNHPCETLGL SHVAGLCHPQ
360 370 380 390 400
LSCSVSEDTG LPLAFTVAHE LGHSFGIQHD GTGNDCESIG KRPFIMSPQL
410 420 430 440 450
LYDRGIPLTW SRCSREYITR FLDRGWGLCL DDRPSKGVIN FPSVLPGVLY
460 470 480 490 500
DVNHQCRLQY GPSSAYCEDV DNVCYTLWCS VGTTCHSKMD AAVDGTSCGK
510 520 530 540 550
NKWCLNGECV PEGFQPETVD GGWSGWSAWS VCSRSCGVGV RSSERQCTQP
560 570 580 590 600
VPKNKGKYCV GERKRYRLCN LQACPPDRPS FRHTQCSQFD SMLYKGKLHK
610 620 630 640 650
WVPVLNDENP CELHCRPFNY SNREKLRDAV MDGTPCYQGR ISRDICIDGI
660 670 680 690 700
CKKVGCDFEL DSGAEEDRCG VCRGDGSTCH TVSRTFKEAE GMGYVDVGLI
710 720 730 740 750
PAGAREILIE EVAEAANFLA LRSEDPDKYF LNGGWTIQWN GDYQVAGTTF
760 770 780 790 800
TYTRKGNWET LTSPGPTTEP VWIQLLFQER NPGVHYKYTI QRASHSEAQP
810 820 830 840 850
PEFSWHYGPW SKCPVTCGTG VQRQSLYCME KQAGIVDEGH CDHLSRPRDR
860 870 880 890 900
KRKCNEEPCP ARWWVGDWQP CSRSCGPGGF FRRAVFCTRS VGLDEQRALE
910 920 930 940 950
PSACGHLPRP LAEIPCYHYV ACPSSWGVGN WSQCSVTCGA GIRQRSVLCI
960 970 980 990 1000
NNTGVPCDGA ERPITETFCF LQPCQYSTYI VDTGASGSGS SSPELFNEVD
1010 1020 1030 1040 1050
FDPHQPVPRP SPASSPKPVS ISNAIDEEDP ELDPPGPVFV DDFYYDYNFI
1060 1070 1080 1090 1100
NFHEDLSYGS FEESHSDLVD IGGQTVPPHI RPTEPPSDSP VPTAGAPGAE
1110 1120 1130 1140 1150
EEGIQGSWSP SPLLSEASHS PPVLLENTPV NPLANFLTEE ESPIGAPELG
1160 1170 1180 1190 1200
LPSVSWPPAS VDGMVTSVAP GNPDELLVRE DTQSQPSTPW SDRNKLSKDG
1210 1220 1230 1240 1250
NPLGPTSPAL PKSPFPTQPS SPSNSTTQAS LSPDAVEVST GWNVALDPVL
1260 1270 1280 1290 1300
EADLKPVHAP TDPGLLDQIQ TPHTEGTQSP GLLPRPAQET QTNSSKDPAV
1310 1320 1330 1340 1350
QPLQPSLVED GAPTDLLPAK NASWQVGNWS QCSTTCGLGA IWRLVRCSSG
1360 1370 1380 1390 1400
NDEDCTLSSR PQPARHCHLR PCAAWRAGNW SKCSRNCGGG SATRDVQCVD
1410 1420 1430 1440 1450
TRDLRPLRPF HCQPGPTKPP TRQLCGTQPC LPWYTSSWRE CSEACGGGEQ
1460 1470 1480 1490 1500
QRLVTCPEPG LCEESLRPNN TRPCNTHPCT QWVVGPWGQC SAPCGGGVQR
1510 1520 1530 1540 1550
RLVKCVNTQT GLAEEDSDLC SHEAWPESSR PCATEDCELV EPSRCERDRL
1560 1570 1580 1590
PFNFCETLRL LGRCQLPTIR AQCCRSCPPL SRGVPSRGHQ RVARR
Length:1,595
Mass (Da):175,814
Last modified:July 11, 2006 - v1
Checksum:i4025D80EBFCF0C4C
GO
Isoform 2 (identifier: Q1EHB3-2) [UniParc]FASTAAdd to basket

Also known as: ADAMTS7B

The sequence of this isoform differs from the canonical sequence as follows:
     1-24: MHRGLNLLLILCALAPHVLGPASG → MAEEDIGTES...LSCRVGTVLR

Show »
Length:1,808
Mass (Da):199,891
Checksum:i47EEFD2A80EC5BC1
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2424MHRGL…GPASG → MAEEDIGTESFGEEGERGPQ SPDEIIFQQCKMFALHIQRK RKQLGASFWHLCTGRCSGRW GSLSCSCHCQRCQRWRERED GTRRSQGQREKKDDKGLEKP KRKVQKGKQMQKASGDKESE NSISRKKPLPSLEGPRPLSW VDFGHKSRSPPRRSCLLSVP SRSLAGFQVSFSEGQAFFAW DPETSETQIGDKKLQNSRSF GGTSEGTDGLGLLHRQGTSV ALQAVQSLSCRVGTVLR in isoform 2. 1 PublicationVSP_035114Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY327121 mRNA. Translation: AAQ94615.1.
AY257482 mRNA. Translation: AAP79641.1.
RefSeqiNP_001040566.1. NM_001047101.1. [Q1EHB3-2]
XP_006243587.1. XM_006243525.1. [Q1EHB3-1]
UniGeneiRn.23850.

Genome annotation databases

EnsembliENSRNOT00000068394; ENSRNOP00000060069; ENSRNOG00000028036. [Q1EHB3-2]
GeneIDi315879.
KEGGirno:315879.
UCSCiRGD:1306713. rat. [Q1EHB3-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY327121 mRNA. Translation: AAQ94615.1.
AY257482 mRNA. Translation: AAP79641.1.
RefSeqiNP_001040566.1. NM_001047101.1. [Q1EHB3-2]
XP_006243587.1. XM_006243525.1. [Q1EHB3-1]
UniGeneiRn.23850.

3D structure databases

ProteinModelPortaliQ1EHB3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000060069.

PTM databases

PhosphoSiteiQ1EHB3.

Proteomic databases

PaxDbiQ1EHB3.
PRIDEiQ1EHB3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000068394; ENSRNOP00000060069; ENSRNOG00000028036. [Q1EHB3-2]
GeneIDi315879.
KEGGirno:315879.
UCSCiRGD:1306713. rat. [Q1EHB3-1]

Organism-specific databases

CTDi11173.
RGDi1306713. Adamts7.

Phylogenomic databases

eggNOGiKOG3538. Eukaryota.
ENOG410XPKZ. LUCA.
GeneTreeiENSGT00760000118880.
HOGENOMiHOG000015092.
HOVERGENiHBG050620.
InParanoidiQ1EHB3.
KOiK08622.
OMAiQCCRSCP.
OrthoDBiEOG7V765X.
TreeFamiTF313537.

Enzyme and pathway databases

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

Miscellaneous databases

NextBioi669994.
PROiQ1EHB3.

Gene expression databases

GenevisibleiQ1EHB3. RN.

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. TSP1_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]
ProtoNetiSearch...

Publicationsi

  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] (ISOFORMS 1 AND 2), INTERACTION WITH COMP, TISSUE SPECIFICITY.
    Strain: Brown Norway.
    Tissue: Brain.

Entry informationi

Entry nameiATS7_RAT
AccessioniPrimary (citable) accession number: Q1EHB3
Secondary accession number(s): Q1XD63
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: July 11, 2006
Last modified: May 11, 2016
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. 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.