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 10

Gene

Adamts10

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Metalloprotease that participate in microfibrils assembly. Microfibrils are extracellular matrix components occurring independently or along with elastin in the formation of elastic tissues (By similarity).By similarity

Cofactori

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi392Zinc; catalyticBy similarity1
Active sitei393PROSITE-ProRule annotation1
Metal bindingi396Zinc; catalyticBy similarity1
Metal bindingi402Zinc; catalyticBy similarity1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM12.235.

Names & Taxonomyi

Protein namesi
Recommended name:
A disintegrin and metalloproteinase with thrombospondin motifs 10 (EC:3.4.24.-)
Short name:
ADAM-TS 10
Short name:
ADAM-TS10
Short name:
ADAMTS-10
Gene namesi
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:2449112. Adamts10.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 25Sequence analysisAdd BLAST25
PropeptideiPRO_000027014926 – 233By similarityAdd BLAST208
ChainiPRO_0000078211234 – 1104A disintegrin and metalloproteinase with thrombospondin motifs 10Add BLAST871

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi90N-linked (GlcNAc...)Sequence analysis1
Glycosylationi222N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi315 ↔ 376By similarity
Disulfide bondi351 ↔ 358By similarity
Disulfide bondi370 ↔ 452By similarity
Disulfide bondi409 ↔ 436By similarity
Disulfide bondi479 ↔ 501By similarity
Disulfide bondi490 ↔ 508By similarity
Disulfide bondi496 ↔ 531By similarity
Disulfide bondi521 ↔ 536By similarity
Disulfide bondi559 ↔ 596By similarity
Disulfide bondi563 ↔ 601By similarity
Disulfide bondi574 ↔ 586By similarity
Glycosylationi740N-linked (GlcNAc...)Sequence analysis1
Glycosylationi795N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi837 ↔ 879By similarity
Disulfide bondi841 ↔ 884By similarity
Disulfide bondi852 ↔ 866By similarity
Glycosylationi892N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

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, and N-glycosylated. These other glycosylations can also facilitate secretion (By similarity).By similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP58459.
PRIDEiP58459.

PTM databases

iPTMnetiP58459.
PhosphoSitePlusiP58459.

Expressioni

Tissue specificityi

Widely expressed in adult tissues.1 Publication

Developmental stagei

Widely expressed throughout embryo development. Widespread expression in embryo until 12.5 days of gestation, after which it is then expressed in a more restricted fashion, with especially strong expression in developing lung, bone, and craniofacial region.1 Publication

Gene expression databases

BgeeiENSMUSG00000024299.
ExpressionAtlasiP58459. baseline and differential.
GenevisibleiP58459. MM.

Interactioni

Subunit structurei

Interacts with FBN1; this interaction promotes microfibrils assembly.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000084905.

Structurei

3D structure databases

ProteinModelPortaliP58459.
SMRiP58459.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini239 – 457Peptidase M12BPROSITE-ProRule annotationAdd BLAST219
Domaini460 – 546DisintegrinAdd BLAST87
Domaini547 – 602TSP type-1 1PROSITE-ProRule annotationAdd BLAST56
Domaini825 – 885TSP type-1 2PROSITE-ProRule annotationAdd BLAST61
Domaini888 – 943TSP type-1 3PROSITE-ProRule annotationAdd BLAST56
Domaini944 – 1003TSP type-1 4PROSITE-ProRule annotationAdd BLAST60
Domaini1004 – 1058TSP type-1 5PROSITE-ProRule annotationAdd BLAST55
Domaini1066 – 1104PLACPROSITE-ProRule annotationAdd BLAST39

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni706 – 818SpacerBy similarityAdd BLAST113

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi568 – 571Poly-Ser4
Compositional biasi604 – 705Cys-richAdd BLAST102

Domaini

The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix.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 5 TSP type-1 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiKOG3538. Eukaryota.
ENOG410XPKZ. LUCA.
GeneTreeiENSGT00760000118880.
HOGENOMiHOG000004800.
HOVERGENiHBG004315.
InParanoidiP58459.
KOiK08625.
OMAiICQTNTI.
OrthoDBiEOG091G14M8.
PhylomeDBiP58459.
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.
PF08686. PLAC. 1 hit.
PF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 5 hits.
[Graphical view]
PRINTSiPR01857. ADAMTSFAMILY.
SMARTiSM00209. TSP1. 5 hits.
[Graphical view]
SUPFAMiSSF82895. SSF82895. 5 hits.
PROSITEiPS50215. ADAM_MEPRO. 1 hit.
PS50900. PLAC. 1 hit.
PS50092. TSP1. 5 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P58459-1) [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
MASACQILRW ALALGLGLTF KVTHAFRSQD ELLSSLESYE IAFPTRVDHN
60 70 80 90 100
GAMLAFSPPA FRRQRRGAGA TTESRLFYKV AAPSTHFLLN LTRSPRLLAG
110 120 130 140 150
HVSVEYWTRE GLAWQRAARA HCLYAGHLQG QAGSSHVAVS TCGGLHGLIV
160 170 180 190 200
ADDEEYLIEP LQGGPKGHRG PEESGPHVVY KRSSLRHPHL DTACGVRDEK
210 220 230 240 250
PWKGRPWWLR TLKPPPARPL GNESERGQLG LKRSVSRERY VETLVVADKM
260 270 280 290 300
MVAYHGRRDV EQYVLAIMNI VAKLFQDSSL GNIVNILVTR LILLTEDQPT
310 320 330 340 350
LEITHHAGKS LDSFCKWQKS IVSHSGHGNA IPENGVANHD TAVLITRYDI
360 370 380 390 400
CIYKNKPCGT LGLAPVGGMC ERERSCSINE DIGLATAFTI AHEIGHTFGM
410 420 430 440 450
NHDGVGNGCG ARGQDPAKLM AAHITMKTNP FVWSSCSRDY ITSFLDSGLG
460 470 480 490 500
LCLNNRPPRQ DFVYPTVAPG QAYDADEQCR FQHGVKSRQC KYGEVCSELW
510 520 530 540 550
CLSKSNRCIT NSIPAAEGTL CQTHTIDKGW CYKRVCVPFG SRPEGVDGAW
560 570 580 590 600
GPWTPWGDCS RSCGGGVSSS SRHCDSPRPT IGGKYCLGER RRHRSCNTND
610 620 630 640 650
CPPGSQDFRE MQCSEFDSVP FRGKFYTWKT YRGGGVKACS LTCLAEGFNF
660 670 680 690 700
YTERAAAVVD GTPCRPDTVD ICVSGECKHV GCDRVLGSDL REDKCRVCGG
710 720 730 740 750
DGSACETIEG VFSPALPGTG YEDVVWIPKG SVHIFIQDLN LSLSHLALKG
760 770 780 790 800
DQESLLLEGL PGTPQPHRLP LAGTTFHLRQ GPDQAQSLEA LGPINASLII
810 820 830 840 850
MVLAQAELPA LHYRFNAPIA RDALPPYSWH YAPWTKCSAQ CAGGSQVQVV
860 870 880 890 900
ECRNQLDSSA VAPHYCSGHS KLPKRQRACN TEPCPPDWVV GNWSRCSRSC
910 920 930 940 950
DAGVRSRSVV CQRRVSAAEE KALDDSACPQ PRPPVLEACQ GPMCPPEWAT
960 970 980 990 1000
LDWSECTPSC GPGLRHRVVL CKSADQRSTL PPGHCLPAAK PPSTMRCNLR
1010 1020 1030 1040 1050
RCPPARWVTS EWGECSTQCG LGQQQRTVRC TSHTGQPSRE CTEALRPSTM
1060 1070 1080 1090 1100
QQCEAKCDSV VPPGDGPEEC KDVNKVAYCP LVLKFQFCSR AYFRQMCCKT

CQGR
Length:1,104
Mass (Da):121,086
Last modified:June 12, 2007 - v3
Checksum:i57811356FCB390FF
GO
Isoform 2 (identifier: P58459-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     146-147: HG → VS
     148-1104: Missing.

Note: May be due to intron retention. No experimental confirmation available.
Show »
Length:147
Mass (Da):16,041
Checksum:iE2833F8A51970103
GO
Isoform 3 (identifier: P58459-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     80-145: Missing.
     272-279: AKLFQDSS → SAFLGLES
     280-1104: Missing.

Show »
Length:213
Mass (Da):23,990
Checksum:i7DA18F920CAF53BF
GO

Sequence cautioni

The sequence AAI00559 differs from that shown. Reason: Frameshift at position 261.Curated
The sequence AAI00559 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAO17380 differs from that shown. Reason: Erroneous gene model prediction.Curated

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_02610880 – 145Missing in isoform 3. 1 PublicationAdd BLAST66
Alternative sequenceiVSP_026109146 – 147HG → VS in isoform 2. 1 Publication2
Alternative sequenceiVSP_026110148 – 1104Missing in isoform 2. 1 PublicationAdd BLAST957
Alternative sequenceiVSP_026111272 – 279AKLFQDSS → SAFLGLES in isoform 3. 1 Publication8
Alternative sequenceiVSP_026112280 – 1104Missing in isoform 3. 1 PublicationAdd BLAST825

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK046333 mRNA. Translation: BAC32684.1.
AF528163 Genomic DNA. Translation: AAO17380.1. Sequence problems.
BC100558 mRNA. Translation: AAI00559.1. Sequence problems.
AF302012 mRNA. Translation: AAK97226.1.
CCDSiCCDS37566.1. [P58459-1]
RefSeqiNP_766207.2. NM_172619.4. [P58459-1]
UniGeneiMm.29304.

Genome annotation databases

EnsembliENSMUST00000087623; ENSMUSP00000084905; ENSMUSG00000024299. [P58459-1]
GeneIDi224697.
KEGGimmu:224697.
UCSCiuc008bym.2. mouse. [P58459-2]
uc008byn.2. mouse. [P58459-3]
uc008byp.2. mouse. [P58459-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK046333 mRNA. Translation: BAC32684.1.
AF528163 Genomic DNA. Translation: AAO17380.1. Sequence problems.
BC100558 mRNA. Translation: AAI00559.1. Sequence problems.
AF302012 mRNA. Translation: AAK97226.1.
CCDSiCCDS37566.1. [P58459-1]
RefSeqiNP_766207.2. NM_172619.4. [P58459-1]
UniGeneiMm.29304.

3D structure databases

ProteinModelPortaliP58459.
SMRiP58459.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000084905.

Protein family/group databases

MEROPSiM12.235.

PTM databases

iPTMnetiP58459.
PhosphoSitePlusiP58459.

Proteomic databases

PaxDbiP58459.
PRIDEiP58459.

Protocols and materials databases

DNASUi224697.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000087623; ENSMUSP00000084905; ENSMUSG00000024299. [P58459-1]
GeneIDi224697.
KEGGimmu:224697.
UCSCiuc008bym.2. mouse. [P58459-2]
uc008byn.2. mouse. [P58459-3]
uc008byp.2. mouse. [P58459-1]

Organism-specific databases

CTDi81794.
MGIiMGI:2449112. Adamts10.

Phylogenomic databases

eggNOGiKOG3538. Eukaryota.
ENOG410XPKZ. LUCA.
GeneTreeiENSGT00760000118880.
HOGENOMiHOG000004800.
HOVERGENiHBG004315.
InParanoidiP58459.
KOiK08625.
OMAiICQTNTI.
OrthoDBiEOG091G14M8.
PhylomeDBiP58459.
TreeFamiTF313537.

Miscellaneous databases

PROiP58459.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000024299.
ExpressionAtlasiP58459. baseline and differential.
GenevisibleiP58459. MM.

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.
PF08686. PLAC. 1 hit.
PF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 5 hits.
[Graphical view]
PRINTSiPR01857. ADAMTSFAMILY.
SMARTiSM00209. TSP1. 5 hits.
[Graphical view]
SUPFAMiSSF82895. SSF82895. 5 hits.
PROSITEiPS50215. ADAM_MEPRO. 1 hit.
PS50900. PLAC. 1 hit.
PS50092. TSP1. 5 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiATS10_MOUSE
AccessioniPrimary (citable) accession number: P58459
Secondary accession number(s): Q497H1, Q78TI1, Q8CG28
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 5, 2001
Last sequence update: June 12, 2007
Last modified: November 2, 2016
This is version 121 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, 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.