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Protein

A disintegrin and metalloproteinase with thrombospondin motifs 15

Gene

Adamts15

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

Functioni

Cofactori

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi174 – 1741Zinc; in inhibited formBy similarity
Metal bindingi361 – 3611Zinc; catalyticBy similarity
Active sitei362 – 3621PROSITE-ProRule annotation
Metal bindingi365 – 3651Zinc; catalyticBy similarity
Metal bindingi371 – 3711Zinc; catalyticBy similarity

GO - Molecular functioni

  • endopeptidase activity Source: MGI
  • extracellular matrix binding Source: MGI
  • heparin binding Source: MGI
  • metalloendopeptidase activity Source: InterPro
  • zinc ion binding Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM12.025.

Names & Taxonomyi

Protein namesi
Recommended name:
A disintegrin and metalloproteinase with thrombospondin motifs 15 (EC:3.4.24.-)
Short name:
ADAM-TS 15
Short name:
ADAM-TS15
Short name:
ADAMTS-15
Gene namesi
Name:Adamts15
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:2449569. Adamts15.

Subcellular locationi

GO - Cellular componenti

  • cell surface Source: MGI
  • extracellular space 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 – 1818Sequence analysisAdd
BLAST
Propeptidei19 – 212194By similarityPRO_0000270787Add
BLAST
Chaini213 – 950738A disintegrin and metalloproteinase with thrombospondin motifs 15PRO_0000078212Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi141 – 1411N-linked (GlcNAc...)Sequence analysis
Disulfide bondi293 ↔ 345By similarity
Disulfide bondi322 ↔ 327By similarity
Disulfide bondi339 ↔ 422By similarity
Disulfide bondi377 ↔ 406By similarity
Disulfide bondi448 ↔ 470By similarity
Disulfide bondi459 ↔ 480By similarity
Disulfide bondi465 ↔ 499By similarity
Disulfide bondi493 ↔ 504By similarity
Disulfide bondi528 ↔ 565By similarity
Disulfide bondi532 ↔ 570By similarity
Disulfide bondi543 ↔ 555By similarity
Glycosylationi591 – 5911N-linked (GlcNAc...)Sequence analysis
Glycosylationi623 – 6231N-linked (GlcNAc...)Sequence analysis
Glycosylationi679 – 6791N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

The precursor is cleaved by a furin endopeptidase.By similarity
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, Zymogen

Proteomic databases

MaxQBiP59384.
PaxDbiP59384.
PRIDEiP59384.

PTM databases

iPTMnetiP59384.
PhosphoSiteiP59384.

Expressioni

Gene expression databases

BgeeiP59384.
GenevisibleiP59384. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000067022.

Structurei

3D structure databases

ProteinModelPortaliP59384.
SMRiP59384. Positions 218-690.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini218 – 427210Peptidase M12BPROSITE-ProRule annotationAdd
BLAST
Domaini428 – 51588DisintegrinAdd
BLAST
Domaini516 – 57156TSP type-1 1PROSITE-ProRule annotationAdd
BLAST
Domaini839 – 89557TSP type-1 2PROSITE-ProRule annotationAdd
BLAST
Domaini896 – 94954TSP type-1 3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni701 – 838138SpacerBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi172 – 1798Cysteine switchBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi572 – 700129Cys-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.

Sequence similaritiesi

Contains 1 disintegrin domain.Curated
Contains 1 peptidase M12B domain.PROSITE-ProRule annotation
Contains 3 TSP type-1 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiKOG3538. Eukaryota.
ENOG410XPKZ. LUCA.
GeneTreeiENSGT00760000118880.
HOGENOMiHOG000004799.
HOVERGENiHBG004313.
InParanoidiP59384.
KOiK08629.
OMAiFQEDFYL.
OrthoDBiEOG7WDN1M.
PhylomeDBiP59384.
TreeFamiTF331949.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR006586. ADAM_Cys-rich.
IPR010294. ADAM_spacer1.
IPR024079. MetalloPept_cat_dom.
IPR013277. Pept_M12B_ADAM-TS8.
IPR001590. Peptidase_M12B.
IPR013273. Peptidase_M12B_ADAM-TS.
IPR002870. Peptidase_M12B_N.
IPR000884. TSP1_rpt.
[Graphical view]
PfamiPF05986. ADAM_spacer1. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 3 hits.
[Graphical view]
PRINTSiPR01861. ADAMTS8.
PR01857. ADAMTSFAMILY.
SMARTiSM00608. ACR. 1 hit.
SM00209. TSP1. 3 hits.
[Graphical view]
SUPFAMiSSF82895. SSF82895. 3 hits.
PROSITEiPS50215. ADAM_MEPRO. 1 hit.
PS50092. TSP1. 3 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P59384-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLLLGISILA LAWRPAGSSE PEWEVVVPIR RDPDINGRHY YRRGTEDSGD
60 70 80 90 100
QGLIFQITAF QQDFYLHLTP DAQFLAPAFA TEYLGVPLQR LTGSSLDLRR
110 120 130 140 150
CFYSGYVNAE PDSFAAVSLC GGLRGAFGYR GAEYVISPLP NTSAPEAQRH
160 170 180 190 200
SQGAHLLQRR GAPVGPSGDP TSRCGVASGW NPAILRALDP YKPRRTGAGE
210 220 230 240 250
SHNRRRSGRA KRFVSIPRYV ETLVVADESM VKFHGADLEH YLLTLLATAA
260 270 280 290 300
RLYRHPSILN PINIVVVKVL LLGDRDTGPK VTGNAALTLR NFCAWQKKLN
310 320 330 340 350
KVSDKHPEYW DTAILFTRQD LCGATTCDTL GMADVGTMCD PKRSCSVIED
360 370 380 390 400
DGLPSAFTTA HELGHVFNMP HDNVKVCEEV FGKLRANHMM SPTLIQIDRA
410 420 430 440 450
NPWSACSAAI ITDFLDSGHG DCLLDQPSKP ITLPEDLPGT SYSLSQQCEL
460 470 480 490 500
AFGVGSKPCP YMQYCTKLWC TGKAKGQMVC QTRHFPWADG TSCGEGKFCL
510 520 530 540 550
KGACVERHNP NKYRVDGSWA KWEPYGSCSR TCGGGVQLAR RQCSNPTPAN
560 570 580 590 600
GGKYCEGVRV KYRSCNLEPC PSSASGKSFR EEQCEAFNGY NHSTNRLTLA
610 620 630 640 650
VAWVPKYSGV SPRDKCKLIC RANGTGYFYV LAPKVVDGTL CTPDSTSVCV
660 670 680 690 700
QGKCIKAGCD GNLGSKKKFD KCGVCGGDNK SCKRVTGLFT KPMHGYNFVV
710 720 730 740 750
AIPAGASSID IRQRGYKGLI GDDNYLALKN SQGKYLLNGH FVVSAVERDL
760 770 780 790 800
VVKGSVLRYS GTGTAVESLQ ASRPILEPLT VEVLSVGKMT PPRVRYSFYL
810 820 830 840 850
PKEPREDKST RPKDPRGSPV LRNSVLSLSN QVEQPDNRPP ARWVAGSWGP
860 870 880 890 900
CSVSCGSGLQ KRAVDCRDSP GQQGASACDV DHRPLEKRAC GEPCPTWELG
910 920 930 940 950
NWSPCSKSCG RGFKRRPLKC VGHGGRLLAR DQCDLRRKPQ ELDFCVLRPC
Length:950
Mass (Da):103,938
Last modified:January 9, 2007 - v2
Checksum:i891926F281E92010
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti389 – 3968MMSPTLIQ → AIPAGASS in AAH43308 (PubMed:15489334).Curated
Sequence conflicti611 – 6144SPRD → PRVR in AAH09667 (PubMed:15489334).Curated
Sequence conflicti819 – 8191P → L in AAH09667 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC009667 mRNA. Translation: AAH09667.1.
BC043308 mRNA. Translation: AAH43308.1.
BC094677 mRNA. Translation: AAH94677.1.
CCDSiCCDS22945.1.
RefSeqiNP_001019310.1. NM_001024139.1.
UniGeneiMm.65867.

Genome annotation databases

EnsembliENSMUST00000065112; ENSMUSP00000067022; ENSMUSG00000033453.
GeneIDi235130.
KEGGimmu:235130.
UCSCiuc009oqz.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC009667 mRNA. Translation: AAH09667.1.
BC043308 mRNA. Translation: AAH43308.1.
BC094677 mRNA. Translation: AAH94677.1.
CCDSiCCDS22945.1.
RefSeqiNP_001019310.1. NM_001024139.1.
UniGeneiMm.65867.

3D structure databases

ProteinModelPortaliP59384.
SMRiP59384. Positions 218-690.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000067022.

Protein family/group databases

MEROPSiM12.025.

PTM databases

iPTMnetiP59384.
PhosphoSiteiP59384.

Proteomic databases

MaxQBiP59384.
PaxDbiP59384.
PRIDEiP59384.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000065112; ENSMUSP00000067022; ENSMUSG00000033453.
GeneIDi235130.
KEGGimmu:235130.
UCSCiuc009oqz.1. mouse.

Organism-specific databases

CTDi170689.
MGIiMGI:2449569. Adamts15.

Phylogenomic databases

eggNOGiKOG3538. Eukaryota.
ENOG410XPKZ. LUCA.
GeneTreeiENSGT00760000118880.
HOGENOMiHOG000004799.
HOVERGENiHBG004313.
InParanoidiP59384.
KOiK08629.
OMAiFQEDFYL.
OrthoDBiEOG7WDN1M.
PhylomeDBiP59384.
TreeFamiTF331949.

Miscellaneous databases

PROiP59384.
SOURCEiSearch...

Gene expression databases

BgeeiP59384.
GenevisibleiP59384. MM.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR006586. ADAM_Cys-rich.
IPR010294. ADAM_spacer1.
IPR024079. MetalloPept_cat_dom.
IPR013277. Pept_M12B_ADAM-TS8.
IPR001590. Peptidase_M12B.
IPR013273. Peptidase_M12B_ADAM-TS.
IPR002870. Peptidase_M12B_N.
IPR000884. TSP1_rpt.
[Graphical view]
PfamiPF05986. ADAM_spacer1. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 3 hits.
[Graphical view]
PRINTSiPR01861. ADAMTS8.
PR01857. ADAMTSFAMILY.
SMARTiSM00608. ACR. 1 hit.
SM00209. TSP1. 3 hits.
[Graphical view]
SUPFAMiSSF82895. SSF82895. 3 hits.
PROSITEiPS50215. ADAM_MEPRO. 1 hit.
PS50092. TSP1. 3 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "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].
    Strain: C57BL/6J and FVB/N.
    Tissue: Brain and Kidney.

Entry informationi

Entry nameiATS15_MOUSE
AccessioniPrimary (citable) accession number: P59384
Secondary accession number(s): Q504Z2, Q91Z56
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 28, 2003
Last sequence update: January 9, 2007
Last modified: June 8, 2016
This is version 114 of the entry and version 2 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.