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Protein

A disintegrin and metalloproteinase with thrombospondin motifs 2

Gene

Adamts2

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

Functioni

Cleaves the propeptides of type I and II collagen prior to fibril assembly. Does not act on type III collagen. May also play a role in development that is independent of its role in collagen biosynthesis (By similarity).By similarity

Catalytic activityi

Cleaves the N-propeptide of collagen chain alpha-1(I) at Pro-|-Gln and of alpha-1(II) and alpha-2(I) at Ala-|-Gln.

Cofactori

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi409Zinc; catalyticPROSITE-ProRule annotation1
Active sitei410PROSITE-ProRule annotation1
Metal bindingi413Zinc; catalyticPROSITE-ProRule annotation1
Metal bindingi419Zinc; catalyticPROSITE-ProRule annotation1

GO - Molecular functioni

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

GO - Biological processi

  • collagen catabolic process Source: UniProtKB-KW
  • collagen fibril organization Source: MGI
  • lung development Source: MGI
  • protein processing Source: MGI
  • skin development Source: MGI
  • spermatogenesis Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Collagen degradation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-1650814. Collagen biosynthesis and modifying enzymes.

Protein family/group databases

MEROPSiM12.301.

Names & Taxonomyi

Protein namesi
Recommended name:
A disintegrin and metalloproteinase with thrombospondin motifs 2 (EC:3.4.24.14)
Short name:
ADAM-TS 2
Short name:
ADAM-TS2
Short name:
ADAMTS-2
Alternative name(s):
Procollagen I N-proteinase
Short name:
PC I-NP
Procollagen I/II amino propeptide-processing enzyme
Procollagen N-endopeptidase
Short name:
pNPI
Gene namesi
Name:Adamts2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1347356. Adamts2.

Subcellular locationi

GO - Cellular componenti

  • proteinaceous extracellular matrix Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 28Sequence analysisAdd BLAST28
PropeptideiPRO_000002916129 – 260By similarityAdd BLAST232
ChainiPRO_0000029160261 – 1213A disintegrin and metalloproteinase with thrombospondin motifs 2Add BLAST953

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi111N-linked (GlcNAc...)Sequence analysis1
Glycosylationi252N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi344 ↔ 393By similarity
Disulfide bondi387 ↔ 466By similarity
Disulfide bondi426 ↔ 452By similarity
Disulfide bondi493 ↔ 518By similarity
Disulfide bondi504 ↔ 527By similarity
Disulfide bondi513 ↔ 546By similarity
Disulfide bondi540 ↔ 551By similarity
Disulfide bondi574 ↔ 611By similarity
Disulfide bondi578 ↔ 616By similarity
Disulfide bondi589 ↔ 601By similarity
Glycosylationi949N-linked (GlcNAc...)Sequence analysis1
Glycosylationi950N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi988 ↔ 1024By similarity
Disulfide bondi992 ↔ 1029By similarity
Glycosylationi994N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1003 ↔ 1013By similarity
Glycosylationi1032N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1099N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1147N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1152N-linked (GlcNAc...)Sequence analysis1

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

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

MaxQBiQ8C9W3.
PaxDbiQ8C9W3.
PRIDEiQ8C9W3.

PTM databases

PhosphoSitePlusiQ8C9W3.

Expressioni

Gene expression databases

BgeeiENSMUSG00000036545.
GenevisibleiQ8C9W3. MM.

Interactioni

Subunit structurei

May belong to a multimeric complex. Binds specifically to collagen type XIV (By similarity).By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000040171.

Structurei

3D structure databases

ProteinModelPortaliQ8C9W3.
SMRiQ8C9W3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini267 – 471Peptidase M12BPROSITE-ProRule annotationAdd BLAST205
Domaini480 – 560DisintegrinAdd BLAST81
Domaini561 – 617TSP type-1 1PROSITE-ProRule annotationAdd BLAST57
Domaini855 – 913TSP type-1 2PROSITE-ProRule annotationAdd BLAST59
Domaini915 – 975TSP type-1 3PROSITE-ProRule annotationAdd BLAST61
Domaini976 – 1030TSP type-1 4PROSITE-ProRule annotationAdd BLAST55
Domaini1060 – 1098PLACPROSITE-ProRule annotationAdd BLAST39

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni723 – 851SpacerAdd BLAST129

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi692 – 694Cell attachment siteSequence analysis3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi618 – 722Cys-richAdd BLAST105

Domaini

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

Sequence similaritiesi

Contains 1 disintegrin domain.Curated
Contains 1 peptidase M12B domain.PROSITE-ProRule annotation
Contains 1 PLAC domain.PROSITE-ProRule annotation
Contains 4 TSP type-1 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG410INDA. Eukaryota.
ENOG410XSRH. LUCA.
GeneTreeiENSGT00760000118880.
HOGENOMiHOG000034222.
HOVERGENiHBG004314.
InParanoidiQ8C9W3.
KOiK08618.
OMAiIHEDSLN.
OrthoDBiEOG091G0790.
PhylomeDBiQ8C9W3.
TreeFamiTF313537.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR010294. ADAM_spacer1.
IPR024079. MetalloPept_cat_dom.
IPR013275. Pept_M12B_ADAM-TS2.
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. 4 hits.
[Graphical view]
PRINTSiPR01859. ADAMTS2.
PR01857. ADAMTSFAMILY.
SMARTiSM00209. TSP1. 4 hits.
[Graphical view]
SUPFAMiSSF82895. SSF82895. 4 hits.
PROSITEiPS50215. ADAM_MEPRO. 1 hit.
PS50900. PLAC. 1 hit.
PS50092. TSP1. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q8C9W3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDPPAGAARR LLCPALLLLL LPPPPLLLLP PPPASVRLVA ATEPPGGPPG
60 70 80 90 100
QGAERILAVP VRTDAQGRLV SHVVSLETAG AGVRARRAAL DQTSGLPGGA
110 120 130 140 150
AQDPGGRLFY NLTVFGRDLH LRLRPNARLV APGATVEWQG ETGDTRVEPL
160 170 180 190 200
LGSCLYVGDV ADLPKASSVA LSNCDGLAGL IRMEEEEFFI EPLEKGQTDQ
210 220 230 240 250
EAEQGRVHVV YRRPPTPKPP PVSEPQALDT GVSQGNLDSL SRALGVLEER
260 270 280 290 300
INSSRRRVRR HATDDDYNIE VLLGVDDSVV QFHGKEHVQK YLLTLMNIVN
310 320 330 340 350
EIYHDESLGA HINVVLVRII LLSHAKSMSL IEIGNPSQSL ENVCRWAYLQ
360 370 380 390 400
QKPDTDHDEY HDHAIFLTRQ DFGPSGMQGY APVTGMCHPV RSCTLNHEDG
410 420 430 440 450
FSSAFVVAHE TGHVLGMEHD GQGNRCGDEV RLGSIMAPLV QAAFHRFHWS
460 470 480 490 500
RCSQQELSRY LHSYDCLRDD PFAHDWPALP QLPGLHYSMN EQCRFDFGLG
510 520 530 540 550
YMMCTAFRTF DPCKQLWCSH PDNPYFCKTK KGPPLDGTMC APGKHCFKGH
560 570 580 590 600
CIWLTPDILK RDGNWGAWTP FGSCSRTCGT GVKFRTRQCD NPHPANGGRT
610 620 630 640 650
CSGLAYDFQL CNPQDCPNSL ADFREEQCQQ WDLYFEHGDV QHHWLPHEHR
660 670 680 690 700
DAKERCHLYC ESKETGEVVS MKRMVHDGTR CSYKDAFSLC VRGDCRKVGC
710 720 730 740 750
DGVIGSRKQE DKCGVCGGDN THCKVVKGTF TRSPRKQDYI KMFEIPAGAR
760 770 780 790 800
HLLIQEADTT SHHLSVKNLE TGKFILNEEN HLDPNSRSFI AMGVEWEYRN
810 820 830 840 850
EDERETLQTI GPLHGTITVL VIPEGDTRIS LTYKYMIHED SLNVDDNNVL
860 870 880 890 900
EDDAVRHEWA LKKWSPCSKP CGGGSQFTKY GCRRRLDSKM VHRAFCSALA
910 920 930 940 950
KPKAIRRACN PQECSQPVWV TGEWEPCTQS CGRTGMQVRS VRCIQPLHNN
960 970 980 990 1000
TTRSVHTKHC NDHRPESRRA CNRELCPGRW RAGSWSQCSV TCGNGTQERP
1010 1020 1030 1040 1050
VLCRTADDNF GVCREERPET ARICRLAPCP RNGSDPSKKS YVVQWLSRPD
1060 1070 1080 1090 1100
PDSPIQKISS KDQCQGDKSM FCRMEVLSRY CSIPSYNKLC CKSCNPPRNL
1110 1120 1130 1140 1150
SNTEDGGVEP PPGKHNDIDV FMPTLPGPTV ATQVQPSPGP PLEAPLNVSS
1160 1170 1180 1190 1200
TNATEDHPET NAVDVPYKIH GVDEEVPSPN LIPRRPSLYV KTRNQRIQEL
1210
INAVQRKEKP GKF
Length:1,213
Mass (Da):135,299
Last modified:June 20, 2003 - v2
Checksum:iB27431E00443EDB5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK040370 mRNA. Translation: BAC30572.1.
BC046456 mRNA. Translation: AAH46456.1.
CCDSiCCDS24636.1.
RefSeqiNP_783574.1. NM_175643.3.
UniGeneiMm.110597.
Mm.339048.

Genome annotation databases

EnsembliENSMUST00000040523; ENSMUSP00000040171; ENSMUSG00000036545.
GeneIDi216725.
KEGGimmu:216725.
UCSCiuc007iso.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK040370 mRNA. Translation: BAC30572.1.
BC046456 mRNA. Translation: AAH46456.1.
CCDSiCCDS24636.1.
RefSeqiNP_783574.1. NM_175643.3.
UniGeneiMm.110597.
Mm.339048.

3D structure databases

ProteinModelPortaliQ8C9W3.
SMRiQ8C9W3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000040171.

Protein family/group databases

MEROPSiM12.301.

PTM databases

PhosphoSitePlusiQ8C9W3.

Proteomic databases

MaxQBiQ8C9W3.
PaxDbiQ8C9W3.
PRIDEiQ8C9W3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000040523; ENSMUSP00000040171; ENSMUSG00000036545.
GeneIDi216725.
KEGGimmu:216725.
UCSCiuc007iso.2. mouse.

Organism-specific databases

CTDi9509.
MGIiMGI:1347356. Adamts2.

Phylogenomic databases

eggNOGiENOG410INDA. Eukaryota.
ENOG410XSRH. LUCA.
GeneTreeiENSGT00760000118880.
HOGENOMiHOG000034222.
HOVERGENiHBG004314.
InParanoidiQ8C9W3.
KOiK08618.
OMAiIHEDSLN.
OrthoDBiEOG091G0790.
PhylomeDBiQ8C9W3.
TreeFamiTF313537.

Enzyme and pathway databases

ReactomeiR-MMU-1650814. Collagen biosynthesis and modifying enzymes.

Miscellaneous databases

PROiQ8C9W3.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000036545.
GenevisibleiQ8C9W3. MM.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR010294. ADAM_spacer1.
IPR024079. MetalloPept_cat_dom.
IPR013275. Pept_M12B_ADAM-TS2.
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. 4 hits.
[Graphical view]
PRINTSiPR01859. ADAMTS2.
PR01857. ADAMTSFAMILY.
SMARTiSM00209. TSP1. 4 hits.
[Graphical view]
SUPFAMiSSF82895. SSF82895. 4 hits.
PROSITEiPS50215. ADAM_MEPRO. 1 hit.
PS50900. PLAC. 1 hit.
PS50092. TSP1. 4 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiATS2_MOUSE
AccessioniPrimary (citable) accession number: Q8C9W3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: June 20, 2003
Last modified: November 2, 2016
This is version 129 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, 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.