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Protein

A disintegrin and metalloproteinase with thrombospondin motifs 2

Gene

ADAMTS2

Organism
Bos taurus (Bovine)
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.

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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi402 – 4021Zinc; catalyticPROSITE-ProRule annotation
Active sitei403 – 4031PROSITE-ProRule annotation
Metal bindingi406 – 4061Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi412 – 4121Zinc; catalyticPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • collagen biosynthetic process Source: BHF-UCL
  • collagen catabolic process Source: UniProtKB-KW
  • collagen fibril organization Source: BHF-UCL
  • extracellular fibril organization Source: BHF-UCL
  • lung development Source: Ensembl
  • protein processing Source: BHF-UCL
  • skin development Source: Ensembl
  • spermatogenesis Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Collagen degradation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.4.24.14. 908.
ReactomeiR-BTA-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
Synonyms:NPI
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 7

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Defects in ADAMTS2 are the cause of dermatosparaxis, a recessively inherited disorder characterized by severe skin fragility and biochemically by the presence in skin of procollagen incompletely processed at the N-terminus.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828Sequence analysisAdd
BLAST
Propeptidei29 – 253225By similarityPRO_0000029156Add
BLAST
Chaini254 – 1205952A disintegrin and metalloproteinase with thrombospondin motifs 2PRO_0000029157Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi104 – 1041N-linked (GlcNAc...)Sequence analysis
Glycosylationi245 – 2451N-linked (GlcNAc...)Sequence analysis
Disulfide bondi337 ↔ 386By similarity
Disulfide bondi380 ↔ 459By similarity
Disulfide bondi419 ↔ 445By similarity
Disulfide bondi486 ↔ 511By similarity
Disulfide bondi497 ↔ 520By similarity
Disulfide bondi506 ↔ 539By similarity
Disulfide bondi533 ↔ 544By similarity
Disulfide bondi567 ↔ 604By similarity
Disulfide bondi571 ↔ 609By similarity
Disulfide bondi582 ↔ 594By similarity
Glycosylationi942 – 9421N-linked (GlcNAc...)Sequence analysis
Glycosylationi943 – 9431N-linked (GlcNAc...)Sequence analysis
Disulfide bondi981 ↔ 1017By similarity
Disulfide bondi985 ↔ 1022By similarity
Glycosylationi987 – 9871N-linked (GlcNAc...)Sequence analysis
Disulfide bondi996 ↔ 1006By similarity
Glycosylationi1025 – 10251N-linked (GlcNAc...)Sequence analysis
Glycosylationi1092 – 10921N-linked (GlcNAc...)Sequence analysis
Glycosylationi1139 – 11391N-linked (GlcNAc...)Sequence analysis
Glycosylationi1144 – 11441N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

The N-terminus is blocked.
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

PaxDbiP79331.
PRIDEiP79331.

Expressioni

Tissue specificityi

Enzymatic activity is detected at high level in all type I collagen-rich tissues such as skin, bones, tendons and aorta and at low level in brain and thymus. The mRNA levels were disproportionately high in heart, liver, retina and muscle.

Interactioni

Subunit structurei

May belong to a multimeric complex. Binds specifically to collagen type XIV.

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000019526.

Structurei

3D structure databases

ProteinModelPortaliP79331.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini260 – 464205Peptidase M12BPROSITE-ProRule annotationAdd
BLAST
Domaini474 – 55481DisintegrinAdd
BLAST
Domaini555 – 61056TSP type-1 1PROSITE-ProRule annotationAdd
BLAST
Domaini848 – 90659TSP type-1 2PROSITE-ProRule annotationAdd
BLAST
Domaini908 – 96861TSP type-1 3PROSITE-ProRule annotationAdd
BLAST
Domaini969 – 102355TSP type-1 4PROSITE-ProRule annotationAdd
BLAST
Domaini1053 – 109139PLACPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni717 – 845129SpacerAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi685 – 6873Cell attachment siteSequence analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi31 – 355Poly-Ala
Compositional biasi177 – 1804Poly-Glu
Compositional biasi612 – 716105Cys-richAdd
BLAST

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.
InParanoidiP79331.
KOiK08618.
OMAiIHEDSLN.
OrthoDBiEOG76HQ0N.
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.

P79331-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDPPAGAAGR LLCPALLLLL LLPLPADARL AAAAADPPGG PQGHGAERIL
60 70 80 90 100
AVPVRTDAQG RLVSHVVSAA TAPAGVRTRR AAPAQIPGLS GGSEEDPGGR
110 120 130 140 150
LFYNVTVFGR DLHLRLRPNA RLVAPGATVE WQGESGATRV EPLLGTCLYV
160 170 180 190 200
GDVAGLAESS SVALSNCDGL AGLIRMEEEE FFIEPLEKGL AAKEAEQGRV
210 220 230 240 250
HVVYHRPTTS RPPPLGGPQA LDTGISADSL DSLSRALGVL EERVNSSRRR
260 270 280 290 300
MRRHAADDDY NIEVLLGVDD SVVQFHGTEH VQKYLLTLMN IVNEIYHDES
310 320 330 340 350
LGAHINVVLV RIILLSYGKS MSLIEIGNPS QSLENVCRWA YLQQKPDTDH
360 370 380 390 400
DEYHDHAIFL TRQDFGPSGM QGYAPVTGMC HPVRSCTLNH EDGFSSAFVV
410 420 430 440 450
AHETGHVLGM EHDGQGNRCG DEVRLGSIMA PLVQAAFHRF HWSRCSQQEL
460 470 480 490 500
SRYLHSYDCL RDDPFTHDWP ALPQLPGLHY SMNEQCRFDF GLGYMMCTAF
510 520 530 540 550
RTFDPCKQLW CSHPDNPYFC KTKKGPPLDG TMCAPGKHCF KGHCIWLTPD
560 570 580 590 600
ILKRDGNWGA WSPFGSCSRT CGTGVKFRTR QCDNPHPANG GRTCSGLAYD
610 620 630 640 650
FQLCNSQDCP DALADFREEQ CRQWDLYFEH GDAQHHWLPH EHRDAKERCH
660 670 680 690 700
LYCESKETGE VVSMKRMVHD GTRCSYKDAF SLCVRGDCRK VGCDGVIGSS
710 720 730 740 750
KQEDKCGVCG GDNSHCKVVK GTFSRSPKKL GYIKMFEIPA GARHLLIQEA
760 770 780 790 800
DTTSHHLAVK NLETGKFILN EENDVDPNSK TFIAMGVEWE YRDEDGRETL
810 820 830 840 850
QTMGPLHGTI TVLVIPEGDA RISLTYKYMI HEDSLNVDDN NVLEDDSVGY
860 870 880 890 900
EWALKKWSPC SKPCGGGSQF TKYGCRRRLD HKMVHRGFCD SVSKPKAIRR
910 920 930 940 950
TCNPQECSQP VWVTGEWEPC SRSCGRTGMQ VRSVRCVQPL HNNTTRSVHT
960 970 980 990 1000
KHCNDARPEG RRACNRELCP GRWRAGSWSQ CSVTCGNGTQ ERPVLCRTAD
1010 1020 1030 1040 1050
DSFGVCREER PETARICRLG PCPRNTSDPS KKSYVVQWLS RPDPNSPVQE
1060 1070 1080 1090 1100
TSSKGRCQGD KSVFCRMEVL SRYCSIPGYN KLCCKSCNPH DNLTDVDDRA
1110 1120 1130 1140 1150
EPPSGKHNDI EELMPTLSVP TLVMEVQPPP GIPLEVPLNT SSTNATEDHP
1160 1170 1180 1190 1200
ETNAVDVPYK IPGLEDEVQP PNLIPRRPSP YEKTRNQRIQ ELIDEMRKKE

MLGKF
Length:1,205
Mass (Da):133,888
Last modified:May 1, 1997 - v1
Checksum:i7B5B232A45320371
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X96389 mRNA. Translation: CAA65253.1.
PIRiT18517.
RefSeqiNP_777056.1. NM_174631.2.
UniGeneiBt.96865.

Genome annotation databases

EnsembliENSBTAT00000019526; ENSBTAP00000019526; ENSBTAG00000014665.
GeneIDi282401.
KEGGibta:282401.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X96389 mRNA. Translation: CAA65253.1.
PIRiT18517.
RefSeqiNP_777056.1. NM_174631.2.
UniGeneiBt.96865.

3D structure databases

ProteinModelPortaliP79331.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000019526.

Protein family/group databases

MEROPSiM12.301.

Proteomic databases

PaxDbiP79331.
PRIDEiP79331.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000019526; ENSBTAP00000019526; ENSBTAG00000014665.
GeneIDi282401.
KEGGibta:282401.

Organism-specific databases

CTDi9509.

Phylogenomic databases

eggNOGiENOG410INDA. Eukaryota.
ENOG410XSRH. LUCA.
GeneTreeiENSGT00760000118880.
HOGENOMiHOG000034222.
HOVERGENiHBG004314.
InParanoidiP79331.
KOiK08618.
OMAiIHEDSLN.
OrthoDBiEOG76HQ0N.
TreeFamiTF313537.

Enzyme and pathway databases

BRENDAi3.4.24.14. 908.
ReactomeiR-BTA-1650814. Collagen biosynthesis and modifying enzymes.

Miscellaneous databases

NextBioi20806187.

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...

Publicationsi

  1. "cDNA cloning and expression of bovine procollagen I N-proteinase: a new member of the superfamily of zinc-metalloproteinases with binding sites for cells and other matrix components."
    Colige A., Li S.W., Sieron A.L., Nusgens B.V., Prockop D.J., Lapiere C.M.
    Proc. Natl. Acad. Sci. U.S.A. 94:2374-2379(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Skin.
  2. "Characterization and partial amino acid sequencing of a 107-kDa procollagen I N-proteinase purified by affinity chromatography on immobilized type XIV collagen."
    Colige A., Beschin A., Samyn B., Goebels Y., Van Beeumen J., Nusgens B.V., Lapiere C.M.
    J. Biol. Chem. 270:16724-16730(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE.

Entry informationi

Entry nameiATS2_BOVIN
AccessioniPrimary (citable) accession number: P79331
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 1997
Last modified: January 20, 2016
This is version 144 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Has sometimes been referred to as ADAMTS3.Curated

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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.