Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P79331 (ATS2_BOVIN)

Last modified September 22, 2009. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein namesRecommended name:
    A disintegrin and metalloproteinase with thrombospondin motifs 2
      Short name=ADAMTS-2
      Short name=ADAM-TS 2
      Short name=ADAM-TS2
    EC=3.4.24.14
Alternative name(s):
    Procollagen I/II amino propeptide-processing enzyme
    Procollagen I N-proteinase
      Short name=PC I-NP
    Procollagen N-endopeptidase
      Short name=pNPI
Gene names
Name: ADAMTS2
Synonyms: NPI
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Hide | Top

Protein attributes

Sequence length1205 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

Hide | Top

General annotation (Comments)

Function

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 activity

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.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subunit structure

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

Subcellular location

Secreted › extracellular space › extracellular matrix By similarity.

Tissue specificity

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.

Domain

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

Post-translational modification

The N-terminus is blocked.

The precursor is cleaved by a furin endopeptidase By similarity.

Involvement in disease

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.

Sequence similarities

Contains 1 disintegrin domain.

Contains 1 peptidase M12B domain.

Contains 1 PLAC domain.

Contains 4 TSP type-1 domains.

Caution

Has sometimes been referred to as ADAMTS3.

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Potential
Propeptide29 – 253225 By similarity
PRO_0000029156
Chain254 – 1205952A disintegrin and metalloproteinase with thrombospondin motifs 2
PRO_0000029157

Regions

Domain260 – 464205Peptidase M12B
Domain474 – 55481Disintegrin
Domain555 – 61056TSP type-1 1
Domain848 – 90659TSP type-1 2
Domain908 – 96861TSP type-1 3
Domain969 – 102355TSP type-1 4
Domain1053 – 109139PLAC
Region717 – 845129Spacer
Motif685 – 6873Cell attachment site Potential
Compositional bias31 – 355Poly-Ala
Compositional bias177 – 1804Poly-Glu
Compositional bias612 – 716105Cys-rich

Sites

Active site4031 By similarity
Metal binding4021Zinc; catalytic Potential
Metal binding4061Zinc; catalytic By similarity
Metal binding4121Zinc; catalytic By similarity

Amino acid modifications

Glycosylation1041N-linked (GlcNAc...) Potential
Glycosylation2451N-linked (GlcNAc...) Potential
Glycosylation9421N-linked (GlcNAc...) Potential
Glycosylation9431N-linked (GlcNAc...) Potential
Glycosylation9871N-linked (GlcNAc...) Potential
Glycosylation10251N-linked (GlcNAc...) Potential
Glycosylation10921N-linked (GlcNAc...) Potential
Glycosylation11391N-linked (GlcNAc...) Potential
Glycosylation11441N-linked (GlcNAc...) Potential
Disulfide bond380 ↔ 459 By similarity
Disulfide bond419 ↔ 445 By similarity
Disulfide bond567 ↔ 604 By similarity
Disulfide bond571 ↔ 609 By similarity
Disulfide bond582 ↔ 594 By similarity
Disulfide bond981 ↔ 1017 By similarity
Disulfide bond985 ↔ 1022 By similarity
Disulfide bond996 ↔ 1006 By similarity

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
P79331-1 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 7B5B232A45320371

FASTA1,205133,888
        10         20         30         40         50         60 
MDPPAGAAGR LLCPALLLLL LLPLPADARL AAAAADPPGG PQGHGAERIL AVPVRTDAQG 

        70         80         90        100        110        120 
RLVSHVVSAA TAPAGVRTRR AAPAQIPGLS GGSEEDPGGR LFYNVTVFGR DLHLRLRPNA 

       130        140        150        160        170        180 
RLVAPGATVE WQGESGATRV EPLLGTCLYV GDVAGLAESS SVALSNCDGL AGLIRMEEEE 

       190        200        210        220        230        240 
FFIEPLEKGL AAKEAEQGRV HVVYHRPTTS RPPPLGGPQA LDTGISADSL DSLSRALGVL 

       250        260        270        280        290        300 
EERVNSSRRR MRRHAADDDY NIEVLLGVDD SVVQFHGTEH VQKYLLTLMN IVNEIYHDES 

       310        320        330        340        350        360 
LGAHINVVLV RIILLSYGKS MSLIEIGNPS QSLENVCRWA YLQQKPDTDH DEYHDHAIFL 

       370        380        390        400        410        420 
TRQDFGPSGM QGYAPVTGMC HPVRSCTLNH EDGFSSAFVV AHETGHVLGM EHDGQGNRCG 

       430        440        450        460        470        480 
DEVRLGSIMA PLVQAAFHRF HWSRCSQQEL SRYLHSYDCL RDDPFTHDWP ALPQLPGLHY 

       490        500        510        520        530        540 
SMNEQCRFDF GLGYMMCTAF RTFDPCKQLW CSHPDNPYFC KTKKGPPLDG TMCAPGKHCF 

       550        560        570        580        590        600 
KGHCIWLTPD ILKRDGNWGA WSPFGSCSRT CGTGVKFRTR QCDNPHPANG GRTCSGLAYD 

       610        620        630        640        650        660 
FQLCNSQDCP DALADFREEQ CRQWDLYFEH GDAQHHWLPH EHRDAKERCH LYCESKETGE 

       670        680        690        700        710        720 
VVSMKRMVHD GTRCSYKDAF SLCVRGDCRK VGCDGVIGSS KQEDKCGVCG GDNSHCKVVK 

       730        740        750        760        770        780 
GTFSRSPKKL GYIKMFEIPA GARHLLIQEA DTTSHHLAVK NLETGKFILN EENDVDPNSK 

       790        800        810        820        830        840 
TFIAMGVEWE YRDEDGRETL QTMGPLHGTI TVLVIPEGDA RISLTYKYMI HEDSLNVDDN 

       850        860        870        880        890        900 
NVLEDDSVGY EWALKKWSPC SKPCGGGSQF TKYGCRRRLD HKMVHRGFCD SVSKPKAIRR 

       910        920        930        940        950        960 
TCNPQECSQP VWVTGEWEPC SRSCGRTGMQ VRSVRCVQPL HNNTTRSVHT KHCNDARPEG 

       970        980        990       1000       1010       1020 
RRACNRELCP GRWRAGSWSQ CSVTCGNGTQ ERPVLCRTAD DSFGVCREER PETARICRLG 

      1030       1040       1050       1060       1070       1080 
PCPRNTSDPS KKSYVVQWLS RPDPNSPVQE TSSKGRCQGD KSVFCRMEVL SRYCSIPGYN 

      1090       1100       1110       1120       1130       1140 
KLCCKSCNPH DNLTDVDDRA EPPSGKHNDI EELMPTLSVP TLVMEVQPPP GIPLEVPLNT 

      1150       1160       1170       1180       1190       1200 
SSTNATEDHP ETNAVDVPYK IPGLEDEVQP PNLIPRRPSP YEKTRNQRIQ ELIDEMRKKE 


MLGKF

« Hide

Hide | Top

References

[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: 9122202] [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: 7622483] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE.

Hide | Top

Cross-references

Sequence databases

X96389 mRNA. Translation: CAA65253.1.
IPIIPI00695630.
PIRT18517.
RefSeqNP_777056.1.
UniGeneBt.96865

3D structure databases

HSSPHSSP built from PDB template 1LSL based on UniProtKB P07996.
ModBaseSearch...

Protein family/group databases

MEROPSM12.301.

Genome annotation databases

EnsemblENSBTAT00000019526; ENSBTAP00000019526; ENSBTAG00000014665; Bos taurus. [Genome view]
GeneID282401.
KEGGbta:282401.

Organism-specific databases

CTD282401.

Phylogenomic databases

HOVERGENP79331.

Enzyme and pathway databases

BRENDA3.4.24.14. 251.

Family and domain databases

InterProIPR010294. ADAM_spacer1.
IPR018358. Disintegrin_CS.
IPR013275. Pept_M12B_ADAM-TS2.
IPR006025. Pept_M_Zn_BS.
IPR001590. Peptidase_M12B.
IPR013273. Peptidase_M12B_ADAM-TS.
IPR002870. Peptidase_M12B_N.
IPR010909. PLAC.
IPR000884. Thrombospondin_1_rpt.
[Graphical view]
PfamPF05986. ADAM_spacer1. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 4 hits.
[Graphical view]
PRINTSPR01859. ADAMTS2.
PR01857. ADAMTSFAMILY.
SMARTSM00209. TSP1. 4 hits.
[Graphical view]
PROSITEPS50215. ADAM_MEPRO. 1 hit.
PS00427. DISINTEGRIN_1. False negative.
PS50214. DISINTEGRIN_2. False negative.
PS50900. PLAC. 1 hit.
PS50092. TSP1. 4 hits.
PS00142. ZINC_PROTEASE. False negative.
[Graphical view]
ProtoNetSearch...

Hide | Top

Entry information

Entry nameATS2_BOVIN
AccessionPrimary (citable) accession number: P79331
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 1997
Last modified: September 22, 2009
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Hide | Top

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents