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Protein

A disintegrin and metalloproteinase with thrombospondin motifs 2

Gene

ADAMTS2

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: -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.

Caution

Has sometimes been referred to as ADAMTS3.Curated

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 bindingi402Zinc; catalyticPROSITE-ProRule annotation1
Active sitei403PROSITE-ProRule annotation1
Metal bindingi406Zinc; catalyticPROSITE-ProRule annotation1
Metal bindingi412Zinc; catalyticPROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

  • collagen biosynthetic process Source: BHF-UCL
  • collagen catabolic process Source: UniProtKB-KW
  • collagen fibril organization Source: BHF-UCL
  • lung development Source: Ensembl
  • protein processing Source: BHF-UCL
  • skin development Source: Ensembl
  • spermatogenesis Source: Ensembl
  • supramolecular fiber organization Source: BHF-UCL

Keywordsi

Molecular functionHydrolase, Metalloprotease, Protease
Biological processCollagen degradation
LigandMetal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.4.24.14 908
ReactomeiR-BTA-1650814 Collagen biosynthesis and modifying enzymes
R-BTA-5173214 O-glycosylation of TSR domain-containing proteins

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

Organism-specific databases

VGNCiVGNC:25624 ADAMTS2

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 28Sequence analysisAdd BLAST28
PropeptideiPRO_000002915629 – 253By similarityAdd BLAST225
ChainiPRO_0000029157254 – 1205A disintegrin and metalloproteinase with thrombospondin motifs 2Add BLAST952

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi104N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi245N-linked (GlcNAc...) asparagineSequence analysis1
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
Glycosylationi942N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi943N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi981 ↔ 1017By similarity
Disulfide bondi985 ↔ 1022By similarity
Glycosylationi987N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi996 ↔ 1006By similarity
Glycosylationi1025N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1092N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1139N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1144N-linked (GlcNAc...) asparagineSequence analysis1

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-X2-(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.

Gene expression databases

BgeeiENSBTAG00000014665

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
SMRiP79331
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini260 – 464Peptidase M12BPROSITE-ProRule annotationAdd BLAST205
Domaini474 – 554DisintegrinAdd BLAST81
Domaini555 – 610TSP type-1 1PROSITE-ProRule annotationAdd BLAST56
Domaini848 – 906TSP type-1 2PROSITE-ProRule annotationAdd BLAST59
Domaini908 – 968TSP type-1 3PROSITE-ProRule annotationAdd BLAST61
Domaini969 – 1023TSP type-1 4PROSITE-ProRule annotationAdd BLAST55
Domaini1053 – 1091PLACPROSITE-ProRule annotationAdd BLAST39

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni717 – 845SpacerAdd BLAST129

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi685 – 687Cell attachment siteSequence analysis3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi31 – 35Poly-Ala5
Compositional biasi177 – 180Poly-Glu4
Compositional biasi612 – 716Cys-richAdd BLAST105

Domaini

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

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG410INDA Eukaryota
ENOG410XSRH LUCA
GeneTreeiENSGT00900000140815
HOGENOMiHOG000034222
HOVERGENiHBG004314
InParanoidiP79331
KOiK08618
OMAiGVEWEYR
OrthoDBiEOG091G0790
TreeFamiTF313537

Family and domain databases

Gene3Di2.20.100.10, 4 hits
3.40.390.10, 1 hit
InterProiView protein in InterPro
IPR010294 ADAM_spacer1
IPR024079 MetalloPept_cat_dom_sf
IPR013275 Pept_M12B_ADAM-TS2
IPR001590 Peptidase_M12B
IPR002870 Peptidase_M12B_N
IPR010909 PLAC
IPR000884 TSP1_rpt
IPR036383 TSP1_rpt_sf
PfamiView protein in Pfam
PF05986 ADAM_spacer1, 1 hit
PF01562 Pep_M12B_propep, 1 hit
PF01421 Reprolysin, 1 hit
PF00090 TSP_1, 4 hits
PRINTSiPR01859 ADAMTS2
SMARTiView protein in SMART
SM00209 TSP1, 4 hits
SUPFAMiSSF82895 SSF82895, 4 hits
PROSITEiView protein in PROSITE
PS50215 ADAM_MEPRO, 1 hit
PS50900 PLAC, 1 hit
PS50092 TSP1, 4 hits

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

Similar proteinsi

Entry informationi

Entry nameiATS2_BOVIN
AccessioniPrimary (citable) accession number: P79331
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 1997
Last modified: May 23, 2018
This is version 156 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health