Primary Information |
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| BoMiProt ID | Bomi3573 |
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| Protein Name | A disintegrin and metalloproteinase with thrombospondin motifs 2/ADAM-TS 2/Procollagen I N-proteinase/Procollagen I/II amino propeptide-processing enzyme/Procollagen N-endopeptidase |
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| Organism | Bos taurus |
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| Uniprot ID | P79331 |
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| Milk Fraction | Whey |
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| Ref Sequence ID | NP_777056.1 |
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| Aminoacid Length | 1205 |
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| Molecular Weight | 133888 |
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| FASTA Sequence |
Download |
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| Gene Name | ADAMTS2/NPI |
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| Gene ID | 282401 |
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| Protein Existence Status | reviewed |
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Secondary Information |
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| Protein Function | a disintegrin and metalloproteinase with thrombospondin motifs.The amino-propeptide of collagen is usually processed by procollagen N-proteinases such as ADAMTS2. LOX(Lysyl oxidase) precursor is proteolytically processed by the procollagen N-proteinases ADAMTS2 |
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| Biochemical Properties | Contains several distinct protein modules, including a propeptide region, a metalloproteinase domain, a disintegrin-like domain, and a thrombospondin type 1 (TS) motif. possesses two potential cleavage sites by mammalian subtilisins such as furin.Recombinant ADAMTS2 mutated at the furin-cleavage site separating the pro domain and the metalloprotease domain lacks enzymatic activity, demonstrating that ADAMTS2 is synthesized as a proenzyme. |
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| Significance in milk | associated with protein processing upregulated during lactation |
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| PTMs | Cleavage by Furin .Glycosylation.O-fucosylated by POFUT2 on a serine or a threonine residue found within the consensus sequence C1-X2-(S/T)-C2-G |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| >sp|P79331|ATS2_BOVIN A disintegrin and metalloproteinase with thrombospondin motifs 2 OS=Bos taurus OX=9913 GN=ADAMTS2 PE=1 SV=1
MDPPAGAAGRLLCPALLLLLLLPLPADARLAAAAADPPGGPQGHGAERILAVPVRTDAQG
RLVSHVVSAATAPAGVRTRRAAPAQIPGLSGGSEEDPGGRLFYN*104VTVFGRDLHLRLRPNA
RLVAPGATVEWQGESGATRVEPLLGTCLYVGDVAGLAESSSVALSNCDGLAGLIRMEEEE
FFIEPLEKGLAAKEAEQGRVHVVYHRPTTSRPPPLGGPQALDTGISADSLDSLSRALGVL
EERVN*245SSRRRMRRHAADDDYNIEVLLGVDDSVVQFHGTEHVQKYLLTLMNIVNEIYHDES
LGAHINVVLVRIILLSYGKSMSLIEIGNPSQSLENVCRWAYLQQKPDTDHDEYHDHAIFL
TRQDFGPSGMQGYAPVTGMCHPVRSCTLNHEDGFSSAFVVAHETGHVLGMEHDGQGNRCG
DEVRLGSIMAPLVQAAFHRFHWSRCSQQELSRYLHSYDCLRDDPFTHDWPALPQLPGLHY
SMNEQCRFDFGLGYMMCTAFRTFDPCKQLWCSHPDNPYFCKTKKGPPLDGTMCAPGKHCF
KGHCIWLTPDILKRDGNWGAWSPFGSCSRTCGTGVKFRTRQCDNPHPANGGRTCSGLAYD
FQLCNSQDCPDALADFREEQCRQWDLYFEHGDAQHHWLPHEHRDAKERCHLYCESKETGE
VVSMKRMVHDGTRCSYKDAFSLCVRGDCRKVGCDGVIGSSKQEDKCGVCGGDNSHCKVVK
GTFSRSPKKLGYIKMFEIPAGARHLLIQEADTTSHHLAVKNLETGKFILNEENDVDPNSK
TFIAMGVEWEYRDEDGRETLQTMGPLHGTITVLVIPEGDARISLTYKYMIHEDSLNVDDN
NVLEDDSVGYEWALKKWSPCSKPCGGGSQFTKYGCRRRLDHKMVHRGFCDSVSKPKAIRR
TCNPQECSQPVWVTGEWEPCSRSCGRTGMQVRSVRCVQPLHN*942N*943TTRSVHTKHCNDARPEG
RRACNRELCPGRWRAGSWSQCSVTCGNGT*987QERPVLCRTADDSFGVCREERPETARICRLG
PCPRN*1025TSDPSKKSYVVQWLSRPDPNSPVQETSSKGRCQGDKSVFCRMEVLSRYCSIPGYN
KLCCKSCNPHDN*1092LTDVDDRAEPPSGKHNDIEELMPTLSVPTLVMEVQPPPGIPLEVPLN*1139TSSTN*1144ATEDHPETNAVDVPYKIPGLEDEVQPPNLIPRRPSPYEKTRNQRIQELIDEMRKKE
MLGKF
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| Predicted Disorder Regions | NA |
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| DisProt Annotation | |
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| TM Helix Prediction | No TM helices |
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| Significance of PTMs | Cleaved by furin endopeptidase which is needed for its activation. O-fucosylated by POFUT2 on a serine or a threonine residue found within the consensus sequence C1-X2-(S/T)-C2-G.Fucosylation mediates the efficient secretion of ADAMTS family members |
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| Bibliography | 1.Colige, A., Ruggiero, F., Vandenberghe, I., Dubail, J., Kesteloot, F., Van Beeumen, J., ... & Nusgens, B. (2005). Domains and maturation processes that regulate the activity of ADAMTS-2, a metalloproteinase cleaving the aminopropeptide of fibrillar procollagens types I–III and V. Journal of Biological Chemistry, 280(41), 34397-34408. 2.Bekhouche M, Colige A. The procollagen N-proteinases ADAMTS2, 3 and 14 in pathophysiology. Matrix Biol. 2015 May-Jul;44-46:46-53. doi: 10.1016/j.matbio.2015.04.001. Epub 2015 Apr 8. PMID: 25863161. |
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