Search by BoMiProt ID - Bomi3573


Primary Information

BoMiProt ID Bomi3573
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
Organism Bos taurus
Uniprot IdP79331
Milk FractionWhey
Ref Sequence Id NP_777056.1
Aminoacid Length 1205
Molecular Weight 133888
Fasta Sequence https://www.uniprot.org/uniprot/P79331.fasta
Gene Name ADAMTS2/NPI
Gene Id 282401
Protein Existence Status reviewed

Secondary Information

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
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.
Significance in milk associated with protein processing upregulated during lactation
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
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
Predicted Disorder Regions NA
DisProt Annotation
TM Helix Prediction No TM helices
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
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.