Protein detail
ATS2
A disintegrin and metalloproteinase with thrombospondin motifs 2 (ADAM-TS 2) (ADAM-TS2) (ADAMTS-2) (EC 3.4.24.14) (Procollagen I N-proteinase) (PC I-NP) (Procollagen I/II amino propeptide-processing enzyme) (Procollagen N-endopeptidase) (pNPI)
Entry name ATS2 | UniProt ID | EVMP score 0.38 |
Frequency 1 | Transmembrane count | Protein classification Disease related genesEnzymesHuman disease related genesPlasma proteinsPotential drug targetsPredicted secreted proteins |
EVMP score: annotation confidence score.
Extremely high >= 0.85High >= 0.70Medium >= 0.55Low >= 0.40
Basic Information
Protein Names
A disintegrin and metalloproteinase with thrombospondin motifs 2 (ADAM-TS 2) (ADAM-TS2) (ADAMTS-2) (EC 3.4.24.14) (Procollagen I N-proteinase) (PC I-NP) (Procollagen I/II amino propeptide-processing enzyme) (Procollagen N-endopeptidase) (pNPI)
Protein Class
Disease related genesEnzymesHuman disease related genesPlasma proteinsPotential drug targetsPredicted secreted proteins
Protein Function
- Potential drug targets
- Enzymes
- Predicted secreted proteins
- Human disease related genes:Congenital malformations:Congenital malformations of skin
- ENZYME proteins:Hydrolases
- Disease related genes
Ensembl
Entrez Gene Symbol
Gene Synonym
ADAM-TS2ADAMTS-3hPCPNINPIPCINP
Gene Description
ADAM metallopeptidase with thrombospondin type 1 motif 2
Chromosome
5
Position
179110853-179345461
Frequency
1
EVMP Score
0.38
Fluorescence & Localization
Tissue SpecificprostateCell SpecificAlveolar cells type 2Single-Nuclei Brain Specificchoroid plexus epithelial cellSecretome LocationSecreted in other tissuesSecretome FunctionEnzyme
Function & Pathway
Protein Function
- Potential drug targets
- Enzymes
- Predicted secreted proteins
- Human disease related genes:Congenital malformations:Congenital malformations of skin
- ENZYME proteins:Hydrolases
- Disease related genes
Cellular Component
Molecular Function
Biological Process
Reactome
- R-hsa-1650814 collagen biosynthesis and modifying enzymes
- R-hsa-1474290 collagen formation
- R-hsa-3906995 diseases associated with o glycosylation of proteins
- R-hsa-3781865 diseases of glycosylation
- R-hsa-5668914 diseases of metabolism
- R-hsa-1474244 extracellular matrix organization
- R-hsa-5173214 o glycosylation of tsr domain containing proteins
- R-hsa-5173105 o linked glycosylation
- R-hsa-597592 post translational protein modification
Mediation Categories
Clinical-translation mediationMetabolism mediation
Relations & Evidence
Enzyme-Mediated Modification
0 records.
Ligand-Receptor Signaling
22 records.
| Category | Parent | Database | Transmitter | Receiver | Secreted | Plasma Membrane (Transmembrane) | Plasma Membrane (Peripheral) |
|---|---|---|---|---|---|---|---|
| secreted | secreted | OmniPath | No | No | Yes | No | No |
| receptor | receptor | scConnect | No | Yes | Yes | No | No |
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Regulatory Interaction Network
0 records.
Protein Complex Composition
0 records.
Sequence, Structure & Domains
Sequences
Length
1,211
Mass
134,755
Sequence
MDPPAGAARRLLCPALLLLLLLLPPPLLPPPPPPANARLAAAADPPGGPLGHGAERILAVPVRTDAQGRLVSHVVSAATSRAGVRARRAAPVRTPSFPGGNEEEPGSHLFYNVTVFGRDLHLRLRPNARLVAPGATMEWQGEKGTTRVEPLLGSCLYVGDVAGLAEASSVALSNCDGLAGLIRMEEEEFFIEPLEKGLAAQEAEQGRVHVVYRRPPTSPPLGGPQALDTGASLDSLDSLSRALGVLEEHANSSRRRARRHAADDDYNIEVLLGVDDSVVQFHGKEHVQKYLLTLMNIVNEIYHDESLGAHINVVLVRIILLSYGKSMSLIEIGNPSQSLENVCRWAYLQQKPDTGHDEYHDHAIFLTRQDFGPSGMQGYAPVTGMCHPVRSCTLNHEDGFSSAFVVAHETGHVLGMEHDGQGNRCGDEVRLGSIMAPLVQAAFHRFHWSRCSQQELSRYLHSYDCLLDDPFAHDWPALPQLPGLHYSMNEQCRFDFGLGYMMCTAFRTFDPCKQLWCSHPDNPYFCKTKKGPPLDGTMCAPGKHCFKGHCIWLTPDILKRDGSWGAWSPFGSCSRTCGTGVKFRTRQCDNPHPANGGRTCSGLAYDFQLCSRQDCPDSLADFREEQCRQWDLYFEHGDAQHHWLPHEHRDAKERCHLYCESRETGEVVSMKRMVHDGTRCSYKDAFSLCVRGDCRKVGCDGVIGSSKQEDKCGVCGGDNSHCKVVKGTFTRSPKKHGYIKMFEIPAGARHLLIQEVDATSHHLAVKNLETGKFILNEENDVDASSKTFIAMGVEWEYRDEDGRETLQTMGPLHGTITVLVIPVGDTRVSLTYKYMIHEDSLNVDDNNVLEEDSVVYEWALKKWSPCSKPCGGGSQFTKYGCRRRLDHKMVHRGFCAALSKPKAIRRACNPQECSQPVWVTGEWEPCSQTCGRTGMQVRSVRCIQPLHDNTTRSVHAKHCNDARPESRRACSRELCPGRWRAGPWSQCSVTCGNGTQERPVLCRTADDSFGICQEERPETARTCRLGPCPRNISDPSKKSYVVQWLSRPDPDSPIRKISSKGHCQGDKSIFCRMEVLSRYCSIPGYNKLCCKSCNLYNNLTNVEGRIEPPPGKHNDIDVFMPTLPVPTVAMEVRPSPSTPLEVPLNASSTNATEDHPETNAVDEPYKIHGLEDEVQPPNLIPRRPSPYEKTRNQRIQELIDEMRKKEMLGKF
Alternative Products
Event=Alternative splicing; Named isoforms=2; Name=LpNPI; IsoId=O95450-1; Sequence=Displayed; Name=SpNPI; IsoId=O95450-2; Sequence=VSP_005497, VSP_005498
Alternative Sequence
544..566; HCFKGHCIWLTPDILKRDGSWGA -> FRPGAVAHACYPSTLGGQGRWIA (in isoform SpNPI); 567..1211; Missing (in isoform SpNPI)
3D Structural Models
Domain & Motif Annotations
Motif
691..693; Cell attachment site
Domain (CC)
The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix.
Domain (FT)
266..470; Peptidase M12B; 480..560; Disintegrin; 561..616; TSP type-1 1; 854..912; TSP type-1 2; 914..971; TSP type-1 3; 975..1029; TSP type-1 4; 1059..1097; PLAC
Region
723..851; Spacer; 1170..1191; Disordered