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Q8C9W3 (ATS2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
A disintegrin and metalloproteinase with thrombospondin motifs 2

Short name=ADAM-TS 2
Short name=ADAM-TS2
Short name=ADAMTS-2
EC=3.4.24.14
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 names
Name:Adamts2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1213 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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 By similarity.

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 By similarity.

Subcellular location

Secretedextracellular spaceextracellular matrix By similarity.

Domain

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

Post-translational modification

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-X(2)-(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.

Sequence similarities

Contains 1 disintegrin domain.

Contains 1 peptidase M12B domain.

Contains 1 PLAC domain.

Contains 4 TSP type-1 domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Potential
Propeptide29 – 260232 By similarity
PRO_0000029161
Chain261 – 1213953A disintegrin and metalloproteinase with thrombospondin motifs 2
PRO_0000029160

Regions

Domain267 – 471205Peptidase M12B
Domain480 – 56081Disintegrin
Domain561 – 61757TSP type-1 1
Domain855 – 91359TSP type-1 2
Domain915 – 97561TSP type-1 3
Domain976 – 103055TSP type-1 4
Domain1060 – 109839PLAC
Region723 – 851129Spacer
Motif692 – 6943Cell attachment site Potential
Compositional bias618 – 722105Cys-rich

Sites

Active site4101 By similarity
Metal binding4091Zinc; catalytic By similarity
Metal binding4131Zinc; catalytic By similarity
Metal binding4191Zinc; catalytic By similarity

Amino acid modifications

Glycosylation1111N-linked (GlcNAc...) Potential
Glycosylation2521N-linked (GlcNAc...) Potential
Glycosylation9491N-linked (GlcNAc...) Potential
Glycosylation9501N-linked (GlcNAc...) Potential
Glycosylation9941N-linked (GlcNAc...) Potential
Glycosylation10321N-linked (GlcNAc...) Potential
Glycosylation10991N-linked (GlcNAc...) Potential
Glycosylation11471N-linked (GlcNAc...) Potential
Glycosylation11521N-linked (GlcNAc...) Potential
Disulfide bond344 ↔ 393 By similarity
Disulfide bond387 ↔ 466 By similarity
Disulfide bond426 ↔ 452 By similarity
Disulfide bond493 ↔ 518 By similarity
Disulfide bond504 ↔ 527 By similarity
Disulfide bond513 ↔ 546 By similarity
Disulfide bond540 ↔ 551 By similarity
Disulfide bond574 ↔ 611 By similarity
Disulfide bond578 ↔ 616 By similarity
Disulfide bond589 ↔ 601 By similarity
Disulfide bond988 ↔ 1024 By similarity
Disulfide bond992 ↔ 1029 By similarity
Disulfide bond1003 ↔ 1013 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8C9W3 [UniParc].

Last modified June 20, 2003. Version 2.
Checksum: B27431E00443EDB5

FASTA1,213135,299
        10         20         30         40         50         60 
MDPPAGAARR LLCPALLLLL LPPPPLLLLP PPPASVRLVA ATEPPGGPPG QGAERILAVP 

        70         80         90        100        110        120 
VRTDAQGRLV SHVVSLETAG AGVRARRAAL DQTSGLPGGA AQDPGGRLFY NLTVFGRDLH 

       130        140        150        160        170        180 
LRLRPNARLV APGATVEWQG ETGDTRVEPL LGSCLYVGDV ADLPKASSVA LSNCDGLAGL 

       190        200        210        220        230        240 
IRMEEEEFFI EPLEKGQTDQ EAEQGRVHVV YRRPPTPKPP PVSEPQALDT GVSQGNLDSL 

       250        260        270        280        290        300 
SRALGVLEER INSSRRRVRR HATDDDYNIE VLLGVDDSVV QFHGKEHVQK YLLTLMNIVN 

       310        320        330        340        350        360 
EIYHDESLGA HINVVLVRII LLSHAKSMSL IEIGNPSQSL ENVCRWAYLQ QKPDTDHDEY 

       370        380        390        400        410        420 
HDHAIFLTRQ DFGPSGMQGY APVTGMCHPV RSCTLNHEDG FSSAFVVAHE TGHVLGMEHD 

       430        440        450        460        470        480 
GQGNRCGDEV RLGSIMAPLV QAAFHRFHWS RCSQQELSRY LHSYDCLRDD PFAHDWPALP 

       490        500        510        520        530        540 
QLPGLHYSMN EQCRFDFGLG YMMCTAFRTF DPCKQLWCSH PDNPYFCKTK KGPPLDGTMC 

       550        560        570        580        590        600 
APGKHCFKGH CIWLTPDILK RDGNWGAWTP FGSCSRTCGT GVKFRTRQCD NPHPANGGRT 

       610        620        630        640        650        660 
CSGLAYDFQL CNPQDCPNSL ADFREEQCQQ WDLYFEHGDV QHHWLPHEHR DAKERCHLYC 

       670        680        690        700        710        720 
ESKETGEVVS MKRMVHDGTR CSYKDAFSLC VRGDCRKVGC DGVIGSRKQE DKCGVCGGDN 

       730        740        750        760        770        780 
THCKVVKGTF TRSPRKQDYI KMFEIPAGAR HLLIQEADTT SHHLSVKNLE TGKFILNEEN 

       790        800        810        820        830        840 
HLDPNSRSFI AMGVEWEYRN EDERETLQTI GPLHGTITVL VIPEGDTRIS LTYKYMIHED 

       850        860        870        880        890        900 
SLNVDDNNVL EDDAVRHEWA LKKWSPCSKP CGGGSQFTKY GCRRRLDSKM VHRAFCSALA 

       910        920        930        940        950        960 
KPKAIRRACN PQECSQPVWV TGEWEPCTQS CGRTGMQVRS VRCIQPLHNN TTRSVHTKHC 

       970        980        990       1000       1010       1020 
NDHRPESRRA CNRELCPGRW RAGSWSQCSV TCGNGTQERP VLCRTADDNF GVCREERPET 

      1030       1040       1050       1060       1070       1080 
ARICRLAPCP RNGSDPSKKS YVVQWLSRPD PDSPIQKISS KDQCQGDKSM FCRMEVLSRY 

      1090       1100       1110       1120       1130       1140 
CSIPSYNKLC CKSCNPPRNL SNTEDGGVEP PPGKHNDIDV FMPTLPGPTV ATQVQPSPGP 

      1150       1160       1170       1180       1190       1200 
PLEAPLNVSS TNATEDHPET NAVDVPYKIH GVDEEVPSPN LIPRRPSLYV KTRNQRIQEL 

      1210 
INAVQRKEKP GKF 

« Hide

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Thymus.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Mammary tumor.
[3]Lubec G., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 1058-1068, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: OF1.
Tissue: Hippocampus.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK040370 mRNA. Translation: BAC30572.1.
BC046456 mRNA. Translation: AAH46456.1.
CCDSCCDS24636.1.
RefSeqNP_783574.1. NM_175643.3.
UniGeneMm.110597.
Mm.339048.

3D structure databases

ProteinModelPortalQ8C9W3.
SMRQ8C9W3. Positions 269-786.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSM12.301.

PTM databases

PhosphoSiteQ8C9W3.

Proteomic databases

PaxDbQ8C9W3.
PRIDEQ8C9W3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000040523; ENSMUSP00000040171; ENSMUSG00000036545.
GeneID216725.
KEGGmmu:216725.
UCSCuc007iso.1. mouse.

Organism-specific databases

CTD9509.
MGIMGI:1347356. Adamts2.

Phylogenomic databases

eggNOGNOG307411.
GeneTreeENSGT00740000114846.
HOGENOMHOG000034222.
HOVERGENHBG004314.
InParanoidQ8C9W3.
KOK08618.
OMAIHEDSLN.
OrthoDBEOG76HQ0N.
PhylomeDBQ8C9W3.
TreeFamTF313537.

Gene expression databases

BgeeQ8C9W3.
GenevestigatorQ8C9W3.

Family and domain databases

Gene3D3.40.390.10. 1 hit.
InterProIPR010294. ADAM_spacer1.
IPR024079. MetalloPept_cat_dom.
IPR013275. Pept_M12B_ADAM-TS2.
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]
SUPFAMSSF82895. SSF82895. 4 hits.
PROSITEPS50215. ADAM_MEPRO. 1 hit.
PS50900. PLAC. 1 hit.
PS50092. TSP1. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio375268.
PROQ8C9W3.
SOURCESearch...

Entry information

Entry nameATS2_MOUSE
AccessionPrimary (citable) accession number: Q8C9W3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: June 20, 2003
Last modified: July 9, 2014
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot