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Q8C9W3

- ATS2_MOUSE

UniProt

Q8C9W3 - ATS2_MOUSE

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Protein

A disintegrin and metalloproteinase with thrombospondin motifs 2

Gene

Adamts2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- 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 (By similarity).By similarity

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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi409 – 4091Zinc; catalyticPROSITE-ProRule annotation
Active sitei410 – 4101PROSITE-ProRule annotation
Metal bindingi413 – 4131Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi419 – 4191Zinc; catalyticPROSITE-ProRule annotation

GO - Molecular functioni

  1. metalloendopeptidase activity Source: InterPro
  2. peptidase activity Source: MGI
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. collagen catabolic process Source: UniProtKB-KW
  2. collagen fibril organization Source: MGI
  3. lung development Source: MGI
  4. protein processing Source: MGI
  5. skin development Source: MGI
  6. spermatogenesis Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Collagen degradation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_198984. Collagen biosynthesis and modifying enzymes.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:1347356. Adamts2.

Subcellular locationi

GO - Cellular componenti

  1. extracellular matrix Source: MGI
  2. proteinaceous extracellular matrix Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828Sequence AnalysisAdd
BLAST
Propeptidei29 – 260232By similarityPRO_0000029161Add
BLAST
Chaini261 – 1213953A disintegrin and metalloproteinase with thrombospondin motifs 2PRO_0000029160Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi111 – 1111N-linked (GlcNAc...)Sequence Analysis
Glycosylationi252 – 2521N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi344 ↔ 393By similarity
Disulfide bondi387 ↔ 466By similarity
Disulfide bondi426 ↔ 452By similarity
Disulfide bondi493 ↔ 518By similarity
Disulfide bondi504 ↔ 527By similarity
Disulfide bondi513 ↔ 546By similarity
Disulfide bondi540 ↔ 551By similarity
Disulfide bondi574 ↔ 611By similarity
Disulfide bondi578 ↔ 616By similarity
Disulfide bondi589 ↔ 601By similarity
Glycosylationi949 – 9491N-linked (GlcNAc...)Sequence Analysis
Glycosylationi950 – 9501N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi988 ↔ 1024By similarity
Disulfide bondi992 ↔ 1029By similarity
Glycosylationi994 – 9941N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1003 ↔ 1013By similarity
Glycosylationi1032 – 10321N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1099 – 10991N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1147 – 11471N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1152 – 11521N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

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).By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiQ8C9W3.
PRIDEiQ8C9W3.

PTM databases

PhosphoSiteiQ8C9W3.

Expressioni

Gene expression databases

BgeeiQ8C9W3.
GenevestigatoriQ8C9W3.

Interactioni

Subunit structurei

May belong to a multimeric complex. Binds specifically to collagen type XIV (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliQ8C9W3.
SMRiQ8C9W3. Positions 269-786.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini267 – 471205Peptidase M12BPROSITE-ProRule annotationAdd
BLAST
Domaini480 – 56081DisintegrinAdd
BLAST
Domaini561 – 61757TSP type-1 1PROSITE-ProRule annotationAdd
BLAST
Domaini855 – 91359TSP type-1 2PROSITE-ProRule annotationAdd
BLAST
Domaini915 – 97561TSP type-1 3PROSITE-ProRule annotationAdd
BLAST
Domaini976 – 103055TSP type-1 4PROSITE-ProRule annotationAdd
BLAST
Domaini1060 – 109839PLACPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni723 – 851129SpacerAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi692 – 6943Cell attachment siteSequence Analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi618 – 722105Cys-richAdd
BLAST

Domaini

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

Sequence similaritiesi

Contains 1 disintegrin domain.Curated
Contains 1 peptidase M12B domain.PROSITE-ProRule annotation
Contains 1 PLAC domain.PROSITE-ProRule annotation
Contains 4 TSP type-1 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG307411.
GeneTreeiENSGT00760000118880.
HOGENOMiHOG000034222.
HOVERGENiHBG004314.
InParanoidiQ8C9W3.
KOiK08618.
OMAiIHEDSLN.
OrthoDBiEOG76HQ0N.
PhylomeDBiQ8C9W3.
TreeFamiTF313537.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR010294. 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]
PfamiPF05986. ADAM_spacer1. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 4 hits.
[Graphical view]
PRINTSiPR01859. ADAMTS2.
PR01857. ADAMTSFAMILY.
SMARTiSM00209. TSP1. 4 hits.
[Graphical view]
SUPFAMiSSF82895. SSF82895. 4 hits.
PROSITEiPS50215. ADAM_MEPRO. 1 hit.
PS50900. PLAC. 1 hit.
PS50092. TSP1. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8C9W3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDPPAGAARR LLCPALLLLL LPPPPLLLLP PPPASVRLVA ATEPPGGPPG
60 70 80 90 100
QGAERILAVP VRTDAQGRLV SHVVSLETAG AGVRARRAAL DQTSGLPGGA
110 120 130 140 150
AQDPGGRLFY NLTVFGRDLH LRLRPNARLV APGATVEWQG ETGDTRVEPL
160 170 180 190 200
LGSCLYVGDV ADLPKASSVA LSNCDGLAGL IRMEEEEFFI EPLEKGQTDQ
210 220 230 240 250
EAEQGRVHVV YRRPPTPKPP PVSEPQALDT GVSQGNLDSL SRALGVLEER
260 270 280 290 300
INSSRRRVRR HATDDDYNIE VLLGVDDSVV QFHGKEHVQK YLLTLMNIVN
310 320 330 340 350
EIYHDESLGA HINVVLVRII LLSHAKSMSL IEIGNPSQSL ENVCRWAYLQ
360 370 380 390 400
QKPDTDHDEY HDHAIFLTRQ DFGPSGMQGY APVTGMCHPV RSCTLNHEDG
410 420 430 440 450
FSSAFVVAHE TGHVLGMEHD GQGNRCGDEV RLGSIMAPLV QAAFHRFHWS
460 470 480 490 500
RCSQQELSRY LHSYDCLRDD PFAHDWPALP QLPGLHYSMN EQCRFDFGLG
510 520 530 540 550
YMMCTAFRTF DPCKQLWCSH PDNPYFCKTK KGPPLDGTMC APGKHCFKGH
560 570 580 590 600
CIWLTPDILK RDGNWGAWTP FGSCSRTCGT GVKFRTRQCD NPHPANGGRT
610 620 630 640 650
CSGLAYDFQL CNPQDCPNSL ADFREEQCQQ WDLYFEHGDV QHHWLPHEHR
660 670 680 690 700
DAKERCHLYC ESKETGEVVS MKRMVHDGTR CSYKDAFSLC VRGDCRKVGC
710 720 730 740 750
DGVIGSRKQE DKCGVCGGDN THCKVVKGTF TRSPRKQDYI KMFEIPAGAR
760 770 780 790 800
HLLIQEADTT SHHLSVKNLE TGKFILNEEN HLDPNSRSFI AMGVEWEYRN
810 820 830 840 850
EDERETLQTI GPLHGTITVL VIPEGDTRIS LTYKYMIHED SLNVDDNNVL
860 870 880 890 900
EDDAVRHEWA LKKWSPCSKP CGGGSQFTKY GCRRRLDSKM VHRAFCSALA
910 920 930 940 950
KPKAIRRACN PQECSQPVWV TGEWEPCTQS CGRTGMQVRS VRCIQPLHNN
960 970 980 990 1000
TTRSVHTKHC NDHRPESRRA CNRELCPGRW RAGSWSQCSV TCGNGTQERP
1010 1020 1030 1040 1050
VLCRTADDNF GVCREERPET ARICRLAPCP RNGSDPSKKS YVVQWLSRPD
1060 1070 1080 1090 1100
PDSPIQKISS KDQCQGDKSM FCRMEVLSRY CSIPSYNKLC CKSCNPPRNL
1110 1120 1130 1140 1150
SNTEDGGVEP PPGKHNDIDV FMPTLPGPTV ATQVQPSPGP PLEAPLNVSS
1160 1170 1180 1190 1200
TNATEDHPET NAVDVPYKIH GVDEEVPSPN LIPRRPSLYV KTRNQRIQEL
1210
INAVQRKEKP GKF
Length:1,213
Mass (Da):135,299
Last modified:June 20, 2003 - v2
Checksum:iB27431E00443EDB5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK040370 mRNA. Translation: BAC30572.1.
BC046456 mRNA. Translation: AAH46456.1.
CCDSiCCDS24636.1.
RefSeqiNP_783574.1. NM_175643.3.
UniGeneiMm.110597.
Mm.339048.

Genome annotation databases

EnsembliENSMUST00000040523; ENSMUSP00000040171; ENSMUSG00000036545.
GeneIDi216725.
KEGGimmu:216725.
UCSCiuc007iso.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK040370 mRNA. Translation: BAC30572.1 .
BC046456 mRNA. Translation: AAH46456.1 .
CCDSi CCDS24636.1.
RefSeqi NP_783574.1. NM_175643.3.
UniGenei Mm.110597.
Mm.339048.

3D structure databases

ProteinModelPortali Q8C9W3.
SMRi Q8C9W3. Positions 269-786.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi M12.301.

PTM databases

PhosphoSitei Q8C9W3.

Proteomic databases

PaxDbi Q8C9W3.
PRIDEi Q8C9W3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000040523 ; ENSMUSP00000040171 ; ENSMUSG00000036545 .
GeneIDi 216725.
KEGGi mmu:216725.
UCSCi uc007iso.1. mouse.

Organism-specific databases

CTDi 9509.
MGIi MGI:1347356. Adamts2.

Phylogenomic databases

eggNOGi NOG307411.
GeneTreei ENSGT00760000118880.
HOGENOMi HOG000034222.
HOVERGENi HBG004314.
InParanoidi Q8C9W3.
KOi K08618.
OMAi IHEDSLN.
OrthoDBi EOG76HQ0N.
PhylomeDBi Q8C9W3.
TreeFami TF313537.

Enzyme and pathway databases

Reactomei REACT_198984. Collagen biosynthesis and modifying enzymes.

Miscellaneous databases

NextBioi 375268.
PROi Q8C9W3.
SOURCEi Search...

Gene expression databases

Bgeei Q8C9W3.
Genevestigatori Q8C9W3.

Family and domain databases

Gene3Di 3.40.390.10. 1 hit.
InterProi IPR010294. 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 ]
Pfami PF05986. ADAM_spacer1. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 4 hits.
[Graphical view ]
PRINTSi PR01859. ADAMTS2.
PR01857. ADAMTSFAMILY.
SMARTi SM00209. TSP1. 4 hits.
[Graphical view ]
SUPFAMi SSF82895. SSF82895. 4 hits.
PROSITEi PS50215. ADAM_MEPRO. 1 hit.
PS50900. PLAC. 1 hit.
PS50092. TSP1. 4 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiATS2_MOUSE
AccessioniPrimary (citable) accession number: Q8C9W3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: June 20, 2003
Last modified: November 26, 2014
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3