Reviewed, UniProtKB/Swiss-Prot Q8C9W3 (ATS2_MOUSE)

Names and origin

Protein names

Recommended name:
    A disintegrin and metalloproteinase with thrombospondin motifs 2
      Short name=ADAMTS-2
      Short name=ADAM-TS 2
      Short name=ADAM-TS2
    EC=3.4.24.14
Alternative name(s):
    Procollagen I/II amino propeptide-processing enzyme
    Procollagen I N-proteinase
      Short name=PC I-NP
    Procollagen N-endopeptidase
      Short name=pNPI

Gene names

Name:

Adamts2

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	1213 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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	Secreted › extracellular space › extracellular 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.
Sequence similarities	Contains 1 disintegrin domain. Contains 1 peptidase M12B domain. Contains 1 PLAC domain. Contains 4 TSP type-1 domains.

Ontologies

Keywords
Biological process	Collagen degradation
Cellular component	Extracellular matrix Secreted
Domain	Repeat Signal
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Disulfide bond Glycoprotein Zymogen
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	collagen catabolic process Inferred from electronic annotation. Source: UniProtKB-KW collagen fibril organization Inferred from mutant phenotype. Source: MGI lung development Inferred from mutant phenotype. Source: MGI protein maturation by peptide bond cleavage Inferred from mutant phenotype. Source: MGI proteolysis Inferred from electronic annotation. Source: InterPro skin development Inferred from mutant phenotype. Source: MGI spermatogenesis Inferred from mutant phenotype. Source: MGI
Cellular component	proteinaceous extracellular matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 28	28	Potential
	Chain	29 – 1213	1185	A disintegrin and metalloproteinase with thrombospondin motifs 2		PRO_0000029160
	Propeptide	29 – 260	232	By similarity		PRO_0000029161
Regions
	Domain	267 – 471	205	Peptidase M12B
	Domain	480 – 560	81	Disintegrin
	Domain	561 – 617	57	TSP type-1 1
	Domain	855 – 913	59	TSP type-1 2
	Domain	915 – 975	61	TSP type-1 3
	Domain	976 – 1030	55	TSP type-1 4
	Domain	1060 – 1098	39	PLAC
	Region	723 – 851	129	Spacer
	Motif	692 – 694	3	Cell attachment site Potential
	Compositional bias	618 – 722	105	Cys-rich
Sites
	Active site	410	1	By similarity
	Metal binding	409	1	Zinc; catalytic By similarity
	Metal binding	413	1	Zinc; catalytic By similarity
	Metal binding	419	1	Zinc; catalytic By similarity
Amino acid modifications
	Glycosylation	111	1	N-linked (GlcNAc...) Potential
	Glycosylation	252	1	N-linked (GlcNAc...) Potential
	Glycosylation	949	1	N-linked (GlcNAc...) Potential
	Glycosylation	950	1	N-linked (GlcNAc...) Potential
	Glycosylation	994	1	N-linked (GlcNAc...) Potential
	Glycosylation	1032	1	N-linked (GlcNAc...) Potential
	Glycosylation	1099	1	N-linked (GlcNAc...) Potential
	Glycosylation	1147	1	N-linked (GlcNAc...) Potential
	Glycosylation	1152	1	N-linked (GlcNAc...) Potential
	Disulfide bond	387 ↔ 466		By similarity
	Disulfide bond	426 ↔ 452		By similarity
	Disulfide bond	574 ↔ 611		By similarity
	Disulfide bond	578 ↔ 616		By similarity
	Disulfide bond	589 ↔ 601		By similarity
	Disulfide bond	988 ↔ 1024		By similarity
	Disulfide bond	992 ↔ 1029		By similarity
	Disulfide bond	1003 ↔ 1013		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8C9W3-1 [UniParc]. Last modified June 20, 2003. Version 2. Checksum: B27431E00443EDB5	FASTA	1,213	135,299
	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

References

	« Hide 'large scale' referencesShow '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. , 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: 16141072] [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: 15489334] [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, 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.
IPI	IPI00331280.
RefSeq	NP_783574.1.
UniGene	Mm.110597 Mm.339048
3D structure databases
SMR	Q8C9W3. Positions 269-552, 862-946, 922-1029.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8C9W3.
Protein family/group databases
MEROPS	M12.301.
Proteomic databases
PRIDE	Q8C9W3.
Genome annotation databases
Ensembl	ENSMUST00000040523; ENSMUSP00000040171; ENSMUSG00000036545; Mus musculus. [Genome view]
GeneID	216725.
KEGG	mmu:216725.
UCSC	uc007iso.1. mouse.
Organism-specific databases
CTD	216725.
MGI	MGI:1347356. Adamts2.
Phylogenomic databases
HOGENOM	HBG355191.
HOVERGEN	Q8C9W3.
InParanoid	Q8C9W3.
OMA	KKWSPCS.
OrthoDB	EOG9M0HM0.
PhylomeDB	Q8C9W3.
Enzyme and pathway databases
BRENDA	3.4.24.14. 244.
Gene expression databases
ArrayExpress	Q8C9W3.
Bgee	Q8C9W3.
Genevestigator	Q8C9W3.
GermOnline	ENSMUSG00000036545. Mus musculus.
Family and domain databases
InterPro	IPR010294. ADAM_spacer1. 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]
Pfam	PF05986. ADAM_spacer1. 1 hit. PF01562. Pep_M12B_propep. 1 hit. PF01421. Reprolysin. 1 hit. PF00090. TSP_1. 4 hits. [Graphical view]
PRINTS	PR01859. ADAMTS2. PR01857. ADAMTSFAMILY.
SMART	SM00209. TSP1. 4 hits. [Graphical view]
PROSITE	PS50215. ADAM_MEPRO. 1 hit. PS00427. DISINTEGRIN_1. False negative. PS50214. DISINTEGRIN_2. False negative. PS50900. PLAC. 1 hit. PS50092. TSP1. 4 hits. PS00142. ZINC_PROTEASE. False negative. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	375268.
SOURCE	Search...

Entry information

Entry name

ATS2_MOUSE

Accession

Primary (citable) accession number: Q8C9W3

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2003
Last sequence update:	June 20, 2003
Last modified:	January 19, 2010
This is version 72 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)