O15072 (ATS3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
A disintegrin and metalloproteinase with thrombospondin motifs 3
Short name=ADAM-TS 3
Short name=ADAM-TS3
Short name=ADAMTS-3
EC=3.4.24.-

Alternative name(s):
Procollagen II N-proteinase
Short name=PC II-NP
Procollagen II amino propeptide-processing enzyme

Gene names

Name:	ADAMTS3
Synonyms:	KIAA0366

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1205 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Cleaves the propeptides of type II collagen prior to fibril assembly. Does not act on types I and III collagens.
Cofactor	Binds 1 zinc ion per subunit By similarity.
Subcellular location	Secreted › extracellular space › extracellular matrix By similarity.
Tissue specificity	Found in cartilage and skin.
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.
Caution	Has sometimes been referred to as ADAMTS4.

Ontologies

Keywords
Cellular component	Extracellular matrix Secreted
Coding sequence diversity	Polymorphism
Domain	Repeat Signal
Ligand	Heparin-binding Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Zymogen
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	collagen catabolic process Non-traceable author statement Ref.3. Source: UniProtKB collagen fibril organization Non-traceable author statement. Source: UniProtKB proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	proteinaceous extracellular matrix Non-traceable author statement. Source: UniProtKB
Molecular function	heparin binding Inferred from electronic annotation. Source: UniProtKB-KW metalloendopeptidase activity Non-traceable author statement. Source: UniProtKB zinc ion binding Non-traceable author statement Ref.3. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 20	20	Potential
	Propeptide	21 – 249	229	By similarity		PRO_0000029162
	Chain	250 – 1205	956	A disintegrin and metalloproteinase with thrombospondin motifs 3		PRO_0000029163
Regions
	Domain	256 – 460	205	Peptidase M12B
	Domain	470 – 550	81	Disintegrin
	Domain	551 – 606	56	TSP type-1 1
	Domain	845 – 905	61	TSP type-1 2
	Domain	906 – 965	60	TSP type-1 3
	Domain	966 – 1014	49	TSP type-1 4
	Domain	1015 – 1054	40	PLAC
	Region	713 – 844	132	Spacer
	Compositional bias	246 – 249	4	Poly-Arg
	Compositional bias	608 – 712	105	Cys-rich
Sites
	Active site	399	1	By similarity
	Metal binding	398	1	Zinc; catalytic By similarity
	Metal binding	402	1	Zinc; catalytic By similarity
	Metal binding	408	1	Zinc; catalytic By similarity
Amino acid modifications
	Glycosylation	83	1	N-linked (GlcNAc...) Potential
	Glycosylation	119	1	N-linked (GlcNAc...) Potential
	Glycosylation	242	1	N-linked (GlcNAc...) Potential
	Glycosylation	345	1	N-linked (GlcNAc...) Potential
	Glycosylation	475	1	N-linked (GlcNAc...) Potential
	Glycosylation	814	1	N-linked (GlcNAc...) Potential
	Glycosylation	942	1	N-linked (GlcNAc...) Potential
	Disulfide bond	376 ↔ 455		By similarity
	Disulfide bond	415 ↔ 441		By similarity
	Disulfide bond	563 ↔ 600		By similarity
	Disulfide bond	567 ↔ 605		By similarity
	Disulfide bond	578 ↔ 590		By similarity
	Disulfide bond	978 ↔ 1010		By similarity
	Disulfide bond	982 ↔ 1015		By similarity
	Disulfide bond	993 ↔ 999		By similarity
Natural variations
	Natural variant	138	1	R → K. Ref.2 Ref.3 Ref.4 Corresponds to variant rs788908 [ dbSNP | Ensembl ].		VAR_055012
	Natural variant	1074	1	S → P. Corresponds to variant rs35864003 [ dbSNP | Ensembl ].		VAR_055013
Experimental info
	Sequence conflict	857	1	C → V in BAA20821. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	O15072 [UniParc]. Last modified January 11, 2011. Version 4. Checksum: 01FA661B1C6BFF1B	FASTA	1,205	135,603
	10 20 30 40 50 60 MVLLSLWLIA AALVEVRTSA DGQAGNEEMV QIDLPIKRYR EYELVTPVST NLEGRYLSHT 70 80 90 100 110 120 LSASHKKRSA RDVSSNPEQL FFNITAFGKD FHLRLKPNTQ LVAPGAVVEW HETSLVPGNI 130 140 150 160 170 180 TDPINNHQPG SATYRIRRTE PLQTNCAYVG DIVDIPGTSV AISNCDGLAG MIKSDNEEYF 190 200 210 220 230 240 IEPLERGKQM EEEKGRIHVV YKRSAVEQAP IDMSKDFHYR ESDLEGLDDL GTVYGNIHQQ 250 260 270 280 290 300 LNETMRRRRH AGENDYNIEV LLGVDDSVVR FHGKEHVQNY LLTLMNIVNE IYHDESLGVH 310 320 330 340 350 360 INVVLVRMIM LGYAKSISLI ERGNPSRSLE NVCRWASQQQ RSDLNHSEHH DHAIFLTRQD 370 380 390 400 410 420 FGPAGMQGYA PVTGMCHPVR SCTLNHEDGF SSAFVVAHET GHVLGMEHDG QGNRCGDETA 430 440 450 460 470 480 MGSVMAPLVQ AAFHRYHWSR CSGQELKRYI HSYDCLLDDP FDHDWPKLPE LPGINYSMDE 490 500 510 520 530 540 QCRFDFGVGY KMCTAFRTFD PCKQLWCSHP DNPYFCKTKK GPPLDGTECA AGKWCYKGHC 550 560 570 580 590 600 MWKNANQQKQ DGNWGSWTKF GSCSRTCGTG VRFRTRQCNN PMPINGGQDC PGVNFEYQLC 610 620 630 640 650 660 NTEECQKHFE DFRAQQCQQR NSHFEYQNTK HHWLPYEHPD PKKRCHLYCQ SKETGDVAYM 670 680 690 700 710 720 KQLVHDGTHC SYKDPYSICV RGECVKVGCD KEIGSNKVED KCGVCGGDNS HCRTVKGTFT 730 740 750 760 770 780 RTPRKLGYLK MFDIPPGARH VLIQEDEASP HILAIKNQAT GHYILNGKGE EAKSRTFIDL 790 800 810 820 830 840 GVEWDYNIED DIESLHTDGP LHDPVIVLII PQENDTRSSL TYKYIIHEDS VPTINSNNVI 850 860 870 880 890 900 QEELDTFEWA LKSWSQCSKP CGGGFQYTKY GCRRKSDNKM VHRSFCEANK KPKPIRRMCN 910 920 930 940 950 960 IQECTHPLWV AEEWEHCTKT CGSSGYQLRT VRCLQPLLDG TNRSVHSKYC MGDRPESRRP 970 980 990 1000 1010 1020 CNRVPCPAQW KTGPWSECSV TCGEGTEVRQ VLCRAGDHCD GEKPESVRAC QLPPCNDEPC 1030 1040 1050 1060 1070 1080 LGDKSIFCQM EVLARYCSIP GYNKLCCESC SKRSSTLPPP YLLEAAETHD DVISNPSDLP 1090 1100 1110 1120 1130 1140 RSLVMPTSLV PYHSETPAKK MSLSSISSVG GPNAYAAFRP NSKPDGANLR QRSAQQAGSK 1150 1160 1170 1180 1190 1200 TVRLVTVPSS PPTKRVHLSS ASQMAAASFF AASDSIGASS QARTSKKDGK IIDNRRPTRS STLER

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed: 15815621] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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], VARIANT LYS-138.
[3]	"Procollagen II amino propeptide processing by ADAMTS-3. Insights on dermatosparaxis." Fernandes R.J., Hirohata S., Engle J.M., Colige A., Cohn D.H., Eyre D.R., Apte S.S. J. Biol. Chem. 276:31502-31509(2001) [PubMed: 11408482] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-227, VARIANT LYS-138.
[4]	"Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro." Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 4:141-150(1997) [PubMed: 9205841] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-1205, VARIANT LYS-138. Tissue: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AC093790 Genomic DNA. No translation available. AC095056 Genomic DNA. No translation available. AC104814 Genomic DNA. No translation available. BC130287 mRNA. Translation: AAI30288.1. BC132735 mRNA. Translation: AAI32736.1. AF247668 mRNA. Translation: AAK28400.1. AB002364 mRNA. Translation: BAA20821.1.
IPI	IPI00307729.
RefSeq	NP_055058.2. NM_014243.2.
UniGene	Hs.590919.
3D structure databases
ProteinModelPortal	O15072.
SMR	O15072. Positions 254-828, 843-1016.
ModBase	Search...
Protein-protein interaction databases
STRING	O15072.
Protein family/group databases
MEROPS	M12.220.
PTM databases
PhosphoSite	O15072.
Proteomic databases
PRIDE	O15072.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000286657; ENSP00000286657; ENSG00000156140.
GeneID	9508.
KEGG	hsa:9508.
Organism-specific databases
CTD	9508.
GeneCards	GC04M073136.
H-InvDB	HIX0004274.
HGNC	HGNC:219. ADAMTS3.
MIM	605011. gene.
neXtProt	NX_O15072.
PharmGKB	PA24547.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
HOGENOM	HBG355191.
HOVERGEN	HBG004314.
InParanoid	O15072.
OMA	AEEWEHC.
OrthoDB	EOG43FGW5.
PhylomeDB	O15072.
Gene expression databases
ArrayExpress	O15072.
Bgee	O15072.
CleanEx	HS_ADAMTS3.
Genevestigator	O15072.
GermOnline	ENSG00000156140. Homo sapiens.
Family and domain databases
InterPro	IPR010294. ADAM_spacer1. IPR024079. MetalloPept_cat_dom. IPR001590. Peptidase_M12B. IPR013273. Peptidase_M12B_ADAM-TS. IPR002870. Peptidase_M12B_N. IPR010909. PLAC. IPR000884. Thrombospondin_1_rpt. [Graphical view]
Gene3D	G3DSA:3.40.390.10. G3DSA:3.40.390.10. 1 hit.
KO	K08619.
Pfam	PF05986. ADAM_spacer1. 1 hit. PF01562. Pep_M12B_propep. 1 hit. PF01421. Reprolysin. 1 hit. PF00090. TSP_1. 4 hits. [Graphical view]
PRINTS	PR01857. ADAMTSFAMILY.
SMART	SM00209. TSP1. 4 hits. [Graphical view]
SUPFAM	SSF82895. TSP1. 4 hits.
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
NextBio	35628.
SOURCE	Search...

Entry information

Entry name

ATS3_HUMAN

Accession

Primary (citable) accession number: O15072
Secondary accession number(s): A1L3U9, Q9BXZ8

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	January 11, 2011
Last modified:	January 25, 2012
This is version 121 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.