Q9H324 (ATS10_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
A disintegrin and metalloproteinase with thrombospondin motifs 10
Short name=ADAM-TS 10
Short name=ADAM-TS10
Short name=ADAMTS-10
EC=3.4.24.-

Gene names

Name:

ADAMTS10

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1103 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	Metalloprotease that participate in microfibrils assembly. Microfibrils are extracellular matrix components occurring independently or along with elastin in the formation of elastic tissues. Ref.4
Cofactor	Binds 1 zinc ion per subunit By similarity.
Subunit structure	Interacts with FBN1; this interaction promotes microfibrils assembly. Ref.4
Subcellular location	Secreted › extracellular space › extracellular matrix Ref.4.
Tissue specificity	Widely expressed in adult tissues. Ref.2
Domain	The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix By similarity.
Post-translational modification	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.
Involvement in disease	Weill-Marchesani syndrome 1 (WMS1) [MIM:277600]: A rare connective tissue disorder characterized by short stature, brachydactyly, joint stiffness, and eye abnormalities including microspherophakia, ectopia lentis, severe myopia and glaucoma. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.3 Ref.5
Sequence similarities	Contains 1 disintegrin domain. Contains 1 peptidase M12B domain. Contains 1 PLAC domain. Contains 5 TSP type-1 domains.

Ontologies

Keywords
Cellular component	Extracellular matrix Secreted
Coding sequence diversity	Polymorphism
Disease	Disease mutation Dwarfism
Domain	Repeat Signal
Ligand	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	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	microfibril Inferred from direct assay Ref.4. Source: UniProtKB
Molecular_function	metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 25	25	Potential
	Propeptide	26 – 233	208	By similarity		PRO_0000029184
	Chain	234 – 1103	870	A disintegrin and metalloproteinase with thrombospondin motifs 10		PRO_0000029185
Regions
	Domain	239 – 457	219	Peptidase M12B
	Domain	460 – 546	87	Disintegrin
	Domain	547 – 602	56	TSP type-1 1
	Domain	825 – 883	59	TSP type-1 2
	Domain	884 – 945	62	TSP type-1 3
	Domain	947 – 1001	55	TSP type-1 4
	Domain	1003 – 1058	56	TSP type-1 5
	Domain	1065 – 1103	39	PLAC
	Region	706 – 828	123	Spacer
	Compositional bias	58 – 61	4	Poly-Pro
	Compositional bias	568 – 571	4	Poly-Ser
	Compositional bias	604 – 705	102	Cys-rich
Sites
	Active site	393	1	By similarity
	Metal binding	392	1	Zinc; catalytic By similarity
	Metal binding	396	1	Zinc; catalytic By similarity
	Metal binding	402	1	Zinc; catalytic By similarity
Amino acid modifications
	Glycosylation	90	1	N-linked (GlcNAc...) Potential
	Glycosylation	222	1	N-linked (GlcNAc...) Potential
	Glycosylation	323	1	N-linked (GlcNAc...) Potential
	Glycosylation	740	1	N-linked (GlcNAc...) Potential
	Glycosylation	795	1	N-linked (GlcNAc...) Potential
	Glycosylation	892	1	N-linked (GlcNAc...) Potential
	Disulfide bond	370 ↔ 452		By similarity
	Disulfide bond	409 ↔ 436		By similarity
	Disulfide bond	559 ↔ 596		By similarity
	Disulfide bond	563 ↔ 601		By similarity
	Disulfide bond	574 ↔ 586		By similarity
Natural variations
	Natural variant	25	1	A → T in WMS1; shows consistent and significantly diminished protein secretion. Ref.5		VAR_054439
	Natural variant	119	1	R → Q. Corresponds to variant rs3814291 [ dbSNP | Ensembl ].		VAR_054440
	Natural variant	134	1	T → S. Ref.2 Corresponds to variant rs7255721 [ dbSNP | Ensembl ].		VAR_054441
Experimental info
	Sequence conflict	385 – 386	2	AT → PQ in AAG35563. Ref.2
	Sequence conflict	437	1	S → N in AAG35563. Ref.2
	Sequence conflict	643	1	C → S in AAG35563. Ref.2
	Sequence conflict	1101	1	H → Q in AAG35563. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9H324 [UniParc]. Last modified June 12, 2007. Version 2. Checksum: D7558271C303A87C	FASTA	1,103	120,874
	10 20 30 40 50 60 MAPACQILRW ALALGLGLMF EVTHAFRSQD EFLSSLESYE IAFPTRVDHN GALLAFSPPP 70 80 90 100 110 120 PRRQRRGTGA TAESRLFYKV ASPSTHFLLN LTRSSRLLAG HVSVEYWTRE GLAWQRAARP 130 140 150 160 170 180 HCLYAGHLQG QASTSHVAIS TCGGLHGLIV ADEEEYLIEP LHGGPKGSRS PEESGPHVVY 190 200 210 220 230 240 KRSSLRHPHL DTACGVRDEK PWKGRPWWLR TLKPPPARPL GNETERGQPG LKRSVSRERY 250 260 270 280 290 300 VETLVVADKM MVAYHGRRDV EQYVLAIMNI VAKLFQDSSL GSTVNILVTR LILLTEDQPT 310 320 330 340 350 360 LEITHHAGKS LDSFCKWQKS IVNHSGHGNA IPENGVANHD TAVLITRYDI CIYKNKPCGT 370 380 390 400 410 420 LGLAPVGGMC ERERSCSVNE DIGLATAFTI AHEIGHTFGM NHDGVGNSCG ARGQDPAKLM 430 440 450 460 470 480 AAHITMKTNP FVWSSCSRDY ITSFLDSGLG LCLNNRPPRQ DFVYPTVAPG QAYDADEQCR 490 500 510 520 530 540 FQHGVKSRQC KYGEVCSELW CLSKSNRCIT NSIPAAEGTL CQTHTIDKGW CYKRVCVPFG 550 560 570 580 590 600 SRPEGVDGAW GPWTPWGDCS RTCGGGVSSS SRHCDSPRPT IGGKYCLGER RRHRSCNTDD 610 620 630 640 650 660 CPPGSQDFRE VQCSEFDSIP FRGKFYKWKT YRGGGVKACS LTCLAEGFNF YTERAAAVVD 670 680 690 700 710 720 GTPCRPDTVD ICVSGECKHV GCDRVLGSDL REDKCRVCGG DGSACETIEG VFSPASPGAG 730 740 750 760 770 780 YEDVVWIPKG SVHIFIQDLN LSLSHLALKG DQESLLLEGL PGTPQPHRLP LAGTTFQLRQ 790 800 810 820 830 840 GPDQVQSLEA LGPINASLIV MVLARTELPA LRYRFNAPIA RDSLPPYSWH YAPWTKCSAQ 850 860 870 880 890 900 CAGGSQVQAV ECRNQLDSSA VAPHYCSAHS KLPKRQRACN TEPCPPDWVV GNWSLCSRSC 910 920 930 940 950 960 DAGVRSRSVV CQRRVSAAEE KALDDSACPQ PRPPVLEACH GPTCPPEWAA LDWSECTPSC 970 980 990 1000 1010 1020 GPGLRHRVVL CKSADHRATL PPAHCSPAAK PPATMRCNLR RCPPARWVAG EWGECSAQCG 1030 1040 1050 1060 1070 1080 VGQRQRSVRC TSHTGQASHE CTEALRPPTT QQCEAKCDSP TPGDGPEECK DVNKVAYCPL 1090 1100 VLKFQFCSRA YFRQMCCKTC HGH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The DNA sequence and biology of human chromosome 19." Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M. Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	"Discovery and characterization of a novel, widely expressed metalloprotease, ADAMTS10, and its proteolytic activation." Somerville R.P.T., Jungers K.A., Apte S.S. J. Biol. Chem. 279:51208-51217(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 27-1103, TISSUE SPECIFICITY, VARIANT SER-134.
[3]	"ADAMTS10 mutations in autosomal recessive Weill-Marchesani syndrome." Dagoneau N., Benoist-Lasselin C., Huber C., Faivre L., Megarbane A., Alswaid A., Dollfus H., Alembik Y., Munnich A., Legeai-Mallet L., Cormier-Daire V. Am. J. Hum. Genet. 75:801-806(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN WMS1.
[4]	"ADAMTS10 protein interacts with fibrillin-1 and promotes its deposition in extracellular matrix of cultured fibroblasts." Kutz W.E., Wang L.W., Bader H.L., Majors A.K., Iwata K., Traboulsi E.I., Sakai L.Y., Keene D.R., Apte S.S. J. Biol. Chem. 286:17156-17167(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH FBN1.
[5]	"Functional analysis of an ADAMTS10 signal peptide mutation in Weill-Marchesani syndrome demonstrates a long-range effect on secretion of the full-length enzyme." Kutz W.E., Wang L.W., Dagoneau N., Odrcic K.J., Cormier-Daire V., Traboulsi E.I., Apte S.S. Hum. Mutat. 29:1425-1434(2008) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT WMS1 THR-25, CHARACTERIZATION OF VARIANT WMS1 THR-25.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	AC092315 Genomic DNA. No translation available. AC130469 Genomic DNA. No translation available. AF163762 mRNA. Translation: AAG35563.1.
IPI	IPI00215794.
RefSeq	NP_112219.2. NM_030957.2.
UniGene	Hs.657508.
3D structure databases
ProteinModelPortal	Q9H324.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000270328.
Protein family/group databases
MEROPS	M12.235.
PTM databases
PhosphoSite	Q9H324.
Polymorphism databases
DMDM	148887344.
Proteomic databases
PaxDb	Q9H324.
PRIDE	Q9H324.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000270328; ENSP00000270328; ENSG00000142303. ENST00000597188; ENSP00000471851; ENSG00000142303.
GeneID	81794.
KEGG	hsa:81794.
UCSC	uc002mkj.1. human.
Organism-specific databases
CTD	81794.
GeneCards	GC19M008645.
HGNC	HGNC:13201. ADAMTS10.
HPA	HPA040223.
MIM	277600. phenotype. 608990. gene.
neXtProt	NX_Q9H324.
Orphanet	3449. Weill-Marchesani syndrome.
PharmGKB	PA24537.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG288089.
HOGENOM	HOG000004800.
HOVERGEN	HBG004315.
InParanoid	Q9H324.
KO	K08625.
OMA	GRRDIEQ.
OrthoDB	EOG4K9BBC.
PhylomeDB	Q9H324.
Gene expression databases
Bgee	Q9H324.
CleanEx	HS_ADAMTS10.
Genevestigator	Q9H324.
GermOnline	ENSG00000142303. Homo sapiens.
Family and domain databases
Gene3D	3.40.390.10. 1 hit.
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]
Pfam	PF05986. ADAM_spacer1. 1 hit. PF01562. Pep_M12B_propep. 1 hit. PF08686. PLAC. 1 hit. PF01421. Reprolysin. 1 hit. PF00090. TSP_1. 5 hits. [Graphical view]
PRINTS	PR01857. ADAMTSFAMILY.
SMART	SM00209. TSP1. 5 hits. [Graphical view]
SUPFAM	SSF82895. TSP1. 5 hits.
PROSITE	PS50215. ADAM_MEPRO. 1 hit. PS00427. DISINTEGRIN_1. False negative. PS50214. DISINTEGRIN_2. False negative. PS50900. PLAC. 1 hit. PS50092. TSP1. 5 hits. PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	81794.
NextBio	72110.
SOURCE	Search...

Entry information

Entry name

ATS10_HUMAN

Accession

Primary (citable) accession number: Q9H324

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 5, 2001
Last sequence update:	June 12, 2007
Last modified:	May 1, 2013
This is version 117 of the entry and version 2 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.