Q8TE59 (ATS19_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
A disintegrin and metalloproteinase with thrombospondin motifs 19
Short name=ADAM-TS 19
Short name=ADAM-TS19
Short name=ADAMTS-19
EC=3.4.24.-

Gene names

Name:

ADAMTS19

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	1207 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)

Cofactor	Binds 1 zinc ion per subunit By similarity.
Subcellular location	Secreted › extracellular space › extracellular matrix By similarity.
Tissue specificity	Expressed in fetal lung, but not in any adult tissues examined. Expression was detected in an osteosarcoma cDNA library.
Domain	The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.
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 5 TSP type-1 domains.

Ontologies

Keywords
Cellular component	Extracellular matrix Secreted
Coding sequence diversity	Polymorphism
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	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: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 21	21	Potential
	Propeptide	22 – 316	295	By similarity		PRO_0000029202
	Chain	317 – 1207	891	A disintegrin and metalloproteinase with thrombospondin motifs 19		PRO_0000029203
Regions
	Domain	325 – 545	221	Peptidase M12B
	Domain	546 – 633	88	Disintegrin
	Domain	634 – 686	53	TSP type-1 1
	Domain	915 – 975	61	TSP type-1 2
	Domain	976 – 1037	62	TSP type-1 3
	Domain	1039 – 1083	45	TSP type-1 4
	Domain	1087 – 1144	58	TSP type-1 5
	Domain	1160 – 1199	40	PLAC
	Region	791 – 914	124	Spacer
	Motif	292 – 299	8	Cysteine switch By similarity
	Compositional bias	88 – 216	129	Pro-rich
	Compositional bias	687 – 790	104	Cys-rich
Sites
	Active site	483	1	By similarity
	Metal binding	294	1	Zinc; in inhibited form By similarity
	Metal binding	482	1	Zinc; catalytic By similarity
	Metal binding	486	1	Zinc; catalytic By similarity
	Metal binding	492	1	Zinc; catalytic By similarity
Amino acid modifications
	Glycosylation	260	1	N-linked (GlcNAc...) Potential
	Glycosylation	797	1	N-linked (GlcNAc...) Potential
	Glycosylation	907	1	N-linked (GlcNAc...) Potential
	Glycosylation	949	1	N-linked (GlcNAc...) Potential
	Glycosylation	1009	1	N-linked (GlcNAc...) Potential
	Disulfide bond	460 ↔ 540		By similarity
	Disulfide bond	499 ↔ 524		By similarity
	Disulfide bond	645 ↔ 680		By similarity
	Disulfide bond	649 ↔ 685		By similarity
	Disulfide bond	660 ↔ 670		By similarity
	Disulfide bond	988 ↔ 1031		By similarity
	Disulfide bond	992 ↔ 1036		By similarity
	Disulfide bond	1003 ↔ 1020		By similarity
Natural variations
	Natural variant	360	1	L → I in a breast cancer sample; somatic mutation. Ref.3		VAR_036154
	Natural variant	582	1	E → G. Corresponds to variant rs10062501 [ dbSNP | Ensembl ].		VAR_057087
	Natural variant	1089	1	Y → F. Corresponds to variant rs11749126 [ dbSNP | Ensembl ].		VAR_024599
Experimental info
	Sequence conflict	367	1	S → G in CAC84565. Ref.1
	Sequence conflict	1048	1	C → F in CAC84565. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q8TE59 [UniParc]. Last modified May 18, 2010. Version 2. Checksum: 21EFB26660DEB6D9	FASTA	1,207	134,048
	10 20 30 40 50 60 MRLTHICCCC LLYQLGFLSN GIVSELQFAP DREEWEVVFP ALWRREPVDP AGGSGGSADP 70 80 90 100 110 120 GWVRGVGGGG SARAQAAGSS REVRSVAPVP LEEPVEGRSE SRLRPPPPSE GEEDEELESQ 130 140 150 160 170 180 ELPRGSSGAA ALSPGAPASW QPPPPPQPPP SPPPAQHAEP DGDEVLLRIP AFSRDLYLLL 190 200 210 220 230 240 RRDGRFLAPR FAVEQRPNPG PGPTGAASAP QPPAPPDAGC FYTGAVLRHP GSLASFSTCG 250 260 270 280 290 300 GGLMGFIQLN EDFIFIEPLN DTMAITGHPH RVYRQKRSME EKVTEKSALH SHYCGIISDK 310 320 330 340 350 360 GRPRSRKIAE SGRGKRYSYK LPQEYNIETV VVADPAMVSY HGADAARRFI LTILNMVFNL 370 380 390 400 410 420 FQHKSLSVQV NLRVIKLILL HETPPELYIG HHGEKMLESF CKWQHEEFGK KNDIHLEMST 430 440 450 460 470 480 NWGEDMTSVD AAILITRKDF CVHKDEPCDT VGIAYLSGMC SEKRKCIIAE DNGLNLAFTI 490 500 510 520 530 540 AHEMGHNMGI NHDNDHPSCA DGLHIMSGEW IKGQNLGDVS WSRCSKEDLE RFLRSKASNC 550 560 570 580 590 600 LLQTNPQSVN SVMVPSKLPG MTYTADEQCQ ILFGPLASFC QEMQHVICTG LWCKVEGEKE 610 620 630 640 650 660 CRTKLDPPMD GTDCDLGKWC KAGECTSRTS APEHLAGEWS LWSPCSRTCS AGISSRERKC 670 680 690 700 710 720 PGLDSEARDC NGPRKQYRIC ENPPCPAGLP GFRDWQCQAY SVRTSSPKHI LQWQAVLDEE 730 740 750 760 770 780 KPCALFCSPV GKEQPILLSE KVMDGTSCGY QGLDICANGR CQKVGCDGLL GSLAREDHCG 790 800 810 820 830 840 VCNGNGKSCK IIKGDFNHTR GAGYVEVLVI PAGARRIKVV EEKPAHSYLA LRDAGKQSIN 850 860 870 880 890 900 SDWKIEHSGA FNLAGTTVHY VRRGLWEKIS AKGPTTAPLH LLVLLFQDQN YGLHYEYTIP 910 920 930 940 950 960 SDPLPENQSS KAPEPLFMWT HTSWEDCDAT CGGGERKTTV SCTKIMSKNI SIVDNEKCKY 970 980 990 1000 1010 1020 LTKPEPQIRK CNEQPCQTRW MMTEWTPCSR TCGKGMQSRQ VACTQQLSNG TLIRARERDC 1030 1040 1050 1060 1070 1080 IGPKPASAQR CEGQDCMTVW EAGVWSECSV KCGKGIRHRT VRCTNPRKKC VLSTRPREAE 1090 1100 1110 1120 1130 1140 DCEDYSKCYV WRMGDWSKCS ITCGKGMQSR VIQCMHKITG RHGNECFSSE KPAAYRPCHL 1150 1160 1170 1180 1190 1200 QPCNEKINVN TITSPRLAAL TFKCLGDQWP VYCRVIREKN LCQDMRWYQR CCETCRDFYA QKLQQKS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, expression analysis, and structural characterization of seven novel human ADAMTSs, a family of metalloproteinases with disintegrin and thrombospondin-1 domains." Cal S., Obaya A.J., Llamazares M., Garabaya C., Quesada V., Lopez-Otin C. Gene 283:49-62(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The DNA sequence and comparative analysis of human chromosome 5." Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M. Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] ILE-360.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ311904 mRNA. Translation: CAC84565.1. AC008425 Genomic DNA. No translation available. AC008528 Genomic DNA. No translation available. AC008591 Genomic DNA. No translation available. AC106781 Genomic DNA. No translation available. AC129713 Genomic DNA. No translation available.
IPI	IPI00152639.
RefSeq	NP_598377.3. NM_133638.3.
UniGene	Hs.23751.
3D structure databases
ProteinModelPortal	Q8TE59.
SMR	Q8TE59. Positions 327-902, 978-1038, 1041-1067.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000274487.
Protein family/group databases
MEROPS	M12.029.
PTM databases
PhosphoSite	Q8TE59.
Polymorphism databases
DMDM	296434402.
Proteomic databases
PaxDb	Q8TE59.
PRIDE	Q8TE59.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000274487; ENSP00000274487; ENSG00000145808.
GeneID	171019.
KEGG	hsa:171019.
UCSC	uc003kvb.1. human.
Organism-specific databases
CTD	171019.
GeneCards	GC05P128824.
H-InvDB	HIX0024810.
HGNC	HGNC:17111. ADAMTS19.
MIM	607513. gene.
neXtProt	NX_Q8TE59.
PharmGKB	PA24545.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG259740.
HOGENOM	HOG000004800.
HOVERGEN	HBG050621.
InParanoid	Q8TE59.
KO	K08633.
OMA	GHNMGIN.
OrthoDB	EOG4KSPJ0.
PhylomeDB	Q8TE59.
Gene expression databases
ArrayExpress	Q8TE59.
Bgee	Q8TE59.
CleanEx	HS_ADAMTS19.
Genevestigator	Q8TE59.
GermOnline	ENSG00000145808. 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. 4 hits. [Graphical view]
PRINTS	PR01857. ADAMTSFAMILY.
SMART	SM00209. TSP1. 5 hits. [Graphical view]
SUPFAM	SSF82895. TSP1. 5 hits.
PROSITE	PS50215. ADAM_MEPRO. 1 hit. PS00546. CYSTEINE_SWITCH. False negative. 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	171019.
NextBio	89186.
SOURCE	Search...

Entry information

Entry name

ATS19_HUMAN

Accession

Primary (citable) accession number: Q8TE59

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 25, 2003
Last sequence update:	May 18, 2010
Last modified:	May 1, 2013
This is version 104 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.