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Q8TE59 (ATS19_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1207 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subcellular location

Secretedextracellular spaceextracellular 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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Propeptide22 – 316295 By similarity
PRO_0000029202
Chain317 – 1207891A disintegrin and metalloproteinase with thrombospondin motifs 19
PRO_0000029203

Regions

Domain325 – 545221Peptidase M12B
Domain546 – 63388Disintegrin
Domain634 – 68653TSP type-1 1
Domain915 – 97561TSP type-1 2
Domain976 – 103762TSP type-1 3
Domain1039 – 108345TSP type-1 4
Domain1087 – 114458TSP type-1 5
Domain1160 – 119940PLAC
Region791 – 914124Spacer
Motif292 – 2998Cysteine switch By similarity
Compositional bias88 – 216129Pro-rich
Compositional bias687 – 790104Cys-rich

Sites

Active site4831 By similarity
Metal binding2941Zinc; in inhibited form By similarity
Metal binding4821Zinc; catalytic By similarity
Metal binding4861Zinc; catalytic By similarity
Metal binding4921Zinc; catalytic By similarity

Amino acid modifications

Glycosylation2601N-linked (GlcNAc...) Potential
Glycosylation7971N-linked (GlcNAc...) Potential
Glycosylation9071N-linked (GlcNAc...) Potential
Glycosylation9491N-linked (GlcNAc...) Potential
Glycosylation10091N-linked (GlcNAc...) Potential
Disulfide bond401 ↔ 466 By similarity
Disulfide bond441 ↔ 448 By similarity
Disulfide bond460 ↔ 540 By similarity
Disulfide bond499 ↔ 524 By similarity
Disulfide bond569 ↔ 593 By similarity
Disulfide bond580 ↔ 601 By similarity
Disulfide bond588 ↔ 620 By similarity
Disulfide bond614 ↔ 625 By similarity
Disulfide bond645 ↔ 680 By similarity
Disulfide bond649 ↔ 685 By similarity
Disulfide bond660 ↔ 670 By similarity
Disulfide bond988 ↔ 1031 By similarity
Disulfide bond992 ↔ 1036 By similarity
Disulfide bond1003 ↔ 1020 By similarity

Natural variations

Natural variant3601L → I in a breast cancer sample; somatic mutation. Ref.3
VAR_036154
Natural variant5821E → G.
Corresponds to variant rs10062501 [ dbSNP | Ensembl ].
VAR_057087
Natural variant10891Y → F.
Corresponds to variant rs11749126 [ dbSNP | Ensembl ].
VAR_024599

Experimental info

Sequence conflict3671S → G in CAC84565. Ref.1
Sequence conflict10481C → F in CAC84565. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8TE59 [UniParc].

Last modified May 18, 2010. Version 2.
Checksum: 21EFB26660DEB6D9

FASTA1,207134,048
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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.
CCDSCCDS4146.1.
RefSeqNP_598377.3. NM_133638.3.
UniGeneHs.23751.

3D structure databases

ProteinModelPortalQ8TE59.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000274487.

Protein family/group databases

MEROPSM12.029.

PTM databases

PhosphoSiteQ8TE59.

Polymorphism databases

DMDM296434402.

Proteomic databases

PaxDbQ8TE59.
PRIDEQ8TE59.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000274487; ENSP00000274487; ENSG00000145808.
GeneID171019.
KEGGhsa:171019.
UCSCuc003kvb.1. human.

Organism-specific databases

CTD171019.
GeneCardsGC05P128824.
H-InvDBHIX0024810.
HGNCHGNC:17111. ADAMTS19.
HPAHPA056171.
MIM607513. gene.
neXtProtNX_Q8TE59.
PharmGKBPA24545.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG259740.
HOGENOMHOG000004800.
HOVERGENHBG050621.
InParanoidQ8TE59.
KOK08633.
OMAEKECKTK.
OrthoDBEOG722J7P.
PhylomeDBQ8TE59.
TreeFamTF313537.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.

Gene expression databases

BgeeQ8TE59.
CleanExHS_ADAMTS19.
GenevestigatorQ8TE59.

Family and domain databases

Gene3D3.40.390.10. 1 hit.
InterProIPR010294. 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]
PfamPF05986. 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]
PRINTSPR01857. ADAMTSFAMILY.
SMARTSM00209. TSP1. 5 hits.
[Graphical view]
SUPFAMSSF82895. SSF82895. 5 hits.
PROSITEPS50215. ADAM_MEPRO. 1 hit.
PS50900. PLAC. 1 hit.
PS50092. TSP1. 5 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi171019.
NextBio89186.
PROQ8TE59.
SOURCESearch...

Entry information

Entry nameATS19_HUMAN
AccessionPrimary (citable) accession number: Q8TE59
Entry history
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: May 18, 2010
Last modified: July 9, 2014
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM