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Q8TE57 (ATS16_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 109. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
A disintegrin and metalloproteinase with thrombospondin motifs 16

Short name=ADAM-TS 16
Short name=ADAM-TS16
Short name=ADAMTS-16
EC=3.4.24.-
Gene names
Name:ADAMTS16
Synonyms:KIAA2029
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1224 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 and kidney and in adult prostate and ovary.

Domain

The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix By similarity.

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 6 TSP type-1 domains.

Ontologies

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8TE57-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8TE57-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1063-1072: CSVTCERGTQ → VGALVSRERG
     1073-1224: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Propeptide25 – 279255 By similarity
PRO_0000029194
Chain280 – 1224945A disintegrin and metalloproteinase with thrombospondin motifs 16
PRO_0000029195

Regions

Domain290 – 495206Peptidase M12B
Domain496 – 58590Disintegrin
Domain586 – 64156TSP type-1 1
Domain874 – 92249TSP type-1 2
Domain927 – 98761TSP type-1 3
Domain988 – 104861TSP type-1 4
Domain1051 – 111565TSP type-1 5
Domain1127 – 118155TSP type-1 6
Domain1186 – 122338PLAC
Region747 – 873127Spacer
Motif247 – 2548Cysteine switch By similarity
Compositional bias642 – 746105Cys-rich

Sites

Active site4341 By similarity
Metal binding2491Zinc; in inhibited form By similarity
Metal binding4331Zinc; catalytic By similarity
Metal binding4371Zinc; catalytic By similarity
Metal binding4431Zinc; catalytic By similarity

Amino acid modifications

Glycosylation1561N-linked (GlcNAc...) Potential
Glycosylation3101N-linked (GlcNAc...) Potential
Glycosylation7411N-linked (GlcNAc...) Potential
Glycosylation7801N-linked (GlcNAc...) Potential
Glycosylation8351N-linked (GlcNAc...) Potential
Glycosylation9051N-linked (GlcNAc...) Potential
Glycosylation9351N-linked (GlcNAc...) Potential
Disulfide bond366 ↔ 417 By similarity
Disulfide bond392 ↔ 399 By similarity
Disulfide bond411 ↔ 490 By similarity
Disulfide bond450 ↔ 474 By similarity
Disulfide bond518 ↔ 543 By similarity
Disulfide bond529 ↔ 550 By similarity
Disulfide bond538 ↔ 569 By similarity
Disulfide bond563 ↔ 574 By similarity
Disulfide bond598 ↔ 635 By similarity
Disulfide bond602 ↔ 640 By similarity
Disulfide bond613 ↔ 625 By similarity
Disulfide bond939 ↔ 981 By similarity
Disulfide bond943 ↔ 986 By similarity
Disulfide bond954 ↔ 970 By similarity

Natural variations

Alternative sequence1063 – 107210CSVTCERGTQ → VGALVSRERG in isoform 2.
VSP_007664
Alternative sequence1073 – 1224152Missing in isoform 2.
VSP_007665
Natural variant1101M → V.
Corresponds to variant rs1863968 [ dbSNP | Ensembl ].
VAR_057076
Natural variant4861A → T.
Corresponds to variant rs16875054 [ dbSNP | Ensembl ].
VAR_057077
Natural variant7891R → C.
Corresponds to variant rs9313105 [ dbSNP | Ensembl ].
VAR_057078
Natural variant8591R → L.
Corresponds to variant rs16875122 [ dbSNP | Ensembl ].
VAR_057079
Natural variant8631E → K.
Corresponds to variant rs35394775 [ dbSNP | Ensembl ].
VAR_057080

Experimental info

Sequence conflict901P → A in CAC86015. Ref.1
Sequence conflict1041S → P in CAC86015. Ref.1
Sequence conflict2841S → Y in BAC23125. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 18, 2010. Version 3.
Checksum: FB6115E6C97A9683

FASTA1,224136,203
        10         20         30         40         50         60 
MKPRARGWRG LAALWMLLAQ VAEQAPACAM GPAAAAPGSP SVPRPPPPAE RPGWMEKGEY 

        70         80         90        100        110        120 
DLVSAYEVDH RGDYVSHEIM HHQRRRRAVP VSEVESLHLR LKGSRHDFHM DLRTSSSLVA 

       130        140        150        160        170        180 
PGFIVQTLGK TGTKSVQTLP PEDFCFYQGS LRSHRNSSVA LSTCQGLSGM IRTEEADYFL 

       190        200        210        220        230        240 
RPLPSHLSWK LGRAAQGSSP SHVLYKRSTE PHAPGASEVL VTSRTWELAH QPLHSSDLRL 

       250        260        270        280        290        300 
GLPQKQHFCG RRKKYMPQPP KEDLFILPDE YKSCLRHKRS LLRSHRNEEL NVETLVVVDK 

       310        320        330        340        350        360 
KMMQNHGHEN ITTYVLTILN MVSALFKDGT IGGNINIAIV GLILLEDEQP GLVISHHADH 

       370        380        390        400        410        420 
TLSSFCQWQS GLMGKDGTRH DHAILLTGLD ICSWKNEPCD TLGFAPISGM CSKYRSCTIN 

       430        440        450        460        470        480 
EDTGLGLAFT IAHESGHNFG MIHDGEGNMC KKSEGNIMSP TLAGRNGVFS WSPCSRQYLH 

       490        500        510        520        530        540 
KFLSTAQAIC LADQPKPVKE YKYPEKLPGE LYDANTQCKW QFGEKAKLCM LDFKKDICKA 

       550        560        570        580        590        600 
LWCHRIGRKC ETKFMPAAEG TICGHDMWCR GGQCVKYGDE GPKPTHGHWS DWSSWSPCSR 

       610        620        630        640        650        660 
TCGGGVSHRS RLCTNPKPSH GGKFCEGSTR TLKLCNSQKC PRDSVDFRAA QCAEHNSRRF 

       670        680        690        700        710        720 
RGRHYKWKPY TQVEDQDLCK LYCIAEGFDF FFSLSNKVKD GTPCSEDSRN VCIDGICERV 

       730        740        750        760        770        780 
GCDNVLGSDA VEDVCGVCNG NNSACTIHRG LYTKHHHTNQ YYHMVTIPSG ARSIRIYEMN 

       790        800        810        820        830        840 
VSTSYISVRN ALRRYYLNGH WTVDWPGRYK FSGTTFDYRR SYNEPENLIA TGPTNETLIV 

       850        860        870        880        890        900 
ELLFQGRNPG VAWEYSMPRL GTEKQPPAQP SYTWAIVRSE CSVSCGGGQM TVREGCYRDL 

       910        920        930        940        950        960 
KFQVNMSFCN PKTRPVTGLV PCKVSACPPS WSVGNWSACS RTCGGGAQSR PVQCTRRVHY 

       970        980        990       1000       1010       1020 
DSEPVPASLC PQPAPSSRQA CNSQSCPPAW SAGPWAECSH TCGKGWRKRA VACKSTNPSA 

      1030       1040       1050       1060       1070       1080 
RAQLLPDAVC TSEPKPRMHE ACLLQRCHKP KKLQWLVSAW SQCSVTCERG TQKRFLKCAE 

      1090       1100       1110       1120       1130       1140 
KYVSGKYREL ASKKCSHLPK PSLELERACA PLPCPRHPPF AAAGPSRGSW FASPWSQCTA 

      1150       1160       1170       1180       1190       1200 
SCGGGVQTRS VQCLAGGRPA SGCLLHQKPS ASLACNTHFC PIAEKKDAFC KDYFHWCYLV 

      1210       1220 
PQHGMCSHKF YGKQCCKTCS KSNL 

« Hide

Isoform 2 [UniParc].

Checksum: 3E2C0FF34194E631
Show »

FASTA1,072119,507

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] (ISOFORM 2).
[2]NHLBI resequencing and genotyping service (RS&G)
Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"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].
[4]"The nucleotide sequence of a long cDNA clone isolated from human."
Nagase T., Kikuno R., Ohara O.
Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 204-1224 (ISOFORM 1).
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ315734 mRNA. Translation: CAC86015.1.
FJ515844 Genomic DNA. Translation: ACS13738.1.
AC010269 Genomic DNA. No translation available.
AC022424 Genomic DNA. No translation available.
AC091978 Genomic DNA. No translation available.
AB095949 mRNA. Translation: BAC23125.1.
RefSeqNP_620687.2. NM_139056.2.
UniGeneHs.661915.

3D structure databases

ProteinModelPortalQ8TE57.
SMRQ8TE57. Positions 292-860, 869-1181.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSM12.026.

PTM databases

PhosphoSiteQ8TE57.

Polymorphism databases

DMDM296439429.

Proteomic databases

PaxDbQ8TE57.
PRIDEQ8TE57.

Protocols and materials databases

DNASU170690.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000274181; ENSP00000274181; ENSG00000145536. [Q8TE57-1]
GeneID170690.
KEGGhsa:170690.
UCSCuc003jdk.1. human. [Q8TE57-2]
uc003jdl.3. human. [Q8TE57-1]

Organism-specific databases

CTD170690.
GeneCardsGC05P005140.
HGNCHGNC:17108. ADAMTS16.
MIM607510. gene.
neXtProtNX_Q8TE57.
PharmGKBPA24542.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG237764.
HOGENOMHOG000004800.
HOVERGENHBG004315.
InParanoidQ8TE57.
KOK08630.
OMAEDQDLCK.
PhylomeDBQ8TE57.
TreeFamTF313537.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressQ8TE57.
BgeeQ8TE57.
CleanExHS_ADAMTS16.
GenevestigatorQ8TE57.

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. 5 hits.
[Graphical view]
PRINTSPR01857. ADAMTSFAMILY.
SMARTSM00209. TSP1. 6 hits.
[Graphical view]
SUPFAMSSF82895. SSF82895. 5 hits.
PROSITEPS50215. ADAM_MEPRO. 1 hit.
PS50900. PLAC. 1 hit.
PS50092. TSP1. 5 hits.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi170690.
NextBio89102.
PROQ8TE57.
SOURCESearch...

Entry information

Entry nameATS16_HUMAN
AccessionPrimary (citable) accession number: Q8TE57
Secondary accession number(s): C6G490, Q8IVE2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2003
Last sequence update: May 18, 2010
Last modified: March 19, 2014
This is version 109 of the entry and version 3 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