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Protein

A disintegrin and metalloproteinase with thrombospondin motifs 16

Gene

ADAMTS16

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi249Zinc; in inhibited formBy similarity1
Metal bindingi433Zinc; catalyticPROSITE-ProRule annotation1
Active sitei434PROSITE-ProRule annotation1
Metal bindingi437Zinc; catalyticPROSITE-ProRule annotation1
Metal bindingi443Zinc; catalyticPROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000145536-MONOMER.
ReactomeiR-HSA-1474228. Degradation of the extracellular matrix.
R-HSA-5083635. Defective B3GALTL causes Peters-plus syndrome (PpS).
R-HSA-5173214. O-glycosylation of TSR domain-containing proteins.

Protein family/group databases

MEROPSiM12.026.

Names & Taxonomyi

Protein namesi
Recommended name:
A disintegrin and metalloproteinase with thrombospondin motifs 16 (EC:3.4.24.-)
Short name:
ADAM-TS 16
Short name:
ADAM-TS16
Short name:
ADAMTS-16
Gene namesi
Name:ADAMTS16
Synonyms:KIAA2029
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:17108. ADAMTS16.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Organism-specific databases

DisGeNETi170690.
OpenTargetsiENSG00000145536.
PharmGKBiPA24542.

Polymorphism and mutation databases

BioMutaiADAMTS16.
DMDMi296439429.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 24Sequence analysisAdd BLAST24
PropeptideiPRO_000002919425 – 279By similarityAdd BLAST255
ChainiPRO_0000029195280 – 1224A disintegrin and metalloproteinase with thrombospondin motifs 16Add BLAST945

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi156N-linked (GlcNAc...)Sequence analysis1
Glycosylationi310N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi366 ↔ 417By similarity
Disulfide bondi392 ↔ 399By similarity
Disulfide bondi411 ↔ 490By similarity
Disulfide bondi450 ↔ 474By similarity
Disulfide bondi518 ↔ 543By similarity
Disulfide bondi529 ↔ 550By similarity
Disulfide bondi538 ↔ 569By similarity
Disulfide bondi563 ↔ 574By similarity
Disulfide bondi598 ↔ 635By similarity
Disulfide bondi602 ↔ 640By similarity
Disulfide bondi613 ↔ 625By similarity
Glycosylationi741N-linked (GlcNAc...)Sequence analysis1
Glycosylationi780N-linked (GlcNAc...)Sequence analysis1
Glycosylationi835N-linked (GlcNAc...)Sequence analysis1
Glycosylationi905N-linked (GlcNAc...)Sequence analysis1
Glycosylationi935N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi939 ↔ 981By similarity
Disulfide bondi943 ↔ 986By similarity
Disulfide bondi954 ↔ 970By similarity

Post-translational modificationi

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).By similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

EPDiQ8TE57.
PaxDbiQ8TE57.
PeptideAtlasiQ8TE57.
PRIDEiQ8TE57.

PTM databases

iPTMnetiQ8TE57.
PhosphoSitePlusiQ8TE57.

Expressioni

Tissue specificityi

Expressed in fetal lung and kidney and in adult prostate and ovary.

Gene expression databases

BgeeiENSG00000145536.
CleanExiHS_ADAMTS16.
ExpressionAtlasiQ8TE57. baseline and differential.
GenevisibleiQ8TE57. HS.

Organism-specific databases

HPAiCAB022462.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000274181.

Structurei

3D structure databases

ProteinModelPortaliQ8TE57.
SMRiQ8TE57.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini290 – 495Peptidase M12BPROSITE-ProRule annotationAdd BLAST206
Domaini496 – 585DisintegrinAdd BLAST90
Domaini586 – 641TSP type-1 1PROSITE-ProRule annotationAdd BLAST56
Domaini874 – 922TSP type-1 2PROSITE-ProRule annotationAdd BLAST49
Domaini927 – 987TSP type-1 3PROSITE-ProRule annotationAdd BLAST61
Domaini988 – 1048TSP type-1 4PROSITE-ProRule annotationAdd BLAST61
Domaini1051 – 1115TSP type-1 5PROSITE-ProRule annotationAdd BLAST65
Domaini1127 – 1181TSP type-1 6PROSITE-ProRule annotationAdd BLAST55
Domaini1186 – 1223PLACPROSITE-ProRule annotationAdd BLAST38

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni747 – 873SpacerAdd BLAST127

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi247 – 254Cysteine switchBy similarity8

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi642 – 746Cys-richAdd BLAST105

Domaini

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.

Sequence similaritiesi

Contains 1 disintegrin domain.Curated
Contains 1 peptidase M12B domain.PROSITE-ProRule annotation
Contains 1 PLAC domain.PROSITE-ProRule annotation
Contains 6 TSP type-1 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiKOG3538. Eukaryota.
ENOG410XPKZ. LUCA.
GeneTreeiENSGT00760000118880.
HOGENOMiHOG000004800.
HOVERGENiHBG004315.
InParanoidiQ8TE57.
KOiK08630.
OMAiEDQDLCK.
OrthoDBiEOG091G14M8.
PhylomeDBiQ8TE57.
TreeFamiTF313537.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR010294. ADAM_spacer1.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR013273. Peptidase_M12B_ADAM-TS.
IPR002870. Peptidase_M12B_N.
IPR010909. PLAC.
IPR000884. TSP1_rpt.
[Graphical view]
PfamiPF05986. 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]
PRINTSiPR01857. ADAMTSFAMILY.
SMARTiSM00209. TSP1. 6 hits.
[Graphical view]
SUPFAMiSSF82895. SSF82895. 5 hits.
PROSITEiPS50215. ADAM_MEPRO. 1 hit.
PS50900. PLAC. 1 hit.
PS50092. TSP1. 5 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8TE57-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MKPRARGWRG LAALWMLLAQ VAEQAPACAM GPAAAAPGSP SVPRPPPPAE
60 70 80 90 100
RPGWMEKGEY DLVSAYEVDH RGDYVSHEIM HHQRRRRAVP VSEVESLHLR
110 120 130 140 150
LKGSRHDFHM DLRTSSSLVA PGFIVQTLGK TGTKSVQTLP PEDFCFYQGS
160 170 180 190 200
LRSHRNSSVA LSTCQGLSGM IRTEEADYFL RPLPSHLSWK LGRAAQGSSP
210 220 230 240 250
SHVLYKRSTE PHAPGASEVL VTSRTWELAH QPLHSSDLRL GLPQKQHFCG
260 270 280 290 300
RRKKYMPQPP KEDLFILPDE YKSCLRHKRS LLRSHRNEEL NVETLVVVDK
310 320 330 340 350
KMMQNHGHEN ITTYVLTILN MVSALFKDGT IGGNINIAIV GLILLEDEQP
360 370 380 390 400
GLVISHHADH TLSSFCQWQS GLMGKDGTRH DHAILLTGLD ICSWKNEPCD
410 420 430 440 450
TLGFAPISGM CSKYRSCTIN EDTGLGLAFT IAHESGHNFG MIHDGEGNMC
460 470 480 490 500
KKSEGNIMSP TLAGRNGVFS WSPCSRQYLH KFLSTAQAIC LADQPKPVKE
510 520 530 540 550
YKYPEKLPGE LYDANTQCKW QFGEKAKLCM LDFKKDICKA LWCHRIGRKC
560 570 580 590 600
ETKFMPAAEG TICGHDMWCR GGQCVKYGDE GPKPTHGHWS DWSSWSPCSR
610 620 630 640 650
TCGGGVSHRS RLCTNPKPSH GGKFCEGSTR TLKLCNSQKC PRDSVDFRAA
660 670 680 690 700
QCAEHNSRRF RGRHYKWKPY TQVEDQDLCK LYCIAEGFDF FFSLSNKVKD
710 720 730 740 750
GTPCSEDSRN VCIDGICERV GCDNVLGSDA VEDVCGVCNG NNSACTIHRG
760 770 780 790 800
LYTKHHHTNQ YYHMVTIPSG ARSIRIYEMN VSTSYISVRN ALRRYYLNGH
810 820 830 840 850
WTVDWPGRYK FSGTTFDYRR SYNEPENLIA TGPTNETLIV ELLFQGRNPG
860 870 880 890 900
VAWEYSMPRL GTEKQPPAQP SYTWAIVRSE CSVSCGGGQM TVREGCYRDL
910 920 930 940 950
KFQVNMSFCN PKTRPVTGLV PCKVSACPPS WSVGNWSACS RTCGGGAQSR
960 970 980 990 1000
PVQCTRRVHY DSEPVPASLC PQPAPSSRQA CNSQSCPPAW SAGPWAECSH
1010 1020 1030 1040 1050
TCGKGWRKRA VACKSTNPSA RAQLLPDAVC TSEPKPRMHE ACLLQRCHKP
1060 1070 1080 1090 1100
KKLQWLVSAW SQCSVTCERG TQKRFLKCAE KYVSGKYREL ASKKCSHLPK
1110 1120 1130 1140 1150
PSLELERACA PLPCPRHPPF AAAGPSRGSW FASPWSQCTA SCGGGVQTRS
1160 1170 1180 1190 1200
VQCLAGGRPA SGCLLHQKPS ASLACNTHFC PIAEKKDAFC KDYFHWCYLV
1210 1220
PQHGMCSHKF YGKQCCKTCS KSNL
Length:1,224
Mass (Da):136,203
Last modified:May 18, 2010 - v3
Checksum:iFB6115E6C97A9683
GO
Isoform 2 (identifier: Q8TE57-2) [UniParc]FASTAAdd to basket

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

Show »
Length:1,072
Mass (Da):119,507
Checksum:i3E2C0FF34194E631
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti90P → A in CAC86015 (PubMed:11867212).Curated1
Sequence conflicti104S → P in CAC86015 (PubMed:11867212).Curated1
Sequence conflicti284S → Y in BAC23125 (Ref. 4) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_057076110M → V.Corresponds to variant rs1863968dbSNPEnsembl.1
Natural variantiVAR_057077486A → T.Corresponds to variant rs16875054dbSNPEnsembl.1
Natural variantiVAR_057078789R → C.Corresponds to variant rs9313105dbSNPEnsembl.1
Natural variantiVAR_057079859R → L.Corresponds to variant rs16875122dbSNPEnsembl.1
Natural variantiVAR_057080863E → K.Corresponds to variant rs35394775dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0076641063 – 1072CSVTCERGTQ → VGALVSRERG in isoform 2. 1 Publication10
Alternative sequenceiVSP_0076651073 – 1224Missing in isoform 2. 1 PublicationAdd BLAST152

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS43299.1. [Q8TE57-1]
RefSeqiNP_620687.2. NM_139056.3. [Q8TE57-1]
UniGeneiHs.661915.

Genome annotation databases

EnsembliENST00000274181; ENSP00000274181; ENSG00000145536. [Q8TE57-1]
GeneIDi170690.
KEGGihsa:170690.
UCSCiuc003jdl.4. human. [Q8TE57-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS43299.1. [Q8TE57-1]
RefSeqiNP_620687.2. NM_139056.3. [Q8TE57-1]
UniGeneiHs.661915.

3D structure databases

ProteinModelPortaliQ8TE57.
SMRiQ8TE57.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000274181.

Protein family/group databases

MEROPSiM12.026.

PTM databases

iPTMnetiQ8TE57.
PhosphoSitePlusiQ8TE57.

Polymorphism and mutation databases

BioMutaiADAMTS16.
DMDMi296439429.

Proteomic databases

EPDiQ8TE57.
PaxDbiQ8TE57.
PeptideAtlasiQ8TE57.
PRIDEiQ8TE57.

Protocols and materials databases

DNASUi170690.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000274181; ENSP00000274181; ENSG00000145536. [Q8TE57-1]
GeneIDi170690.
KEGGihsa:170690.
UCSCiuc003jdl.4. human. [Q8TE57-1]

Organism-specific databases

CTDi170690.
DisGeNETi170690.
GeneCardsiADAMTS16.
HGNCiHGNC:17108. ADAMTS16.
HPAiCAB022462.
MIMi607510. gene.
neXtProtiNX_Q8TE57.
OpenTargetsiENSG00000145536.
PharmGKBiPA24542.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3538. Eukaryota.
ENOG410XPKZ. LUCA.
GeneTreeiENSGT00760000118880.
HOGENOMiHOG000004800.
HOVERGENiHBG004315.
InParanoidiQ8TE57.
KOiK08630.
OMAiEDQDLCK.
OrthoDBiEOG091G14M8.
PhylomeDBiQ8TE57.
TreeFamiTF313537.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000145536-MONOMER.
ReactomeiR-HSA-1474228. Degradation of the extracellular matrix.
R-HSA-5083635. Defective B3GALTL causes Peters-plus syndrome (PpS).
R-HSA-5173214. O-glycosylation of TSR domain-containing proteins.

Miscellaneous databases

GenomeRNAii170690.
PROiQ8TE57.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000145536.
CleanExiHS_ADAMTS16.
ExpressionAtlasiQ8TE57. baseline and differential.
GenevisibleiQ8TE57. HS.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR010294. ADAM_spacer1.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR013273. Peptidase_M12B_ADAM-TS.
IPR002870. Peptidase_M12B_N.
IPR010909. PLAC.
IPR000884. TSP1_rpt.
[Graphical view]
PfamiPF05986. 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]
PRINTSiPR01857. ADAMTSFAMILY.
SMARTiSM00209. TSP1. 6 hits.
[Graphical view]
SUPFAMiSSF82895. SSF82895. 5 hits.
PROSITEiPS50215. ADAM_MEPRO. 1 hit.
PS50900. PLAC. 1 hit.
PS50092. TSP1. 5 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiATS16_HUMAN
AccessioniPrimary (citable) accession number: Q8TE57
Secondary accession number(s): C6G490, Q8IVE2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2003
Last sequence update: May 18, 2010
Last modified: November 2, 2016
This is version 131 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Peptidase families
    Classification of peptidase families and list of entries
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.