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Q8TE57

- ATS16_HUMAN

UniProt

Q8TE57 - ATS16_HUMAN

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Protein

A disintegrin and metalloproteinase with thrombospondin motifs 16

Gene

ADAMTS16

Organism
Homo sapiens (Human)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi249 – 2491Zinc; in inhibited formBy similarity
Metal bindingi433 – 4331Zinc; catalyticPROSITE-ProRule annotation
Active sitei434 – 4341PROSITE-ProRule annotation
Metal bindingi437 – 4371Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi443 – 4431Zinc; catalyticPROSITE-ProRule annotation

GO - Molecular functioni

  1. metalloendopeptidase activity Source: InterPro
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. branching involved in ureteric bud morphogenesis Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_118572. Degradation of the extracellular matrix.
REACT_200626. 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
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:17108. ADAMTS16.

Subcellular locationi

GO - Cellular componenti

  1. proteinaceous extracellular matrix Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24542.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence AnalysisAdd
BLAST
Propeptidei25 – 279255By similarityPRO_0000029194Add
BLAST
Chaini280 – 1224945A disintegrin and metalloproteinase with thrombospondin motifs 16PRO_0000029195Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi156 – 1561N-linked (GlcNAc...)Sequence Analysis
Glycosylationi310 – 3101N-linked (GlcNAc...)Sequence Analysis
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
Glycosylationi741 – 7411N-linked (GlcNAc...)Sequence Analysis
Glycosylationi780 – 7801N-linked (GlcNAc...)Sequence Analysis
Glycosylationi835 – 8351N-linked (GlcNAc...)Sequence Analysis
Glycosylationi905 – 9051N-linked (GlcNAc...)Sequence Analysis
Glycosylationi935 – 9351N-linked (GlcNAc...)Sequence Analysis
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

PaxDbiQ8TE57.
PRIDEiQ8TE57.

PTM databases

PhosphoSiteiQ8TE57.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ8TE57.
CleanExiHS_ADAMTS16.
ExpressionAtlasiQ8TE57. baseline.
GenevestigatoriQ8TE57.

Structurei

3D structure databases

ProteinModelPortaliQ8TE57.
SMRiQ8TE57. Positions 292-789.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini290 – 495206Peptidase M12BPROSITE-ProRule annotationAdd
BLAST
Domaini496 – 58590DisintegrinAdd
BLAST
Domaini586 – 64156TSP type-1 1PROSITE-ProRule annotationAdd
BLAST
Domaini874 – 92249TSP type-1 2PROSITE-ProRule annotationAdd
BLAST
Domaini927 – 98761TSP type-1 3PROSITE-ProRule annotationAdd
BLAST
Domaini988 – 104861TSP type-1 4PROSITE-ProRule annotationAdd
BLAST
Domaini1051 – 111565TSP type-1 5PROSITE-ProRule annotationAdd
BLAST
Domaini1127 – 118155TSP type-1 6PROSITE-ProRule annotationAdd
BLAST
Domaini1186 – 122338PLACPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni747 – 873127SpacerAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi247 – 2548Cysteine switchBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi642 – 746105Cys-richAdd
BLAST

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

eggNOGiNOG237764.
GeneTreeiENSGT00760000118880.
HOGENOMiHOG000004800.
HOVERGENiHBG004315.
InParanoidiQ8TE57.
KOiK08630.
OMAiEDQDLCK.
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. Thrombospondin_1_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. Align

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti90 – 901P → A in CAC86015. (PubMed:11867212)Curated
Sequence conflicti104 – 1041S → P in CAC86015. (PubMed:11867212)Curated
Sequence conflicti284 – 2841S → Y in BAC23125. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti110 – 1101M → V.
Corresponds to variant rs1863968 [ dbSNP | Ensembl ].
VAR_057076
Natural varianti486 – 4861A → T.
Corresponds to variant rs16875054 [ dbSNP | Ensembl ].
VAR_057077
Natural varianti789 – 7891R → C.
Corresponds to variant rs9313105 [ dbSNP | Ensembl ].
VAR_057078
Natural varianti859 – 8591R → L.
Corresponds to variant rs16875122 [ dbSNP | Ensembl ].
VAR_057079
Natural varianti863 – 8631E → K.
Corresponds to variant rs35394775 [ dbSNP | Ensembl ].
VAR_057080

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1063 – 107210CSVTCERGTQ → VGALVSRERG in isoform 2. 1 PublicationVSP_007664
Alternative sequencei1073 – 1224152Missing in isoform 2. 1 PublicationVSP_007665Add
BLAST

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_139056.2. [Q8TE57-1]
UniGeneiHs.661915.

Genome annotation databases

EnsembliENST00000274181; ENSP00000274181; ENSG00000145536. [Q8TE57-1]
GeneIDi170690.
KEGGihsa:170690.
UCSCiuc003jdk.1. human. [Q8TE57-2]
uc003jdl.3. human. [Q8TE57-1]

Polymorphism databases

DMDMi296439429.

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 .
CCDSi CCDS43299.1. [Q8TE57-1 ]
RefSeqi NP_620687.2. NM_139056.2. [Q8TE57-1 ]
UniGenei Hs.661915.

3D structure databases

ProteinModelPortali Q8TE57.
SMRi Q8TE57. Positions 292-789.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi M12.026.

PTM databases

PhosphoSitei Q8TE57.

Polymorphism databases

DMDMi 296439429.

Proteomic databases

PaxDbi Q8TE57.
PRIDEi Q8TE57.

Protocols and materials databases

DNASUi 170690.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000274181 ; ENSP00000274181 ; ENSG00000145536 . [Q8TE57-1 ]
GeneIDi 170690.
KEGGi hsa:170690.
UCSCi uc003jdk.1. human. [Q8TE57-2 ]
uc003jdl.3. human. [Q8TE57-1 ]

Organism-specific databases

CTDi 170690.
GeneCardsi GC05P005140.
HGNCi HGNC:17108. ADAMTS16.
MIMi 607510. gene.
neXtProti NX_Q8TE57.
PharmGKBi PA24542.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG237764.
GeneTreei ENSGT00760000118880.
HOGENOMi HOG000004800.
HOVERGENi HBG004315.
InParanoidi Q8TE57.
KOi K08630.
OMAi EDQDLCK.
PhylomeDBi Q8TE57.
TreeFami TF313537.

Enzyme and pathway databases

Reactomei REACT_118572. Degradation of the extracellular matrix.
REACT_200626. O-glycosylation of TSR domain-containing proteins.

Miscellaneous databases

GenomeRNAii 170690.
NextBioi 89102.
PROi Q8TE57.
SOURCEi Search...

Gene expression databases

Bgeei Q8TE57.
CleanExi HS_ADAMTS16.
ExpressionAtlasi Q8TE57. baseline.
Genevestigatori Q8TE57.

Family and domain databases

Gene3Di 3.40.390.10. 1 hit.
InterProi 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 ]
Pfami 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 ]
PRINTSi PR01857. ADAMTSFAMILY.
SMARTi SM00209. TSP1. 6 hits.
[Graphical view ]
SUPFAMi SSF82895. SSF82895. 5 hits.
PROSITEi PS50215. ADAM_MEPRO. 1 hit.
PS50900. PLAC. 1 hit.
PS50092. TSP1. 5 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

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 26, 2014
This is version 116 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

External Data

Dasty 3