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Protein

A disintegrin and metalloproteinase with thrombospondin motifs 8

Gene

ADAMTS8

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

Functioni

Has anti-angiogenic properties.

Cofactori

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi363 – 3631Zinc; catalyticBy similarity
Active sitei364 – 3641PROSITE-ProRule annotation
Metal bindingi367 – 3671Zinc; catalyticBy similarity
Metal bindingi373 – 3731Zinc; catalyticBy similarity

GO - Molecular functioni

  1. heparin binding Source: UniProtKB-KW
  2. integrin binding Source: ProtInc
  3. low-affinity phosphate transmembrane transporter activity Source: ProtInc
  4. metalloendopeptidase activity Source: InterPro
  5. metallopeptidase activity Source: ProtInc
  6. zinc ion binding Source: InterPro

GO - Biological processi

  1. negative regulation of cell proliferation Source: ProtInc
  2. phosphate ion transmembrane transport Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Heparin-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_118572. Degradation of the extracellular matrix.
REACT_264269. O-glycosylation of TSR domain-containing proteins.

Protein family/group databases

MEROPSiM12.226.

Names & Taxonomyi

Protein namesi
Recommended name:
A disintegrin and metalloproteinase with thrombospondin motifs 8 (EC:3.4.24.-)
Short name:
ADAM-TS 8
Short name:
ADAM-TS8
Short name:
ADAMTS-8
Alternative name(s):
METH-2
METH-8
Gene namesi
Name:ADAMTS8
Synonyms:METH2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:224. ADAMTS8.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626Sequence AnalysisAdd
BLAST
Propeptidei27 – 213187By similarityPRO_0000029178Add
BLAST
Chaini214 – 889676A disintegrin and metalloproteinase with thrombospondin motifs 8PRO_0000029179Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi294 ↔ 347By similarity
Disulfide bondi323 ↔ 329By similarity
Disulfide bondi341 ↔ 424By similarity
Glycosylationi344 – 3441N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi379 ↔ 408By similarity
Glycosylationi400 – 4001N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi452 ↔ 477By similarity
Disulfide bondi463 ↔ 486By similarity
Glycosylationi465 – 4651N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi472 ↔ 507By similarity
Glycosylationi490 – 4901N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi501 ↔ 512By similarity
Disulfide bondi538 ↔ 575By similarity
Disulfide bondi542 ↔ 580By similarity
Disulfide bondi553 ↔ 565By similarity
Glycosylationi599 – 5991N-linked (GlcNAc...)Sequence Analysis

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

PaxDbiQ9UP79.
PRIDEiQ9UP79.

PTM databases

PhosphoSiteiQ9UP79.

Expressioni

Tissue specificityi

Highly expressed in adult and fetal lung, lower expression in brain, placenta, heart, stomach and fetal brain and kidney.

Gene expression databases

BgeeiQ9UP79.
CleanExiHS_ADAMTS8.
GenevestigatoriQ9UP79.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000257359.

Structurei

3D structure databases

SMRiQ9UP79. Positions 219-809.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini219 – 429211Peptidase M12BPROSITE-ProRule annotationAdd
BLAST
Domaini438 – 52588DisintegrinAdd
BLAST
Domaini526 – 58156TSP type-1 1PROSITE-ProRule annotationAdd
BLAST
Domaini833 – 88856TSP type-1 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni690 – 831142SpacerAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi201 – 2044Poly-Pro
Compositional biasi583 – 689107Cys-richAdd
BLAST

Domaini

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

Sequence similaritiesi

Contains 1 disintegrin domain.Curated
Contains 1 peptidase M12B domain.PROSITE-ProRule annotation
Contains 2 TSP type-1 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG285519.
GeneTreeiENSGT00760000118880.
HOGENOMiHOG000004799.
HOVERGENiHBG004313.
InParanoidiQ9UP79.
KOiK08623.
OMAiYELDQQC.
OrthoDBiEOG7WDN1M.
PhylomeDBiQ9UP79.
TreeFamiTF331949.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR010294. ADAM_spacer1.
IPR024079. MetalloPept_cat_dom.
IPR013277. Pept_M12B_ADAM-TS8.
IPR001590. Peptidase_M12B.
IPR013273. Peptidase_M12B_ADAM-TS.
IPR002870. Peptidase_M12B_N.
IPR000884. Thrombospondin_1_rpt.
[Graphical view]
PfamiPF05986. ADAM_spacer1. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 2 hits.
[Graphical view]
PRINTSiPR01861. ADAMTS8.
PR01857. ADAMTSFAMILY.
SMARTiSM00209. TSP1. 2 hits.
[Graphical view]
SUPFAMiSSF82895. SSF82895. 2 hits.
PROSITEiPS50215. ADAM_MEPRO. 1 hit.
PS50092. TSP1. 2 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9UP79-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLPAPAAPRW PPLLLLLLLL LPLARGAPAR PAAGGQASEL VVPTRLPGSA
60 70 80 90 100
GELALHLSAF GKGFVLRLAP DDSFLAPEFK IERLGGSGRA TGGERGLRGC
110 120 130 140 150
FFSGTVNGEP ESLAAVSLCR GLSGSFLLDG EEFTIQPQGA GGSLAQPHRL
160 170 180 190 200
QRWGPAGARP LPRGPEWEVE TGEGQRQERG DHQEDSEEES QEEEAEGASE
210 220 230 240 250
PPPPLGATSR TKRFVSEARF VETLLVADAS MAAFYGADLQ NHILTLMSVA
260 270 280 290 300
ARIYKHPSIK NSINLMVVKV LIVEDEKWGP EVSDNGGLTL RNFCNWQRRF
310 320 330 340 350
NQPSDRHPEH YDTAILLTRQ NFCGQEGLCD TLGVADIGTI CDPNKSCSVI
360 370 380 390 400
EDEGLQAAHT LAHELGHVLS MPHDDSKPCT RLFGPMGKHH VMAPLFVHLN
410 420 430 440 450
QTLPWSPCSA MYLTELLDGG HGDCLLDAPA AALPLPTGLP GRMALYQLDQ
460 470 480 490 500
QCRQIFGPDF RHCPNTSAQD VCAQLWCHTD GAEPLCHTKN GSLPWADGTP
510 520 530 540 550
CGPGHLCSEG SCLPEEEVER PKPVADGGWA PWGPWGECSR TCGGGVQFSH
560 570 580 590 600
RECKDPEPQN GGRYCLGRRA KYQSCHTEEC PPDGKSFREQ QCEKYNAYNY
610 620 630 640 650
TDMDGNLLQW VPKYAGVSPR DRCKLFCRAR GRSEFKVFEA KVIDGTLCGP
660 670 680 690 700
ETLAICVRGQ CVKAGCDHVV DSPRKLDKCG VCGGKGNSCR KVSGSLTPTN
710 720 730 740 750
YGYNDIVTIP AGATNIDVKQ RSHPGVQNDG NYLALKTADG QYLLNGNLAI
760 770 780 790 800
SAIEQDILVK GTILKYSGSI ATLERLQSFR PLPEPLTVQL LTVPGEVFPP
810 820 830 840 850
KVKYTFFVPN DVDFSMQSSK ERATTNIIQP LLHAQWVLGD WSECSSTCGA
860 870 880
GWQRRTVECR DPSGQASATC NKALKPEDAK PCESQLCPL
Length:889
Mass (Da):96,460
Last modified:November 29, 2010 - v2
Checksum:iE1767A6524BCEBAB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21L → F in AAD48081 (PubMed:10438512).Curated
Sequence conflicti11 – 122PP → LPF in AAD48081 (PubMed:10438512).Curated
Sequence conflicti194 – 1941E → R in AAF25806 (PubMed:10610729).Curated
Sequence conflicti412 – 43928YLTEL…LPTGL → FSGCHLQGWIHFKYLCKCVS ELKCDLMP in AAF25806 (PubMed:10610729).CuratedAdd
BLAST
Sequence conflicti430 – 4301A → G in AAD48081 (PubMed:10438512).Curated
Sequence conflicti525 – 5251A → V in AAD48081 (PubMed:10438512).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF060153 mRNA. Translation: AAD48081.1.
AP002986 Genomic DNA. No translation available.
AF175283 mRNA. Translation: AAF25806.1.
CCDSiCCDS41732.1.
RefSeqiNP_008968.4. NM_007037.4.
XP_006718821.1. XM_006718758.1.
UniGeneiHs.271605.

Genome annotation databases

EnsembliENST00000257359; ENSP00000257359; ENSG00000134917.
GeneIDi11095.
KEGGihsa:11095.
UCSCiuc001qgg.4. human.

Polymorphism databases

DMDMi313104077.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF060153 mRNA. Translation: AAD48081.1.
AP002986 Genomic DNA. No translation available.
AF175283 mRNA. Translation: AAF25806.1.
CCDSiCCDS41732.1.
RefSeqiNP_008968.4. NM_007037.4.
XP_006718821.1. XM_006718758.1.
UniGeneiHs.271605.

3D structure databases

SMRiQ9UP79. Positions 219-809.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000257359.

Protein family/group databases

MEROPSiM12.226.

PTM databases

PhosphoSiteiQ9UP79.

Polymorphism databases

DMDMi313104077.

Proteomic databases

PaxDbiQ9UP79.
PRIDEiQ9UP79.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000257359; ENSP00000257359; ENSG00000134917.
GeneIDi11095.
KEGGihsa:11095.
UCSCiuc001qgg.4. human.

Organism-specific databases

CTDi11095.
GeneCardsiGC11M130308.
H-InvDBHIX0026131.
HGNCiHGNC:224. ADAMTS8.
MIMi605175. gene.
neXtProtiNX_Q9UP79.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG285519.
GeneTreeiENSGT00760000118880.
HOGENOMiHOG000004799.
HOVERGENiHBG004313.
InParanoidiQ9UP79.
KOiK08623.
OMAiYELDQQC.
OrthoDBiEOG7WDN1M.
PhylomeDBiQ9UP79.
TreeFamiTF331949.

Enzyme and pathway databases

ReactomeiREACT_118572. Degradation of the extracellular matrix.
REACT_264269. O-glycosylation of TSR domain-containing proteins.

Miscellaneous databases

GeneWikiiADAMTS8.
GenomeRNAii11095.
NextBioi42178.
PROiQ9UP79.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UP79.
CleanExiHS_ADAMTS8.
GenevestigatoriQ9UP79.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR010294. ADAM_spacer1.
IPR024079. MetalloPept_cat_dom.
IPR013277. Pept_M12B_ADAM-TS8.
IPR001590. Peptidase_M12B.
IPR013273. Peptidase_M12B_ADAM-TS.
IPR002870. Peptidase_M12B_N.
IPR000884. Thrombospondin_1_rpt.
[Graphical view]
PfamiPF05986. ADAM_spacer1. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 2 hits.
[Graphical view]
PRINTSiPR01861. ADAMTS8.
PR01857. ADAMTSFAMILY.
SMARTiSM00209. TSP1. 2 hits.
[Graphical view]
SUPFAMiSSF82895. SSF82895. 2 hits.
PROSITEiPS50215. ADAM_MEPRO. 1 hit.
PS50092. TSP1. 2 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "METH-1, a human ortholog of ADAMTS-1, and METH-2 are members of a new family of proteins with angio-inhibitory activity."
    Vazquez F., Hastings G., Ortega M.-A., Lane T.F., Oikemus S., Lombardo M., Iruela-Arispe M.L.
    J. Biol. Chem. 274:23349-23357(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Lung.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "ADAM-TS8, a novel metalloprotease of the ADAM-TS family located on mouse chromosome 9 and human chromosome 11."
    Georgiadis K.E., Hirohata S., Seldin M.F., Apte S.S.
    Genomics 62:312-315(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 194-439.

Entry informationi

Entry nameiATS8_HUMAN
AccessioniPrimary (citable) accession number: Q9UP79
Secondary accession number(s): Q9NZS0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 30, 2000
Last sequence update: November 29, 2010
Last modified: March 31, 2015
This is version 139 of the entry and version 2 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 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.