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O15072

- ATS3_HUMAN

UniProt

O15072 - ATS3_HUMAN

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Protein

A disintegrin and metalloproteinase with thrombospondin motifs 3

Gene

ADAMTS3

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

Functioni

Cleaves the propeptides of type II collagen prior to fibril assembly. Does not act on types I and III collagens.

Cofactori

Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi398 – 3981Zinc; catalyticPROSITE-ProRule annotation
Active sitei399 – 3991PROSITE-ProRule annotation
Metal bindingi402 – 4021Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi408 – 4081Zinc; catalyticPROSITE-ProRule annotation

GO - Molecular functioni

  1. endopeptidase activity Source: BHF-UCL
  2. heparin binding Source: UniProtKB-KW
  3. metalloendopeptidase activity Source: UniProtKB
  4. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. collagen biosynthetic process Source: BHF-UCL
  2. collagen catabolic process Source: UniProtKB
  3. collagen fibril organization Source: UniProtKB
  4. extracellular fibril organization Source: BHF-UCL
  5. extracellular matrix organization Source: Reactome
  6. positive regulation of vascular endothelial growth factor signaling pathway Source: BHF-UCL
  7. protein processing Source: BHF-UCL
  8. vascular endothelial growth factor production Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Heparin-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_121139. Collagen biosynthesis and modifying enzymes.
REACT_200626. O-glycosylation of TSR domain-containing proteins.

Protein family/group databases

MEROPSiM12.220.

Names & Taxonomyi

Protein namesi
Recommended name:
A disintegrin and metalloproteinase with thrombospondin motifs 3 (EC:3.4.24.-)
Short name:
ADAM-TS 3
Short name:
ADAM-TS3
Short name:
ADAMTS-3
Alternative name(s):
Procollagen II N-proteinase
Short name:
PC II-NP
Procollagen II amino propeptide-processing enzyme
Gene namesi
Name:ADAMTS3
Synonyms:KIAA0366
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:219. ADAMTS3.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: Reactome
  2. extracellular space Source: BHF-UCL
  3. extracellular vesicular exosome Source: UniProt
  4. proteinaceous extracellular matrix Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24547.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Propeptidei21 – 249229By similarityPRO_0000029162Add
BLAST
Chaini250 – 1205956A disintegrin and metalloproteinase with thrombospondin motifs 3PRO_0000029163Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi83 – 831N-linked (GlcNAc...)Sequence Analysis
Glycosylationi119 – 1191N-linked (GlcNAc...)Sequence Analysis
Glycosylationi242 – 2421N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi333 ↔ 382By similarity
Glycosylationi345 – 3451N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi376 ↔ 455By similarity
Disulfide bondi415 ↔ 441By similarity
Glycosylationi475 – 4751N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi482 ↔ 507By similarity
Disulfide bondi493 ↔ 516By similarity
Disulfide bondi502 ↔ 535By similarity
Disulfide bondi529 ↔ 540By similarity
Disulfide bondi563 ↔ 600By similarity
Disulfide bondi567 ↔ 605By similarity
Disulfide bondi578 ↔ 590By similarity
Glycosylationi814 – 8141N-linked (GlcNAc...)Sequence Analysis
Glycosylationi942 – 9421N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi978 ↔ 1010By similarity
Disulfide bondi982 ↔ 1015By similarity
Disulfide bondi993 ↔ 999By 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

PaxDbiO15072.
PRIDEiO15072.

PTM databases

PhosphoSiteiO15072.

Expressioni

Tissue specificityi

Found in cartilage and skin.

Gene expression databases

BgeeiO15072.
CleanExiHS_ADAMTS3.
ExpressionAtlasiO15072. baseline and differential.
GenevestigatoriO15072.

Organism-specific databases

HPAiHPA021368.
HPA021369.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000286657.

Structurei

3D structure databases

ProteinModelPortaliO15072.
SMRiO15072. Positions 258-824.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini256 – 460205Peptidase M12BPROSITE-ProRule annotationAdd
BLAST
Domaini470 – 55081DisintegrinAdd
BLAST
Domaini551 – 60656TSP type-1 1PROSITE-ProRule annotationAdd
BLAST
Domaini845 – 90561TSP type-1 2PROSITE-ProRule annotationAdd
BLAST
Domaini906 – 96560TSP type-1 3PROSITE-ProRule annotationAdd
BLAST
Domaini966 – 101449TSP type-1 4PROSITE-ProRule annotationAdd
BLAST
Domaini1015 – 105440PLACPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni713 – 844132SpacerAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi246 – 2494Poly-Arg
Compositional biasi608 – 712105Cys-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 1 PLAC domain.PROSITE-ProRule annotation
Contains 4 TSP type-1 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG307411.
GeneTreeiENSGT00760000118880.
HOGENOMiHOG000034222.
HOVERGENiHBG004314.
InParanoidiO15072.
KOiK08619.
OMAiAEEWEHC.
OrthoDBiEOG76HQ0N.
PhylomeDBiO15072.
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.
PF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 4 hits.
[Graphical view]
PRINTSiPR01857. ADAMTSFAMILY.
SMARTiSM00209. TSP1. 4 hits.
[Graphical view]
SUPFAMiSSF82895. SSF82895. 4 hits.
PROSITEiPS50215. ADAM_MEPRO. 1 hit.
PS50900. PLAC. 1 hit.
PS50092. TSP1. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O15072-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVLLSLWLIA AALVEVRTSA DGQAGNEEMV QIDLPIKRYR EYELVTPVST
60 70 80 90 100
NLEGRYLSHT LSASHKKRSA RDVSSNPEQL FFNITAFGKD FHLRLKPNTQ
110 120 130 140 150
LVAPGAVVEW HETSLVPGNI TDPINNHQPG SATYRIRRTE PLQTNCAYVG
160 170 180 190 200
DIVDIPGTSV AISNCDGLAG MIKSDNEEYF IEPLERGKQM EEEKGRIHVV
210 220 230 240 250
YKRSAVEQAP IDMSKDFHYR ESDLEGLDDL GTVYGNIHQQ LNETMRRRRH
260 270 280 290 300
AGENDYNIEV LLGVDDSVVR FHGKEHVQNY LLTLMNIVNE IYHDESLGVH
310 320 330 340 350
INVVLVRMIM LGYAKSISLI ERGNPSRSLE NVCRWASQQQ RSDLNHSEHH
360 370 380 390 400
DHAIFLTRQD FGPAGMQGYA PVTGMCHPVR SCTLNHEDGF SSAFVVAHET
410 420 430 440 450
GHVLGMEHDG QGNRCGDETA MGSVMAPLVQ AAFHRYHWSR CSGQELKRYI
460 470 480 490 500
HSYDCLLDDP FDHDWPKLPE LPGINYSMDE QCRFDFGVGY KMCTAFRTFD
510 520 530 540 550
PCKQLWCSHP DNPYFCKTKK GPPLDGTECA AGKWCYKGHC MWKNANQQKQ
560 570 580 590 600
DGNWGSWTKF GSCSRTCGTG VRFRTRQCNN PMPINGGQDC PGVNFEYQLC
610 620 630 640 650
NTEECQKHFE DFRAQQCQQR NSHFEYQNTK HHWLPYEHPD PKKRCHLYCQ
660 670 680 690 700
SKETGDVAYM KQLVHDGTHC SYKDPYSICV RGECVKVGCD KEIGSNKVED
710 720 730 740 750
KCGVCGGDNS HCRTVKGTFT RTPRKLGYLK MFDIPPGARH VLIQEDEASP
760 770 780 790 800
HILAIKNQAT GHYILNGKGE EAKSRTFIDL GVEWDYNIED DIESLHTDGP
810 820 830 840 850
LHDPVIVLII PQENDTRSSL TYKYIIHEDS VPTINSNNVI QEELDTFEWA
860 870 880 890 900
LKSWSQCSKP CGGGFQYTKY GCRRKSDNKM VHRSFCEANK KPKPIRRMCN
910 920 930 940 950
IQECTHPLWV AEEWEHCTKT CGSSGYQLRT VRCLQPLLDG TNRSVHSKYC
960 970 980 990 1000
MGDRPESRRP CNRVPCPAQW KTGPWSECSV TCGEGTEVRQ VLCRAGDHCD
1010 1020 1030 1040 1050
GEKPESVRAC QLPPCNDEPC LGDKSIFCQM EVLARYCSIP GYNKLCCESC
1060 1070 1080 1090 1100
SKRSSTLPPP YLLEAAETHD DVISNPSDLP RSLVMPTSLV PYHSETPAKK
1110 1120 1130 1140 1150
MSLSSISSVG GPNAYAAFRP NSKPDGANLR QRSAQQAGSK TVRLVTVPSS
1160 1170 1180 1190 1200
PPTKRVHLSS ASQMAAASFF AASDSIGASS QARTSKKDGK IIDNRRPTRS

STLER
Length:1,205
Mass (Da):135,603
Last modified:January 11, 2011 - v4
Checksum:i01FA661B1C6BFF1B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti857 – 8571C → V in BAA20821. (PubMed:9205841)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti138 – 1381R → K.3 Publications
Corresponds to variant rs788908 [ dbSNP | Ensembl ].
VAR_055012
Natural varianti1074 – 10741S → P.
Corresponds to variant rs35864003 [ dbSNP | Ensembl ].
VAR_055013

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AC093790 Genomic DNA. No translation available.
AC095056 Genomic DNA. No translation available.
AC104814 Genomic DNA. No translation available.
BC130287 mRNA. Translation: AAI30288.1.
BC132735 mRNA. Translation: AAI32736.1.
AF247668 mRNA. Translation: AAK28400.1.
AB002364 mRNA. Translation: BAA20821.1.
CCDSiCCDS3553.1.
RefSeqiNP_055058.2. NM_014243.2.
UniGeneiHs.590919.

Genome annotation databases

EnsembliENST00000286657; ENSP00000286657; ENSG00000156140.
ENST00000622135; ENSP00000480055; ENSG00000156140.
GeneIDi9508.
KEGGihsa:9508.
UCSCiuc003hgk.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AC093790 Genomic DNA. No translation available.
AC095056 Genomic DNA. No translation available.
AC104814 Genomic DNA. No translation available.
BC130287 mRNA. Translation: AAI30288.1 .
BC132735 mRNA. Translation: AAI32736.1 .
AF247668 mRNA. Translation: AAK28400.1 .
AB002364 mRNA. Translation: BAA20821.1 .
CCDSi CCDS3553.1.
RefSeqi NP_055058.2. NM_014243.2.
UniGenei Hs.590919.

3D structure databases

ProteinModelPortali O15072.
SMRi O15072. Positions 258-824.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9606.ENSP00000286657.

Protein family/group databases

MEROPSi M12.220.

PTM databases

PhosphoSitei O15072.

Proteomic databases

PaxDbi O15072.
PRIDEi O15072.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000286657 ; ENSP00000286657 ; ENSG00000156140 .
ENST00000622135 ; ENSP00000480055 ; ENSG00000156140 .
GeneIDi 9508.
KEGGi hsa:9508.
UCSCi uc003hgk.2. human.

Organism-specific databases

CTDi 9508.
GeneCardsi GC04M073136.
H-InvDB HIX0004274.
HGNCi HGNC:219. ADAMTS3.
HPAi HPA021368.
HPA021369.
MIMi 605011. gene.
neXtProti NX_O15072.
PharmGKBi PA24547.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG307411.
GeneTreei ENSGT00760000118880.
HOGENOMi HOG000034222.
HOVERGENi HBG004314.
InParanoidi O15072.
KOi K08619.
OMAi AEEWEHC.
OrthoDBi EOG76HQ0N.
PhylomeDBi O15072.
TreeFami TF313537.

Enzyme and pathway databases

Reactomei REACT_121139. Collagen biosynthesis and modifying enzymes.
REACT_200626. O-glycosylation of TSR domain-containing proteins.

Miscellaneous databases

GeneWikii ADAMTS3.
GenomeRNAii 9508.
NextBioi 35628.
PROi O15072.
SOURCEi Search...

Gene expression databases

Bgeei O15072.
CleanExi HS_ADAMTS3.
ExpressionAtlasi O15072. baseline and differential.
Genevestigatori O15072.

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.
PF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 4 hits.
[Graphical view ]
PRINTSi PR01857. ADAMTSFAMILY.
SMARTi SM00209. TSP1. 4 hits.
[Graphical view ]
SUPFAMi SSF82895. SSF82895. 4 hits.
PROSITEi PS50215. ADAM_MEPRO. 1 hit.
PS50900. PLAC. 1 hit.
PS50092. TSP1. 4 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT LYS-138.
  3. "Procollagen II amino propeptide processing by ADAMTS-3. Insights on dermatosparaxis."
    Fernandes R.J., Hirohata S., Engle J.M., Colige A., Cohn D.H., Eyre D.R., Apte S.S.
    J. Biol. Chem. 276:31502-31509(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-227, VARIANT LYS-138.
  4. "Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
    Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 4:141-150(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-1205, VARIANT LYS-138.
    Tissue: Brain.

Entry informationi

Entry nameiATS3_HUMAN
AccessioniPrimary (citable) accession number: O15072
Secondary accession number(s): A1L3U9, Q9BXZ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: January 11, 2011
Last modified: October 29, 2014
This is version 147 of the entry and version 4 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

Caution

Has sometimes been referred to as ADAMTS4.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: 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