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O15072 (ATS3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 141. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
A disintegrin and metalloproteinase with thrombospondin motifs 3

Short name=ADAM-TS 3
Short name=ADAM-TS3
Short name=ADAMTS-3
EC=3.4.24.-
Alternative name(s):
Procollagen II N-proteinase
Short name=PC II-NP
Procollagen II amino propeptide-processing enzyme
Gene names
Name:ADAMTS3
Synonyms:KIAA0366
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1205 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subcellular location

Secretedextracellular spaceextracellular matrix By similarity.

Tissue specificity

Found in cartilage and skin.

Domain

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

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 4 TSP type-1 domains.

Caution

Has sometimes been referred to as ADAMTS4.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Propeptide21 – 249229 By similarity
PRO_0000029162
Chain250 – 1205956A disintegrin and metalloproteinase with thrombospondin motifs 3
PRO_0000029163

Regions

Domain256 – 460205Peptidase M12B
Domain470 – 55081Disintegrin
Domain551 – 60656TSP type-1 1
Domain845 – 90561TSP type-1 2
Domain906 – 96560TSP type-1 3
Domain966 – 101449TSP type-1 4
Domain1015 – 105440PLAC
Region713 – 844132Spacer
Compositional bias246 – 2494Poly-Arg
Compositional bias608 – 712105Cys-rich

Sites

Active site3991 By similarity
Metal binding3981Zinc; catalytic By similarity
Metal binding4021Zinc; catalytic By similarity
Metal binding4081Zinc; catalytic By similarity

Amino acid modifications

Glycosylation831N-linked (GlcNAc...) Potential
Glycosylation1191N-linked (GlcNAc...) Potential
Glycosylation2421N-linked (GlcNAc...) Potential
Glycosylation3451N-linked (GlcNAc...) Potential
Glycosylation4751N-linked (GlcNAc...) Potential
Glycosylation8141N-linked (GlcNAc...) Potential
Glycosylation9421N-linked (GlcNAc...) Potential
Disulfide bond333 ↔ 382 By similarity
Disulfide bond376 ↔ 455 By similarity
Disulfide bond415 ↔ 441 By similarity
Disulfide bond482 ↔ 507 By similarity
Disulfide bond493 ↔ 516 By similarity
Disulfide bond502 ↔ 535 By similarity
Disulfide bond529 ↔ 540 By similarity
Disulfide bond563 ↔ 600 By similarity
Disulfide bond567 ↔ 605 By similarity
Disulfide bond578 ↔ 590 By similarity
Disulfide bond978 ↔ 1010 By similarity
Disulfide bond982 ↔ 1015 By similarity
Disulfide bond993 ↔ 999 By similarity

Natural variations

Natural variant1381R → K. Ref.2 Ref.3 Ref.4
Corresponds to variant rs788908 [ dbSNP | Ensembl ].
VAR_055012
Natural variant10741S → P.
Corresponds to variant rs35864003 [ dbSNP | Ensembl ].
VAR_055013

Experimental info

Sequence conflict8571C → V in BAA20821. Ref.4

Sequences

Sequence LengthMass (Da)Tools
O15072 [UniParc].

Last modified January 11, 2011. Version 4.
Checksum: 01FA661B1C6BFF1B

FASTA1,205135,603
        10         20         30         40         50         60 
MVLLSLWLIA AALVEVRTSA DGQAGNEEMV QIDLPIKRYR EYELVTPVST NLEGRYLSHT 

        70         80         90        100        110        120 
LSASHKKRSA RDVSSNPEQL FFNITAFGKD FHLRLKPNTQ LVAPGAVVEW HETSLVPGNI 

       130        140        150        160        170        180 
TDPINNHQPG SATYRIRRTE PLQTNCAYVG DIVDIPGTSV AISNCDGLAG MIKSDNEEYF 

       190        200        210        220        230        240 
IEPLERGKQM EEEKGRIHVV YKRSAVEQAP IDMSKDFHYR ESDLEGLDDL GTVYGNIHQQ 

       250        260        270        280        290        300 
LNETMRRRRH AGENDYNIEV LLGVDDSVVR FHGKEHVQNY LLTLMNIVNE IYHDESLGVH 

       310        320        330        340        350        360 
INVVLVRMIM LGYAKSISLI ERGNPSRSLE NVCRWASQQQ RSDLNHSEHH DHAIFLTRQD 

       370        380        390        400        410        420 
FGPAGMQGYA PVTGMCHPVR SCTLNHEDGF SSAFVVAHET GHVLGMEHDG QGNRCGDETA 

       430        440        450        460        470        480 
MGSVMAPLVQ AAFHRYHWSR CSGQELKRYI HSYDCLLDDP FDHDWPKLPE LPGINYSMDE 

       490        500        510        520        530        540 
QCRFDFGVGY KMCTAFRTFD PCKQLWCSHP DNPYFCKTKK GPPLDGTECA AGKWCYKGHC 

       550        560        570        580        590        600 
MWKNANQQKQ DGNWGSWTKF GSCSRTCGTG VRFRTRQCNN PMPINGGQDC PGVNFEYQLC 

       610        620        630        640        650        660 
NTEECQKHFE DFRAQQCQQR NSHFEYQNTK HHWLPYEHPD PKKRCHLYCQ SKETGDVAYM 

       670        680        690        700        710        720 
KQLVHDGTHC SYKDPYSICV RGECVKVGCD KEIGSNKVED KCGVCGGDNS HCRTVKGTFT 

       730        740        750        760        770        780 
RTPRKLGYLK MFDIPPGARH VLIQEDEASP HILAIKNQAT GHYILNGKGE EAKSRTFIDL 

       790        800        810        820        830        840 
GVEWDYNIED DIESLHTDGP LHDPVIVLII PQENDTRSSL TYKYIIHEDS VPTINSNNVI 

       850        860        870        880        890        900 
QEELDTFEWA LKSWSQCSKP CGGGFQYTKY GCRRKSDNKM VHRSFCEANK KPKPIRRMCN 

       910        920        930        940        950        960 
IQECTHPLWV AEEWEHCTKT CGSSGYQLRT VRCLQPLLDG TNRSVHSKYC MGDRPESRRP 

       970        980        990       1000       1010       1020 
CNRVPCPAQW KTGPWSECSV TCGEGTEVRQ VLCRAGDHCD GEKPESVRAC QLPPCNDEPC 

      1030       1040       1050       1060       1070       1080 
LGDKSIFCQM EVLARYCSIP GYNKLCCESC SKRSSTLPPP YLLEAAETHD DVISNPSDLP 

      1090       1100       1110       1120       1130       1140 
RSLVMPTSLV PYHSETPAKK MSLSSISSVG GPNAYAAFRP NSKPDGANLR QRSAQQAGSK 

      1150       1160       1170       1180       1190       1200 
TVRLVTVPSS PPTKRVHLSS ASQMAAASFF AASDSIGASS QARTSKKDGK IIDNRRPTRS 


STLER 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_055058.2. NM_014243.2.
UniGeneHs.590919.

3D structure databases

ProteinModelPortalO15072.
SMRO15072. Positions 258-824, 843-1016.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000286657.

Protein family/group databases

MEROPSM12.220.

PTM databases

PhosphoSiteO15072.

Proteomic databases

PaxDbO15072.
PRIDEO15072.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000286657; ENSP00000286657; ENSG00000156140.
GeneID9508.
KEGGhsa:9508.
UCSCuc003hgk.2. human.

Organism-specific databases

CTD9508.
GeneCardsGC04M073136.
H-InvDBHIX0004274.
HGNCHGNC:219. ADAMTS3.
HPAHPA021368.
HPA021369.
MIM605011. gene.
neXtProtNX_O15072.
PharmGKBPA24547.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG307411.
HOGENOMHOG000034222.
HOVERGENHBG004314.
InParanoidO15072.
KOK08619.
OMAAEEWEHC.
OrthoDBEOG76HQ0N.
PhylomeDBO15072.
TreeFamTF313537.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressO15072.
BgeeO15072.
CleanExHS_ADAMTS3.
GenevestigatorO15072.

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.
PF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 4 hits.
[Graphical view]
PRINTSPR01857. ADAMTSFAMILY.
SMARTSM00209. TSP1. 4 hits.
[Graphical view]
SUPFAMSSF82895. SSF82895. 4 hits.
PROSITEPS50215. ADAM_MEPRO. 1 hit.
PS50900. PLAC. 1 hit.
PS50092. TSP1. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiADAMTS3.
GenomeRNAi9508.
NextBio35628.
PROO15072.
SOURCESearch...

Entry information

Entry nameATS3_HUMAN
AccessionPrimary (citable) accession number: O15072
Secondary accession number(s): A1L3U9, Q9BXZ8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: January 11, 2011
Last modified: April 16, 2014
This is version 141 of the entry and version 4 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 4

Human chromosome 4: entries, gene names and cross-references to MIM