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Reviewed, UniProtKB/Swiss-Prot P59510 (ATS20_HUMAN)

Last modified November 24, 2009. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    A disintegrin and metalloproteinase with thrombospondin motifs 20
      Short name=ADAMTS-20
      Short name=ADAM-TS 20
      Short name=ADAM-TS20
    EC=3.4.24.-
Gene names
Name: ADAMTS20
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1910 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

May play a role in tissue-remodeling process occurring in both normal and pathological conditions.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subcellular location

Secretedextracellular spaceextracellular matrix By similarity.

Tissue specificity

Very sparingly expressed, although is detected at low levels in testis, prostate, ovary, heart, placenta, lung and pancreas. Overexpressed in several brain, colon and breast carcinomas.

Post-translational modification

The precursor is cleaved by a furin endopeptidase By similarity.

Sequence similarities

Contains 1 disintegrin domain.

Contains 1 GON domain.

Contains 1 peptidase M12B domain.

Contains 15 TSP type-1 domains.

Ontologies

Keywords
   Cellular componentExtracellular matrix
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
Signal
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
Zymogen
   Technical termComplete proteome
Gene Ontology (GO)
   Cellular componentproteinaceous extracellular matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionzinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P59510-1)

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.
Isoform 2 (identifier: P59510-2)

The sequence of this isoform differs from the canonical sequence as follows:
     683-693: THDICVQGQCM → SYNIDCNCVLK
     1429-1504: CSASCGKGRK...QRDVYCRLKG → EDLKVKLLPQ...GDLKYYKNSL
     1505-1910: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Propeptide22 – 253232 By similarity
PRO_0000029206
Chain254 – 19101657A disintegrin and metalloproteinase with thrombospondin motifs 20
PRO_0000029207

Regions

Domain259 – 467209Peptidase M12B
Domain468 – 55588Disintegrin
Domain556 – 61156TSP type-1 1
Domain846 – 90459TSP type-1 2
Domain905 – 96157TSP type-1 3
Domain966 – 102358TSP type-1 4
Domain1024 – 107350TSP type-1 5
Domain1076 – 113560TSP type-1 6
Domain1152 – 120655TSP type-1 7
Domain1207 – 126458TSP type-1 8
Domain1304 – 135653TSP type-1 9
Domain1358 – 141659TSP type-1 10
Domain1417 – 147559TSP type-1 11
Domain1476 – 153156TSP type-1 12
Domain1535 – 158854TSP type-1 13
Domain1589 – 165264TSP type-1 14
Domain1654 – 171057TSP type-1 15
Domain1711 – 1910200GON
Region724 – 846123Spacer
Compositional bias612 – 723112Cys-rich

Sites

Active site4041 By similarity
Metal binding4031Zinc; catalytic By similarity
Metal binding4071Zinc; catalytic By similarity
Metal binding4131Zinc; catalytic By similarity

Amino acid modifications

Glycosylation921N-linked (GlcNAc...) Potential
Glycosylation1911N-linked (GlcNAc...) Potential
Glycosylation4451N-linked (GlcNAc...) Potential
Glycosylation7021N-linked (GlcNAc...) Potential
Glycosylation7171N-linked (GlcNAc...) Potential
Glycosylation7281N-linked (GlcNAc...) Potential
Glycosylation8091N-linked (GlcNAc...) Potential
Glycosylation8701N-linked (GlcNAc...) Potential
Glycosylation10611N-linked (GlcNAc...) Potential
Glycosylation14561N-linked (GlcNAc...) Potential
Glycosylation15421N-linked (GlcNAc...) Potential
Glycosylation15721N-linked (GlcNAc...) Potential
Glycosylation17631N-linked (GlcNAc...) Potential
Glycosylation17811N-linked (GlcNAc...) Potential
Glycosylation18521N-linked (GlcNAc...) Potential
Disulfide bond381 ↔ 462 By similarity
Disulfide bond419 ↔ 446 By similarity
Disulfide bond568 ↔ 605 By similarity
Disulfide bond572 ↔ 610 By similarity
Disulfide bond583 ↔ 595 By similarity

Natural variations

Alternative sequence683 – 69311THDICVQGQCM → SYNIDCNCVLK in isoform 2.
VSP_007106
Alternative sequence1429 – 150476CSASC…CRLKG → EDLKVKLLPQRTIILWELMK NIFCHGKHSHMYLINVVTDH LLYPRHCDPETIETYFLSLW SLQFTWGDLKYYKNSL in isoform 2.
VSP_007107
Alternative sequence1505 – 1910406Missing in isoform 2.
VSP_007108
Natural variant8761K → M: dbSNP rs7302446.
VAR_057088
Natural variant10001R → H: dbSNP rs7297737.
VAR_057089
Natural variant12731S → F: dbSNP rs7310011.
VAR_057090

Experimental info

Sequence conflict1521T → V in CAD56159. Ref.2
Sequence conflict1521T → V in CAD56160. Ref.2
Sequence conflict3601E → Y in CAD56159. Ref.2
Sequence conflict3601E → Y in CAD56160. Ref.2
Sequence conflict3711M → T in AAO15766. Ref.1
Sequence conflict4561D → E in CAD56159. Ref.2
Sequence conflict4561D → E in CAD56160. Ref.2
Sequence conflict6481I → V in CAD56159. Ref.2
Sequence conflict6481I → V in CAD56160. Ref.2
Sequence conflict792 – 7932Missing in CAD56159. Ref.2
Sequence conflict792 – 7932Missing in CAD56160. Ref.2
Sequence conflict818 – 8214ILIE → LILQ in AAO15766. Ref.1
Sequence conflict908 – 9125WHVIG → GMLLAK in AAO15766. Ref.1
Sequence conflict13151S → Q in CAD56159. Ref.2
Sequence conflict13151S → Q in CAD56160. Ref.2
Sequence conflict13271R → T in AAO15766. Ref.1
Sequence conflict18161T → A in CAD56159. Ref.2
Sequence conflict18811E → Q in CAD56159. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 16, 2008. Version 2.
Checksum: D7FFCB0D56F4B6D9

FASTA1,910214,721
        10         20         30         40         50         60 
MWVAKWLTGL LYHLSLFITR SWEVDFHPRQ EALVRTLTSY EVVIPERVNE FGEVFPQSHH 

        70         80         90        100        110        120 
FSRQKRSSEA LEPMPFRTHY RFTAYGQLFQ LNLTADASFL AAGYTEVHLG TPERGAWESD 

       130        140        150        160        170        180 
AGPSDLRHCF YRGQVNSQED YKAVVSLCGG LTGTFKGQNG EYFLEPIMKA DGNEYEDGHN 

       190        200        210        220        230        240 
KPHLIYRQDL NNSFLQTLKY CSVSESQIKE TSLPFHTYSN MNEDLNVMKE RVLGHTSKNV 

       250        260        270        280        290        300 
PLKDERRHSR KKRLISYPRY IEIMVTADAK VVSAHGSNLQ NYILTLMSIV ATIYKDPSIG 

       310        320        330        340        350        360 
NLIHIVVVKL VMIHREEEGP VINFDGATTL KNFCSWQQTQ NDLDDVHPSH HDTAVLITRE 

       370        380        390        400        410        420 
DICSSKEKCN MLGLSYLGTI CDPLQSCFIN EEKGLISAFT IAHELGHTLG VQHDDNPRCK 

       430        440        450        460        470        480 
EMKVTKYHVM APALSFHMSP WSWSNCSRKY VTEFLDTGYG ECLLDKPDEE IYNLPSELPG 

       490        500        510        520        530        540 
SRYDGNKQCE LAFGPGSQMC PHINICMHLW CTSTEKLHKG CFTQHVPPAD GTDCGPGMHC 

       550        560        570        580        590        600 
RHGLCVNKET ETRPVNGEWG PWEPYSSCSR TCGGGIESAT RRCNRPEPRN GGNYCVGRRM 

       610        620        630        640        650        660 
KFRSCNTDSC PKGTQDFREK QCSDFNGKHL DISGIPSNVR WLPRYSGIGT KDRCKLYCQV 

       670        680        690        700        710        720 
AGTNYFYLLK DMVEDGTPCG TETHDICVQG QCMAAGCDHV LNSSAKIDKC GVCGGDNSSC 

       730        740        750        760        770        780 
KTITGVFNSS HYGYNVVVKI PAGATNVDIR QYSYSGQPDD SYLALSDAEG NFLFNGNFLL 

       790        800        810        820        830        840 
STSKKEINVQ GTRTVIEYSG SNNAVERINS TNRQEKEILI EVLCVGNLYN PDVHYSFNIP 

       850        860        870        880        890        900 
LEERSDMFTW DPYGPWEGCT KMCQGLQRRN ITCIHKSDHS VVSDKECDHL PLPSFVTQSC 

       910        920        930        940        950        960 
NTDCELRWHV IGKSECSSQC GQGYRTLDIH CMKYSIHEGQ TVQVDDHYCG DQLKPPTQEL 

       970        980        990       1000       1010       1020 
CHGNCVFTRW HYSEWSQCSR SCGGGERSRE SYCMNNFGHR LADNECQELS RVTRENCNEF 

      1030       1040       1050       1060       1070       1080 
SCPSWAASEW SECLVTCGKG TKQRQVWCQL NVDHLSDGFC NSSTKPESLS PCELHTCASW 

      1090       1100       1110       1120       1130       1140 
QVGPWGPCTT TCGHGYQMRD VKCVNELASA VLEDTECHEA SRPSDRQSCV LTPCSFISKL 

      1150       1160       1170       1180       1190       1200 
ETALLPTVLI KKMAQWRHGS WTPCSVSCGR GTQARYVSCR DALDRIADES YCAHLPRPAE 

      1210       1220       1230       1240       1250       1260 
IWDCFTPCGE WQAGDWSPCS ASCGHGKTTR QVLCMNYHQP IDENYCDPEV RPLMEQECSL 

      1270       1280       1290       1300       1310       1320 
AACPPAHSHF PSSPVQPSYY LSTNLPLTQK LEDNENQVVH PSVRGNQWRT GPWGSCSSSC 

      1330       1340       1350       1360       1370       1380 
SGGLQHRAVV CQDENGQSAS YCDAASKPPE LQQCGPGPCP QWNYGNWGEC SQTCGGGIKS 

      1390       1400       1410       1420       1430       1440 
RLVICQFPNG QILEDHNCEI VNKPPSVIQC HMHACPADVS WHQEPWTSCS ASCGKGRKYR 

      1450       1460       1470       1480       1490       1500 
EVFCIDQFQR KLEDTNCSQV QKPPTHKACR SVRCPSWKAN SWNECSVTCG SGVQQRDVYC 

      1510       1520       1530       1540       1550       1560 
RLKGVGQVVE EMCDQSTRPC SQRRCWSQDC VQHKGMERGR LNCSTSCERK DSHQRMECTD 

      1570       1580       1590       1600       1610       1620 
NQIRQVNEIV YNSSTISLTS KNCRNPPCNY IVVTADSSQC ANNCGFSYRQ RITYCTEIPS 

      1630       1640       1650       1660       1670       1680 
TKKHKLHRLR PIVYQECPVV PSSQVYQCIN SCLHLATWKV GKWSKCSVTC GIGIMKRQVK 

      1690       1700       1710       1720       1730       1740 
CITKHGLSSD LCLNHLKPGA QKKCYANDCK SFTTCKEIQV KNHIRKDGDY YLNIKGRIIK 

      1750       1760       1770       1780       1790       1800 
IYCADMYLEN PKEYLTLVQG EENFSEVYGF RLKNPYQCPF NGSRREDCEC DNGHLAAGYT 

      1810       1820       1830       1840       1850       1860 
VFSKIRIDLT SMQIKTTDLL FSKTIFGNAV PFATAGDCYS AFRCPQGQFS INLSGTGMKI 

      1870       1880       1890       1900       1910 
SSTAKWLTQG SYTSVSIRRS EDGTRFFGKC GGYCGKCLPH MTTGLPIQVI 

« Hide

Isoform 2.

Checksum: 2F9D75248EE885DF
Show »

FASTA1,504169,506

References

« Hide 'large scale' references
[1]"Characterization of ADAMTS-9 and ADAMTS-20 as a distinct ADAMTS subfamily related to Caenorhabditis elegans GON-1."
Somerville R.P., Longpre J.-M., Jungers K.A., Engle J.M., Ross M., Evanko S., Wight T.N., Leduc R., Apte S.S.
J. Biol. Chem. 278:9503-9513(2003) [PubMed: 12514189] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Identification and characterization of ADAMTS-20 defines a novel subfamily of metalloproteinases-disintegrins with multiple thrombospondin-1 repeats and a unique GON domain."
Llamazares M., Cal S., Quesada V., Lopez-Otin C.
J. Biol. Chem. 278:13382-13389(2003) [PubMed: 12562771] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
Tissue: Liver.
[3]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed: 16541075] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AF488804 mRNA. Translation: AAO15766.1.
AJ515153 mRNA. Translation: CAD56159.3.
AJ515154 mRNA. Translation: CAD56160.2.
AC107018 Genomic DNA. No translation available.
IPIIPI00414321.
IPI00874153.
RefSeqNP_079279.3.
UniGeneHs.287554

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGP59510.

Protein family/group databases

MEROPSM12.246.

Proteomic databases

PRIDEP59510.

Genome annotation databases

EnsemblENST00000389420; ENSP00000374071; ENSG00000173157; Homo sapiens. [Genome view]
GeneID80070.
KEGGhsa:80070.

Organism-specific databases

CTD80070.
GeneCardsGC12M042034.
H-InvDBHIX0010556.
HGNCHGNC:17178. ADAMTS20.
MIM611681. gene.
PharmGKBPA134901626.
GenAtlasSearch...

Phylogenomic databases

HOVERGENP59510.
OMALTRWHYS
OrthoDBEOG9G1Q20

Gene expression databases

ArrayExpressP59510.
BgeeP59510.
CleanExHS_ADAMTS20.
GenevestigatorP59510.
GermOnlineENSG00000173157. Homo sapiens.

Family and domain databases

InterProIPR010294. ADAM_spacer1.
IPR012314. Pept_M12B_GON-ADAMTSs.
IPR001590. Peptidase_M12B.
IPR013273. Peptidase_M12B_ADAM-TS.
IPR002870. Peptidase_M12B_N.
IPR000884. Thrombospondin_1_rpt.
[Graphical view]
PfamPF05986. ADAM_spacer1. 1 hit.
PF08685. GON. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 11 hits.
[Graphical view]
PRINTSPR01857. ADAMTSFAMILY.
SMARTSM00209. TSP1. 13 hits.
[Graphical view]
PROSITEPS50215. ADAM_MEPRO. 1 hit.
PS00427. DISINTEGRIN_1. False negative.
PS50214. DISINTEGRIN_2. False negative.
PS51046. GON. 1 hit.
PS50092. TSP1. 12 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio70275.
SOURCESearch...

Entry information

Entry nameATS20_HUMAN
AccessionPrimary (citable) accession number: P59510
Secondary accession number(s): A6NNC9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2003
Last sequence update: December 16, 2008
Last modified: November 24, 2009
This is version 72 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents