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Q811B3 (ATS12_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
A disintegrin and metalloproteinase with thrombospondin motifs 12

Short name=ADAM-TS 12
Short name=ADAM-TS12
Short name=ADAMTS-12
EC=3.4.24.-
Gene names
Name:Adamts12
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1600 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Metalloprotease that plays a role in the degradation of COMP By similarity. Cleaves also alpha-2 macroglobulin and aggregan. Has anti-tumorigenic properties By similarity.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Enzyme regulation

Inhibited by alpha-2 macroglobulin By similarity.

Subunit structure

Interacts with COMP By similarity.

Subcellular location

Secretedextracellular spaceextracellular matrix By similarity.

Domain

The C-terminal four TSP1-like repeats are necessary and sufficient for binding COMP By similarity.

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.

Post-translational modification

The precursor is cleaved by a furin endopeptidase By similarity.

Subjected to an intracellular maturation process yielding a 120 kDa N-terminal fragment containing the metalloproteinase, disintegrin, one TSP type-1 and the Cys-rich domains and a 83 kDa C-terminal fragment containing the spacer 2 and four TSP type-1 domains 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 8 TSP type-1 domains.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q811B3-1)

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: Q811B3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     167-171: GFFHL → VLITL
     172-1600: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Propeptide26 – 244219 By similarity
PRO_0000029188
Chain245 – 16001356A disintegrin and metalloproteinase with thrombospondin motifs 12
PRO_0000029189

Regions

Domain250 – 460211Peptidase M12B
Domain469 – 54880Disintegrin
Domain546 – 60156TSP type-1 1
Domain827 – 88761TSP type-1 2
Domain891 – 94757TSP type-1 3
Domain948 – 100154TSP type-1 4
Domain1318 – 137154TSP type-1 5
Domain1373 – 142856TSP type-1 6
Domain1429 – 147749TSP type-1 7
Domain1478 – 153861TSP type-1 8
Domain1541 – 158141PLAC
Region705 – 831127Spacer 1
Region1001 – 1321321Spacer 2
Motif210 – 2178Cysteine switch By similarity
Compositional bias306 – 3094Poly-Glu
Compositional bias601 – 704104Cys-rich

Sites

Active site3971 By similarity
Metal binding2121Zinc; in inhibited form By similarity
Metal binding3961Zinc; catalytic By similarity
Metal binding4001Zinc; catalytic By similarity
Metal binding4061Zinc; catalytic By similarity

Amino acid modifications

Glycosylation1051N-linked (GlcNAc...) Potential
Disulfide bond326 ↔ 380 By similarity
Disulfide bond355 ↔ 362 By similarity
Disulfide bond374 ↔ 455 By similarity
Disulfide bond413 ↔ 439 By similarity
Disulfide bond482 ↔ 505 By similarity
Disulfide bond493 ↔ 511 By similarity
Disulfide bond500 ↔ 530 By similarity
Disulfide bond524 ↔ 535 By similarity
Disulfide bond558 ↔ 595 By similarity
Disulfide bond562 ↔ 600 By similarity
Disulfide bond573 ↔ 585 By similarity

Natural variations

Alternative sequence167 – 1715GFFHL → VLITL in isoform 2.
VSP_013149
Alternative sequence172 – 16001429Missing in isoform 2.
VSP_013150

Experimental info

Sequence conflict10101N → H in CAD60967. Ref.1

Sequences

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

Last modified July 27, 2011. Version 2.
Checksum: F125753A42D4AD04

FASTA1,600177,769
        10         20         30         40         50         60 
MPCARGSWLA KLSIVAQLIN FGAFCHGRQT QPWPVRFPDP RQEHFIKSLP EYHIVSPVQV 

        70         80         90        100        110        120 
DAGGHVLSYG LHHPVTSSRK KRAAGGSGDQ LYYRISHEEK DLFFNLTVNW EFLSNGYVVE 

       130        140        150        160        170        180 
KRYGNLSHVK MVASSGQPCH LRGTVLQQGT TVGIGTAALS ACQGLTGFFH LPHGDFFIEP 

       190        200        210        220        230        240 
VKKHPLTEEG SYPHVVYRRQ SIRAPETKEP ICGLKDSLDN SVKQELQREK WERKTLRSRS 

       250        260        270        280        290        300 
LSRRSISKER WVETLVVADT KTVEYHGSEN VESYILTIMN MVTGLFHSPS IGNLVHIVVV 

       310        320        330        340        350        360 
RLILLEEEEQ GLKIVHHAEK TLSSFCKWQK SINPKSDLNP VHHDVAVLIT RKDICAGVNR 

       370        380        390        400        410        420 
PCETLGLSQL SGMCQPHRSC NINEDSGLPL AFTIAHELGH SFGIQHDGKE NDCEPVGRHP 

       430        440        450        460        470        480 
YIMSQQIQYD PTPLTWSKCS KEYITRFLDR GRGFCLDDIP SKKGLKSNVI APGVIYDVHH 

       490        500        510        520        530        540 
QCQLQYGPNA TFCQEVENVC QTLWCSVKGF CRSKLDAAAD GTRCGEKKWC MAGKCITVGK 

       550        560        570        580        590        600 
KPESIPGGWG RWSPWSHCSR TCGAGAQSAE RLCNNPEPKF GGKYCTGERK RYRLCNVHPC 

       610        620        630        640        650        660 
RSDTPTFRQM QCSEFDTVPY KNQFYRWFPV FNAAHPCELY CRPIDEQFSE RMLEAVIDGT 

       670        680        690        700        710        720 
PCFEGGNSRN VCINGICKRV GCDYEIDSNA TEDRCGVCLG DGSACQTVKK LFRQKEGSGY 

       730        740        750        760        770        780 
VDIGLIPKGA RDIRVMEIKA AGNFLAIRSE DPEKYYLNGG FIIQWNGNYK LAGTVFQYDR 

       790        800        810        820        830        840 
KGDLEKLIAP GPTNESVWLQ LLFQVTNPGI KYEYTVRKDG LDNDVEKLLY FWQFGRWTEC 

       850        860        870        880        890        900 
SVTCGTGIRR QAAHCVKKGH GIVKTTFCNP ETQPSVRQKK CHEKDCPPRW WAGEWEACST 

       910        920        930        940        950        960 
TCGPYGEKKR TVLCIQTMGS DEQALPATDC QHLLKPKALV SCNRDILCPS DWTVGNWSEC 

       970        980        990       1000       1010       1020 
SVSCGGGVRI RSVTCAKNLN EPCDKTRKPN SRALCGLQQC PFSRRVLKPN KDIAPSGKNQ 

      1030       1040       1050       1060       1070       1080 
STAEHDPFKP IPAPTSRPTP LSTPTVPESM STSTPTINSL GSTIASQEDA NGMGWQNNST 

      1090       1100       1110       1120       1130       1140 
QAEEGSHFPT SSGSTSQVPV TSWSLSIQPD DENVSSSAIG PTSEGDFWAT TTSDSGLSSS 

      1150       1160       1170       1180       1190       1200 
DAMTWQVTPF YSTMTTDPEV EIHSGSGEDS DQPLNKDKSN SVIWNKIGVP EHDAPMETDA 

      1210       1220       1230       1240       1250       1260 
ELPLGPPPTS YMGEEPSWPP FSTKMEGSLP AWSFKNETPR DDGMIAEKSR KIPLPLAGDH 

      1270       1280       1290       1300       1310       1320 
HPATSEKLEN HDKLALPNTT NPTQGFGPVL TEEDASNLIA EGFLLNASDY KHLMKDHSPA 

      1330       1340       1350       1360       1370       1380 
YWIVGNWSKC STTCGLGAYW RSVECSSGVD ADCTTIQRPD PAKKCHLRPC AGWRVGNWSK 

      1390       1400       1410       1420       1430       1440 
CSRNCSGGFK IREVQCMDSL DHHRSLRPFH CQFLAGAPPP LSMSCNLEPC GEWQVEPWSQ 

      1450       1460       1470       1480       1490       1500 
CSRSCGGGVQ ERGVSCPGGL CDWTKRPATT VPCNRHLCCH WATGNWELCN TSCGGGSQKR 

      1510       1520       1530       1540       1550       1560 
TIHCIPSENS TTEDQDQCLC DHQVKPPEFQ TCNQQACRKS ADLTCLKDRL SISFCQTLKS 

      1570       1580       1590       1600 
MRKCSVPSVR AQCCLSCPQA PSIHTQRQRK QQLLQNHDML 

« Hide

Isoform 2 [UniParc].

Checksum: 6846F3A8C242B832
Show »

FASTA17118,843

References

« Hide 'large scale' references
[1]"Mouse ADAMTS-12."
Cal S., Lopez-Otin C.
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1009 (ISOFORM 1).
Strain: C57BL/6J.
Tissue: Embryonic head and Oviduct.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ537452 mRNA. Translation: CAD60967.1.
AK048612 mRNA. Translation: BAC33391.1.
AK054015 mRNA. Translation: BAC35621.1.
AC102219 Genomic DNA. No translation available.
AC156609 Genomic DNA. No translation available.
AC159963 Genomic DNA. No translation available.
CCDSCCDS27384.1. [Q811B3-1]
RefSeqNP_780710.2. NM_175501.2. [Q811B3-1]
UniGeneMm.482727.

3D structure databases

ProteinModelPortalQ811B3.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSM12.237.

PTM databases

PhosphoSiteQ811B3.

Proteomic databases

PRIDEQ811B3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000061318; ENSMUSP00000057796; ENSMUSG00000047497. [Q811B3-1]
GeneID239337.
KEGGmmu:239337.
UCSCuc007vha.1. mouse. [Q811B3-2]
uc007vhb.1. mouse. [Q811B3-1]

Organism-specific databases

CTD81792.
MGIMGI:2146046. Adamts12.

Phylogenomic databases

eggNOGNOG237764.
GeneTreeENSGT00750000117354.
HOGENOMHOG000015092.
HOVERGENHBG050620.
InParanoidQ811B3.
KOK08626.
OMAPFIMSRQ.
OrthoDBEOG7V765X.
TreeFamTF313537.

Gene expression databases

BgeeQ811B3.
GenevestigatorQ811B3.

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. 7 hits.
[Graphical view]
PRINTSPR01857. ADAMTSFAMILY.
SMARTSM00209. TSP1. 8 hits.
[Graphical view]
SUPFAMSSF82895. SSF82895. 8 hits.
PROSITEPS50215. ADAM_MEPRO. 1 hit.
PS50900. PLAC. 1 hit.
PS50092. TSP1. 6 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio384074.
PROQ811B3.
SOURCESearch...

Entry information

Entry nameATS12_MOUSE
AccessionPrimary (citable) accession number: Q811B3
Secondary accession number(s): E9QKD6, Q8BK92, Q8BKY1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 91 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot