A disintegrin and metalloproteinase with thrombospondin motifs 13 precursor

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Q769J6 (ATS13_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 72. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
A disintegrin and metalloproteinase with thrombospondin motifs 13
Short name=ADAM-TS 13
Short name=ADAM-TS13
Short name=ADAMTS-13
EC=3.4.24.87

Alternative name(s):
von Willebrand factor-cleaving protease
Short name=vWF-CP
Short name=vWF-cleaving protease

Gene names

Name:	Adamts13
Synonyms:	Gm710

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1426 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Cleaves the vWF multimers in plasma into smaller forms. Ref.3
Catalytic activity	Cleaves the vWF at the 842-Tyr-\|-Met-843 in the A2 domain of the vWF subunit. The enzyme cleaves the von Willebrand factor at bond Tyr(842)-\|-Met(843) within the A2 domain.
Cofactor	Binds 1 zinc ion per subunit By similarity. Binds 4 calcium ions By similarity.
Enzyme regulation	Zinc and calcium ions cooperatively modulate enzyme activity. The cleavage of the pro-domain is not required for protease activity By similarity.
Subcellular location	Secreted. Note: Secretion enhanced by O-fucosylation of TSP type-1 repeats By similarity. Ref.1
Tissue specificity	Plasma. Expression is consistently high in liver, medium in lung and spleen, low in skeletal muscle and undetectable in heart, brain, kidney and testis. Ref.1 Ref.3
Developmental stage	Increases steadly with the age of embryo, reaching highest levels in embryonic tissues of 19 days of gestation. Ref.3
Domain	The pro-domain is not required for folding or secretion and does not perform the common function of maintening enzyme latency By similarity. The spacer domain is necessary to recognize and cleave vWF. The C-terminal TSP type-1 and CUB domains may modulate this interaction By similarity.
Post-translational modification	The precursor is processed by a furin endopeptidase which cleaves off the pro-domain By similarity. O-glycosylated By similarity. 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 ADAMTS13. May also be C-glycosylated on tryptophan residues within the consensus sequence W-X-X-W of the TPRs, and also N-glycosylated. These other glycosylations can also facilitate secretion By similarity.
Polymorphism	Two variants (Adamts13L and Adamts13S) were isolated that differed in the insertion of an intracisternal A particle (IAP) retrotransposon including a premature stop at the position 1036. In Adamts13S the C-terminal two TSP type-1 and two CUB domains are replaced with a 16-amino acid sequence derived from the IAP, this variant exhibited vWF cleaving activities in vitro. The IAP insertion is strain-specific and is found in BALB/c, C3H/He, C57BL/6 and DBA/2 strains, but not in the 129/Sv strain.
Sequence similarities	Contains 2 CUB domains. Contains 1 disintegrin domain. Contains 1 peptidase M12B domain. Contains 8 TSP type-1 domains.

Ontologies

Keywords
Biological process	Blood coagulation Hemostasis
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Domain	Repeat Signal
Ligand	Calcium Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Zymogen
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	blood coagulation Inferred from electronic annotation. Source: UniProtKB-KW peptide catabolic process Inferred from electronic annotation. Source: Compara proteolysis Inferred from direct assay Ref.1. Source: MGI
Cellular_component	extracellular space Inferred from direct assay Ref.1. Source: MGI proteinaceous extracellular matrix Inferred from electronic annotation. Source: InterPro
Molecular_function	endopeptidase activity Inferred from direct assay Ref.1. Source: MGI metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 33

Potential

Propeptide

34 – 76

By similarity

PRO_0000247512

Chain

77 – 1426

1350

A disintegrin and metalloproteinase with thrombospondin motifs 13

PRO_0000247513

Regions

Domain

74 – 291

218

Peptidase M12B

Domain

295 – 388

Disintegrin

Domain

389 – 444

TSP type-1 1

Domain

687 – 746

TSP type-1 2

Domain

747 – 810

TSP type-1 3

Domain

808 – 871

TSP type-1 4

Domain

904 – 957

TSP type-1 5

Domain

958 – 1019

TSP type-1 6

Domain

1020 – 1078

TSP type-1 7

Domain

1079 – 1137

TSP type-1 8

Domain

1195 – 1302

108

CUB 1

Domain

1293 – 1426

134

CUB 2

Region

305 – 379

Cysteine-rich

Region

556 – 685

130

Spacer

Motif

503 – 505

Cell attachment site Potential

Sites

Active site

227

By similarity

Metal binding

Calcium By similarity

Metal binding

175

Calcium By similarity

Metal binding

226

Zinc; catalytic By similarity

Metal binding

230

Zinc; catalytic By similarity

Metal binding

236

Zinc; catalytic By similarity

Metal binding

281

Calcium By similarity

Metal binding

289

Calcium By similarity

Amino acid modifications

Glycosylation

144

N-linked (GlcNAc...) Potential

Glycosylation

148

N-linked (GlcNAc...) Potential

Glycosylation

557

N-linked (GlcNAc...) Potential

Glycosylation

564

N-linked (GlcNAc...) Potential

Glycosylation

584

N-linked (GlcNAc...) Potential

Glycosylation

619

N-linked (GlcNAc...) Potential

Glycosylation

703

O-linked (Fuc...) By similarity

Glycosylation

762

O-linked (Fuc...) By similarity

Glycosylation

834

N-linked (GlcNAc...) Potential

Glycosylation

914

O-linked (Fuc...) By similarity

Glycosylation

973

O-linked (Fuc...) By similarity

Glycosylation

1033

O-linked (Fuc...) By similarity

Glycosylation

1057

N-linked (GlcNAc...) Potential

Glycosylation

1093

O-linked (Fuc...) By similarity

Disulfide bond

204 ↔ 286

By similarity

Disulfide bond

246 ↔ 270

By similarity

Disulfide bond

401 ↔ 438

By similarity

Disulfide bond

405 ↔ 443

By similarity

Disulfide bond

416 ↔ 428

By similarity

Natural variations

Natural variant

1022 – 1037

WKVLS…SCGLG → ALVWEAAPTFAVTRWR in Adamts13S.

Natural variant

1038 – 1426

389

Missing in Adamts13S.

Experimental info

Sequence conflict

354

R → H in BAC55159. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Q769J6 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 62E9F672B91F6772
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FASTA

1,426

155,357

        10         20         30         40         50         60 
MSQLCLWLTC QPCYAVSVRG ILTGAIFILG CWGLSDFQKS LLQDLEPKDV SSYFGHHAAP 

        70         80         90        100        110        120 
FTGHPPSHLQ RLRRRRTLED ILHLELLVAV GPDVSRAHQE DTERYVLTNL NIGSELLRNP 

       130        140        150        160        170        180 
SLGVQFQVHL VKLITLSDSE STPNITANIT SSLMSVCEWS QTINPHDDRD PSHADLILYI 

       190        200        210        220        230        240 
TRFDLELPDG NQQVRGVTQL GGACSLSWSC LITEDTGFDL GVTIAHEIGH SFGLDHDGAP 

       250        260        270        280        290        300 
GSGSTCKASG HVMAADGATP TGGTLEWSAC SQRQLQHLLS TGQMHCFQDP PGLQSGLTRH 

       310        320        330        340        350        360 
QLMAQPGLYY SADDQCRVAF GSGAVACTFS REGLDVCQAL SCHTDPLDQS SCSRLLVPLL 

       370        380        390        400        410        420 
DGTECGVEKW CSKARCRSLA ELAPVAAVHG HWSSWGPHSP CSRSCGGGVI TRRRWCNNPR 

       430        440        450        460        470        480 
PAFGGRACVG EDLQAKMCNT QACEKTQLEF MSEQCAQTDR QPLQLSQGTA SFYHWDAAVQ 

       490        500        510        520        530        540 
YSQGDTLCRH MCWAVGESFI VSRGDRFLDG TRCVPSGPQD DGTLSLCLLG SCRTFGCDGR 

       550        560        570        580        590        600 
MDSQKVWDAC QVCGGDNSTC SSRNGSFTAG RAREYVTFLI VTPNMTNAHI VNRRPLFTHL 

       610        620        630        640        650        660 
AVRIQGHYIV AGKTSISPNT TYPSLLEDYR VEYRVTLTED QLPHLEEIHI RGPVRDDIEI 

       670        680        690        700        710        720 
QVYRRYGGEY GDLTHPDITF SYFQLKQQAA WVWTAKRGPC SVSCGAGLRW VTYSCQDQAQ 

       730        740        750        760        770        780 
DKWVKNAQCQ GSPQPPAWQE PCVSAPCSPY WVAGDFSPCS VSCGGGLRER SLRCVETQDG 

       790        800        810        820        830        840 
FLKTLPPARC RAVAQQPAAE VENCNSQPCP TRWEVSDPGP CMSSACEAGL DSRNVTCVSR 

       850        860        870        880        890        900 
AGDPEKPETA GPCRTDEMSA MLEPCSRSLC SPGLGQVDNT MSLGEEAPSP VGSDKPGAQA 

       910        920        930        940        950        960 
EHVWTPLVGL CSISCGRGLK ELYFLCMDSV LKMPVQEELC GLASKPPSRW EVCRARPCPA 

       970        980        990       1000       1010       1020 
RWETQVLAPC PVTCGGGRVP LSVRCVQLDR GHPISVPHSK CSPVPKPGSF EDCSPEPCPA 

      1030       1040       1050       1060       1070       1080 
RWKVLSLGPC SASCGLGTAT QMVACMQLDQ GHDNEVNETF CKALVRPQAS VPCLIADCAF 

      1090       1100       1110       1120       1130       1140 
RWHISAWTEC SVSCGDGIQR RHDTCLGPQA QVPVPANFCQ HLPKPMTVRG CWAGPCAGQE 

      1150       1160       1170       1180       1190       1200 
TSSSLPHKEA TLPSQTQAAA TVASLQWSQP RARTPTLFSA SQSLGLQENL EEHGACGRQY 

      1210       1220       1230       1240       1250       1260 
LEPTGTIHMR DQGRLDCVVA IGRPLGEVVT LQILESSLKC SAGEQLLLWG RFTWRKTCRK 

      1270       1280       1290       1300       1310       1320 
MPGMTFSTKT NTVVVKQHRV LPGGGVLLRY WSQPAPGTFY KECDRQLFGP RGEIVSPSLS 

      1330       1340       1350       1360       1370       1380 
PDGRKAGTCR VFISVAPQAR IAIRALASDM GTASEGTNAN YVSIRDIHSL RTTTFWGQQV 

      1390       1400       1410       1420 
LYWESEGSEA ELEFSPGFLE AHASLQGEYW TISPRTSEQD DSLALS

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of strain-specific variants of mouse Adamts13 gene encoding von Willebrand factor-cleaving protease." Banno F., Kaminaka K., Soejima K., Kokame K., Miyata T. J. Biol. Chem. 279:30896-30903(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION, POLYMORPHISM. Strain: 129 and 129/Sv. Tissue: Liver.
[2]	"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. Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[3]	"Cloning, expression and functional characterization of the full-length murine ADAMTS13." Bruno K., Voelkel D., Plaimauer B., Antoine G., Pable S., Motto D.G., Lemmerhirt H.L., Dorner F., Zimmermann K., Scheiflinger F. J. Thromb. Haemost. 3:1064-1073(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB071302 mRNA. Translation: BAC55159.2. AB095445 Genomic DNA. Translation: BAD04062.1. AB112362 mRNA. Translation: BAD18090.1. AL773563, AL845266 Genomic DNA. Translation: CAM23711.1. AL845266, AL773563 Genomic DNA. Translation: CAM24664.1.
IPI	IPI00416064.
RefSeq	NP_001001322.1. NM_001001322.2.
UniGene	Mm.330084.
3D structure databases
ProteinModelPortal	Q769J6.
SMR	Q769J6. Positions 83-686, 690-811, 815-841, 904-1080, 1083-1139.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000099955.
Protein family/group databases
MEROPS	M12.241.
PTM databases
PhosphoSite	Q769J6.
Proteomic databases
PRIDE	Q769J6.
Protocols and materials databases
DNASU	279028.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000102891; ENSMUSP00000099955; ENSMUSG00000014852.
GeneID	279028.
KEGG	mmu:279028.
UCSC	uc008iwp.1. mouse.
Organism-specific databases
CTD	11093.
MGI	MGI:2685556. Adamts13.
Phylogenomic databases
eggNOG	NOG239882.
GeneTree	ENSGT00650000093225.
HOGENOM	HOG000231627.
HOVERGEN	HBG080358.
InParanoid	A2ALB4.
KO	K08627.
OMA	SWSCLIT.
OrthoDB	EOG4ZS92J.
Gene expression databases
ArrayExpress	Q769J6.
Bgee	Q769J6.
Genevestigator	Q769J6.
Family and domain databases
Gene3D	3.40.390.10. 1 hit.
InterPro	IPR000859. CUB_dom. IPR024079. MetalloPept_cat_dom. IPR001590. Peptidase_M12B. IPR013273. Peptidase_M12B_ADAM-TS. IPR000884. Thrombospondin_1_rpt. [Graphical view]
Pfam	PF01421. Reprolysin. 1 hit. PF00090. TSP_1. 3 hits. [Graphical view]
PRINTS	PR01857. ADAMTSFAMILY.
SMART	SM00209. TSP1. 6 hits. [Graphical view]
SUPFAM	SSF49854. CUB. 2 hits. SSF82895. TSP1. 5 hits.
PROSITE	PS50215. ADAM_MEPRO. 1 hit. PS01180. CUB. False negative. PS00427. DISINTEGRIN_1. False negative. PS50214. DISINTEGRIN_2. False negative. PS50092. TSP1. 4 hits. PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	393955.
SOURCE	Search...

Entry information

Entry name

ATS13_MOUSE

Accession

Primary (citable) accession number: Q769J6
Secondary accession number(s): A2ALB4, Q76LW1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 25, 2006
Last sequence update:	July 19, 2004
Last modified:	May 1, 2013
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents