Q76LX8 (ATS13_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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:	C9orf8
ORF Names:	UNQ6102/PRO20085

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1427 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Cleaves the vWF multimers in plasma into smaller forms.
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 Potential.
Enzyme regulation	Zinc and calcium ions cooperatively modulate enzyme activity. The cleavage of the pro-domain is not required for protease activity. Ref.12 Ref.14
Subcellular location	Secreted. Note: Secretion enhanced by O-fucosylation of TSP type-1 repeats. Ref.11
Tissue specificity	Plasma. Expressed primarily in liver. Ref.1
Domain	The pro-domain is not required for folding or secretion and does not perform the common function of maintening enzyme latency. The spacer domain is necessary to recognize and cleave vWF. The C-terminal TSP type-1 and CUB domains may modulate this interaction.
Post-translational modification	Glycosylated. 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. Ref.2 Ref.15 The precursor is processed by a furin endopeptidase which cleaves off the pro-domain.
Polymorphism	Genetic variations in ADAMTS13 coding region influence plasmatic ADAMTS13 activity levels. Dependent on the sequence context, the same polymorphisms might be either positive or negative modifiers of gene expression, thereby altering the phenotype of ADAMTS13 deficiency.
Involvement in disease	Thrombotic thrombocytopenic purpura congenital (TTP) [MIM:274150]: A hematologic disease characterized by hemolytic anemia with fragmentation of erythrocytes, thrombocytopenia, diffuse and non-focal neurologic findings, decreased renal function and fever. recessive. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.3 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.34 Ref.35 Ref.36
Sequence similarities	Contains 2 CUB domains. Contains 1 disintegrin domain. Contains 1 peptidase M12B domain. Contains 8 TSP type-1 domains.
Sequence caution	The sequence AAQ88485.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence CAB66743.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Blood coagulation Hemostasis
Cellular component	Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
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	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell-matrix adhesion Non-traceable author statement Ref.2. Source: UniProtKB glycoprotein metabolic process Non-traceable author statement Ref.2. Source: UniProtKB integrin-mediated signaling pathway Non-traceable author statement Ref.2. Source: UniProtKB peptide catabolic process Inferred from direct assay Ref.10. Source: UniProtKB platelet activation Non-traceable author statement Ref.2. Source: UniProtKB protein processing Traceable author statement Ref.2. Source: UniProtKB proteolysis Inferred from direct assay Ref.10. Source: UniProtKB
Cellular_component	cell surface Non-traceable author statement Ref.2. Source: UniProtKB extracellular space Inferred from electronic annotation. Source: Compara proteinaceous extracellular matrix Traceable author statement Ref.2. Source: UniProtKB
Molecular_function	calcium ion binding Traceable author statement Ref.2. Source: UniProtKB integrin binding Traceable author statement Ref.2. Source: UniProtKB metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro metallopeptidase activity Traceable author statement Ref.2. Source: UniProtKB zinc ion binding Traceable author statement Ref.2. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
VWF	P04275	5	EBI-981764,EBI-981819

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q76LX8-1)

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: Q76LX8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1135-1190: Missing.

Isoform 3 (identifier: Q76LX8-3)

The sequence of this isoform differs from the canonical sequence as follows:
     275-305: Missing.
     1135-1190: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 29

29

Potential

Propeptide

30 – 74

45

PRO_0000247510

Chain

75 – 1427

1353

A disintegrin and metalloproteinase with thrombospondin motifs 13

PRO_0000247511

Regions

Domain

80 – 286

207

Peptidase M12B

Domain

287 – 383

97

Disintegrin

Domain

384 – 439

56

TSP type-1 1

Domain

682 – 730

49

TSP type-1 2

Domain

742 – 805

64

TSP type-1 3

Domain

808 – 859

52

TSP type-1 4

Domain

896 – 950

55

TSP type-1 5

Domain

951 – 1011

61

TSP type-1 6

Domain

1012 – 1068

57

TSP type-1 7

Domain

1072 – 1131

60

TSP type-1 8

Domain

1192 – 1298

107

CUB 1

Domain

1299 – 1427

129

CUB 2

Region

300 – 374

75

Cysteine-rich

Region

556 – 685

130

Spacer

Motif

498 – 500

3

Cell attachment site Potential

Sites

Active site

225

1

By similarity

Metal binding

83

1

Calcium Potential

Metal binding

173

1

Calcium Potential

Metal binding

224

1

Zinc; catalytic By similarity

Metal binding

228

1

Zinc; catalytic By similarity

Metal binding

234

1

Zinc; catalytic By similarity

Metal binding

281

1

Calcium Potential

Metal binding

284

1

Calcium Potential

Amino acid modifications

Glycosylation

142

1

N-linked (GlcNAc...) Potential

Glycosylation

146

1

N-linked (GlcNAc...) Potential

Glycosylation

552

1

N-linked (GlcNAc...) Potential

Glycosylation

579

1

N-linked (GlcNAc...) Potential

Glycosylation

614

1

N-linked (GlcNAc...) Ref.13

Glycosylation

667

1

N-linked (GlcNAc...) Ref.13

Glycosylation

698

1

O-linked (Fuc...) Ref.15

Glycosylation

707

1

N-linked (GlcNAc...) Potential

Glycosylation

757

1

O-linked (Fuc...) Ref.15

Glycosylation

828

1

N-linked (GlcNAc...) Potential

Glycosylation

907

1

O-linked (Fuc...) Ref.15

Glycosylation

965

1

O-linked (Fuc...) Ref.15

Glycosylation

1027

1

O-linked (Fuc...) Ref.15

Glycosylation

1087

1

O-linked (Fuc...) Ref.15

Glycosylation

1235

1

N-linked (GlcNAc...) Potential

Glycosylation

1354

1

N-linked (GlcNAc...) Ref.13

Disulfide bond

202 ↔ 281

By similarity

Disulfide bond

242 ↔ 265

By similarity

Disulfide bond

396 ↔ 433

By similarity

Disulfide bond

400 ↔ 438

By similarity

Disulfide bond

411 ↔ 423

By similarity

Natural variations

Alternative sequence

275 – 305

31

Missing in isoform 3.

VSP_020002

Alternative sequence

1135 – 1190

56

Missing in isoform 2 and isoform 3.

VSP_020003

Natural variant

7

1

R → W Does not affect protein secretion. Ref.3 Ref.5 Ref.27
Corresponds to variant rs34024143 [ dbSNP | Ensembl ].

VAR_027109

Natural variant

79

1

I → M in TTP. Ref.24

VAR_067770

Natural variant

88

1

V → M in TTP; reduces protein secretion and proteolytic activity. Ref.28

VAR_027110

Natural variant

96

1

H → D in TTP. Ref.3
Corresponds to variant rs121908467 [ dbSNP | Ensembl ].

VAR_027111

Natural variant

102

1

R → C in TTP. Ref.3
Corresponds to variant rs121908469 [ dbSNP | Ensembl ].

VAR_027112

Natural variant

119

1

S → F in TTP. Ref.33

VAR_067771

Natural variant

178

1

I → T in TTP. Ref.34

VAR_067772

Natural variant

193

1

R → W in TTP; low activity. Ref.22 Ref.34

VAR_027113

Natural variant

196

1

T → I in TTP. Ref.3 Ref.21 Ref.31
Corresponds to variant rs121908470 [ dbSNP | Ensembl ].

VAR_027114

Natural variant

203

1

S → P in TTP. Ref.24

VAR_067773

Natural variant

232

1

L → Q in TTP. Ref.18

VAR_067774

Natural variant

234

1

H → Q in TTP. Ref.30

VAR_027115

Natural variant

235

1

D → H in TTP. Ref.20

VAR_067775

Natural variant

250

1

A → V in TTP; mild effect on protein secretion; strong reduction of proteolytic activity. Ref.23
Corresponds to variant rs121908478 [ dbSNP | Ensembl ].

VAR_027116

Natural variant

263

1

S → C in TTP. Ref.18 Ref.31

VAR_067776

Natural variant

268

1

R → P in TTP; affects protein secretion. Ref.17 Ref.24
Corresponds to variant rs121908477 [ dbSNP | Ensembl ].

VAR_027117

Natural variant

304

1

Y → C in TTP. Ref.34

VAR_067777

Natural variant

311

1

C → Y in TTP. Ref.20

VAR_067778

Natural variant

339

1

T → R. Ref.34
Corresponds to variant rs149517360 [ dbSNP | Ensembl ].

VAR_067779

Natural variant

347

1

C → S in TTP. Ref.31

VAR_067780

Natural variant

349

1

R → C in TTP. Ref.34

VAR_067781

Natural variant

353

1

P → L in TTP. Ref.18 Ref.20 Ref.31

VAR_067782

Natural variant

390

1

W → C in TTP. Ref.25

VAR_027118

Natural variant

398

1

R → H in TTP. Ref.3
Corresponds to variant rs121908471 [ dbSNP | Ensembl ].

VAR_027119

Natural variant

448

1

Q → E Does not affect protein secretion; normal proteolytic activity. Ref.3 Ref.5 Ref.7 Ref.17 Ref.21 Ref.22 Ref.27 Ref.32 Ref.34
Corresponds to variant rs2301612 [ dbSNP | Ensembl ].

VAR_027120

Natural variant

456

1

Q → H. Ref.5
Corresponds to variant rs36220239 [ dbSNP | Ensembl ].

VAR_027162

Natural variant

457

1

P → L. Ref.5 Ref.20
Corresponds to variant rs36220240 [ dbSNP | Ensembl ].

VAR_027163

Natural variant

475

1

P → S. Ref.17
Corresponds to variant rs11575933 [ dbSNP | Ensembl ].

VAR_027121

Natural variant

507

1

R → Q in TTP. Ref.24 Ref.31

VAR_067783

Natural variant

508

1

C → Y in TTP; impairs protein secretion. Ref.17

VAR_027122

Natural variant

525

1

G → D in TTP. Ref.34

VAR_067784

Natural variant

528

1

R → G in TTP. Ref.3
Corresponds to variant rs121908473 [ dbSNP | Ensembl ].

VAR_027123

Natural variant

596

1

A → V in TTP. Ref.24

VAR_067785

Natural variant

606

1

A → P in TTP. Ref.34

VAR_067786

Natural variant

618

1

P → A. Ref.3 Ref.5 Ref.27 Ref.34
Corresponds to variant rs28647808 [ dbSNP | Ensembl ].

VAR_027124

Natural variant

625

1

R → H. Ref.3 Ref.5
Corresponds to variant rs36090624 [ dbSNP | Ensembl ].

VAR_027125

Natural variant

658

1

Y → C in TTP. Ref.36

VAR_067787

Natural variant

671

1

P → L in TTP. Ref.31

VAR_067788

Natural variant

673

1

I → F in TTP; impairs protein secretion. Ref.22

VAR_027126

Natural variant

692

1

R → C in TTP. Ref.3
Corresponds to variant rs121908475 [ dbSNP | Ensembl ].

VAR_027127

Natural variant

732

1

A → V. Ref.3 Ref.19 Ref.27
Corresponds to variant rs41314453 [ dbSNP | Ensembl ].

VAR_027128

Natural variant

740

1

E → K. Ref.5
Corresponds to variant rs36221451 [ dbSNP | Ensembl ].

VAR_027164

Natural variant

758

1

C → R in TTP. Ref.24

VAR_067789

Natural variant

900

1

A → V. Ref.2 Ref.3 Ref.5
Corresponds to variant rs685523 [ dbSNP | Ensembl ].

VAR_027129

Natural variant

903

1

S → L. Ref.26 Ref.30
Corresponds to variant rs78977446 [ dbSNP | Ensembl ].

VAR_027130

Natural variant

908

1

C → S in TTP. Ref.24

VAR_067790

Natural variant

908

1

C → Y in TTP; impairs protein secretion. Ref.22

VAR_027131

Natural variant

951

1

C → G in TTP. Ref.3
Corresponds to variant rs121908468 [ dbSNP | Ensembl ].

VAR_027132

Natural variant

977 – 979

3

CAR → W in TTP.

VAR_067791

Natural variant

982

1

G → R. Ref.5
Corresponds to variant rs36222275 [ dbSNP | Ensembl ].

VAR_027165

Natural variant

1024

1

C → G in TTP. Ref.3
Corresponds to variant rs121908472 [ dbSNP | Ensembl ].

VAR_027133

Natural variant

1033

1

A → T. Ref.3 Ref.5
Corresponds to variant rs28503257 [ dbSNP | Ensembl ].

VAR_027134

Natural variant

1060

1

R → W in TTP; affects protein secretion; the mutant protein has reduced protease activity. Ref.29 Ref.31 Ref.32
Corresponds to variant rs142572218 [ dbSNP | Ensembl ].

VAR_067792

Natural variant

1095

1

R → W in a patient with thrombotic thrombocytopenic purpura. Ref.26

VAR_027135

Natural variant

1123

1

R → C in TTP; impairs protein secretion; the mutant protein has reduced protease activity. Ref.22 Ref.32

VAR_027136

Natural variant

1213

1

C → Y in TTP. Ref.3
Corresponds to variant rs121908474 [ dbSNP | Ensembl ].

VAR_027137

Natural variant

1219

1

R → W in TTP; affects protein secretion; the mutant protein has reduced protease activity. Ref.32

VAR_067793

Natural variant

1226

1

T → I. Ref.5
Corresponds to variant rs36222894 [ dbSNP | Ensembl ].

VAR_027166

Natural variant

1239

1

G → V in TTP; impairs protein secretion. Ref.28

VAR_027138

Natural variant

1314

1

S → L Found in a patient with hemolytic uremic syndrome. Ref.37

VAR_067794

Natural variant

1336

1

R → W in TTP; impairs protein secretion and proteolytic activity. Ref.19 Ref.27

VAR_027139

Experimental info

Mutagenesis

71

1

R → K: Abolishes pro-domain removal but no loss of proteolytic activity; when associated with D-73. Ref.12

Mutagenesis

73

1

R → D: Abolishes pro-domain removal but no loss of proteolytic activity; when associated with K-71. Ref.12

Mutagenesis

399

1

S → A: No effect on cleavage of VWF and little change in secretion of ADAMTS13. Abolishes secretion of ADAMTS13; when associated with A-698. Ref.15

Mutagenesis

698

1

S → A: No effect on cleavage of VWF and greatly reduced secretion of ADAMTS13. Abolishes secretion of ADAMTS13; when associated with A-399. Ref.15

Mutagenesis

757

1

S → A: No effect on cleavage of VWF and little change in secretion of ADAMTS13. Ref.15

Mutagenesis

907

1

S → A: No effect on cleavage of VWF and greatly reduced secretion of ADAMTS13. Abolishes most of the secretion of ADAMTS13; when associated with A-965. Ref.15

Mutagenesis

965

1

S → A: No effect on cleavage of VWF and little change in secretion of ADAMTS13. Abolishes most of the secretion of ADAMTS13; when associated with A-907. Ref.15

Mutagenesis

1027

1

S → A: No effect on cleavage of VWF and little change in secretion of ADAMTS13. Abolishes most of the secretion of ADAMTS13; when associated with A-1087. Ref.15

Mutagenesis

1087

1

S → A: No effect on cleavage of VWF and little change in secretion of ADAMTS13. Abolishes most of the secretion of ADAMTS13; when associated with A-1027. Ref.15

Sequence conflict

101

1

E → R AA sequence Ref.1

Secondary structure

1

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1427

Helix Strand Turn

Details...

Helix

301 – 303

3

Helix

307 – 314

8

Helix

331 – 334

4

Beta strand

337 – 340

4

Beta strand

348 – 351

4

Beta strand

359 – 361

3

Beta strand

364 – 367

4

Beta strand

370 – 373

4

Helix

374 – 377

4

Beta strand

399 – 401

3

Beta strand

403 – 406

4

Beta strand

417 – 419

3

Beta strand

430 – 433

4

Helix

442 – 451

10

Turn

452 – 455

4

Beta strand

470 – 472

3

Turn

474 – 476

3

Helix

479 – 483

5

Beta strand

486 – 489

4

Beta strand

495 – 497

3

Beta strand

519 – 523

5

Beta strand

526 – 530

5

Beta strand

534 – 536

3

Beta strand

554 – 562

9

Beta strand

569 – 576

8

Beta strand

581 – 588

8

Beta strand

592 – 599

8

Beta strand

602 – 605

4

Beta strand

608 – 610

3

Beta strand

614 – 618

5

Beta strand

623 – 632

10

Beta strand

634 – 636

3

Beta strand

638 – 647

10

Beta strand

653 – 661

9

Helix

663 – 665

3

Helix

667 – 669

3

Beta strand

673 – 680

8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: A2103AFABC1A4445	FASTA	1,427	153,604
	10 20 30 40 50 60 MHQRHPRARC PPLCVAGILA CGFLLGCWGP SHFQQSCLQA LEPQAVSSYL SPGAPLKGRP 70 80 90 100 110 120 PSPGFQRQRQ RQRRAAGGIL HLELLVAVGP DVFQAHQEDT ERYVLTNLNI GAELLRDPSL 130 140 150 160 170 180 GAQFRVHLVK MVILTEPEGA PNITANLTSS LLSVCGWSQT INPEDDTDPG HADLVLYITR 190 200 210 220 230 240 FDLELPDGNR QVRGVTQLGG ACSPTWSCLI TEDTGFDLGV TIAHEIGHSF GLEHDGAPGS 250 260 270 280 290 300 GCGPSGHVMA SDGAAPRAGL AWSPCSRRQL LSLLSAGRAR CVWDPPRPQP GSAGHPPDAQ 310 320 330 340 350 360 PGLYYSANEQ CRVAFGPKAV ACTFAREHLD MCQALSCHTD PLDQSSCSRL LVPLLDGTEC 370 380 390 400 410 420 GVEKWCSKGR CRSLVELTPI AAVHGRWSSW GPRSPCSRSC GGGVVTRRRQ CNNPRPAFGG 430 440 450 460 470 480 RACVGADLQA EMCNTQACEK TQLEFMSQQC ARTDGQPLRS SPGGASFYHW GAAVPHSQGD 490 500 510 520 530 540 ALCRHMCRAI GESFIMKRGD SFLDGTRCMP SGPREDGTLS LCVSGSCRTF GCDGRMDSQQ 550 560 570 580 590 600 VWDRCQVCGG DNSTCSPRKG SFTAGRAREY VTFLTVTPNL TSVYIANHRP LFTHLAVRIG 610 620 630 640 650 660 GRYVVAGKMS ISPNTTYPSL LEDGRVEYRV ALTEDRLPRL EEIRIWGPLQ EDADIQVYRR 670 680 690 700 710 720 YGEEYGNLTR PDITFTYFQP KPRQAWVWAA VRGPCSVSCG AGLRWVNYSC LDQARKELVE 730 740 750 760 770 780 TVQCQGSQQP PAWPEACVLE PCPPYWAVGD FGPCSASCGG GLRERPVRCV EAQGSLLKTL 790 800 810 820 830 840 PPARCRAGAQ QPAVALETCN PQPCPARWEV SEPSSCTSAG GAGLALENET CVPGADGLEA 850 860 870 880 890 900 PVTEGPGSVD EKLPAPEPCV GMSCPPGWGH LDATSAGEKA PSPWGSIRTG AQAAHVWTPA 910 920 930 940 950 960 AGSCSVSCGR GLMELRFLCM DSALRVPVQE ELCGLASKPG SRREVCQAVP CPARWQYKLA 970 980 990 1000 1010 1020 ACSVSCGRGV VRRILYCARA HGEDDGEEIL LDTQCQGLPR PEPQEACSLE PCPPRWKVMS 1030 1040 1050 1060 1070 1080 LGPCSASCGL GTARRSVACV QLDQGQDVEV DEAACAALVR PEASVPCLIA DCTYRWHVGT 1090 1100 1110 1120 1130 1140 WMECSVSCGD GIQRRRDTCL GPQAQAPVPA DFCQHLPKPV TVRGCWAGPC VGQGTPSLVP 1150 1160 1170 1180 1190 1200 HEEAAAPGRT TATPAGASLE WSQARGLLFS PAPQPRRLLP GPQENSVQSS ACGRQHLEPT 1210 1220 1230 1240 1250 1260 GTIDMRGPGQ ADCAVAIGRP LGEVVTLRVL ESSLNCSAGD MLLLWGRLTW RKMCRKLLDM 1270 1280 1290 1300 1310 1320 TFSSKTNTLV VRQRCGRPGG GVLLRYGSQL APETFYRECD MQLFGPWGEI VSPSLSPATS 1330 1340 1350 1360 1370 1380 NAGGCRLFIN VAPHARIAIH ALATNMGAGT EGANASYILI RDTHSLRTTA FHGQQVLYWE 1390 1400 1410 1420 SESSQAEMEF SEGFLKAQAS LRGQYWTLQS WVPEMQDPQS WKGKEGT
	Isoform 2 [UniParc]. Checksum: AE4C713AE5B64DFC	FASTA	1,371	147,804
	10 20 30 40 50 60 MHQRHPRARC PPLCVAGILA CGFLLGCWGP SHFQQSCLQA LEPQAVSSYL SPGAPLKGRP 70 80 90 100 110 120 PSPGFQRQRQ RQRRAAGGIL HLELLVAVGP DVFQAHQEDT ERYVLTNLNI GAELLRDPSL 130 140 150 160 170 180 GAQFRVHLVK MVILTEPEGA PNITANLTSS LLSVCGWSQT INPEDDTDPG HADLVLYITR 190 200 210 220 230 240 FDLELPDGNR QVRGVTQLGG ACSPTWSCLI TEDTGFDLGV TIAHEIGHSF GLEHDGAPGS 250 260 270 280 290 300 GCGPSGHVMA SDGAAPRAGL AWSPCSRRQL LSLLSAGRAR CVWDPPRPQP GSAGHPPDAQ 310 320 330 340 350 360 PGLYYSANEQ CRVAFGPKAV ACTFAREHLD MCQALSCHTD PLDQSSCSRL LVPLLDGTEC 370 380 390 400 410 420 GVEKWCSKGR CRSLVELTPI AAVHGRWSSW GPRSPCSRSC GGGVVTRRRQ CNNPRPAFGG 430 440 450 460 470 480 RACVGADLQA EMCNTQACEK TQLEFMSQQC ARTDGQPLRS SPGGASFYHW GAAVPHSQGD 490 500 510 520 530 540 ALCRHMCRAI GESFIMKRGD SFLDGTRCMP SGPREDGTLS LCVSGSCRTF GCDGRMDSQQ 550 560 570 580 590 600 VWDRCQVCGG DNSTCSPRKG SFTAGRAREY VTFLTVTPNL TSVYIANHRP LFTHLAVRIG 610 620 630 640 650 660 GRYVVAGKMS ISPNTTYPSL LEDGRVEYRV ALTEDRLPRL EEIRIWGPLQ EDADIQVYRR 670 680 690 700 710 720 YGEEYGNLTR PDITFTYFQP KPRQAWVWAA VRGPCSVSCG AGLRWVNYSC LDQARKELVE 730 740 750 760 770 780 TVQCQGSQQP PAWPEACVLE PCPPYWAVGD FGPCSASCGG GLRERPVRCV EAQGSLLKTL 790 800 810 820 830 840 PPARCRAGAQ QPAVALETCN PQPCPARWEV SEPSSCTSAG GAGLALENET CVPGADGLEA 850 860 870 880 890 900 PVTEGPGSVD EKLPAPEPCV GMSCPPGWGH LDATSAGEKA PSPWGSIRTG AQAAHVWTPA 910 920 930 940 950 960 AGSCSVSCGR GLMELRFLCM DSALRVPVQE ELCGLASKPG SRREVCQAVP CPARWQYKLA 970 980 990 1000 1010 1020 ACSVSCGRGV VRRILYCARA HGEDDGEEIL LDTQCQGLPR PEPQEACSLE PCPPRWKVMS 1030 1040 1050 1060 1070 1080 LGPCSASCGL GTARRSVACV QLDQGQDVEV DEAACAALVR PEASVPCLIA DCTYRWHVGT 1090 1100 1110 1120 1130 1140 WMECSVSCGD GIQRRRDTCL GPQAQAPVPA DFCQHLPKPV TVRGCWAGPC VGQGACGRQH 1150 1160 1170 1180 1190 1200 LEPTGTIDMR GPGQADCAVA IGRPLGEVVT LRVLESSLNC SAGDMLLLWG RLTWRKMCRK 1210 1220 1230 1240 1250 1260 LLDMTFSSKT NTLVVRQRCG RPGGGVLLRY GSQLAPETFY RECDMQLFGP WGEIVSPSLS 1270 1280 1290 1300 1310 1320 PATSNAGGCR LFINVAPHAR IAIHALATNM GAGTEGANAS YILIRDTHSL RTTAFHGQQV 1330 1340 1350 1360 1370 LYWESESSQA EMEFSEGFLK AQASLRGQYW TLQSWVPEMQ DPQSWKGKEG T
	Isoform 3 [UniParc]. Checksum: 0BFBEF4C3D58B2C2	FASTA	1,340	144,517
	10 20 30 40 50 60 MHQRHPRARC PPLCVAGILA CGFLLGCWGP SHFQQSCLQA LEPQAVSSYL SPGAPLKGRP 70 80 90 100 110 120 PSPGFQRQRQ RQRRAAGGIL HLELLVAVGP DVFQAHQEDT ERYVLTNLNI GAELLRDPSL 130 140 150 160 170 180 GAQFRVHLVK MVILTEPEGA PNITANLTSS LLSVCGWSQT INPEDDTDPG HADLVLYITR 190 200 210 220 230 240 FDLELPDGNR QVRGVTQLGG ACSPTWSCLI TEDTGFDLGV TIAHEIGHSF GLEHDGAPGS 250 260 270 280 290 300 GCGPSGHVMA SDGAAPRAGL AWSPCSRRQL LSLLSANEQC RVAFGPKAVA CTFAREHLDM 310 320 330 340 350 360 CQALSCHTDP LDQSSCSRLL VPLLDGTECG VEKWCSKGRC RSLVELTPIA AVHGRWSSWG 370 380 390 400 410 420 PRSPCSRSCG GGVVTRRRQC NNPRPAFGGR ACVGADLQAE MCNTQACEKT QLEFMSQQCA 430 440 450 460 470 480 RTDGQPLRSS PGGASFYHWG AAVPHSQGDA LCRHMCRAIG ESFIMKRGDS FLDGTRCMPS 490 500 510 520 530 540 GPREDGTLSL CVSGSCRTFG CDGRMDSQQV WDRCQVCGGD NSTCSPRKGS FTAGRAREYV 550 560 570 580 590 600 TFLTVTPNLT SVYIANHRPL FTHLAVRIGG RYVVAGKMSI SPNTTYPSLL EDGRVEYRVA 610 620 630 640 650 660 LTEDRLPRLE EIRIWGPLQE DADIQVYRRY GEEYGNLTRP DITFTYFQPK PRQAWVWAAV 670 680 690 700 710 720 RGPCSVSCGA GLRWVNYSCL DQARKELVET VQCQGSQQPP AWPEACVLEP CPPYWAVGDF 730 740 750 760 770 780 GPCSASCGGG LRERPVRCVE AQGSLLKTLP PARCRAGAQQ PAVALETCNP QPCPARWEVS 790 800 810 820 830 840 EPSSCTSAGG AGLALENETC VPGADGLEAP VTEGPGSVDE KLPAPEPCVG MSCPPGWGHL 850 860 870 880 890 900 DATSAGEKAP SPWGSIRTGA QAAHVWTPAA GSCSVSCGRG LMELRFLCMD SALRVPVQEE 910 920 930 940 950 960 LCGLASKPGS RREVCQAVPC PARWQYKLAA CSVSCGRGVV RRILYCARAH GEDDGEEILL 970 980 990 1000 1010 1020 DTQCQGLPRP EPQEACSLEP CPPRWKVMSL GPCSASCGLG TARRSVACVQ LDQGQDVEVD 1030 1040 1050 1060 1070 1080 EAACAALVRP EASVPCLIAD CTYRWHVGTW MECSVSCGDG IQRRRDTCLG PQAQAPVPAD 1090 1100 1110 1120 1130 1140 FCQHLPKPVT VRGCWAGPCV GQGACGRQHL EPTGTIDMRG PGQADCAVAI GRPLGEVVTL 1150 1160 1170 1180 1190 1200 RVLESSLNCS AGDMLLLWGR LTWRKMCRKL LDMTFSSKTN TLVVRQRCGR PGGGVLLRYG 1210 1220 1230 1240 1250 1260 SQLAPETFYR ECDMQLFGPW GEIVSPSLSP ATSNAGGCRL FINVAPHARI AIHALATNMG 1270 1280 1290 1300 1310 1320 AGTEGANASY ILIRDTHSLR TTAFHGQQVL YWESESSQAE MEFSEGFLKA QASLRGQYWT 1330 1340 LQSWVPEMQD PQSWKGKEGT

References

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[1]	"A novel human metalloprotease synthesized in the liver and secreted into the blood: possibly, the von Willebrand factor-cleaving protease?" Soejima K., Mimura N., Hirashima M., Maeda H., Hamamoto T., Nakagaki T., Nozaki C. J. Biochem. 130:475-480(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 75-103, TISSUE SPECIFICITY. Tissue: Liver.
[2]	"Structure of von Willebrand factor-cleaving protease (ADAMTS13), a metalloprotease involved in thrombotic thrombocytopenic purpura." Zheng X., Chung D., Takayama T.K., Majerus E.M., Sadler J.E., Fujikawa K. J. Biol. Chem. 276:41059-41063(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), GLYCOSYLATION, VARIANT VAL-900. Tissue: Liver.
[3]	"Mutations in a member of the ADAMTS gene family cause thrombotic thrombocytopenic purpura." Levy G.G., Nichols W.C., Lian E.C., Foroud T., McClintick J.N., McGee B.M., Yang A.Y., Siemieniak D.R., Stark K.R., Gruppo R., Sarode R., Shurin S.B., Chandrasekaran V., Stabler S.P., Sabio H., Bouhassira E.E., Upshaw J.D. Jr., Ginsburg D., Tsai H.-M. Nature 413:488-494(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INVOLVEMENT IN THROMBOTIC THROMBOCYTOPENIC PURPURA, VARIANTS TTP ASP-96; CYS-102; ILE-196; HIS-398; GLY-528; CYS-692; GLY-951; GLY-1024 AND TYR-1213, VARIANTS TRP-7; GLU-448; ALA-618; HIS-625; VAL-732; VAL-900 AND THR-1033. Tissue: Liver.
[4]	"Cloning, expression analysis, and structural characterization of seven novel human ADAMTSs, a family of metalloproteinases with disintegrin and thrombospondin-1 domains." Cal S., Obaya A.J., Llamazares M., Garabaya C., Quesada V., Lopez-Otin C. Gene 283:49-62(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3). Tissue: Liver.
[5]	SeattleSNPs variation discovery resource Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS TRP-7; GLU-448; HIS-456; LEU-457; ALA-618; HIS-625; LYS-740; VAL-900; ARG-982; THR-1033 AND ILE-1226.
[6]	"DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I. Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment." Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M. Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 275-1427, VARIANT GLU-448.
[8]	"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs." Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A. Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1191-1427. Tissue: Testis.
[9]	"Partial amino acid sequence of purified von Willebrand factor-cleaving protease." Gerritsen H.E., Robles R., Laemmle B., Furlan M. Blood 98:1654-1661(2001) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 75-89.
[10]	"Purification of human von Willebrand factor-cleaving protease and its identification as a new member of the metalloproteinase family." Fujikawa K., Suzuki H., McMullen B., Chung D. Blood 98:1662-1666(2001) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 75-94.
[11]	"Cleavage of von Willebrand factor requires the spacer domain of the metalloprotease ADAMTS13." Zheng X., Nishio K., Majerus E.M., Sadler J.E. J. Biol. Chem. 278:30136-30141(2003) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION, SUBCELLULAR LOCATION.
[12]	"Cleavage of the ADAMTS13 propeptide is not required for protease activity." Majerus E.M., Zheng X., Tuley E.A., Sadler J.E. J. Biol. Chem. 278:46643-46648(2003) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION, MUTAGENESIS OF ARG-71 AND ARG-73.
[13]	"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry." Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D. J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-614; ASN-667 AND ASN-1354, MASS SPECTROMETRY. Tissue: Plasma.
[14]	"Zinc and calcium ions cooperatively modulate ADAMTS13 activity." Anderson P.J., Kokame K., Sadler J.E. J. Biol. Chem. 281:850-857(2006) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION.
[15]	"O-fucosylation is required for ADAMTS13 secretion." Ricketts L.M., Dlugosz M., Luther K.B., Haltiwanger R.S., Majerus E.M. J. Biol. Chem. 282:17014-17023(2007) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT SER-698; SER-757; SER-907; SER-965; SER-1027 AND SER-1087, MASS SPECTROMETRY, MUTAGENESIS OF SER-399; SER-698; SER-757; SER-907; SER-965; SER-1027 AND SER-1087.
[16]	"ADAMTS13 mutations and polymorphisms in congenital thrombotic thrombocytopenic purpura." Lotta L.A., Garagiola I., Palla R., Cairo A., Peyvandi F. Hum. Mutat. 31:11-19(2010) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON VARIANTS.
[17]	"Mutations and common polymorphisms in ADAMTS13 gene responsible for von Willebrand factor-cleaving protease activity." Kokame K., Matsumoto M., Soejima K., Yagi H., Ishizashi H., Funato M., Tamai H., Konno M., Kamide K., Kawano Y., Miyata T., Fujimura Y. Proc. Natl. Acad. Sci. U.S.A. 99:11902-11907(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS TTP PRO-268 AND TYR-508, VARIANTS GLU-448 AND SER-475, CHARACTERIZATION OF VARIANTS TTP PRO-268 AND TYR-508, CHARACTERIZATION OF VARIANTS GLU-448 AND SER-475.
[18]	"von Willebrand factor cleaving protease and ADAMTS13 mutations in childhood TTP." Schneppenheim R., Budde U., Oyen F., Angerhaus D., Aumann V., Drewke E., Hassenpflug W., Haberle J., Kentouche K., Kohne E., Kurnik K., Mueller-Wiefel D., Obser T., Santer R., Sykora K.W. Blood 101:1845-1850(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS TTP GLN-232; CYS-263 AND LEU-353.
[19]	"ADAMTS13 gene defects in two brothers with constitutional thrombotic thrombocytopenic purpura and normalization of von Willebrand factor-cleaving protease activity by recombinant human ADAMTS13." Antoine G., Zimmermann K., Plaimauer B., Grillowitzer M., Studt J.D., Lammle B., Scheiflinger F. Br. J. Haematol. 120:821-824(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT TTP TRP-1336, VARIANT VAL-732.
[20]	"Mutation analysis and clinical implications of von Willebrand factor-cleaving protease deficiency." Assink K., Schiphorst R., Allford S., Karpman D., Etzioni A., Brichard B., van de Kar N., Monnens L., van den Heuvel L. Kidney Int. 63:1995-1999(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS TTP HIS-235; TYR-311 AND LEU-353, VARIANT LEU-457.
[21]	"Congenital thrombotic thrombocytopenic purpura in association with a mutation in the second CUB domain of ADAMTS13." Pimanda J.E., Maekawa A., Wind T., Paxton J., Chesterman C.N., Hogg P.J. Blood 103:627-629(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT TTP ILE-196, VARIANT GLU-448.
[22]	"Molecular characterization of ADAMTS13 gene mutations in Japanese patients with Upshaw-Schulman syndrome." Matsumoto M., Kokame K., Soejima K., Miura M., Hayashi S., Fujii Y., Iwai A., Ito E., Tsuji Y., Takeda-Shitaka M., Iwadate M., Umeyama H., Yagi H., Ishizashi H., Banno F., Nakagaki T., Miyata T., Fujimura Y. Blood 103:1305-1310(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS TTP TRP-193; PHE-673; TYR-908 AND CYS-1123, VARIANT GLU-448, CHARACTERIZATION OF VARIANTS TTP TRP-193; PHE-673; TYR-908 AND CYS-1123.
[23]	"Identification of novel mutations in ADAMTS13 in an adult patient with congenital thrombotic thrombocytopenic purpura." Uchida T., Wada H., Mizutani M., Iwashita M., Ishihara H., Shibano T., Suzuki M., Matsubara Y., Soejima K., Matsumoto M., Fujimura Y., Ikeda Y., Murata M. Blood 104:2081-2083(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT TTP VAL-250, CHARACTERIZATION OF VARIANT TTP VAL-250.
[24]	"Ten candidate ADAMTS13 mutations in six French families with congenital thrombotic thrombocytopenic purpura (Upshaw-Schulman syndrome)." Veyradier A., Lavergne J.M., Ribba A.S., Obert B., Loirat C., Meyer D., Girma J.P. J. Thromb. Haemost. 2:424-429(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS TTP MET-79; PRO-203; PRO-268; GLN-507; VAL-596; ARG-758 AND SER-908.
[25]	"Two novel ADAMTS13 gene mutations in thrombotic thrombocytopenic purpura/hemolytic-uremic syndrome (TTP/HUS)." Licht C., Stapenhorst L., Simon T., Budde U., Schneppenheim R., Hoppe B. Kidney Int. 66:955-958(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT TTP CYS-390.
[26]	"Identification of two novel mutations in ADAMTS13 gene in a patient with hereditary thrombotic thrombocytopenic purpura." Liu F., Jin J., Dong N.Z., Wang Y.G., Ruan C.G. Zhonghua Xue Ye Xue Za Zhi 26:521-524(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS LEU-903 AND TRP-1095.
[27]	"Modulation of ADAMTS13 secretion and specific activity by a combination of common amino acid polymorphisms and a missense mutation." Plaimauer B., Fuhrmann J., Mohr G., Wernhart W., Bruno K., Ferrari S., Konetschny C., Antoine G., Rieger M., Scheiflinger F. Blood 107:118-125(2006) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF VARIANTS TRP-7; GLU-448; ALA-618 AND VAL-732, CHARACTERIZATION OF VARIANT TTP TRP-1336, DISCUSSION ON MUTUAL MODULATORY EFFECTS OF POLYMORPHISMS.
[28]	"Mechanisms of the interaction between two ADAMTS13 gene mutations leading to severe deficiency of enzymatic activity." Peyvandi F., Lavoretano S., Palla R., Valsecchi C., Merati G., De Cristofaro R., Rossi E., Mannuccio Mannucci P. Hum. Mutat. 27:330-336(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS TTP MET-88 AND VAL-1239, CHARACTERIZATION OF VARIANTS TTP MET-88 AND VAL-1239.
[29]	"Novel ADAMTS-13 mutations in an adult with delayed onset thrombotic thrombocytopenic purpura." Tao Z., Anthony K., Peng Y., Choi H., Nolasco L., Rice L., Moake J.L., Dong J.F. J. Thromb. Haemost. 4:1931-1935(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT TTP TRP-1060, CHARACTERIZATION OF VARIANTS TTP TRP-1060.
[30]	"Novel compound heterozygote mutations (H234Q/R1206X) of the ADAMTS13 gene in an adult patient with Upshaw-Schulman syndrome showing predominant episodes of repeated acute renal failure." Shibagaki Y., Matsumoto M., Kokame K., Ohba S., Miyata T., Fujimura Y., Fujita T. Nephrol. Dial. Transplant. 21:1289-1292(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT TTP GLN-234, VARIANT LEU-903.
[31]	"A common origin of the 4143insA ADAMTS13 mutation." Schneppenheim R., Kremer Hovinga J.A., Becker T., Budde U., Karpman D., Brockhaus W., Hrachovinova I., Korczowski B., Oyen F., Rittich S., von Rosen J., Tjonnfjord G.E., Pimanda J.E., Wienker T.F., Lammle B. Thromb. Haemost. 96:3-6(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS TTP ILE-196; CYS-263; SER-347; LEU-353; GLN-507; LEU-671 AND TRP-1060.
[32]	"In-vitro and in-vivo consequences of mutations in the von Willebrand factor cleaving protease ADAMTS13 in thrombotic thrombocytopenic purpura." Donadelli R., Banterla F., Galbusera M., Capoferri C., Bucchioni S., Gastoldi S., Nosari S., Monteferrante G., Ruggeri Z.M., Bresin E., Scheiflinger F., Rossi E., Martinez C., Coppo R., Remuzzi G., Noris M. Thromb. Haemost. 96:454-464(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS TTP TRP-1060; CYS-1123 AND TRP-1219, CHARACTERIZATION OF VARIANTS TTP TRP-1060; CYS-1123 AND TRP-1219, VARIANT GLU-448.
[33]	"A first case of congenital TTP on the African continent due to a new homozygous mutation in the catalytic domain of ADAMTS13." Meyer S.C., Jeddi R., Meddeb B., Gouider E., Lammle B., Kremer Hovinga J.A. Ann. Hematol. 87:663-666(2008) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT TTP PHE-119.
[34]	"Pregnancy-induced thrombocytopenia and TTP, and the risk of fetal death, in Upshaw-Schulman syndrome: a series of 15 pregnancies in 9 genotyped patients." Fujimura Y., Matsumoto M., Kokame K., Isonishi A., Soejima K., Akiyama N., Tomiyama J., Natori K., Kuranishi Y., Imamura Y., Inoue N., Higasa S., Seike M., Kozuka T., Hara M., Wada H., Murata M., Ikeda Y., Miyata T., George J.N. Br. J. Haematol. 144:742-754(2009) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS TTP THR-178; TRP-193; CYS-304; CYS-349; ASP-525 AND PRO-606, VARIANTS ARG-339; GLU-448 AND ALA-618.
[35]	"The first deletion mutation in the TSP1-6 repeat domain of ADAMTS13 in a family with inherited thrombotic thrombocytopenic purpura." Palla R., Lavoretano S., Lombardi R., Garagiola I., Karimi M., Afrasiabi A., Ramzi M., De Cristofaro R., Peyvandi F. Haematologica 94:289-293(2009) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT TTP 977-CYS--ARG-979 DELINS TRP.
[36]	"A novel homozygous missense ADAMTS13 mutation Y658C in a patient with recurrent thrombotic thrombocytopenic purpura." Lee S.H., Park J.H., Park S.K., Lee E.H., Choi J.I., Visentin G.P., Park T.S., Oh S.H., Kim S.R. Ann. Clin. Lab. Sci. 41:273-276(2011) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT TTP CYS-658.
[37]	"ADAMTS13 gene mutations in children with hemolytic uremic syndrome." Choi H.S., Cheong H.I., Kim N.K., Oh D., Park H.W. Yonsei Med. J. 52:530-534(2011) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT LEU-1314.
+	Additional computationally mapped references.

Web resources

Wikipedia

ADAMTS13 entry

GeneReviews

SeattleSNPs

Mendelian genes ADAM metallopeptidase with thrombospondin type 1 motif, 13 (ADAMTS13)

Leiden Open Variation Database (LOVD)

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB069698 mRNA. Translation: BAB69487.2.
AY055376 mRNA. Translation: AAL17652.1.
AF414401 mRNA. Translation: AAL11095.1.
AJ305314 mRNA. Translation: CAC83682.1.
AJ420810 mRNA. Translation: CAD12729.1.
DQ422807 Genomic DNA. Translation: ABD72606.1.
AL158826, AL593848 Genomic DNA. Translation: CAI12850.1.
AL158826, AL593848 Genomic DNA. Translation: CAI12851.1.
AL158826, AL593848 Genomic DNA. Translation: CAI12852.1.
AY358118 mRNA. Translation: AAQ88485.1. Different initiation.
AL136809 mRNA. Translation: CAB66743.1. Different initiation.

IPI

IPI00427822.
IPI00449028.
IPI00453457.

RefSeq

NP_620594.1. NM_139025.3.
NP_620595.1. NM_139026.3.
NP_620596.2. NM_139027.3.

UniGene

Hs.131433.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3GHM	X-ray	2.60	A	287-685	[»]
3GHN	X-ray	2.80	A	287-685	[»]
3VN4	X-ray	2.80	A	287-685	[»]

ProteinModelPortal

Q76LX8.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-36050N.

IntAct

Q76LX8. 1 interaction.

STRING

9606.ENSP00000360997.

Protein family/group databases

MEROPS

M12.241.

PTM databases

PhosphoSite

Q76LX8.

Polymorphism databases

DMDM

74749836.

Proteomic databases

PaxDb

Q76LX8.

PRIDE

Q76LX8.

Protocols and materials databases

DNASU

11093.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000355699; ENSP00000347927; ENSG00000160323.
ENST00000356589; ENSP00000348997; ENSG00000160323.
ENST00000371910; ENSP00000360978; ENSG00000160323.
ENST00000371929; ENSP00000360997; ENSG00000160323.
ENST00000562382; ENSP00000454450; ENSG00000260099.
ENST00000562694; ENSP00000457843; ENSG00000260099.
ENST00000563979; ENSP00000456186; ENSG00000260099.
ENST00000568644; ENSP00000457774; ENSG00000260099.

GeneID

11093.

KEGG

hsa:11093.

UCSC

uc004cdt.1. human.
uc004cdu.1. human.
uc004cdv.4. human.

Organism-specific databases

CTD

11093.

GeneCards

GC09P136279.

HGNC

HGNC:1366. ADAMTS13.

HPA

HPA042014.
HPA042844.

MIM

274150. phenotype.
604134. gene.

neXtProt

NX_Q76LX8.

Orphanet

93583. Congenital thrombotic thrombocytopenic purpura due to ADAMTS-13 deficiency.

PharmGKB

PA24539.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG239882.

HOGENOM

HOG000231627.

HOVERGEN

HBG080358.

InParanoid

Q76LX8.

KO

K08627.

OMA

SWSCLIT.

OrthoDB

EOG4ZS92J.

PhylomeDB

Q76LX8.

Gene expression databases

ArrayExpress

Q76LX8.

Bgee

Q76LX8.

CleanEx

HS_ADAMTS13.

Genevestigator

Q76LX8.

GermOnline

ENSG00000160323. Homo sapiens.

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. 5 hits.
[Graphical view]

PRINTS

PR01857. ADAMTSFAMILY.

SMART

SM00209. TSP1. 7 hits.
[Graphical view]

SUPFAM

SSF49854. CUB. 1 hit.
SSF82895. TSP1. 6 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

EvolutionaryTrace

Q76LX8.

GenomeRNAi

11093.

NextBio

42166.

SOURCE

Search...

Entry information

Entry name

ATS13_HUMAN

Accession

Primary (citable) accession number: Q76LX8
Secondary accession number(s): Q6UY16 , Q710F6, Q711T8, Q96L37, Q9H0G3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 25, 2006
Last sequence update:	July 19, 2004
Last modified:	May 1, 2013
This is version 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.