ATS13_HUMAN
ID ATS13_HUMAN Reviewed; 1427 AA.
AC Q76LX8; Q6UY16; Q710F6; Q711T8; Q96L37; Q9H0G3; Q9UGQ1;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 13;
DE Short=ADAM-TS 13;
DE Short=ADAM-TS13;
DE Short=ADAMTS-13;
DE EC=3.4.24.87 {ECO:0000269|PubMed:11535495};
DE AltName: Full=von Willebrand factor-cleaving protease;
DE Short=vWF-CP;
DE Short=vWF-cleaving protease;
DE Flags: Precursor;
GN Name=ADAMTS13; Synonyms=C9orf8; ORFNames=UNQ6102/PRO20085;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 75-103, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=11574066; DOI=10.1093/oxfordjournals.jbchem.a003009;
RA Soejima K., Mimura N., Hirashima M., Maeda H., Hamamoto T., Nakagaki T.,
RA Nozaki C.;
RT "A novel human metalloprotease synthesized in the liver and secreted into
RT the blood: possibly, the von Willebrand factor-cleaving protease?";
RL J. Biochem. 130:475-480(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), GLYCOSYLATION, AND VARIANT VAL-900.
RC TISSUE=Liver;
RX PubMed=11557746; DOI=10.1074/jbc.c100515200;
RA Zheng X., Chung D., Takayama T.K., Majerus E.M., Sadler J.E., Fujikawa K.;
RT "Structure of von Willebrand factor-cleaving protease (ADAMTS13), a
RT metalloprotease involved in thrombotic thrombocytopenic purpura.";
RL J. Biol. Chem. 276:41059-41063(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INVOLVEMENT IN THROMBOTIC
RP THROMBOCYTOPENIC PURPURA, VARIANTS TTP ASP-96; CYS-102; ILE-196; HIS-398;
RP GLY-528; CYS-692; GLY-951; GLY-1024 AND TYR-1213, AND VARIANTS TRP-7;
RP GLU-448; ALA-618; HIS-625; VAL-732; VAL-900 AND THR-1033.
RC TISSUE=Liver;
RX PubMed=11586351; DOI=10.1038/35097008;
RA Levy G.G., Nichols W.C., Lian E.C., Foroud T., McClintick J.N., McGee B.M.,
RA Yang A.Y., Siemieniak D.R., Stark K.R., Gruppo R., Sarode R., Shurin S.B.,
RA Chandrasekaran V., Stabler S.P., Sabio H., Bouhassira E.E.,
RA Upshaw J.D. Jr., Ginsburg D., Tsai H.-M.;
RT "Mutations in a member of the ADAMTS gene family cause thrombotic
RT thrombocytopenic purpura.";
RL Nature 413:488-494(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Liver;
RX PubMed=11867212; DOI=10.1016/s0378-1119(01)00861-7;
RA Cal S., Obaya A.J., Llamazares M., Garabaya C., Quesada V., Lopez-Otin C.;
RT "Cloning, expression analysis, and structural characterization of seven
RT novel human ADAMTSs, a family of metalloproteinases with disintegrin and
RT thrombospondin-1 domains.";
RL Gene 283:49-62(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RC TISSUE=Brain;
RA Young J.M., Woodward K.J., Aziz S., Burley M., Kwiatkowski D.J., Povey S.;
RT "Cloning of a sugar transporter gene, a G-beta subunit like gene and three
RT novel genes in human chromosome 9q34.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS TRP-7; GLU-448; HIS-456;
RP LEU-457; ALA-618; HIS-625; LYS-740; VAL-900; ARG-982; THR-1033 AND
RP ILE-1226.
RG SeattleSNPs variation discovery resource;
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 275-1427, AND VARIANT GLU-448.
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1191-1427.
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [11]
RP PROTEIN SEQUENCE OF 75-89.
RX PubMed=11535494; DOI=10.1182/blood.v98.6.1654;
RA Gerritsen H.E., Robles R., Laemmle B., Furlan M.;
RT "Partial amino acid sequence of purified von Willebrand factor-cleaving
RT protease.";
RL Blood 98:1654-1661(2001).
RN [12]
RP PROTEIN SEQUENCE OF 75-94, AND CATALYTIC ACTIVITY.
RX PubMed=11535495; DOI=10.1182/blood.v98.6.1662;
RA Fujikawa K., Suzuki H., McMullen B., Chung D.;
RT "Purification of human von Willebrand factor-cleaving protease and its
RT identification as a new member of the metalloproteinase family.";
RL Blood 98:1662-1666(2001).
RN [13]
RP CHARACTERIZATION, AND SUBCELLULAR LOCATION.
RX PubMed=12791682; DOI=10.1074/jbc.m305331200;
RA Zheng X., Nishio K., Majerus E.M., Sadler J.E.;
RT "Cleavage of von Willebrand factor requires the spacer domain of the
RT metalloprotease ADAMTS13.";
RL J. Biol. Chem. 278:30136-30141(2003).
RN [14]
RP ACTIVITY REGULATION, AND MUTAGENESIS OF ARG-71 AND ARG-73.
RX PubMed=12975358; DOI=10.1074/jbc.m309872200;
RA Majerus E.M., Zheng X., Tuley E.A., Sadler J.E.;
RT "Cleavage of the ADAMTS13 propeptide is not required for protease
RT activity.";
RL J. Biol. Chem. 278:46643-46648(2003).
RN [15]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-614; ASN-667 AND ASN-1354.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [16]
RP ACTIVITY REGULATION.
RX PubMed=16286459; DOI=10.1074/jbc.m504540200;
RA Anderson P.J., Kokame K., Sadler J.E.;
RT "Zinc and calcium ions cooperatively modulate ADAMTS13 activity.";
RL J. Biol. Chem. 281:850-857(2006).
RN [17]
RP GLYCOSYLATION AT SER-698; SER-757; SER-907; SER-965; SER-1027 AND SER-1087,
RP IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS OF SER-399; SER-698;
RP SER-757; SER-907; SER-965; SER-1027 AND SER-1087.
RX PubMed=17395589; DOI=10.1074/jbc.m700317200;
RA Ricketts L.M., Dlugosz M., Luther K.B., Haltiwanger R.S., Majerus E.M.;
RT "O-fucosylation is required for ADAMTS13 secretion.";
RL J. Biol. Chem. 282:17014-17023(2007).
RN [18]
RP ACTIVITY REGULATION, CALCIUM-BINDING SITES, AND MUTAGENESIS OF GLU-83;
RP ASP-173; GLU-184; ASP-187 AND GLU-212.
RX PubMed=19047683; DOI=10.1182/blood-2008-03-144683;
RA Gardner M.D., Chion C.K., de Groot R., Shah A., Crawley J.T., Lane D.A.;
RT "A functional calcium-binding site in the metalloprotease domain of
RT ADAMTS13.";
RL Blood 113:1149-1157(2009).
RN [19]
RP GLYCOSYLATION AT ASN-667 AND ASN-707.
RX PubMed=19139490; DOI=10.1074/mcp.m800504-mcp200;
RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B.,
RA Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L.,
RA Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core fucosylated
RT glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
RN [20]
RP REVIEW ON VARIANTS.
RX PubMed=19847791; DOI=10.1002/humu.21143;
RA Lotta L.A., Garagiola I., Palla R., Cairo A., Peyvandi F.;
RT "ADAMTS13 mutations and polymorphisms in congenital thrombotic
RT thrombocytopenic purpura.";
RL Hum. Mutat. 31:11-19(2010).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 287-685, FUNCTION, GLYCOSYLATION
RP AT TRP-387; SER-399; ASN-552 AND ASN-614, SPACER DOMAIN, AND DISULFIDE
RP BONDS.
RX PubMed=19880749; DOI=10.1073/pnas.0909755106;
RA Akiyama M., Takeda S., Kokame K., Takagi J., Miyata T.;
RT "Crystal structures of the noncatalytic domains of ADAMTS13 reveal multiple
RT discontinuous exosites for von Willebrand factor.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:19274-19279(2009).
RN [22]
RP VARIANTS TTP PRO-268 AND TYR-508, VARIANTS GLU-448 AND SER-475,
RP CHARACTERIZATION OF VARIANTS TTP PRO-268 AND TYR-508, AND CHARACTERIZATION
RP OF VARIANTS GLU-448 AND SER-475.
RX PubMed=12181489; DOI=10.1073/pnas.172277399;
RA Kokame K., Matsumoto M., Soejima K., Yagi H., Ishizashi H., Funato M.,
RA Tamai H., Konno M., Kamide K., Kawano Y., Miyata T., Fujimura Y.;
RT "Mutations and common polymorphisms in ADAMTS13 gene responsible for von
RT Willebrand factor-cleaving protease activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:11902-11907(2002).
RN [23]
RP VARIANTS TTP GLN-232; CYS-263 AND LEU-353.
RX PubMed=12393505; DOI=10.1182/blood-2002-08-2399;
RA Schneppenheim R., Budde U., Oyen F., Angerhaus D., Aumann V., Drewke E.,
RA Hassenpflug W., Haberle J., Kentouche K., Kohne E., Kurnik K.,
RA Mueller-Wiefel D., Obser T., Santer R., Sykora K.W.;
RT "von Willebrand factor cleaving protease and ADAMTS13 mutations in
RT childhood TTP.";
RL Blood 101:1845-1850(2003).
RN [24]
RP VARIANT TTP TRP-1336, AND VARIANT VAL-732.
RX PubMed=12614216; DOI=10.1046/j.1365-2141.2003.04183.x;
RA Antoine G., Zimmermann K., Plaimauer B., Grillowitzer M., Studt J.D.,
RA Lammle B., Scheiflinger F.;
RT "ADAMTS13 gene defects in two brothers with constitutional thrombotic
RT thrombocytopenic purpura and normalization of von Willebrand factor-
RT cleaving protease activity by recombinant human ADAMTS13.";
RL Br. J. Haematol. 120:821-824(2003).
RN [25]
RP VARIANTS TTP HIS-235; TYR-311 AND LEU-353, AND VARIANT LEU-457.
RX PubMed=12753286; DOI=10.1046/j.1523-1755.63.6s.1.x;
RA Assink K., Schiphorst R., Allford S., Karpman D., Etzioni A., Brichard B.,
RA van de Kar N., Monnens L., van den Heuvel L.;
RT "Mutation analysis and clinical implications of von Willebrand factor-
RT cleaving protease deficiency.";
RL Kidney Int. 63:1995-1999(2003).
RN [26]
RP VARIANT TTP ILE-196, AND VARIANT GLU-448.
RX PubMed=14512317; DOI=10.1182/blood-2003-04-1346;
RA Pimanda J.E., Maekawa A., Wind T., Paxton J., Chesterman C.N., Hogg P.J.;
RT "Congenital thrombotic thrombocytopenic purpura in association with a
RT mutation in the second CUB domain of ADAMTS13.";
RL Blood 103:627-629(2004).
RN [27]
RP VARIANTS TTP TRP-193; PHE-673; TYR-908 AND CYS-1123, VARIANT GLU-448, AND
RP CHARACTERIZATION OF VARIANTS TTP TRP-193; PHE-673; TYR-908 AND CYS-1123.
RX PubMed=14563640; DOI=10.1182/blood-2003-06-1796;
RA Matsumoto M., Kokame K., Soejima K., Miura M., Hayashi S., Fujii Y.,
RA Iwai A., Ito E., Tsuji Y., Takeda-Shitaka M., Iwadate M., Umeyama H.,
RA Yagi H., Ishizashi H., Banno F., Nakagaki T., Miyata T., Fujimura Y.;
RT "Molecular characterization of ADAMTS13 gene mutations in Japanese patients
RT with Upshaw-Schulman syndrome.";
RL Blood 103:1305-1310(2004).
RN [28]
RP VARIANT TTP VAL-250, AND CHARACTERIZATION OF VARIANT TTP VAL-250.
RX PubMed=15126318; DOI=10.1182/blood-2004-02-0715;
RA Uchida T., Wada H., Mizutani M., Iwashita M., Ishihara H., Shibano T.,
RA Suzuki M., Matsubara Y., Soejima K., Matsumoto M., Fujimura Y., Ikeda Y.,
RA Murata M.;
RT "Identification of novel mutations in ADAMTS13 in an adult patient with
RT congenital thrombotic thrombocytopenic purpura.";
RL Blood 104:2081-2083(2004).
RN [29]
RP VARIANTS TTP MET-79; PRO-203; PRO-268; GLN-507; VAL-596; ARG-758 AND
RP SER-908.
RX PubMed=15009458; DOI=10.1111/j.1538-7933.2004.00623.x;
RA Veyradier A., Lavergne J.M., Ribba A.S., Obert B., Loirat C., Meyer D.,
RA Girma J.P.;
RT "Ten candidate ADAMTS13 mutations in six French families with congenital
RT thrombotic thrombocytopenic purpura (Upshaw-Schulman syndrome).";
RL J. Thromb. Haemost. 2:424-429(2004).
RN [30]
RP VARIANT TTP CYS-390.
RX PubMed=15327386; DOI=10.1111/j.1523-1755.2004.00841.x;
RA Licht C., Stapenhorst L., Simon T., Budde U., Schneppenheim R., Hoppe B.;
RT "Two novel ADAMTS13 gene mutations in thrombotic thrombocytopenic
RT purpura/hemolytic-uremic syndrome (TTP/HUS).";
RL Kidney Int. 66:955-958(2004).
RN [31]
RP VARIANTS LEU-903 AND TRP-1095.
RX PubMed=16468327;
RA Liu F., Jin J., Dong N.Z., Wang Y.G., Ruan C.G.;
RT "Identification of two novel mutations in ADAMTS13 gene in a patient with
RT hereditary thrombotic thrombocytopenic purpura.";
RL Zhonghua Xue Ye Xue Za Zhi 26:521-524(2005).
RN [32]
RP CHARACTERIZATION OF VARIANTS TRP-7; GLU-448; ALA-618 AND VAL-732,
RP CHARACTERIZATION OF VARIANT TTP TRP-1336, AND DISCUSSION OF MUTUAL
RP MODULATORY EFFECTS OF POLYMORPHISMS.
RX PubMed=16160007; DOI=10.1182/blood-2005-06-2482;
RA Plaimauer B., Fuhrmann J., Mohr G., Wernhart W., Bruno K., Ferrari S.,
RA Konetschny C., Antoine G., Rieger M., Scheiflinger F.;
RT "Modulation of ADAMTS13 secretion and specific activity by a combination of
RT common amino acid polymorphisms and a missense mutation.";
RL Blood 107:118-125(2006).
RN [33]
RP VARIANTS TTP MET-88 AND VAL-1239, AND CHARACTERIZATION OF VARIANTS TTP
RP MET-88 AND VAL-1239.
RX PubMed=16453338; DOI=10.1002/humu.20267;
RA Peyvandi F., Lavoretano S., Palla R., Valsecchi C., Merati G.,
RA De Cristofaro R., Rossi E., Mannuccio Mannucci P.;
RT "Mechanisms of the interaction between two ADAMTS13 gene mutations leading
RT to severe deficiency of enzymatic activity.";
RL Hum. Mutat. 27:330-336(2006).
RN [34]
RP VARIANT TTP TRP-1060, AND CHARACTERIZATION OF VARIANTS TTP TRP-1060.
RX PubMed=16796708; DOI=10.1111/j.1538-7836.2006.02098.x;
RA Tao Z., Anthony K., Peng Y., Choi H., Nolasco L., Rice L., Moake J.L.,
RA Dong J.F.;
RT "Novel ADAMTS-13 mutations in an adult with delayed onset thrombotic
RT thrombocytopenic purpura.";
RL J. Thromb. Haemost. 4:1931-1935(2006).
RN [35]
RP VARIANT TTP GLN-234, AND VARIANT LEU-903.
RX PubMed=16449289; DOI=10.1093/ndt/gfk072;
RA Shibagaki Y., Matsumoto M., Kokame K., Ohba S., Miyata T., Fujimura Y.,
RA Fujita T.;
RT "Novel compound heterozygote mutations (H234Q/R1206X) of the ADAMTS13 gene
RT in an adult patient with Upshaw-Schulman syndrome showing predominant
RT episodes of repeated acute renal failure.";
RL Nephrol. Dial. Transplant. 21:1289-1292(2006).
RN [36]
RP VARIANTS TTP ILE-196; CYS-263; SER-347; LEU-353; GLN-507; LEU-671 AND
RP TRP-1060.
RX PubMed=16807643; DOI=10.1160/th05-12-0817;
RA Schneppenheim R., Kremer Hovinga J.A., Becker T., Budde U., Karpman D.,
RA Brockhaus W., Hrachovinova I., Korczowski B., Oyen F., Rittich S.,
RA von Rosen J., Tjonnfjord G.E., Pimanda J.E., Wienker T.F., Lammle B.;
RT "A common origin of the 4143insA ADAMTS13 mutation.";
RL Thromb. Haemost. 96:3-6(2006).
RN [37]
RP VARIANTS TTP TRP-1060; CYS-1123 AND TRP-1219, CHARACTERIZATION OF VARIANTS
RP TTP TRP-1060; CYS-1123 AND TRP-1219, AND VARIANT GLU-448.
RX PubMed=17003922; DOI=10.1160/th06-05-0236;
RA Donadelli R., Banterla F., Galbusera M., Capoferri C., Bucchioni S.,
RA Gastoldi S., Nosari S., Monteferrante G., Ruggeri Z.M., Bresin E.,
RA Scheiflinger F., Rossi E., Martinez C., Coppo R., Remuzzi G., Noris M.;
RT "In-vitro and in-vivo consequences of mutations in the von Willebrand
RT factor cleaving protease ADAMTS13 in thrombotic thrombocytopenic purpura.";
RL Thromb. Haemost. 96:454-464(2006).
RN [38]
RP VARIANT TTP PHE-119.
RX PubMed=18443791; DOI=10.1007/s00277-008-0496-6;
RA Meyer S.C., Jeddi R., Meddeb B., Gouider E., Lammle B.,
RA Kremer Hovinga J.A.;
RT "A first case of congenital TTP on the African continent due to a new
RT homozygous mutation in the catalytic domain of ADAMTS13.";
RL Ann. Hematol. 87:663-666(2008).
RN [39]
RP VARIANTS TTP THR-178; TRP-193; CYS-304; CYS-349; ASP-525 AND PRO-606, AND
RP VARIANTS ARG-339; GLU-448 AND ALA-618.
RX PubMed=19055667; DOI=10.1111/j.1365-2141.2008.07515.x;
RA Fujimura Y., Matsumoto M., Kokame K., Isonishi A., Soejima K., Akiyama N.,
RA Tomiyama J., Natori K., Kuranishi Y., Imamura Y., Inoue N., Higasa S.,
RA Seike M., Kozuka T., Hara M., Wada H., Murata M., Ikeda Y., Miyata T.,
RA George J.N.;
RT "Pregnancy-induced thrombocytopenia and TTP, and the risk of fetal death,
RT in Upshaw-Schulman syndrome: a series of 15 pregnancies in 9 genotyped
RT patients.";
RL Br. J. Haematol. 144:742-754(2009).
RN [40]
RP VARIANT TTP 977-CYS--ARG-979 DELINS TRP.
RX PubMed=19116307; DOI=10.3324/haematol.13524;
RA Palla R., Lavoretano S., Lombardi R., Garagiola I., Karimi M.,
RA Afrasiabi A., Ramzi M., De Cristofaro R., Peyvandi F.;
RT "The first deletion mutation in the TSP1-6 repeat domain of ADAMTS13 in a
RT family with inherited thrombotic thrombocytopenic purpura.";
RL Haematologica 94:289-293(2009).
RN [41]
RP VARIANT TTP CYS-658.
RX PubMed=22075512;
RA Lee S.H., Park J.H., Park S.K., Lee E.H., Choi J.I., Visentin G.P.,
RA Park T.S., Oh S.H., Kim S.R.;
RT "A novel homozygous missense ADAMTS13 mutation Y658C in a patient with
RT recurrent thrombotic thrombocytopenic purpura.";
RL Ann. Clin. Lab. Sci. 41:273-276(2011).
RN [42]
RP VARIANT LEU-1314.
RX PubMed=21488199; DOI=10.3349/ymj.2011.52.3.530;
RA Choi H.S., Cheong H.I., Kim N.K., Oh D., Park H.W.;
RT "ADAMTS13 gene mutations in children with hemolytic uremic syndrome.";
RL Yonsei Med. J. 52:530-534(2011).
CC -!- FUNCTION: Cleaves the vWF multimers in plasma into smaller forms
CC thereby controlling vWF-mediated platelet thrombus formation.
CC {ECO:0000269|PubMed:19880749}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=The enzyme cleaves the von Willebrand factor at bond 842-
CC Tyr-|-Met-843 within the A2 domain.; EC=3.4.24.87;
CC Evidence={ECO:0000269|PubMed:11535495};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q9UNA0};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9UNA0};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:19047683};
CC Note=Binds 4 Ca(2+) ions. {ECO:0000269|PubMed:19047683};
CC -!- ACTIVITY REGULATION: Zinc and calcium ions cooperatively modulate
CC enzyme activity. The cleavage of the pro-domain is not required for
CC protease activity. Dependence on calcium for proteolytic activity is
CC mediated by the high affinity site. {ECO:0000269|PubMed:12975358,
CC ECO:0000269|PubMed:16286459, ECO:0000269|PubMed:19047683}.
CC -!- INTERACTION:
CC Q76LX8; P04275: VWF; NbExp=19; IntAct=EBI-981764, EBI-981819;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12791682}.
CC Note=Secretion enhanced by O-fucosylation of TSP type-1 repeats.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q76LX8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q76LX8-2; Sequence=VSP_020003;
CC Name=3;
CC IsoId=Q76LX8-3; Sequence=VSP_020002, VSP_020003;
CC Name=4;
CC IsoId=Q76LX8-4; Sequence=VSP_055537, VSP_055538, VSP_055539;
CC -!- TISSUE SPECIFICITY: Plasma. Expressed primarily in liver.
CC {ECO:0000269|PubMed:11574066}.
CC -!- DOMAIN: The pro-domain is not required for folding or secretion and
CC does not perform the common function of maintening enzyme latency.
CC -!- DOMAIN: The globular cysteineless spacer domain adopts a jelly-roll
CC topology, and is necessary to recognize and cleave vWF. The C-terminal
CC TSP type-1 and CUB domains may modulate this interaction.
CC -!- PTM: Glycosylated. O-fucosylated by POFUT2 on a serine or a threonine
CC residue found within the consensus sequence C1-X(2)-(S/T)-C2-G of the
CC TSP type-1 repeat domains where C1 and C2 are the first and second
CC cysteine residue of the repeat, respectively. Fucosylated repeats can
CC then be further glycosylated by the addition of a beta-1,3-glucose
CC residue by the glucosyltransferase, B3GALTL. Fucosylation mediates the
CC efficient secretion of ADAMTS13. May also be C-glycosylated on
CC tryptophan residues within the consensus sequence W-X-X-W of the TPRs,
CC and also N-glycosylated. These other glycosylations can also facilitate
CC secretion. {ECO:0000269|PubMed:11557746, ECO:0000269|PubMed:16335952,
CC ECO:0000269|PubMed:17395589, ECO:0000269|PubMed:19139490,
CC ECO:0000269|PubMed:19880749}.
CC -!- PTM: The precursor is processed by a furin endopeptidase which cleaves
CC off the pro-domain.
CC -!- POLYMORPHISM: Genetic variations in ADAMTS13 coding region influence
CC plasmatic ADAMTS13 activity levels. Dependent on the sequence context,
CC the same polymorphisms might be either positive or negative modifiers
CC of gene expression, thereby altering the phenotype of ADAMTS13
CC deficiency. {ECO:0000305|PubMed:16160007}.
CC -!- DISEASE: Thrombotic thrombocytopenic purpura, hereditary (TTP)
CC [MIM:274150]: An autosomal recessive hematologic disease characterized
CC by hemolytic anemia with fragmentation of erythrocytes,
CC thrombocytopenia, diffuse and non-focal neurologic findings, decreased
CC renal function and fever. {ECO:0000269|PubMed:11586351,
CC ECO:0000269|PubMed:12181489, ECO:0000269|PubMed:12393505,
CC ECO:0000269|PubMed:12614216, ECO:0000269|PubMed:12753286,
CC ECO:0000269|PubMed:14512317, ECO:0000269|PubMed:14563640,
CC ECO:0000269|PubMed:15009458, ECO:0000269|PubMed:15126318,
CC ECO:0000269|PubMed:15327386, ECO:0000269|PubMed:16160007,
CC ECO:0000269|PubMed:16449289, ECO:0000269|PubMed:16453338,
CC ECO:0000269|PubMed:16796708, ECO:0000269|PubMed:16807643,
CC ECO:0000269|PubMed:17003922, ECO:0000269|PubMed:18443791,
CC ECO:0000269|PubMed:19055667, ECO:0000269|PubMed:19116307,
CC ECO:0000269|PubMed:22075512}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAQ88485.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB66743.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Wikipedia; Note=ADAMTS13 entry;
CC URL="https://en.wikipedia.org/wiki/ADAMTS13";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/adamts13/";
CC -!- WEB RESOURCE: Name=Mendelian genes ADAM metallopeptidase with
CC thrombospondin type 1 motif, 13 (ADAMTS13); Note=Leiden Open Variation
CC Database (LOVD);
CC URL="https://databases.lovd.nl/shared/genes/ADAMTS13";
CC ---------------------------------------------------------------------------
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DR EMBL; AB069698; BAB69487.2; -; mRNA.
DR EMBL; AY055376; AAL17652.1; -; mRNA.
DR EMBL; AF414401; AAL11095.1; -; mRNA.
DR EMBL; AJ305314; CAC83682.1; -; mRNA.
DR EMBL; AJ420810; CAD12729.1; -; mRNA.
DR EMBL; AJ011374; CAB66157.1; -; mRNA.
DR EMBL; DQ422807; ABD72606.1; -; Genomic_DNA.
DR EMBL; AL158826; CAI12850.1; -; Genomic_DNA.
DR EMBL; AL593848; CAI12850.1; JOINED; Genomic_DNA.
DR EMBL; AL158826; CAI12851.1; -; Genomic_DNA.
DR EMBL; AL593848; CAI12851.1; JOINED; Genomic_DNA.
DR EMBL; AL158826; CAI12852.1; -; Genomic_DNA.
DR EMBL; AL593848; CAI12852.1; JOINED; Genomic_DNA.
DR EMBL; CH471090; EAW88086.1; -; Genomic_DNA.
DR EMBL; AY358118; AAQ88485.1; ALT_INIT; mRNA.
DR EMBL; AL136809; CAB66743.1; ALT_INIT; mRNA.
DR CCDS; CCDS6970.1; -. [Q76LX8-1]
DR CCDS; CCDS6971.1; -. [Q76LX8-3]
DR CCDS; CCDS6972.1; -. [Q76LX8-2]
DR RefSeq; NP_620594.1; NM_139025.4. [Q76LX8-1]
DR RefSeq; NP_620595.1; NM_139026.4. [Q76LX8-3]
DR RefSeq; NP_620596.2; NM_139027.4. [Q76LX8-2]
DR PDB; 3GHM; X-ray; 2.60 A; A=287-685.
DR PDB; 3GHN; X-ray; 2.80 A; A=287-685.
DR PDB; 3VN4; X-ray; 2.80 A; A=287-685.
DR PDB; 6QIG; X-ray; 2.80 A; A=79-682.
DR PDB; 7B01; X-ray; 2.80 A; A=1185-1427.
DR PDBsum; 3GHM; -.
DR PDBsum; 3GHN; -.
DR PDBsum; 3VN4; -.
DR PDBsum; 6QIG; -.
DR PDBsum; 7B01; -.
DR AlphaFoldDB; Q76LX8; -.
DR SASBDB; Q76LX8; -.
DR SMR; Q76LX8; -.
DR BioGRID; 116274; 24.
DR DIP; DIP-36050N; -.
DR IntAct; Q76LX8; 2.
DR STRING; 9606.ENSP00000360997; -.
DR BindingDB; Q76LX8; -.
DR ChEMBL; CHEMBL2346492; -.
DR DrugBank; DB13133; Von Willebrand factor human.
DR DrugBank; DB12872; Vonicog alfa.
DR MEROPS; M12.241; -.
DR GlyConnect; 637; 10 N-Linked glycans (5 sites), 1 O-Linked glycan (3 sites).
DR GlyGen; Q76LX8; 27 sites, 10 N-linked glycans (5 sites), 4 O-linked glycans (11 sites).
DR iPTMnet; Q76LX8; -.
DR PhosphoSitePlus; Q76LX8; -.
DR BioMuta; ADAMTS13; -.
DR DMDM; 74749836; -.
DR EPD; Q76LX8; -.
DR MassIVE; Q76LX8; -.
DR PaxDb; Q76LX8; -.
DR PeptideAtlas; Q76LX8; -.
DR PRIDE; Q76LX8; -.
DR ProteomicsDB; 68682; -. [Q76LX8-1]
DR ProteomicsDB; 68683; -. [Q76LX8-2]
DR ProteomicsDB; 68684; -. [Q76LX8-3]
DR ProteomicsDB; 84255; -.
DR ABCD; Q76LX8; 61 sequenced antibodies.
DR Antibodypedia; 31871; 382 antibodies from 36 providers.
DR DNASU; 11093; -.
DR Ensembl; ENST00000355699.7; ENSP00000347927.2; ENSG00000160323.19. [Q76LX8-2]
DR Ensembl; ENST00000356589.6; ENSP00000348997.2; ENSG00000160323.19. [Q76LX8-3]
DR Ensembl; ENST00000371929.7; ENSP00000360997.3; ENSG00000160323.19. [Q76LX8-1]
DR Ensembl; ENST00000626597.2; ENSP00000486201.1; ENSG00000281244.2. [Q76LX8-1]
DR Ensembl; ENST00000626744.2; ENSP00000486734.1; ENSG00000281244.2. [Q76LX8-2]
DR Ensembl; ENST00000630465.2; ENSP00000485989.1; ENSG00000281244.2. [Q76LX8-3]
DR GeneID; 11093; -.
DR KEGG; hsa:11093; -.
DR MANE-Select; ENST00000355699.7; ENSP00000347927.2; NM_139027.6; NP_620596.2. [Q76LX8-2]
DR UCSC; uc004cdv.6; human. [Q76LX8-1]
DR CTD; 11093; -.
DR DisGeNET; 11093; -.
DR GeneCards; ADAMTS13; -.
DR HGNC; HGNC:1366; ADAMTS13.
DR HPA; ENSG00000160323; Tissue enriched (liver).
DR MalaCards; ADAMTS13; -.
DR MIM; 274150; phenotype.
DR MIM; 604134; gene.
DR neXtProt; NX_Q76LX8; -.
DR OpenTargets; ENSG00000160323; -.
DR Orphanet; 93583; Congenital thrombotic thrombocytopenic purpura.
DR PharmGKB; PA24539; -.
DR VEuPathDB; HostDB:ENSG00000160323; -.
DR eggNOG; KOG3538; Eukaryota.
DR GeneTree; ENSGT00940000158379; -.
DR HOGENOM; CLU_000660_10_1_1; -.
DR InParanoid; Q76LX8; -.
DR OMA; HQAHQED; -.
DR OrthoDB; 125522at2759; -.
DR PhylomeDB; Q76LX8; -.
DR TreeFam; TF313537; -.
DR BRENDA; 3.4.24.87; 2681.
DR PathwayCommons; Q76LX8; -.
DR Reactome; R-HSA-5083635; Defective B3GALTL causes PpS.
DR Reactome; R-HSA-5173214; O-glycosylation of TSR domain-containing proteins.
DR SignaLink; Q76LX8; -.
DR SIGNOR; Q76LX8; -.
DR BioGRID-ORCS; 11093; 10 hits in 1074 CRISPR screens.
DR ChiTaRS; ADAMTS13; human.
DR EvolutionaryTrace; Q76LX8; -.
DR GeneWiki; ADAMTS13; -.
DR GenomeRNAi; 11093; -.
DR Pharos; Q76LX8; Tbio.
DR PRO; PR:Q76LX8; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q76LX8; protein.
DR Bgee; ENSG00000160323; Expressed in right lobe of liver and 93 other tissues.
DR ExpressionAtlas; Q76LX8; baseline and differential.
DR Genevisible; Q76LX8; HS.
DR GO; GO:0009986; C:cell surface; NAS:UniProtKB.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; TAS:UniProtKB.
DR GO; GO:0005178; F:integrin binding; TAS:UniProtKB.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0008237; F:metallopeptidase activity; TAS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; TAS:UniProtKB.
DR GO; GO:0007160; P:cell-matrix adhesion; NAS:UniProtKB.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IEA:Ensembl.
DR GO; GO:0071353; P:cellular response to interleukin-4; IEA:Ensembl.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0009100; P:glycoprotein metabolic process; NAS:UniProtKB.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; NAS:UniProtKB.
DR GO; GO:0043171; P:peptide catabolic process; IDA:UniProtKB.
DR GO; GO:0030168; P:platelet activation; NAS:UniProtKB.
DR GO; GO:0030163; P:protein catabolic process; IEA:Ensembl.
DR GO; GO:0016485; P:protein processing; TAS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR GO; GO:0014075; P:response to amine; IEA:Ensembl.
DR GO; GO:0035864; P:response to potassium ion; IEA:Ensembl.
DR GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
DR Gene3D; 2.20.100.10; -; 5.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR006586; ADAM_Cys-rich.
DR InterPro; IPR013273; ADAMTS/ADAMTS-like.
DR InterPro; IPR041645; ADAMTS_CR_2.
DR InterPro; IPR045371; ADAMTS_CR_3.
DR InterPro; IPR010294; ADAMTS_spacer1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR Pfam; PF17771; ADAM_CR_2; 1.
DR Pfam; PF19236; ADAM_CR_3; 1.
DR Pfam; PF05986; ADAM_spacer1; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00608; ACR; 1.
DR SMART; SM00209; TSP1; 7.
DR SUPFAM; SSF49854; SSF49854; 2.
DR SUPFAM; SSF82895; SSF82895; 5.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50092; TSP1; 4.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Blood coagulation; Calcium;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Disease variant; Disulfide bond; Glycoprotein; Hemostasis; Hydrolase;
KW Metal-binding; Metalloprotease; Protease; Reference proteome; Repeat;
KW Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT PROPEP 30..74
FT /evidence="ECO:0000269|PubMed:11535494,
FT ECO:0000269|PubMed:11535495, ECO:0000269|PubMed:11574066"
FT /id="PRO_0000247510"
FT CHAIN 75..1427
FT /note="A disintegrin and metalloproteinase with
FT thrombospondin motifs 13"
FT /id="PRO_0000247511"
FT DOMAIN 80..286
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 287..383
FT /note="Disintegrin"
FT DOMAIN 384..439
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 682..730
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 742..805
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 808..859
FT /note="TSP type-1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 896..950
FT /note="TSP type-1 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 951..1011
FT /note="TSP type-1 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1012..1068
FT /note="TSP type-1 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1072..1131
FT /note="TSP type-1 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1192..1298
FT /note="CUB 1"
FT DOMAIN 1299..1427
FT /note="CUB 2"
FT REGION 51..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..556
FT /note="Cysteine-rich"
FT REGION 556..685
FT /note="Spacer"
FT MOTIF 498..500
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT ACT_SITE 225
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 83
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 173
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 182
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="high affinity"
FT /evidence="ECO:0000269|PubMed:19047683"
FT BINDING 184
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="high affinity"
FT /evidence="ECO:0000269|PubMed:19047683"
FT BINDING 187
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="high affinity"
FT /evidence="ECO:0000269|PubMed:19047683"
FT BINDING 212
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="high affinity"
FT /evidence="ECO:0000269|PubMed:19047683"
FT BINDING 224
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9UNA0"
FT BINDING 228
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9UNA0"
FT BINDING 234
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9UNA0"
FT BINDING 281
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 284
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 387
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0007744|PDB:3VN4"
FT CARBOHYD 399
FT /note="O-linked (Fuc...) serine"
FT /evidence="ECO:0007744|PDB:3GHM, ECO:0007744|PDB:3GHN,
FT ECO:0007744|PDB:3VN4"
FT CARBOHYD 552
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19880749,
FT ECO:0007744|PDB:3GHM, ECO:0007744|PDB:3VN4"
FT CARBOHYD 579
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 614
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19880749, ECO:0007744|PDB:3GHM,
FT ECO:0007744|PDB:3GHN, ECO:0007744|PDB:3VN4"
FT CARBOHYD 667
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19139490"
FT CARBOHYD 698
FT /note="O-linked (Fuc...) serine"
FT /evidence="ECO:0000269|PubMed:17395589"
FT CARBOHYD 707
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:19139490"
FT CARBOHYD 757
FT /note="O-linked (Fuc...) serine"
FT /evidence="ECO:0000269|PubMed:17395589"
FT CARBOHYD 828
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 907
FT /note="O-linked (Fuc...) serine"
FT /evidence="ECO:0000269|PubMed:17395589"
FT CARBOHYD 965
FT /note="O-linked (Fuc...) serine"
FT /evidence="ECO:0000269|PubMed:17395589"
FT CARBOHYD 1027
FT /note="O-linked (Fuc...) serine"
FT /evidence="ECO:0000269|PubMed:17395589"
FT CARBOHYD 1087
FT /note="O-linked (Fuc...) serine"
FT /evidence="ECO:0000269|PubMed:17395589"
FT CARBOHYD 1235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT DISULFID 155..208
FT /evidence="ECO:0000250"
FT DISULFID 202..281
FT /evidence="ECO:0000250"
FT DISULFID 242..265
FT /evidence="ECO:0000250"
FT DISULFID 311..337
FT /evidence="ECO:0000269|PubMed:19880749,
FT ECO:0007744|PDB:3GHM, ECO:0007744|PDB:3GHN,
FT ECO:0007744|PDB:3VN4"
FT DISULFID 322..347
FT /evidence="ECO:0000269|PubMed:19880749,
FT ECO:0007744|PDB:3GHM, ECO:0007744|PDB:3GHN,
FT ECO:0007744|PDB:3VN4"
FT DISULFID 332..366
FT /evidence="ECO:0000269|PubMed:19880749,
FT ECO:0007744|PDB:3GHM, ECO:0007744|PDB:3GHN,
FT ECO:0007744|PDB:3VN4"
FT DISULFID 360..371
FT /evidence="ECO:0000269|PubMed:19880749,
FT ECO:0007744|PDB:3GHM, ECO:0007744|PDB:3GHN,
FT ECO:0007744|PDB:3VN4"
FT DISULFID 396..433
FT /evidence="ECO:0000269|PubMed:19880749,
FT ECO:0007744|PDB:3GHM, ECO:0007744|PDB:3GHN,
FT ECO:0007744|PDB:3VN4"
FT DISULFID 400..438
FT /evidence="ECO:0000269|PubMed:19880749,
FT ECO:0007744|PDB:3GHM, ECO:0007744|PDB:3GHN,
FT ECO:0007744|PDB:3VN4"
FT DISULFID 411..423
FT /evidence="ECO:0000269|PubMed:19880749,
FT ECO:0007744|PDB:3GHM, ECO:0007744|PDB:3GHN,
FT ECO:0007744|PDB:3VN4"
FT DISULFID 450..487
FT /evidence="ECO:0007744|PDB:3GHM, ECO:0007744|PDB:3GHN,
FT ECO:0007744|PDB:3VN4"
FT DISULFID 483..522
FT /evidence="ECO:0000269|PubMed:19880749,
FT ECO:0007744|PDB:3GHM, ECO:0007744|PDB:3GHN,
FT ECO:0007744|PDB:3VN4"
FT DISULFID 508..527
FT /evidence="ECO:0000269|PubMed:19880749,
FT ECO:0007744|PDB:3GHM, ECO:0007744|PDB:3GHN,
FT ECO:0007744|PDB:3VN4"
FT DISULFID 532..548
FT /evidence="ECO:0000269|PubMed:19880749,
FT ECO:0007744|PDB:3GHM, ECO:0007744|PDB:3GHN,
FT ECO:0007744|PDB:3VN4"
FT DISULFID 545..555
FT /evidence="ECO:0000269|PubMed:19880749,
FT ECO:0007744|PDB:3GHM, ECO:0007744|PDB:3GHN,
FT ECO:0007744|PDB:3VN4"
FT VAR_SEQ 2..329
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_055537"
FT VAR_SEQ 275..305
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11867212"
FT /id="VSP_020002"
FT VAR_SEQ 658..692
FT /note="YRRYGEEYGNLTRPDITFTYFQPKPRQAWVWAAVR -> GGVRAQLMHISWW
FT SRPGLGERDLCARGRWPGGSSD (in isoform 4)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_055538"
FT VAR_SEQ 693..1427
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_055539"
FT VAR_SEQ 1135..1190
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:11867212"
FT /id="VSP_020003"
FT VARIANT 7
FT /note="R -> W (does not affect protein secretion;
FT dbSNP:rs34024143)"
FT /evidence="ECO:0000269|PubMed:11586351,
FT ECO:0000269|PubMed:16160007, ECO:0000269|Ref.6"
FT /id="VAR_027109"
FT VARIANT 79
FT /note="I -> M (in TTP; dbSNP:rs281875297)"
FT /evidence="ECO:0000269|PubMed:15009458"
FT /id="VAR_067770"
FT VARIANT 88
FT /note="V -> M (in TTP; reduces protein secretion and
FT proteolytic activity; dbSNP:rs281875302)"
FT /evidence="ECO:0000269|PubMed:16453338"
FT /id="VAR_027110"
FT VARIANT 96
FT /note="H -> D (in TTP; dbSNP:rs121908467)"
FT /evidence="ECO:0000269|PubMed:11586351"
FT /id="VAR_027111"
FT VARIANT 102
FT /note="R -> C (in TTP; dbSNP:rs121908469)"
FT /evidence="ECO:0000269|PubMed:11586351"
FT /id="VAR_027112"
FT VARIANT 119
FT /note="S -> F (in TTP; dbSNP:rs281875291)"
FT /evidence="ECO:0000269|PubMed:18443791"
FT /id="VAR_067771"
FT VARIANT 178
FT /note="I -> T (in TTP; dbSNP:rs281875289)"
FT /evidence="ECO:0000269|PubMed:19055667"
FT /id="VAR_067772"
FT VARIANT 193
FT /note="R -> W (in TTP; low activity; dbSNP:rs281875287)"
FT /evidence="ECO:0000269|PubMed:14563640,
FT ECO:0000269|PubMed:19055667"
FT /id="VAR_027113"
FT VARIANT 196
FT /note="T -> I (in TTP; dbSNP:rs121908470)"
FT /evidence="ECO:0000269|PubMed:11586351,
FT ECO:0000269|PubMed:14512317, ECO:0000269|PubMed:16807643"
FT /id="VAR_027114"
FT VARIANT 203
FT /note="S -> P (in TTP; dbSNP:rs281875298)"
FT /evidence="ECO:0000269|PubMed:15009458"
FT /id="VAR_067773"
FT VARIANT 232
FT /note="L -> Q (in TTP; dbSNP:rs281875292)"
FT /evidence="ECO:0000269|PubMed:12393505"
FT /id="VAR_067774"
FT VARIANT 234
FT /note="H -> Q (in TTP; dbSNP:rs281875304)"
FT /evidence="ECO:0000269|PubMed:16449289"
FT /id="VAR_027115"
FT VARIANT 235
FT /note="D -> H (in TTP; dbSNP:rs281875337)"
FT /evidence="ECO:0000269|PubMed:12753286"
FT /id="VAR_067775"
FT VARIANT 250
FT /note="A -> V (in TTP; mild effect on protein secretion;
FT strong reduction of proteolytic activity;
FT dbSNP:rs121908478)"
FT /evidence="ECO:0000269|PubMed:15126318"
FT /id="VAR_027116"
FT VARIANT 263
FT /note="S -> C (in TTP; dbSNP:rs281875293)"
FT /evidence="ECO:0000269|PubMed:12393505,
FT ECO:0000269|PubMed:16807643"
FT /id="VAR_067776"
FT VARIANT 268
FT /note="R -> P (in TTP; affects protein secretion;
FT dbSNP:rs121908477)"
FT /evidence="ECO:0000269|PubMed:12181489,
FT ECO:0000269|PubMed:15009458"
FT /id="VAR_027117"
FT VARIANT 304
FT /note="Y -> C (in TTP; dbSNP:rs281875285)"
FT /evidence="ECO:0000269|PubMed:19055667"
FT /id="VAR_067777"
FT VARIANT 311
FT /note="C -> Y (in TTP; dbSNP:rs281875336)"
FT /evidence="ECO:0000269|PubMed:12753286"
FT /id="VAR_067778"
FT VARIANT 339
FT /note="T -> R (in dbSNP:rs149517360)"
FT /evidence="ECO:0000269|PubMed:19055667"
FT /id="VAR_067779"
FT VARIANT 347
FT /note="C -> S (in TTP; dbSNP:rs281875294)"
FT /evidence="ECO:0000269|PubMed:16807643"
FT /id="VAR_067780"
FT VARIANT 349
FT /note="R -> C (in TTP; dbSNP:rs281875288)"
FT /evidence="ECO:0000269|PubMed:19055667"
FT /id="VAR_067781"
FT VARIANT 353
FT /note="P -> L (in TTP; dbSNP:rs281875338)"
FT /evidence="ECO:0000269|PubMed:12393505,
FT ECO:0000269|PubMed:12753286, ECO:0000269|PubMed:16807643"
FT /id="VAR_067782"
FT VARIANT 390
FT /note="W -> C (in TTP; dbSNP:rs281875306)"
FT /evidence="ECO:0000269|PubMed:15327386"
FT /id="VAR_027118"
FT VARIANT 398
FT /note="R -> H (in TTP; dbSNP:rs121908471)"
FT /evidence="ECO:0000269|PubMed:11586351"
FT /id="VAR_027119"
FT VARIANT 448
FT /note="Q -> E (does not affect protein secretion; normal
FT proteolytic activity; dbSNP:rs2301612)"
FT /evidence="ECO:0000269|PubMed:11586351,
FT ECO:0000269|PubMed:12181489, ECO:0000269|PubMed:12975309,
FT ECO:0000269|PubMed:14512317, ECO:0000269|PubMed:14563640,
FT ECO:0000269|PubMed:16160007, ECO:0000269|PubMed:17003922,
FT ECO:0000269|PubMed:19055667, ECO:0000269|Ref.6"
FT /id="VAR_027120"
FT VARIANT 456
FT /note="Q -> H (in dbSNP:rs36220239)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_027162"
FT VARIANT 457
FT /note="P -> L (in dbSNP:rs36220240)"
FT /evidence="ECO:0000269|PubMed:12753286, ECO:0000269|Ref.6"
FT /id="VAR_027163"
FT VARIANT 475
FT /note="P -> S (in dbSNP:rs11575933)"
FT /evidence="ECO:0000269|PubMed:12181489"
FT /id="VAR_027121"
FT VARIANT 507
FT /note="R -> Q (in TTP; dbSNP:rs281875296)"
FT /evidence="ECO:0000269|PubMed:15009458,
FT ECO:0000269|PubMed:16807643"
FT /id="VAR_067783"
FT VARIANT 508
FT /note="C -> Y (in TTP; impairs protein secretion;
FT dbSNP:rs281875305)"
FT /evidence="ECO:0000269|PubMed:12181489"
FT /id="VAR_027122"
FT VARIANT 525
FT /note="G -> D (in TTP; dbSNP:rs281875286)"
FT /evidence="ECO:0000269|PubMed:19055667"
FT /id="VAR_067784"
FT VARIANT 528
FT /note="R -> G (in TTP; dbSNP:rs121908473)"
FT /evidence="ECO:0000269|PubMed:11586351"
FT /id="VAR_027123"
FT VARIANT 596
FT /note="A -> V (in TTP; dbSNP:rs281875299)"
FT /evidence="ECO:0000269|PubMed:15009458"
FT /id="VAR_067785"
FT VARIANT 606
FT /note="A -> P (in TTP; dbSNP:rs281875290)"
FT /evidence="ECO:0000269|PubMed:19055667"
FT /id="VAR_067786"
FT VARIANT 618
FT /note="P -> A (in dbSNP:rs28647808)"
FT /evidence="ECO:0000269|PubMed:11586351,
FT ECO:0000269|PubMed:16160007, ECO:0000269|PubMed:19055667,
FT ECO:0000269|Ref.6"
FT /id="VAR_027124"
FT VARIANT 625
FT /note="R -> H (in dbSNP:rs36090624)"
FT /evidence="ECO:0000269|PubMed:11586351, ECO:0000269|Ref.6"
FT /id="VAR_027125"
FT VARIANT 658
FT /note="Y -> C (in TTP; dbSNP:rs281875335)"
FT /evidence="ECO:0000269|PubMed:22075512"
FT /id="VAR_067787"
FT VARIANT 671
FT /note="P -> L (in TTP; dbSNP:rs281875295)"
FT /evidence="ECO:0000269|PubMed:16807643"
FT /id="VAR_067788"
FT VARIANT 673
FT /note="I -> F (in TTP; impairs protein secretion;
FT dbSNP:rs281875307)"
FT /evidence="ECO:0000269|PubMed:14563640"
FT /id="VAR_027126"
FT VARIANT 692
FT /note="R -> C (in TTP; dbSNP:rs121908475)"
FT /evidence="ECO:0000269|PubMed:11586351"
FT /id="VAR_027127"
FT VARIANT 732
FT /note="A -> V (in dbSNP:rs41314453)"
FT /evidence="ECO:0000269|PubMed:11586351,
FT ECO:0000269|PubMed:12614216, ECO:0000269|PubMed:16160007"
FT /id="VAR_027128"
FT VARIANT 740
FT /note="E -> K (in dbSNP:rs36221451)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_027164"
FT VARIANT 758
FT /note="C -> R (in TTP; dbSNP:rs281875300)"
FT /evidence="ECO:0000269|PubMed:15009458"
FT /id="VAR_067789"
FT VARIANT 900
FT /note="A -> V (in dbSNP:rs685523)"
FT /evidence="ECO:0000269|PubMed:11557746,
FT ECO:0000269|PubMed:11586351, ECO:0000269|Ref.6"
FT /id="VAR_027129"
FT VARIANT 903
FT /note="S -> L (in dbSNP:rs78977446)"
FT /evidence="ECO:0000269|PubMed:16449289,
FT ECO:0000269|PubMed:16468327"
FT /id="VAR_027130"
FT VARIANT 908
FT /note="C -> S (in TTP; dbSNP:rs281875301)"
FT /evidence="ECO:0000269|PubMed:15009458"
FT /id="VAR_067790"
FT VARIANT 908
FT /note="C -> Y (in TTP; impairs protein secretion;
FT dbSNP:rs281875301)"
FT /evidence="ECO:0000269|PubMed:14563640"
FT /id="VAR_027131"
FT VARIANT 951
FT /note="C -> G (in TTP; dbSNP:rs121908468)"
FT /evidence="ECO:0000269|PubMed:11586351"
FT /id="VAR_027132"
FT VARIANT 977..979
FT /note="CAR -> W (in TTP)"
FT /evidence="ECO:0000269|PubMed:19116307"
FT /id="VAR_067791"
FT VARIANT 982
FT /note="G -> R (in dbSNP:rs36222275)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_027165"
FT VARIANT 1024
FT /note="C -> G (in TTP; dbSNP:rs121908472)"
FT /evidence="ECO:0000269|PubMed:11586351"
FT /id="VAR_027133"
FT VARIANT 1033
FT /note="A -> T (in dbSNP:rs28503257)"
FT /evidence="ECO:0000269|PubMed:11586351, ECO:0000269|Ref.6"
FT /id="VAR_027134"
FT VARIANT 1060
FT /note="R -> W (in TTP; affects protein secretion; the
FT mutant protein has reduced protease activity;
FT dbSNP:rs142572218)"
FT /evidence="ECO:0000269|PubMed:16796708,
FT ECO:0000269|PubMed:16807643, ECO:0000269|PubMed:17003922"
FT /id="VAR_067792"
FT VARIANT 1095
FT /note="R -> W (in a patient with thrombotic
FT thrombocytopenic purpura; dbSNP:rs782383410)"
FT /evidence="ECO:0000269|PubMed:16468327"
FT /id="VAR_027135"
FT VARIANT 1123
FT /note="R -> C (in TTP; impairs protein secretion; the
FT mutant protein has reduced protease activity;
FT dbSNP:rs281875340)"
FT /evidence="ECO:0000269|PubMed:14563640,
FT ECO:0000269|PubMed:17003922"
FT /id="VAR_027136"
FT VARIANT 1213
FT /note="C -> Y (in TTP; dbSNP:rs121908474)"
FT /evidence="ECO:0000269|PubMed:11586351"
FT /id="VAR_027137"
FT VARIANT 1219
FT /note="R -> W (in TTP; affects protein secretion; the
FT mutant protein has reduced protease activity;
FT dbSNP:rs281875339)"
FT /evidence="ECO:0000269|PubMed:17003922"
FT /id="VAR_067793"
FT VARIANT 1226
FT /note="T -> I (in dbSNP:rs36222894)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_027166"
FT VARIANT 1239
FT /note="G -> V (in TTP; impairs protein secretion;
FT dbSNP:rs281875303)"
FT /evidence="ECO:0000269|PubMed:16453338"
FT /id="VAR_027138"
FT VARIANT 1314
FT /note="S -> L (found in a patient with hemolytic uremic
FT syndrome; dbSNP:rs142060916)"
FT /evidence="ECO:0000269|PubMed:21488199"
FT /id="VAR_067794"
FT VARIANT 1336
FT /note="R -> W (in TTP; impairs protein secretion and
FT proteolytic activity; dbSNP:rs281875308)"
FT /evidence="ECO:0000269|PubMed:12614216,
FT ECO:0000269|PubMed:16160007"
FT /id="VAR_027139"
FT MUTAGEN 71
FT /note="R->K: Abolishes pro-domain removal but no loss of
FT proteolytic activity; when associated with D-73."
FT /evidence="ECO:0000269|PubMed:12975358"
FT MUTAGEN 73
FT /note="R->D: Abolishes pro-domain removal but no loss of
FT proteolytic activity; when associated with K-71."
FT /evidence="ECO:0000269|PubMed:12975358"
FT MUTAGEN 83
FT /note="E->A: No change in calcium dependence for
FT proteolysis."
FT /evidence="ECO:0000269|PubMed:19047683"
FT MUTAGEN 173
FT /note="D->A: No change in calcium dependence for
FT proteolysis."
FT /evidence="ECO:0000269|PubMed:19047683"
FT MUTAGEN 184
FT /note="E->A: Dramatically reduced affinity for calcium."
FT /evidence="ECO:0000269|PubMed:19047683"
FT MUTAGEN 187
FT /note="D->A: Dramatically reduced affinity for calcium."
FT /evidence="ECO:0000269|PubMed:19047683"
FT MUTAGEN 212
FT /note="E->A: Dramatically reduced affinity for calcium."
FT /evidence="ECO:0000269|PubMed:19047683"
FT MUTAGEN 399
FT /note="S->A: No effect on cleavage of VWF and little change
FT in secretion of ADAMTS13. Abolishes secretion of ADAMTS13;
FT when associated with A-698."
FT /evidence="ECO:0000269|PubMed:17395589"
FT MUTAGEN 698
FT /note="S->A: No effect on cleavage of VWF and greatly
FT reduced secretion of ADAMTS13. Abolishes secretion of
FT ADAMTS13; when associated with A-399."
FT /evidence="ECO:0000269|PubMed:17395589"
FT MUTAGEN 757
FT /note="S->A: No effect on cleavage of VWF and little change
FT in secretion of ADAMTS13."
FT /evidence="ECO:0000269|PubMed:17395589"
FT MUTAGEN 907
FT /note="S->A: No effect on cleavage of VWF and greatly
FT reduced secretion of ADAMTS13. Abolishes most of the
FT secretion of ADAMTS13; when associated with A-965."
FT /evidence="ECO:0000269|PubMed:17395589"
FT MUTAGEN 965
FT /note="S->A: No effect on cleavage of VWF and little change
FT in secretion of ADAMTS13. Abolishes most of the secretion
FT of ADAMTS13; when associated with A-907."
FT /evidence="ECO:0000269|PubMed:17395589"
FT MUTAGEN 1027
FT /note="S->A: No effect on cleavage of VWF and little change
FT in secretion of ADAMTS13. Abolishes most of the secretion
FT of ADAMTS13; when associated with A-1087."
FT /evidence="ECO:0000269|PubMed:17395589"
FT MUTAGEN 1087
FT /note="S->A: No effect on cleavage of VWF and little change
FT in secretion of ADAMTS13. Abolishes most of the secretion
FT of ADAMTS13; when associated with A-1027."
FT /evidence="ECO:0000269|PubMed:17395589"
FT CONFLICT 101
FT /note="E -> R (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 80..88
FT /evidence="ECO:0007829|PDB:6QIG"
FT HELIX 90..95
FT /evidence="ECO:0007829|PDB:6QIG"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:6QIG"
FT HELIX 100..114
FT /evidence="ECO:0007829|PDB:6QIG"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:6QIG"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:6QIG"
FT HELIX 147..157
FT /evidence="ECO:0007829|PDB:6QIG"
FT TURN 158..160
FT /evidence="ECO:0007829|PDB:6QIG"
FT STRAND 173..179
FT /evidence="ECO:0007829|PDB:6QIG"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:6QIG"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:6QIG"
FT STRAND 209..212
FT /evidence="ECO:0007829|PDB:6QIG"
FT HELIX 218..230
FT /evidence="ECO:0007829|PDB:6QIG"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:6QIG"
FT HELIX 264..275
FT /evidence="ECO:0007829|PDB:6QIG"
FT HELIX 301..303
FT /evidence="ECO:0007829|PDB:3GHM"
FT HELIX 307..314
FT /evidence="ECO:0007829|PDB:3GHM"
FT STRAND 327..329
FT /evidence="ECO:0007829|PDB:6QIG"
FT HELIX 331..334
FT /evidence="ECO:0007829|PDB:3GHN"
FT STRAND 337..340
FT /evidence="ECO:0007829|PDB:3GHM"
FT STRAND 348..351
FT /evidence="ECO:0007829|PDB:3VN4"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:3GHM"
FT STRAND 364..367
FT /evidence="ECO:0007829|PDB:3GHM"
FT STRAND 370..373
FT /evidence="ECO:0007829|PDB:3GHM"
FT HELIX 374..377
FT /evidence="ECO:0007829|PDB:3GHM"
FT STRAND 399..401
FT /evidence="ECO:0007829|PDB:3GHM"
FT STRAND 403..406
FT /evidence="ECO:0007829|PDB:3GHM"
FT STRAND 417..419
FT /evidence="ECO:0007829|PDB:3GHM"
FT STRAND 430..433
FT /evidence="ECO:0007829|PDB:3GHM"
FT HELIX 442..451
FT /evidence="ECO:0007829|PDB:3GHM"
FT TURN 452..455
FT /evidence="ECO:0007829|PDB:3GHM"
FT STRAND 470..472
FT /evidence="ECO:0007829|PDB:3GHM"
FT TURN 474..476
FT /evidence="ECO:0007829|PDB:3GHM"
FT HELIX 479..483
FT /evidence="ECO:0007829|PDB:3GHM"
FT STRAND 486..489
FT /evidence="ECO:0007829|PDB:3GHM"
FT STRAND 495..497
FT /evidence="ECO:0007829|PDB:3GHM"
FT STRAND 519..523
FT /evidence="ECO:0007829|PDB:3GHM"
FT STRAND 526..530
FT /evidence="ECO:0007829|PDB:3GHM"
FT STRAND 534..536
FT /evidence="ECO:0007829|PDB:3GHM"
FT STRAND 554..562
FT /evidence="ECO:0007829|PDB:3GHM"
FT STRAND 569..576
FT /evidence="ECO:0007829|PDB:3GHM"
FT STRAND 581..588
FT /evidence="ECO:0007829|PDB:3GHM"
FT STRAND 592..599
FT /evidence="ECO:0007829|PDB:3GHM"
FT STRAND 602..605
FT /evidence="ECO:0007829|PDB:3GHM"
FT STRAND 608..610
FT /evidence="ECO:0007829|PDB:3GHM"
FT STRAND 614..618
FT /evidence="ECO:0007829|PDB:3GHM"
FT STRAND 623..632
FT /evidence="ECO:0007829|PDB:3GHM"
FT STRAND 634..636
FT /evidence="ECO:0007829|PDB:3GHM"
FT STRAND 638..647
FT /evidence="ECO:0007829|PDB:3GHM"
FT STRAND 653..661
FT /evidence="ECO:0007829|PDB:3GHM"
FT HELIX 663..665
FT /evidence="ECO:0007829|PDB:3GHM"
FT HELIX 667..669
FT /evidence="ECO:0007829|PDB:3GHN"
FT STRAND 673..680
FT /evidence="ECO:0007829|PDB:3GHM"
FT STRAND 1199..1204
FT /evidence="ECO:0007829|PDB:7B01"
FT STRAND 1209..1212
FT /evidence="ECO:0007829|PDB:7B01"
FT STRAND 1216..1218
FT /evidence="ECO:0007829|PDB:7B01"
FT STRAND 1223..1232
FT /evidence="ECO:0007829|PDB:7B01"
FT STRAND 1236..1239
FT /evidence="ECO:0007829|PDB:7B01"
FT STRAND 1241..1245
FT /evidence="ECO:0007829|PDB:7B01"
FT STRAND 1261..1263
FT /evidence="ECO:0007829|PDB:7B01"
FT STRAND 1265..1274
FT /evidence="ECO:0007829|PDB:7B01"
FT STRAND 1282..1290
FT /evidence="ECO:0007829|PDB:7B01"
FT TURN 1297..1299
FT /evidence="ECO:0007829|PDB:7B01"
FT STRAND 1305..1311
FT /evidence="ECO:0007829|PDB:7B01"
FT STRAND 1317..1319
FT /evidence="ECO:0007829|PDB:7B01"
FT STRAND 1326..1328
FT /evidence="ECO:0007829|PDB:7B01"
FT STRAND 1336..1344
FT /evidence="ECO:0007829|PDB:7B01"
FT STRAND 1357..1361
FT /evidence="ECO:0007829|PDB:7B01"
FT STRAND 1369..1373
FT /evidence="ECO:0007829|PDB:7B01"
FT STRAND 1375..1380
FT /evidence="ECO:0007829|PDB:7B01"
FT STRAND 1382..1384
FT /evidence="ECO:0007829|PDB:7B01"
FT STRAND 1387..1390
FT /evidence="ECO:0007829|PDB:7B01"
FT HELIX 1392..1396
FT /evidence="ECO:0007829|PDB:7B01"
FT STRAND 1400..1409
FT /evidence="ECO:0007829|PDB:7B01"
SQ SEQUENCE 1427 AA; 153604 MW; A2103AFABC1A4445 CRC64;
MHQRHPRARC PPLCVAGILA CGFLLGCWGP SHFQQSCLQA LEPQAVSSYL SPGAPLKGRP
PSPGFQRQRQ RQRRAAGGIL HLELLVAVGP DVFQAHQEDT ERYVLTNLNI GAELLRDPSL
GAQFRVHLVK MVILTEPEGA PNITANLTSS LLSVCGWSQT INPEDDTDPG HADLVLYITR
FDLELPDGNR QVRGVTQLGG ACSPTWSCLI TEDTGFDLGV TIAHEIGHSF GLEHDGAPGS
GCGPSGHVMA SDGAAPRAGL AWSPCSRRQL LSLLSAGRAR CVWDPPRPQP GSAGHPPDAQ
PGLYYSANEQ CRVAFGPKAV ACTFAREHLD MCQALSCHTD PLDQSSCSRL LVPLLDGTEC
GVEKWCSKGR CRSLVELTPI AAVHGRWSSW GPRSPCSRSC GGGVVTRRRQ CNNPRPAFGG
RACVGADLQA EMCNTQACEK TQLEFMSQQC ARTDGQPLRS SPGGASFYHW GAAVPHSQGD
ALCRHMCRAI GESFIMKRGD SFLDGTRCMP SGPREDGTLS LCVSGSCRTF GCDGRMDSQQ
VWDRCQVCGG DNSTCSPRKG SFTAGRAREY VTFLTVTPNL TSVYIANHRP LFTHLAVRIG
GRYVVAGKMS ISPNTTYPSL LEDGRVEYRV ALTEDRLPRL EEIRIWGPLQ EDADIQVYRR
YGEEYGNLTR PDITFTYFQP KPRQAWVWAA VRGPCSVSCG AGLRWVNYSC LDQARKELVE
TVQCQGSQQP PAWPEACVLE PCPPYWAVGD FGPCSASCGG GLRERPVRCV EAQGSLLKTL
PPARCRAGAQ QPAVALETCN PQPCPARWEV SEPSSCTSAG GAGLALENET CVPGADGLEA
PVTEGPGSVD EKLPAPEPCV GMSCPPGWGH LDATSAGEKA PSPWGSIRTG AQAAHVWTPA
AGSCSVSCGR GLMELRFLCM DSALRVPVQE ELCGLASKPG SRREVCQAVP CPARWQYKLA
ACSVSCGRGV VRRILYCARA HGEDDGEEIL LDTQCQGLPR PEPQEACSLE PCPPRWKVMS
LGPCSASCGL GTARRSVACV QLDQGQDVEV DEAACAALVR PEASVPCLIA DCTYRWHVGT
WMECSVSCGD GIQRRRDTCL GPQAQAPVPA DFCQHLPKPV TVRGCWAGPC VGQGTPSLVP
HEEAAAPGRT TATPAGASLE WSQARGLLFS PAPQPRRLLP GPQENSVQSS ACGRQHLEPT
GTIDMRGPGQ ADCAVAIGRP LGEVVTLRVL ESSLNCSAGD MLLLWGRLTW RKMCRKLLDM
TFSSKTNTLV VRQRCGRPGG GVLLRYGSQL APETFYRECD MQLFGPWGEI VSPSLSPATS
NAGGCRLFIN VAPHARIAIH ALATNMGAGT EGANASYILI RDTHSLRTTA FHGQQVLYWE
SESSQAEMEF SEGFLKAQAS LRGQYWTLQS WVPEMQDPQS WKGKEGT
