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Antithrombin-III (ATIII) (Serpin C1)

 ANT3_HUMAN              Reviewed;         464 AA.
P01008; B2R6P0; P78439; P78447; Q13815; Q5TC78; Q7KZ43; Q7KZ97;
Q9UC78;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
27-SEP-2017, entry version 224.
RecName: Full=Antithrombin-III;
Short=ATIII;
AltName: Full=Serpin C1;
Flags: Precursor;
Name=SERPINC1; Synonyms=AT3; ORFNames=PRO0309;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6298709; DOI=10.1093/nar/10.24.8113;
Bock S.C., Wion K.L., Vehar G.A., Lawn R.M.;
"Cloning and expression of the cDNA for human antithrombin III.";
Nucleic Acids Res. 10:8113-8125(1982).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6572945; DOI=10.1073/pnas.80.7.1845;
Chandra T., Stackhouse R., Kidd V.J., Woo S.L.C.;
"Isolation and sequence characterization of a cDNA clone of human
antithrombin III.";
Proc. Natl. Acad. Sci. U.S.A. 80:1845-1848(1983).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT AT3D MET-438.
Tsuji H., Takada O., Nakagawa M., Tanaka S., Hashimoto-Gotoh T.;
"Hereditary antithrombin III deficiency: identification of an
arginine-406 to methionine point mutation near protease reactive
site.";
(In) Yoshida T.O., Wilson J.M. (eds.);
Molecular approaches to the study and treatment of Human diseases,
pp.51-55, Elsevier, Amsterdam (1992).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8476848; DOI=10.1021/bi00067a008;
Olds R.J., Lane D.A., Chowdhury V., de Stefano V., Leone G.,
Thein S.L.;
"Complete nucleotide sequence of the antithrombin gene: evidence for
homologous recombination causing thrombophilia.";
Biochemistry 32:4216-4224(1993).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Fetal liver;
Zhang C., Yu Y., Zhang S., Wei H., Bi J., Zhou G., Dong C., Zai Y.,
Xu W., Gao F., Liu M., He F.;
"Functional prediction of the coding sequences of 75 new genes deduced
by analysis of cDNA clones from human fetal liver.";
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLU-30 AND ALA-147.
SeattleSNPs variation discovery resource;
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[10]
PROTEIN SEQUENCE OF 33-464, GLYCOSYLATION AT ASN-128; ASN-167; ASN-187
AND ASN-224, AND DISULFIDE BONDS.
Petersen T.E., Dudek-Wojciechowska G., Sottrup-Jensen L.,
Magnusson S.;
"Primary structure of antithrombin-III (heparin cofactor). Partial
homology between alpha-1-antitrypsin and antithrombin-III.";
(In) Collen D., Wiman B., Verstraete M. (eds.);
The physiological inhibitors of blood coagulation and fibrinolysis,
pp.43-54, Elsevier, Amsterdam (1979).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 42-464.
PubMed=6305982;
Prochownik E.V., Markham A.F., Orkin S.H.;
"Isolation of a cDNA clone for human antithrombin III.";
J. Biol. Chem. 258:8389-8394(1983).
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 137-208, AND VARIANT AT3D
LEU-439.
PubMed=3191114; DOI=10.1021/bi00416a052;
Bock S.C., Marrinan J.A., Radziejewska E.;
"Antithrombin III Utah: proline-407 to leucine mutation in a highly
conserved region near the inhibitor reactive site.";
Biochemistry 27:6171-6178(1988).
[13]
PROTEIN SEQUENCE OF 371-425, MASS SPECTROMETRY, AND VARIANT AT3D
THR-414.
TISSUE=Plasma;
PubMed=7734359; DOI=10.1111/j.1365-2141.1995.tb08368.x;
Lindo V.S., Kakkar V.V., Learmonth M., Melissari E., Zappacosta F.,
Panico M., Morris H.R.;
"Antithrombin-TRI (Ala382 to Thr) causing severe thromboembolic
tendency undergoes the S-to-R transition and is associated with a
plasma-inactive high-molecular-weight complex of aggregated
antithrombin.";
Br. J. Haematol. 89:589-601(1995).
[14]
REACTIVE SITE.
PubMed=7238875; DOI=10.1016/0014-5793(81)80255-4;
Bjoerk I., Danielsson A., Fenton J.W. II, Joernvall H.;
"The site in human antithrombin for functional proteolytic cleavage by
human thrombin.";
FEBS Lett. 126:257-260(1981).
[15]
HEPARIN-BINDING SITE.
PubMed=6693405;
Blackburn M.N., Smith R.L., Carson J., Sibley C.C.;
"The heparin-binding site of antithrombin III. Identification of a
critical tryptophan in the amino acid sequence.";
J. Biol. Chem. 259:939-941(1984).
[16]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-187.
TISSUE=Bile;
PubMed=15084671; DOI=10.1074/mcp.M400015-MCP200;
Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H.,
Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A.;
"A proteomic analysis of human bile.";
Mol. Cell. Proteomics 3:715-728(2004).
[17]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-128 AND ASN-187.
TISSUE=Plasma;
PubMed=14760718; DOI=10.1002/pmic.200300556;
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
"Screening for N-glycosylated proteins by liquid chromatography mass
spectrometry.";
Proteomics 4:454-465(2004).
[18]
FUNCTION IN MEMBRANE-ANCHORED SERINE PROTEASE TMPRSS7 INHIBITION, AND
HETERODIMER WITH TMPRSS7.
PubMed=15853774; DOI=10.1042/BJ20050299;
Szabo R., Netzel-Arnett S., Hobson J.P., Antalis T.M., Bugge T.H.;
"Matriptase-3 is a novel phylogenetically preserved membrane-anchored
serine protease with broad serpin reactivity.";
Biochem. J. 390:231-242(2005).
[19]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-128; ASN-187 AND ASN-224.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[20]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-224.
TISSUE=Platelet;
PubMed=16263699; DOI=10.1074/mcp.M500324-MCP200;
Lewandrowski U., Moebius J., Walter U., Sickmann A.;
"Elucidation of N-glycosylation sites on human platelet proteins: a
glycoproteomic approach.";
Mol. Cell. Proteomics 5:226-233(2006).
[21]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-128 AND ASN-187.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[22]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-187, AND STRUCTURE OF
CARBOHYDRATES.
TISSUE=Cerebrospinal fluid;
PubMed=19838169; DOI=10.1038/nmeth.1392;
Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E.,
Brinkmalm G., Larson G.;
"Enrichment of glycopeptides for glycan structure and attachment site
identification.";
Nat. Methods 6:809-811(2009).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[25]
PHOSPHORYLATION AT THR-63 AND SER-68.
PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
Pinna L.A., Pagliarini D.J., Dixon J.E.;
"A single kinase generates the majority of the secreted
phosphoproteome.";
Cell 161:1619-1632(2015).
[26]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
PubMed=8087553; DOI=10.1016/S0969-2126(00)00028-9;
Carrell R.W., Stein P.E., Fermi G., Wardell M.R.;
"Biological implications of a 3 A structure of dimeric antithrombin.";
Structure 2:257-270(1994).
[27]
X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS).
PubMed=7656006; DOI=10.1038/nsb0194-48;
Schreuder H.A., de Boer B., Dijkema R., Mulders J., Theunissen H.J.M.,
Grootenhuis P.D.J., Hol W.G.J.;
"The intact and cleaved human antithrombin III complex as a model for
serpin-proteinase interactions.";
Nat. Struct. Biol. 1:48-54(1994).
[28]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
PubMed=9067613; DOI=10.1006/jmbi.1996.0798;
Skinner R., Abrahams J.P., Whisstock J.C., Lesk A.M., Carrel R.W.,
Wardell M.R.;
"The 2.6 A structure of antithrombin indicates a conformational change
at the heparin binding site.";
J. Mol. Biol. 266:601-609(1997).
[29]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
PubMed=9761669; DOI=10.1006/jmbi.1998.2083;
Skinner R., Chang W.-S.W., Jin L., Pei X.Y., Huntington J.A.,
Abrahams J.P., Carrell R.W., Lomas D.A.;
"Implications for function and therapy of a 2.9 A structure of binary-
complexed antithrombin.";
J. Mol. Biol. 283:9-14(1998).
[30]
REVIEW.
PubMed=2126464; DOI=10.1016/0300-9084(90)90123-X;
Mourey L., Samama J.-P., Delarue M., Choay J., Lormeau J.C.,
Petitou M., Moras D.;
"Antithrombin III: structural and functional aspects.";
Biochimie 72:599-608(1990).
[31]
REVIEW ON VARIANTS.
PubMed=8236149;
Lane D.A., Olds R.J., Boisclair M., Chowdhury V., Thein S.L.,
Cooper D.N., Blajchman M., Perry D., Emmerich J., Aiach M.;
"Antithrombin III mutation database: first update. For the Thrombin
and its Inhibitors Subcommittee of the Scientific and Standardization
Committee of the International Society on Thrombosis and
Haemostasis.";
Thromb. Haemost. 70:361-369(1993).
[32]
REVIEW ON VARIANTS.
PubMed=7749926; DOI=10.1038/nsb0295-96;
Stein P.E., Carrell R.W.;
"What do dysfunctional serpins tell us about molecular mobility and
disease?";
Nat. Struct. Biol. 2:96-113(1995).
[33]
REVIEW ON VARIANTS.
PubMed=8664906;
DOI=10.1002/(SICI)1098-1004(1996)7:1<7::AID-HUMU2>3.3.CO;2-A;
Perry D.J., Carrell R.W.;
"Molecular genetics of human antithrombin deficiency.";
Hum. Mutat. 7:7-22(1996).
[34]
VARIANTS AT3D SER-17; PRO-23; ASN-39; CYS-56; LEU-73; CYS-79; HIS-79;
SER-79; ASN-87 DEL; CYS-89; LEU-90; CYS-95; SER-95; PRO-98; THR-112;
PHE-131; VAL-131; LYS-133; PHE-138-139-LYS DEL; PRO-148; PRO-150;
PRO-158; TYR-160; GLN-161; CYS-198; HIS-198; ILE-218 DEL; ASP-219;
LYS-219; ARG-257; LYS-269; ILE-283; ASN-316; LYS-334; ARG-412;
THR-414; PRO-416; SER-416; VAL-419; ASP-424; CYS-425; HIS-425;
PRO-425; LEU-426; CYS-434; LEU-434; SER-434; THR-436; LYS-437;
GLY-438; MET-438; LEU-439; THR-439; THR-453; ARG-456; THR-457;
ASP-459; LEU-461 AND PHE-462, AND VARIANTS GLU-30; THR-52 AND CYS-190.
PubMed=9031473;
The plasma coagulation inhibitors subcommittee of the scientific and standardization committee of the international society on thrombosis and haemostasis;
Lane D.A., Bayston T., Olds R.J., Fitches A.C., Cooper D.N.,
Millar D.S., Jochmans K., Perry D.J., Okajima K., Thein S.L.,
Emmerich J.;
"Antithrombin mutation database: 2nd (1997) update.";
Thromb. Haemost. 77:197-211(1997).
[35]
VARIANT AT3D CYS-79.
PubMed=6582486; DOI=10.1073/pnas.81.2.289;
Koide T., Odani S., Takahashi K., Ono T., Sakuragawa N.;
"Antithrombin III Toyama: replacement of arginine-47 by cysteine in
hereditary abnormal antithrombin III that lacks heparin-binding
ability.";
Proc. Natl. Acad. Sci. U.S.A. 81:289-293(1984).
[36]
VARIANT AT3D LEU-73, AND CHARACTERIZATION OF VARIANT AT3D LEU-73.
PubMed=3080419;
Chang J.Y., Tran T.H.;
"Antithrombin III Basel. Identification of a Pro-Leu substitution in a
hereditary abnormal antithrombin with impaired heparin cofactor
activity.";
J. Biol. Chem. 261:1174-1176(1986).
[37]
VARIANT AT3D LEU-426.
PubMed=3805013;
Stephens A.W., Thalley B.S., Hirs C.H.W.;
"Antithrombin-III Denver, a reactive site variant.";
J. Biol. Chem. 262:1044-1048(1987).
[38]
VARIANT AT3D THR-414.
PubMed=3179438;
Devrak-Kizuk R., Chui D.H.K., Prochownik E.V., Carter C.J.,
Ofosu F.A., Blajchman M.A.;
"Antithrombin-III-Hamilton: a gene with a point mutation (guanine to
adenine) in codon 382 causing impaired serine protease reactivity.";
Blood 72:1518-1523(1988).
[39]
VARIANTS AT3D CYS-425 AND HIS-425.
PubMed=3162733;
Erdjument H., Laned D.A., Panico M., di Marzo V., Morris H.R.;
"Single amino acid substitutions in the reactive site of antithrombin
leading to thrombosis. Congenital substitution of arginine 393 to
cysteine in antithrombin Northwick Park and to histidine in
antithrombin Glasgow.";
J. Biol. Chem. 263:5589-5593(1988).
[40]
VARIANT AT3D HIS-425.
PubMed=2781509; DOI=10.1016/0049-3848(89)90127-8;
Erdjument H., Lane D.A., Panico M., di Marzo V., Morris H.R.,
Bauer K., Rosenberg R.D.;
"Antithrombin Chicago, amino acid substitution of arginine 393 to
histidine.";
Thromb. Res. 54:613-619(1989).
[41]
VARIANT AT3D CYS-56.
PubMed=2365065; DOI=10.1016/0014-5793(90)81530-2;
Borg J.Y., Brennan S.O., Carrell R.W., George P., Perry D.J., Shaw J.;
"Antithrombin Rouen-IV 24 Arg-->Cys. The amino-terminal contribution
to heparin binding.";
FEBS Lett. 266:163-166(1990).
[42]
VARIANT GLU-30.
PubMed=1977621; DOI=10.1016/0014-5793(90)81057-U;
Daly M., Bruce D., Perry D.J., Price J., Harper P.L., O'Meara A.,
Carrell R.W.;
"Antithrombin Dublin (-3 Val-->Glu): an N-terminal variant which has
an aberrant signal peptidase cleavage site.";
FEBS Lett. 273:87-90(1990).
[43]
VARIANT AT3D GLN-161.
PubMed=2229057;
Gandrille S., Aiach M., Lane D.A., Vidaud D., Molho-Sabatier P.,
Caso R., de Moerloose P., Fiessinger J.-N., Clauser E.;
"Important role of arginine 129 in heparin-binding site of
antithrombin III. Identification of a novel mutation arginine 129 to
glutamine.";
J. Biol. Chem. 265:18997-19001(1990).
[44]
CHARACTERIZATION OF VARIANT AT3D THR-414, AND MUTAGENESIS OF ALA-414.
PubMed=2013320; DOI=10.1016/0014-5793(91)80305-M;
Austin R.C., Rachubinski R.A., Blachjman M.A.;
"Site-directed mutagenesis of alanine-382 of human antithrombin III.";
FEBS Lett. 280:254-258(1991).
[45]
VARIANT AT3D SER-416.
PubMed=1906811; DOI=10.1016/0014-5793(91)80809-H;
Perry D.J., Daly M., Harper P.L., Tait R.C., Price J., Walker I.D.,
Carrell R.W.;
"Antithrombin Cambridge II, 384 Ala to Ser. Further evidence of the
role of the reactive centre loop in the inhibitory function of the
serpins.";
FEBS Lett. 285:248-250(1991).
[46]
VARIANT AT3D PHE-131.
PubMed=1555650; DOI=10.1016/0014-5793(92)80854-A;
Olds R.J., Lane D.A., Boisclair M., Sas G., Bock S.C., Thein S.L.;
"Antithrombin Budapest 3. An antithrombin variant with reduced heparin
affinity resulting from the substitution L99F.";
FEBS Lett. 300:241-246(1992).
[47]
VARIANT AT3D ASP-424.
PubMed=1547341;
Blajchman M.A., Fernandez-Rachubinski F., Sheffield W.P., Austin R.C.,
Schulman S.;
"Antithrombin-III Stockholm: a codon 392 (Gly-->Asp) mutation with
normal heparin binding and impaired serine protease reactivity.";
Blood 79:1428-1434(1992).
[48]
VARIANT AT3D PRO-148.
PubMed=8443391;
Okajima K., Abe H., Maeda S., Motomura M., Tsujihata M., Nagataki S.,
Okabe H., Takatsuki K.;
"Antithrombin III Nagasaki (Ser116-Pro): a heterozygous variant with
defective heparin binding associated with thrombosis.";
Blood 81:1300-1305(1993).
[49]
VARIANT AT3D 138-PHE-LYS-139 DEL.
PubMed=8486379; DOI=10.1006/geno.1993.1184;
Olds R.J., Lane D.A., Beresford C.H., Abildgaard U., Hughes P.M.,
Thein S.L.;
"A recurrent deletion in the antithrombin gene, AT106-108(-6 bp),
identified by DNA heteroduplex detection.";
Genomics 16:298-299(1993).
[50]
VARIANTS AT3D HIS-79 AND TYR-160.
PubMed=7981186;
Emmerich J., Vidaud D., Alhenc-Gelas M., Chadeuf G.,
Gouault-Heilmann M., Aillaud M.-F., Aiach M.;
"Three novel mutations of antithrombin inducing high-molecular-mass
compounds.";
Arterioscler. Thromb. 14:1958-1965(1994).
[51]
VARIANTS AT3D THR-112; TYR-152 AND ILE-283, AND VARIANT CYS-190.
PubMed=7959685; DOI=10.1007/BF00211016;
Millar D.S., Wacey A.I., Ribando J., Melissari E., Laursen B.,
Woods P., Kakkar V.V., Cooper D.N.;
"Three novel missense mutations in the antithrombin III (AT3) gene
causing recurrent venous thrombosis.";
Hum. Genet. 94:509-512(1994).
[52]
VARIANT AT3D ARG-456.
PubMed=8274732;
Jochmans K., Lissens W., Vervoort R., Peeters S., de Waelwe M.,
Liebaers I.;
"Antithrombin-Gly 424 Arg: a novel point mutation responsible for type
1 antithrombin deficiency and neonatal thrombosis.";
Blood 83:146-151(1994).
[53]
VARIANTS AT3D SER-95; THR-453 AND PHE-462.
PubMed=7994035;
van Boven H.H., Olds R.J., Thein S.L., Reitsma P.H., Lane D.A.,
Briet E., Vandenbroucke J.P., Rosendaal F.R.;
"Hereditary antithrombin deficiency: heterogeneity of the molecular
basis and mortality in Dutch families.";
Blood 84:4209-4213(1994).
[54]
VARIANT AT3D ASP-219.
PubMed=7989582; DOI=10.1172/JCI117589;
Bruce D., Perry D.J., Borg J.-Y., Carrell R.W., Wardell M.R.;
"Thromboembolic disease due to thermolabile conformational changes of
antithrombin Rouen-VI (187 Asn-->Asp).";
J. Clin. Invest. 94:2265-2274(1994).
[55]
VARIANTS AT3D VAL-131 AND PRO-150.
Chowdhury V., Olds R.J., Lane D.A., Mille B., Pabinger I., Thein S.L.;
"Two novel antithrombin variants (L99V and Q118P) which alter the
heparin binding domain.";
Nouv. Rev. Fr. Hematol. 86:268-268(1994).
[56]
VARIANT AT3D 273-LYS--LYS-307 DEL.
PubMed=7878627;
Emmerich J., Chadeuf G., Alhenc-Gelas M., Gouault-Heilman M.,
Toulon P., Fiessinger J.-N., Aiach M.;
"Molecular basis of antithrombin type I deficiency: the first large
in-frame deletion and two novel mutations in exon 6.";
Thromb. Haemost. 72:534-539(1994).
[57]
VARIANT AT3D HIS-425.
PubMed=7832187; DOI=10.1002/ajh.2830480104;
Okajima K., Abe H., Wagatsuma M., Okabe H., Takatsuki K.;
"Antithrombin III Kumamoto II; a single mutation at Arg393-His
increased the affinity of antithrombin III for heparin.";
Am. J. Hematol. 48:12-18(1995).
[58]
VARIANT AT3D ARG-127.
PubMed=9157604;
Ozawa T., Takikawa Y., Niiya K., Fujiwara T., Suzuki K., Sato S.,
Sakuragawa N.;
"Antithrombin Morioka (Cys 95-Arg): a novel missense mutation causing
type I antithrombin deficiency.";
Thromb. Haemost. 77:403-403(1997).
[59]
VARIANT AT3D PRO-23.
PubMed=9845533;
Fitches A.C., Appleby R., Lane D.A., De Stefano V., Leone G.,
Olds R.J.;
"Impaired cotranslational processing as a mechanism for type I
antithrombin deficiency.";
Blood 92:4671-4676(1998).
[60]
VARIANTS AT3D ARG-32; LEU-73; CYS-79; HIS-198; ARG-257 AND ARG-412.
PubMed=9759613;
Jochmans K., Lissens W., Seneca S., Capel P., Chatelain B., Meeus P.,
Osselaer J.C., Peerlinck K., Seghers J., Slacmeulder M., Stibbe J.,
van de Loo J., Vermylen J., Liebaers I., De Waele M.;
"The molecular basis of antithrombin deficiency in Belgian and Dutch
families.";
Thromb. Haemost. 80:376-381(1998).
[61]
VARIANT THR-167.
PubMed=10361121;
Bayston T.A., Tripodi A., Mannucci P.M., Thompson E., Ireland H.,
Fitches A.C., Hananeia L., Olds R.J., Lane D.A.;
"Familial overexpression of beta-antithrombin caused by an Asn135-to-
Thr substitution.";
Blood 93:4242-4247(1999).
[62]
VARIANTS AT3D PHE-214; PRO-223; ILE-243; THR-251; VAL-283 AND PRO-397.
PubMed=10997988; DOI=10.1046/j.1365-2141.2000.02245.x;
Picard V., Bura A., Emmerich J., Alhenc-Gelas M., Biron C.,
Houbouyan-Reveillard L.L., Molho P., Labatide-Alanore A., Sie P.,
Toulon P., Verdy E., Aiach M.;
"Molecular bases of antithrombin deficiency in French families:
identification of seven novel mutations in the antithrombin gene.";
Br. J. Haematol. 110:731-734(2000).
[63]
VARIANT AT3D 152-HIS--PHE-154 DEL.
PubMed=11794707; DOI=10.1007/BF02982095;
Niiya K., Kiguchi T., Dansako H., Fujimura K., Fujimoto T., Iijima K.,
Tanimoto M., Harada M.;
"Two novel gene mutations in type I antithrombin deficiency.";
Int. J. Hematol. 74:469-472(2001).
[64]
VARIANT AT3D PRO-223.
PubMed=11713457; DOI=10.1067/mpd.2001.118191;
Baud O., Picard V., Durand P., Duchemin J., Proulle V.,
Alhenc-Gelas M., Devictor D., Dreyfus M.;
"Intracerebral hemorrhage associated with a novel antithrombin gene
mutation in a neonate.";
J. Pediatr. 139:741-743(2001).
[65]
VARIANT AT3D GLU-146.
PubMed=12353073; DOI=10.1267/THRO88030436;
Mushunje A., Zhou A., Huntington J.A., Conard J., Carrell R.W.;
"Antithrombin 'DREUX' (Lys 114Glu): a variant with complete loss of
heparin affinity.";
Thromb. Haemost. 88:436-443(2002).
[66]
VARIANT AT3D LEU-261.
PubMed=12595305; DOI=10.1182/blood-2002-11-3391;
Picard V., Dautzenberg M.-D., Villoutreix B.O., Orliaguet G.,
Alhenc-Gelas M., Aiach M.;
"Antithrombin Phe229Leu: a new homozygous variant leading to
spontaneous antithrombin polymerization in vivo associated with severe
childhood thrombosis.";
Blood 102:919-925(2003).
[67]
VARIANTS AT3D LYS-121; HIS-178; CYS-425; HIS-425 AND PRO-441.
PubMed=12894857; DOI=10.1007/BF02983246;
Nagaizumi K., Inaba H., Amano K., Suzuki M., Arai M., Fukutake K.;
"Five novel and four recurrent point mutations in the antithrombin
gene causing venous thrombosis.";
Int. J. Hematol. 78:79-83(2003).
[68]
VARIANTS AT3D LEU-179; CYS-425 AND LEU-426.
PubMed=15164384; DOI=10.1002/ajh.20067;
David D., Ribeiro S., Ferrao L., Gago T., Crespo F.;
"Molecular basis of inherited antithrombin deficiency in Portuguese
families: identification of genetic alterations and screening for
additional thrombotic risk factors.";
Am. J. Hematol. 76:163-171(2004).
[69]
VARIANT AT3D HIS-398.
PubMed=16908819; DOI=10.1001/archopht.124.8.1165;
Kuhli C., Jochmans K., Scharrer I., Luechtenberg M., Hattenbach L.-O.;
"Retinal vein occlusion associated with antithrombin deficiency
secondary to a novel G9840C missense mutation.";
Arch. Ophthalmol. 124:1165-1169(2006).
[70]
VARIANTS AT3D PHE-53; LEU-73; ASP-125; PRO-170; ASN-218; GLY-248;
PRO-293; ARG-401; CYS-425; GLY-438 AND ALA-439, AND VARIANT GLU-30.
PubMed=23910795; DOI=10.1111/jth.12364;
Puurunen M., Salo P., Engelbarth S., Javela K., Perola M.;
"Type II antithrombin deficiency caused by a founder mutation Pro73Leu
in the Finnish population: clinical picture.";
J. Thromb. Haemost. 11:1844-1849(2013).
-!- FUNCTION: Most important serine protease inhibitor in plasma that
regulates the blood coagulation cascade. AT-III inhibits thrombin,
matriptase-3/TMPRSS7, as well as factors IXa, Xa and XIa. Its
inhibitory activity is greatly enhanced in the presence of
heparin. {ECO:0000269|PubMed:15853774}.
-!- SUBUNIT: Forms protease inhibiting heterodimer with TMPRSS7.
-!- INTERACTION:
Q8IXL6:FAM20C; NbExp=2; IntAct=EBI-1039832, EBI-7147442;
-!- SUBCELLULAR LOCATION: Secreted, extracellular space.
-!- TISSUE SPECIFICITY: Found in plasma.
-!- PTM: Phosphorylated by FAM20C in the extracellular medium.
{ECO:0000269|PubMed:26091039}.
-!- MASS SPECTROMETRY: Mass=57863; Method=Electrospray; Range=33-464;
Evidence={ECO:0000269|PubMed:7734359};
-!- MASS SPECTROMETRY: Mass=57911; Method=Electrospray; Range=33-464;
Note=Variant Thr-414.; Evidence={ECO:0000269|PubMed:7734359};
-!- DISEASE: Antithrombin III deficiency (AT3D) [MIM:613118]: An
important risk factor for hereditary thrombophilia, a hemostatic
disorder characterized by a tendency to recurrent thrombosis.
Antithrombin-III deficiency is classified into 4 types. Type I:
characterized by a 50% decrease in antigenic and functional
levels. Type II: has defects affecting the thrombin-binding
domain. Type III: alteration of the heparin-binding domain. Plasma
AT-III antigen levels are normal in type II and III. Type IV:
consists of miscellaneous group of unclassifiable mutations.
{ECO:0000269|PubMed:10997988, ECO:0000269|PubMed:11713457,
ECO:0000269|PubMed:11794707, ECO:0000269|PubMed:12353073,
ECO:0000269|PubMed:12595305, ECO:0000269|PubMed:12894857,
ECO:0000269|PubMed:15164384, ECO:0000269|PubMed:1547341,
ECO:0000269|PubMed:1555650, ECO:0000269|PubMed:16908819,
ECO:0000269|PubMed:1906811, ECO:0000269|PubMed:2013320,
ECO:0000269|PubMed:2229057, ECO:0000269|PubMed:2365065,
ECO:0000269|PubMed:23910795, ECO:0000269|PubMed:2781509,
ECO:0000269|PubMed:3080419, ECO:0000269|PubMed:3162733,
ECO:0000269|PubMed:3179438, ECO:0000269|PubMed:3191114,
ECO:0000269|PubMed:3805013, ECO:0000269|PubMed:6582486,
ECO:0000269|PubMed:7734359, ECO:0000269|PubMed:7832187,
ECO:0000269|PubMed:7878627, ECO:0000269|PubMed:7959685,
ECO:0000269|PubMed:7981186, ECO:0000269|PubMed:7989582,
ECO:0000269|PubMed:7994035, ECO:0000269|PubMed:8274732,
ECO:0000269|PubMed:8443391, ECO:0000269|PubMed:8486379,
ECO:0000269|PubMed:9031473, ECO:0000269|PubMed:9157604,
ECO:0000269|PubMed:9759613, ECO:0000269|PubMed:9845533,
ECO:0000269|Ref.3, ECO:0000269|Ref.55}. Note=The disease is caused
by mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Antithrombin entry;
URL="https://en.wikipedia.org/wiki/Antithrombin";
-!- WEB RESOURCE: Name=Antithrombin mutation database;
URL="https://www1.imperial.ac.uk/departmentofmedicine/divisions/experimentalmedicine/haematology/coag/antithrombin/";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/serpinc1/";
-!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
polymorphism database;
URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=SERPINC1";
-----------------------------------------------------------------------
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EMBL; L00185; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; L00186; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; L00190; AAB40025.1; -; Genomic_DNA.
EMBL; D29832; BAA06212.1; -; mRNA.
EMBL; X68793; CAA48690.1; -; Genomic_DNA.
EMBL; AF130100; AAG35525.1; -; mRNA.
EMBL; AK312654; BAG35537.1; -; mRNA.
EMBL; AF386078; AAK60337.1; -; Genomic_DNA.
EMBL; AL136170; CAI19423.1; -; Genomic_DNA.
EMBL; CH471067; EAW90969.1; -; Genomic_DNA.
EMBL; M21643; AAA51793.1; -; Genomic_DNA.
EMBL; M21644; AAA51794.1; -; Genomic_DNA.
EMBL; M21643; AAA51794.1; JOINED; Genomic_DNA.
EMBL; M21642; AAA51796.1; -; Genomic_DNA.
EMBL; M21636; AAA51796.1; JOINED; Genomic_DNA.
EMBL; M21637; AAA51796.1; JOINED; Genomic_DNA.
EMBL; M21638; AAA51796.1; JOINED; Genomic_DNA.
EMBL; M21640; AAA51796.1; JOINED; Genomic_DNA.
EMBL; M21641; AAA51796.1; JOINED; Genomic_DNA.
CCDS; CCDS1313.1; -.
PIR; A49494; XHHU3.
RefSeq; NP_000479.1; NM_000488.3.
UniGene; Hs.75599; -.
PDB; 1ANT; X-ray; 3.00 A; I/L=33-464.
PDB; 1ATH; X-ray; 3.20 A; A/B=33-464.
PDB; 1AZX; X-ray; 2.90 A; I/L=33-464.
PDB; 1BR8; X-ray; 2.90 A; I/L=33-464.
PDB; 1DZG; X-ray; 2.80 A; I/L=33-464.
PDB; 1DZH; X-ray; 2.85 A; I/L=33-464.
PDB; 1E03; X-ray; 2.90 A; I/L=33-464.
PDB; 1E04; X-ray; 2.60 A; I/L=33-464.
PDB; 1E05; X-ray; 2.62 A; I/L=33-464.
PDB; 1JVQ; X-ray; 2.60 A; I/L=33-464.
PDB; 1LK6; X-ray; 2.80 A; I/L=33-464.
PDB; 1NQ9; X-ray; 2.60 A; I/L=33-464.
PDB; 1OYH; X-ray; 2.62 A; I/L=33-464.
PDB; 1R1L; X-ray; 2.70 A; I/L=33-464.
PDB; 1SR5; X-ray; 3.10 A; A=33-464.
PDB; 1T1F; X-ray; 2.75 A; A/B/C=33-464.
PDB; 1TB6; X-ray; 2.50 A; I=33-464.
PDB; 2ANT; X-ray; 2.60 A; I/L=33-464.
PDB; 2B4X; X-ray; 2.80 A; I/L=37-463.
PDB; 2B5T; X-ray; 2.10 A; I=33-464.
PDB; 2BEH; X-ray; 2.70 A; I/L=33-464.
PDB; 2GD4; X-ray; 3.30 A; C/I=22-464.
PDB; 2HIJ; X-ray; 2.90 A; I/L=33-464.
PDB; 2ZNH; X-ray; 2.80 A; A/B=33-464.
PDB; 3EVJ; X-ray; 3.00 A; I/L=33-464.
PDB; 3KCG; X-ray; 1.70 A; I=33-464.
PDB; 4EB1; X-ray; 2.80 A; I/L=33-464.
PDBsum; 1ANT; -.
PDBsum; 1ATH; -.
PDBsum; 1AZX; -.
PDBsum; 1BR8; -.
PDBsum; 1DZG; -.
PDBsum; 1DZH; -.
PDBsum; 1E03; -.
PDBsum; 1E04; -.
PDBsum; 1E05; -.
PDBsum; 1JVQ; -.
PDBsum; 1LK6; -.
PDBsum; 1NQ9; -.
PDBsum; 1OYH; -.
PDBsum; 1R1L; -.
PDBsum; 1SR5; -.
PDBsum; 1T1F; -.
PDBsum; 1TB6; -.
PDBsum; 2ANT; -.
PDBsum; 2B4X; -.
PDBsum; 2B5T; -.
PDBsum; 2BEH; -.
PDBsum; 2GD4; -.
PDBsum; 2HIJ; -.
PDBsum; 2ZNH; -.
PDBsum; 3EVJ; -.
PDBsum; 3KCG; -.
PDBsum; 4EB1; -.
ProteinModelPortal; P01008; -.
SMR; P01008; -.
BioGrid; 106953; 15.
DIP; DIP-38009N; -.
IntAct; P01008; 4.
STRING; 9606.ENSP00000356671; -.
BindingDB; P01008; -.
ChEMBL; CHEMBL1950; -.
DrugBank; DB11598; Antithrombin III human.
DrugBank; DB00407; Ardeparin.
DrugBank; DB06779; Dalteparin.
DrugBank; DB01225; Enoxaparin.
DrugBank; DB00569; Fondaparinux sodium.
DrugBank; DB01109; Heparin.
DrugBank; DB04464; N-Formylmethionine.
DrugBank; DB08813; Nadroparin.
DrugBank; DB05361; SR-123781A.
DrugBank; DB06271; Sulodexide.
DrugBank; DB06822; Tinzaparin.
GuidetoPHARMACOLOGY; 2632; -.
MEROPS; I04.018; -.
iPTMnet; P01008; -.
PhosphoSitePlus; P01008; -.
UniCarbKB; P01008; -.
BioMuta; SERPINC1; -.
DMDM; 113936; -.
DOSAC-COBS-2DPAGE; P01008; -.
REPRODUCTION-2DPAGE; P01008; -.
SWISS-2DPAGE; P01008; -.
EPD; P01008; -.
MaxQB; P01008; -.
PaxDb; P01008; -.
PeptideAtlas; P01008; -.
PRIDE; P01008; -.
Ensembl; ENST00000367698; ENSP00000356671; ENSG00000117601.
GeneID; 462; -.
KEGG; hsa:462; -.
UCSC; uc001gjt.4; human.
CTD; 462; -.
DisGeNET; 462; -.
EuPathDB; HostDB:ENSG00000117601.13; -.
GeneCards; SERPINC1; -.
HGNC; HGNC:775; SERPINC1.
HPA; CAB016790; -.
HPA; HPA001816; -.
HPA; HPA024007; -.
MalaCards; SERPINC1; -.
MIM; 107300; gene.
MIM; 613118; phenotype.
neXtProt; NX_P01008; -.
OpenTargets; ENSG00000117601; -.
Orphanet; 82; Hereditary thrombophilia due to congenital antithrombin deficiency.
PharmGKB; PA35026; -.
eggNOG; KOG2392; Eukaryota.
eggNOG; COG4826; LUCA.
GeneTree; ENSGT00760000118789; -.
HOVERGEN; HBG005957; -.
InParanoid; P01008; -.
KO; K03911; -.
OMA; KFRYRRV; -.
OrthoDB; EOG091G0ION; -.
PhylomeDB; P01008; -.
TreeFam; TF343094; -.
Reactome; R-HSA-140837; Intrinsic Pathway of Fibrin Clot Formation.
Reactome; R-HSA-140875; Common Pathway of Fibrin Clot Formation.
Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
SIGNOR; P01008; -.
ChiTaRS; SERPINC1; human.
EvolutionaryTrace; P01008; -.
GeneWiki; Antithrombin; -.
GenomeRNAi; 462; -.
PMAP-CutDB; P01008; -.
PRO; PR:P01008; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000117601; -.
CleanEx; HS_SERPINC1; -.
ExpressionAtlas; P01008; baseline and differential.
Genevisible; P01008; HS.
GO; GO:0072562; C:blood microparticle; IDA:UniProtKB.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
GO; GO:0002020; F:protease binding; IPI:UniProtKB.
GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central.
GO; GO:0002438; P:acute inflammatory response to antigenic stimulus; IEA:Ensembl.
GO; GO:0007596; P:blood coagulation; TAS:Reactome.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0007595; P:lactation; IEA:Ensembl.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:2000266; P:regulation of blood coagulation, intrinsic pathway; IEA:InterPro.
GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
CDD; cd02045; antithrombin-III_like; 1.
InterPro; IPR033829; Antithrombin_domain.
InterPro; IPR015555; AT-III.
InterPro; IPR023795; Serpin_CS.
InterPro; IPR023796; Serpin_dom.
InterPro; IPR000215; Serpin_fam.
PANTHER; PTHR11461; PTHR11461; 1.
PANTHER; PTHR11461:SF267; PTHR11461:SF267; 1.
Pfam; PF00079; Serpin; 1.
SMART; SM00093; SERPIN; 1.
SUPFAM; SSF56574; SSF56574; 1.
PROSITE; PS00284; SERPIN; 1.
1: Evidence at protein level;
3D-structure; Blood coagulation; Complete proteome;
Direct protein sequencing; Disease mutation; Disulfide bond;
Glycoprotein; Hemostasis; Heparin-binding; Phosphoprotein;
Polymorphism; Protease inhibitor; Reference proteome; Secreted;
Serine protease inhibitor; Signal; Thrombophilia.
SIGNAL 1 32 {ECO:0000269|Ref.10}.
CHAIN 33 464 Antithrombin-III.
/FTId=PRO_0000032489.
BINDING 81 81 Heparin.
BINDING 161 161 Heparin.
BINDING 177 177 Heparin.
SITE 425 426 Reactive bond.
MOD_RES 63 63 Phosphothreonine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
MOD_RES 68 68 Phosphoserine; by FAM20C.
{ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:26091039}.
CARBOHYD 128 128 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:14760718,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218,
ECO:0000269|Ref.10}.
CARBOHYD 167 167 N-linked (GlcNAc...) asparagine.
{ECO:0000269|Ref.10}.
CARBOHYD 187 187 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:14760718,
ECO:0000269|PubMed:15084671,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19838169,
ECO:0000269|Ref.10}.
CARBOHYD 224 224 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16263699,
ECO:0000269|PubMed:16335952,
ECO:0000269|Ref.10}.
DISULFID 40 160 {ECO:0000269|Ref.10}.
DISULFID 53 127 {ECO:0000269|Ref.10}.
DISULFID 279 462 {ECO:0000269|Ref.10}.
VARIANT 17 17 Y -> S (in AT3D; type-I).
{ECO:0000269|PubMed:9031473}.
/FTId=VAR_027450.
VARIANT 23 23 L -> P (in AT3D; type-I; does not undergo
post-translational glycosylation;
dbSNP:rs387906575).
{ECO:0000269|PubMed:9031473,
ECO:0000269|PubMed:9845533}.
/FTId=VAR_012748.
VARIANT 30 30 V -> E (in Dublin; dbSNP:rs2227624).
{ECO:0000269|PubMed:1977621,
ECO:0000269|PubMed:23910795,
ECO:0000269|PubMed:9031473,
ECO:0000269|Ref.7}.
/FTId=VAR_007032.
VARIANT 32 32 C -> R (in AT3D; type-I).
{ECO:0000269|PubMed:9759613}.
/FTId=VAR_027451.
VARIANT 39 39 I -> N (in AT3D; type-II; Rouen-3; lack
of heparin-binding properties;
dbSNP:rs121909558).
{ECO:0000269|PubMed:9031473}.
/FTId=VAR_007033.
VARIANT 52 52 M -> T (previously Whitechapel).
{ECO:0000269|PubMed:9031473}.
/FTId=VAR_007034.
VARIANT 53 53 C -> F (in AT3D).
{ECO:0000269|PubMed:23910795}.
/FTId=VAR_071199.
VARIANT 56 56 R -> C (in AT3D; type-II; Rouen-4; lack
of heparin-binding properties;
dbSNP:rs28929469).
{ECO:0000269|PubMed:2365065,
ECO:0000269|PubMed:9031473}.
/FTId=VAR_007035.
VARIANT 73 73 P -> L (in AT3D; type-II; lacks heparin-
binding ability; dbSNP:rs121909551).
{ECO:0000269|PubMed:23910795,
ECO:0000269|PubMed:3080419,
ECO:0000269|PubMed:9031473,
ECO:0000269|PubMed:9759613}.
/FTId=VAR_007036.
VARIANT 79 79 R -> C (in AT3D; Tours/Alger/Amiens/
Toyama/Paris-1/Paris-2/Padua-2/Barcelona-
2/Kumamoto/Omura/Sasebo; lacks heparin-
binding ability; dbSNP:rs121909547).
{ECO:0000269|PubMed:6582486,
ECO:0000269|PubMed:9031473,
ECO:0000269|PubMed:9759613}.
/FTId=VAR_007037.
VARIANT 79 79 R -> H (in AT3D; type-II; Rouen-1/Padua-
1/Bligny/Budapest-2; lack of heparin-
binding properties; dbSNP:rs121909552).
{ECO:0000269|PubMed:7981186,
ECO:0000269|PubMed:9031473}.
/FTId=VAR_007038.
VARIANT 79 79 R -> S (in AT3D; type-II; Rouen-2; lack
of heparin-binding properties;
dbSNP:rs121909547).
{ECO:0000269|PubMed:9031473}.
/FTId=VAR_007039.
VARIANT 87 87 Missing (in AT3D; type-I).
{ECO:0000269|PubMed:9031473}.
/FTId=VAR_007040.
VARIANT 89 89 R -> C (in AT3D; type-I;
dbSNP:rs147266200).
{ECO:0000269|PubMed:9031473}.
/FTId=VAR_007041.
VARIANT 90 90 F -> L (in AT3D; type-I; Budapest-6).
{ECO:0000269|PubMed:9031473}.
/FTId=VAR_007042.
VARIANT 95 95 Y -> C (in AT3D; type-I).
{ECO:0000269|PubMed:9031473}.
/FTId=VAR_027452.
VARIANT 95 95 Y -> S (in AT3D; type-I).
{ECO:0000269|PubMed:7994035,
ECO:0000269|PubMed:9031473}.
/FTId=VAR_012316.
VARIANT 98 98 L -> P (in AT3D; type-I).
{ECO:0000269|PubMed:9031473}.
/FTId=VAR_027453.
VARIANT 108 109 Missing (in AT3D; type-I).
/FTId=VAR_007043.
VARIANT 112 112 P -> T (in AT3D; type-I).
{ECO:0000269|PubMed:7959685,
ECO:0000269|PubMed:9031473}.
/FTId=VAR_007044.
VARIANT 121 121 M -> K (in AT3D; type-I).
{ECO:0000269|PubMed:12894857}.
/FTId=VAR_027454.
VARIANT 125 125 G -> D (in AT3D).
{ECO:0000269|PubMed:23910795}.
/FTId=VAR_071200.
VARIANT 127 127 C -> R (in AT3D; type-I;
dbSNP:rs121909573).
{ECO:0000269|PubMed:9157604}.
/FTId=VAR_027455.
VARIANT 131 131 L -> F (in AT3D; type-II; Budapest-3/
Budapest-7; dbSNP:rs121909567).
{ECO:0000269|PubMed:1555650,
ECO:0000269|PubMed:9031473}.
/FTId=VAR_007045.
VARIANT 131 131 L -> V (in AT3D; type-II; Southport).
{ECO:0000269|PubMed:9031473,
ECO:0000269|Ref.55}.
/FTId=VAR_007046.
VARIANT 133 133 Q -> K (in AT3D; type I).
{ECO:0000269|PubMed:9031473}.
/FTId=VAR_007047.
VARIANT 138 139 Missing (in AT3D; type-I).
{ECO:0000269|PubMed:8486379}.
/FTId=VAR_007048.
VARIANT 146 146 K -> E (in AT3D; Dreux; complete loss af
heparin binding).
{ECO:0000269|PubMed:12353073}.
/FTId=VAR_027456.
VARIANT 147 147 T -> A (in dbSNP:rs2227606).
{ECO:0000269|Ref.7}.
/FTId=VAR_013085.
VARIANT 148 148 S -> P (in AT3D; type-II; Nagasaki;
defective heparin binding associated with
thrombosis; dbSNP:rs121909569).
{ECO:0000269|PubMed:8443391,
ECO:0000269|PubMed:9031473}.
/FTId=VAR_007049.
VARIANT 150 150 Q -> P (in AT3D; type-II; Vienna;
dbSNP:rs765445413).
{ECO:0000269|PubMed:9031473,
ECO:0000269|Ref.55}.
/FTId=VAR_007050.
VARIANT 152 154 Missing (in AT3D; type-I).
{ECO:0000269|PubMed:11794707}.
/FTId=VAR_012749.
VARIANT 152 152 H -> Y (in AT3D; type-I).
{ECO:0000269|PubMed:7959685}.
/FTId=VAR_007051.
VARIANT 153 153 Missing (in AT3D; type-I).
/FTId=VAR_007052.
VARIANT 158 158 L -> P (in AT3D; type-I).
{ECO:0000269|PubMed:9031473}.
/FTId=VAR_007053.
VARIANT 160 160 C -> Y (in AT3D; type-I).
{ECO:0000269|PubMed:7981186,
ECO:0000269|PubMed:9031473}.
/FTId=VAR_027457.
VARIANT 161 161 R -> Q (in AT3D; type-II; Geneva;
dbSNP:rs121909563).
{ECO:0000269|PubMed:2229057,
ECO:0000269|PubMed:9031473}.
/FTId=VAR_007054.
VARIANT 167 167 N -> T (in dbSNP:rs121909570).
{ECO:0000269|PubMed:10361121}.
/FTId=VAR_012750.
VARIANT 170 170 S -> P (in AT3D).
{ECO:0000269|PubMed:23910795}.
/FTId=VAR_071201.
VARIANT 178 178 L -> H (in AT3D; type-I).
{ECO:0000269|PubMed:12894857}.
/FTId=VAR_027458.
VARIANT 179 179 F -> L (in AT3D; type-I).
{ECO:0000269|PubMed:15164384}.
/FTId=VAR_027459.
VARIANT 190 190 Y -> C (polymorphism in population of
Scandinavian origin).
{ECO:0000269|PubMed:7959685,
ECO:0000269|PubMed:9031473}.
/FTId=VAR_007055.
VARIANT 198 198 Y -> C (in AT3D; type-I and -II;
Whitechapel).
{ECO:0000269|PubMed:9031473}.
/FTId=VAR_007056.
VARIANT 198 198 Y -> H (in AT3D; type-I).
{ECO:0000269|PubMed:9031473,
ECO:0000269|PubMed:9759613}.
/FTId=VAR_027460.
VARIANT 214 214 S -> F (in AT3D; type-I).
{ECO:0000269|PubMed:10997988}.
/FTId=VAR_027461.
VARIANT 214 214 S -> Y (in AT3D; type-I;
dbSNP:rs483352854).
/FTId=VAR_007057.
VARIANT 218 218 I -> N (in AT3D).
{ECO:0000269|PubMed:23910795}.
/FTId=VAR_071202.
VARIANT 218 218 Missing (in AT3D; type-I).
{ECO:0000269|PubMed:9031473}.
/FTId=VAR_027462.
VARIANT 219 219 N -> D (in AT3D; type-II; Rouen-6;
increases affinity for heparin;
dbSNP:rs121909571).
{ECO:0000269|PubMed:7989582,
ECO:0000269|PubMed:9031473}.
/FTId=VAR_007059.
VARIANT 219 219 N -> K (in AT3D; type-II; Glasgow-3).
{ECO:0000269|PubMed:9031473}.
/FTId=VAR_007058.
VARIANT 223 223 S -> P (in AT3D; type-I;
dbSNP:rs121909572).
{ECO:0000269|PubMed:10997988,
ECO:0000269|PubMed:11713457}.
/FTId=VAR_027463.
VARIANT 243 243 T -> I (in AT3D; type-I).
{ECO:0000269|PubMed:10997988}.
/FTId=VAR_027464.
VARIANT 248 248 V -> G (in AT3D).
{ECO:0000269|PubMed:23910795}.
/FTId=VAR_071203.
VARIANT 251 251 I -> T (in AT3D; type-I).
{ECO:0000269|PubMed:10997988}.
/FTId=VAR_027465.
VARIANT 257 257 W -> R (in AT3D; type-I).
{ECO:0000269|PubMed:9031473,
ECO:0000269|PubMed:9759613}.
/FTId=VAR_027466.
VARIANT 261 261 F -> L (in AT3D).
{ECO:0000269|PubMed:12595305}.
/FTId=VAR_027467.
VARIANT 269 269 E -> K (in AT3D; type-II; Truro;
increases affinity for heparin;
dbSNP:rs758087836).
{ECO:0000269|PubMed:9031473}.
/FTId=VAR_007060.
VARIANT 273 307 Missing (in AT3D; type-I).
{ECO:0000269|PubMed:7878627}.
/FTId=VAR_007061.
VARIANT 283 283 M -> I (in AT3D; type-II).
{ECO:0000269|PubMed:7959685,
ECO:0000269|PubMed:9031473}.
/FTId=VAR_007062.
VARIANT 283 283 M -> V (in AT3D; type-II).
{ECO:0000269|PubMed:10997988}.
/FTId=VAR_027468.
VARIANT 293 293 R -> P (in AT3D).
{ECO:0000269|PubMed:23910795}.
/FTId=VAR_071204.
VARIANT 302 302 L -> P (in AT3D; type-I).
/FTId=VAR_007063.
VARIANT 316 316 I -> N (in AT3D; type-II; Haslar/
Whitechapel).
{ECO:0000269|PubMed:9031473}.
/FTId=VAR_007064.
VARIANT 323 323 S -> P (in AT3D).
/FTId=VAR_027469.
VARIANT 334 334 E -> K (in AT3D; type-II).
{ECO:0000269|PubMed:9031473}.
/FTId=VAR_007065.
VARIANT 344 344 Missing (in AT3D; type-I).
/FTId=VAR_007066.
VARIANT 381 381 S -> P (in AT3D; type-I;
dbSNP:rs121909565).
/FTId=VAR_007067.
VARIANT 391 391 R -> Q (in dbSNP:rs201541724).
/FTId=VAR_007068.
VARIANT 397 397 S -> P (in AT3D; type-I).
{ECO:0000269|PubMed:10997988}.
/FTId=VAR_027470.
VARIANT 398 398 D -> H (in AT3D; type-I).
{ECO:0000269|PubMed:16908819}.
/FTId=VAR_027471.
VARIANT 401 401 H -> R (in AT3D).
{ECO:0000269|PubMed:23910795}.
/FTId=VAR_071205.
VARIANT 412 412 S -> R (in AT3D; type-I).
{ECO:0000269|PubMed:9031473,
ECO:0000269|PubMed:9759613}.
/FTId=VAR_027472.
VARIANT 414 414 A -> T (in AT3D; type-II; Hamilton/
Glasgow-2; reduces interaction with
thrombin by 90%; dbSNP:rs121909557).
{ECO:0000269|PubMed:2013320,
ECO:0000269|PubMed:3179438,
ECO:0000269|PubMed:7734359,
ECO:0000269|PubMed:9031473}.
/FTId=VAR_007069.
VARIANT 416 416 A -> P (in AT3D; type-II; Charleville/
Sudbury/Vicenza/Cambridge-1;
dbSNP:rs28930978).
{ECO:0000269|PubMed:9031473}.
/FTId=VAR_007070.
VARIANT 416 416 A -> S (in AT3D; type-II; Cambridge-2;
dbSNP:rs121909548).
{ECO:0000269|PubMed:1906811,
ECO:0000269|PubMed:9031473}.
/FTId=VAR_007071.
VARIANT 419 419 A -> V (in AT3D; type-I;
dbSNP:rs121909568).
{ECO:0000269|PubMed:9031473}.
/FTId=VAR_007072.
VARIANT 424 424 G -> D (in AT3D; type-II; Stockholm;
dbSNP:rs121909566).
{ECO:0000269|PubMed:1547341,
ECO:0000269|PubMed:9031473}.
/FTId=VAR_007073.
VARIANT 425 425 R -> C (in AT3D; type-II;
dbSNP:rs121909554).
{ECO:0000269|PubMed:12894857,
ECO:0000269|PubMed:15164384,
ECO:0000269|PubMed:23910795,
ECO:0000269|PubMed:3162733,
ECO:0000269|PubMed:9031473}.
/FTId=VAR_007075.
VARIANT 425 425 R -> H (in AT3D; type-II; Glasgow/
Sheffield/Chicago/Avranches/Kumamoto-2;
increases affinity for heparin; deprived
of inhibitory activity;
dbSNP:rs121909549).
{ECO:0000269|PubMed:12894857,
ECO:0000269|PubMed:2781509,
ECO:0000269|PubMed:3162733,
ECO:0000269|PubMed:7832187,
ECO:0000269|PubMed:9031473}.
/FTId=VAR_007074.
VARIANT 425 425 R -> P (in AT3D; type-II; Pescara;
deprived of inhibitory of activity;
dbSNP:rs121909549).
{ECO:0000269|PubMed:9031473}.
/FTId=VAR_007076.
VARIANT 426 426 S -> L (in AT3D; type-II; Denver/Milano-
2; deprived of inhibitory activity;
dbSNP:rs121909550).
{ECO:0000269|PubMed:15164384,
ECO:0000269|PubMed:3805013,
ECO:0000269|PubMed:9031473}.
/FTId=VAR_007077.
VARIANT 434 434 F -> C (in AT3D; type-II; Rosny).
{ECO:0000269|PubMed:9031473}.
/FTId=VAR_007078.
VARIANT 434 434 F -> L (in AT3D; type-II; Maisons-
Laffite). {ECO:0000269|PubMed:9031473}.
/FTId=VAR_007080.
VARIANT 434 434 F -> S (in AT3D; type-II; Torino).
{ECO:0000269|PubMed:9031473}.
/FTId=VAR_007079.
VARIANT 436 436 A -> T (in AT3D; type-II; Oslo/Paris-3;
dbSNP:rs121909546).
{ECO:0000269|PubMed:9031473}.
/FTId=VAR_007081.
VARIANT 437 437 N -> K (in AT3D; type-II; La Rochelle).
{ECO:0000269|PubMed:9031473}.
/FTId=VAR_007082.
VARIANT 438 438 R -> G (in AT3D; type I and type-II).
{ECO:0000269|PubMed:23910795,
ECO:0000269|PubMed:9031473}.
/FTId=VAR_009258.
VARIANT 438 438 R -> M (in AT3D; type-II; Kyoto).
{ECO:0000269|PubMed:9031473,
ECO:0000269|Ref.3}.
/FTId=VAR_007083.
VARIANT 439 439 P -> A (in AT3D).
{ECO:0000269|PubMed:23910795}.
/FTId=VAR_071206.
VARIANT 439 439 P -> L (in AT3D; type-II; Utah; deprived
of inhibitory activity;
dbSNP:rs121909555).
{ECO:0000269|PubMed:3191114,
ECO:0000269|PubMed:9031473}.
/FTId=VAR_007084.
VARIANT 439 439 P -> T (in AT3D; type-II; Budapest-5).
{ECO:0000269|PubMed:9031473}.
/FTId=VAR_007085.
VARIANT 441 441 L -> P (in AT3D; type-II).
{ECO:0000269|PubMed:12894857}.
/FTId=VAR_027473.
VARIANT 453 453 I -> T (in AT3D; type-I).
{ECO:0000269|PubMed:7994035,
ECO:0000269|PubMed:9031473}.
/FTId=VAR_007086.
VARIANT 456 456 G -> R (in AT3D; type-I).
{ECO:0000269|PubMed:8274732,
ECO:0000269|PubMed:9031473}.
/FTId=VAR_007087.
VARIANT 457 457 R -> T (in AT3D; type-II).
{ECO:0000269|PubMed:9031473}.
/FTId=VAR_007088.
VARIANT 459 461 Missing (in AT3D; type-I).
/FTId=VAR_007089.
VARIANT 459 459 A -> D (in AT3D; type-I).
{ECO:0000269|PubMed:9031473}.
/FTId=VAR_007090.
VARIANT 461 461 P -> L (in AT3D; type-II; Budapest;
dbSNP:rs121909564).
{ECO:0000269|PubMed:9031473}.
/FTId=VAR_007091.
VARIANT 462 462 C -> F (in AT3D; type-I).
{ECO:0000269|PubMed:7994035,
ECO:0000269|PubMed:9031473}.
/FTId=VAR_007092.
MUTAGEN 414 414 A->K: Reduces interaction with thrombin
by 99%. {ECO:0000269|PubMed:2013320}.
MUTAGEN 414 414 A->Q: Reduces interaction with thrombin
by 80%. {ECO:0000269|PubMed:2013320}.
CONFLICT 69 70 EQ -> QE (in Ref. 10; AA sequence).
{ECO:0000305}.
CONFLICT 77 77 N -> NN (in Ref. 3; BAA06212).
{ECO:0000305}.
CONFLICT 97 97 H -> R (in Ref. 5; AAG35525).
{ECO:0000305}.
CONFLICT 120 120 A -> T (in Ref. 6; BAG35537).
{ECO:0000305}.
CONFLICT 226 226 T -> A (in Ref. 6; BAG35537).
{ECO:0000305}.
CONFLICT 247 249 Missing (in Ref. 10; AA sequence).
{ECO:0000305}.
CONFLICT 388 388 Missing (in Ref. 13; AA sequence).
{ECO:0000305}.
CONFLICT 395 395 Y -> YA (in Ref. 13; AA sequence).
{ECO:0000305}.
HELIX 39 41 {ECO:0000244|PDB:3KCG}.
TURN 44 46 {ECO:0000244|PDB:3KCG}.
STRAND 51 53 {ECO:0000244|PDB:1OYH}.
HELIX 78 101 {ECO:0000244|PDB:3KCG}.
STRAND 104 106 {ECO:0000244|PDB:1DZG}.
STRAND 108 110 {ECO:0000244|PDB:3KCG}.
HELIX 112 123 {ECO:0000244|PDB:3KCG}.
HELIX 128 137 {ECO:0000244|PDB:3KCG}.
HELIX 140 142 {ECO:0000244|PDB:2B5T}.
HELIX 145 149 {ECO:0000244|PDB:3KCG}.
HELIX 151 166 {ECO:0000244|PDB:3KCG}.
TURN 167 169 {ECO:0000244|PDB:3KCG}.
STRAND 170 181 {ECO:0000244|PDB:3KCG}.
STRAND 184 186 {ECO:0000244|PDB:1E04}.
HELIX 188 198 {ECO:0000244|PDB:3KCG}.
STRAND 203 205 {ECO:0000244|PDB:3KCG}.
HELIX 207 225 {ECO:0000244|PDB:3KCG}.
TURN 226 228 {ECO:0000244|PDB:3KCG}.
STRAND 236 239 {ECO:0000244|PDB:2B4X}.
STRAND 240 242 {ECO:0000244|PDB:1DZG}.
STRAND 245 255 {ECO:0000244|PDB:3KCG}.
STRAND 257 259 {ECO:0000244|PDB:3KCG}.
HELIX 263 265 {ECO:0000244|PDB:3KCG}.
STRAND 267 272 {ECO:0000244|PDB:3KCG}.
STRAND 274 276 {ECO:0000244|PDB:2B5T}.
STRAND 278 294 {ECO:0000244|PDB:3KCG}.
HELIX 296 298 {ECO:0000244|PDB:3KCG}.
STRAND 300 306 {ECO:0000244|PDB:3KCG}.
STRAND 309 317 {ECO:0000244|PDB:3KCG}.
STRAND 320 322 {ECO:0000244|PDB:2B5T}.
HELIX 324 329 {ECO:0000244|PDB:3KCG}.
HELIX 333 342 {ECO:0000244|PDB:3KCG}.
STRAND 344 353 {ECO:0000244|PDB:3KCG}.
STRAND 355 362 {ECO:0000244|PDB:3KCG}.
HELIX 364 369 {ECO:0000244|PDB:3KCG}.
HELIX 374 376 {ECO:0000244|PDB:3KCG}.
TURN 378 380 {ECO:0000244|PDB:3KCG}.
TURN 384 386 {ECO:0000244|PDB:3KCG}.
STRAND 389 392 {ECO:0000244|PDB:3KCG}.
STRAND 398 407 {ECO:0000244|PDB:3KCG}.
STRAND 409 413 {ECO:0000244|PDB:2B5T}.
STRAND 419 422 {ECO:0000244|PDB:1E04}.
STRAND 423 426 {ECO:0000244|PDB:3KCG}.
STRAND 432 435 {ECO:0000244|PDB:3KCG}.
STRAND 440 446 {ECO:0000244|PDB:3KCG}.
TURN 447 450 {ECO:0000244|PDB:3KCG}.
STRAND 451 459 {ECO:0000244|PDB:3KCG}.
SEQUENCE 464 AA; 52602 MW; 9A4E324F00683D9D CRC64;
MYSNVIGTVT SGKRKVYLLS LLLIGFWDCV TCHGSPVDIC TAKPRDIPMN PMCIYRSPEK
KATEDEGSEQ KIPEATNRRV WELSKANSRF ATTFYQHLAD SKNDNDNIFL SPLSISTAFA
MTKLGACNDT LQQLMEVFKF DTISEKTSDQ IHFFFAKLNC RLYRKANKSS KLVSANRLFG
DKSLTFNETY QDISELVYGA KLQPLDFKEN AEQSRAAINK WVSNKTEGRI TDVIPSEAIN
ELTVLVLVNT IYFKGLWKSK FSPENTRKEL FYKADGESCS ASMMYQEGKF RYRRVAEGTQ
VLELPFKGDD ITMVLILPKP EKSLAKVEKE LTPEVLQEWL DELEEMMLVV HMPRFRIEDG
FSLKEQLQDM GLVDLFSPEK SKLPGIVAEG RDDLYVSDAF HKAFLEVNEE GSEAAASTAV
VIAGRSLNPN RVTFKANRPF LVFIREVPLN TIIFMGRVAN PCVK


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20-272-190823 Antithrombin III - Mouse monoclonal [BL - AT III _ 3] to Antithrombin III; ATIII Monoclonal 0.25 ml
123-10 ANTITHROMBIN III (ATIII, AT3), Human Lyophilized 1 mg
123-10 ANTITHROMBIN III (ATIII, AT3), Human Lyophilized 100 ug
15-288-20068F Antithrombin-III - ATIII Polyclonal 0.05 mg
15-288-20068F Antithrombin-III - ATIII Polyclonal 0.1 mg
123-10 ANTITHROMBIN III (ATIII, AT3), Human Lyophilized 5 mg
ACL20015B Antithrombin, ATIII, Sheep anti_Mouse, Biotin 0.1 mg.
ACL20017K Antithrombin, ATIII, anti_Mouse, paired antibodies 2 vials
ANT2754 ANTITHROMBIN III (ATIII) Photo-Optical (suitable for RX monza) R1 4x2, R2 4x2


 

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