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Plasma protease C1 inhibitor (C1 Inh) (C1Inh) (C1 esterase inhibitor) (C1-inhibiting factor) (Serpin G1)

 IC1_HUMAN               Reviewed;         500 AA.
P05155; A6NMU0; A8KAI9; B2R6L5; B4E1F0; B4E1H2; Q16304; Q547W3;
Q59EI5; Q7Z455; Q96FE0; Q9UC49; Q9UCF9;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
01-FEB-1991, sequence version 2.
28-FEB-2018, entry version 218.
RecName: Full=Plasma protease C1 inhibitor;
Short=C1 Inh;
Short=C1Inh;
AltName: Full=C1 esterase inhibitor;
AltName: Full=C1-inhibiting factor;
AltName: Full=Serpin G1;
Flags: Precursor;
Name=SERPING1; Synonyms=C1IN, C1NH;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=3488058; DOI=10.1016/0006-291X(86)91123-X;
Que B.G., Petra P.H.;
"Isolation and analysis of a cDNA coding for human C1 inhibitor.";
Biochem. Biophys. Res. Commun. 137:620-625(1986).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, AND
GLYCOSYLATION AT ASN-25; THR-48; SER-64; ASN-69; THR-71; ASN-81;
THR-83; THR-88; THR-92; THR-96; ASN-238; ASN-253 AND ASN-352.
PubMed=3756141; DOI=10.1021/bi00363a018;
Bock S.C., Skriver K., Nielsen E., Thoegersen H.-C., Wiman B.,
Donaldson V.H., Eddy R.L., Marrinan J., Radziejewska E., Huber R.,
Shows T.B., Magnusson S.;
"Human C1 inhibitor: primary structure, cDNA cloning, and chromosomal
localization.";
Biochemistry 25:4292-4301(1986).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
PubMed=3267220; DOI=10.1111/j.1432-1033.1988.tb13980.x;
Carter P.E., Dunbar B., Fothergill J.E.;
"Genomic and cDNA cloning of the human C1 inhibitor. Intron-exon
junctions and comparison with other serpins.";
Eur. J. Biochem. 173:163-169(1988).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2026152; DOI=10.1111/j.1432-1033.1991.tb15911.x;
Carter P.E., Duponchel C., Tosi M., Fothergill J.E.;
"Complete nucleotide sequence of the gene for human C1 inhibitor with
an unusually high density of Alu elements.";
Eur. J. Biochem. 197:301-308(1991).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Foreskin;
Heus J., Platenburg-Kootwijk E., Meershoek E., De Winter R.,
Knijnenburg J., Kupers L., Habex H., Renaers I., Samuel C.,
Bonnarens L., Hoffman S., Brouwer M., Hack E., Horbach D.,
Timmermans M., Nuijens J., Pieper F.;
"Production of recombinant human C1 inhibitor in milk of transgenic
rabbits for potential use in enzyme replacement therapy for hereditary
angioedema.";
Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
TISSUE=Heart, Liver, Ovary, and Uterus;
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 [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
MET-480.
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
MET-480.
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT MET-480.
SeattleSNPs variation discovery resource;
Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[11]
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.
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
MET-480.
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[13]
NUCLEOTIDE SEQUENCE [MRNA] OF 6-500 (ISOFORM 1).
PubMed=3393514;
Rauth G., Schumacher G., Buckel P., Mueller-Esterl W.;
"Molecular cloning of the cDNA coding for human C1 inhibitor.";
Protein Seq. Data Anal. 1:251-257(1988).
[14]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 18-188, AND VARIANT HAE
84-ASP--THR-138 DEL.
TISSUE=Blood;
PubMed=12773530; DOI=10.1074/jbc.M302977200;
Bos I.G.A., Lubbers Y.T.P., Roem D., Abrahams J.P., Hack C.E.,
Eldering E.;
"The functional integrity of the serpin domain of C1-inhibitor depends
on the unique N-terminal domain, as revealed by a pathological
mutant.";
J. Biol. Chem. 278:29463-29470(2003).
[15]
PROTEIN SEQUENCE OF 23-62.
PubMed=6416294; DOI=10.1021/bi00290a019;
Harrison R.A.;
"Human C1 inhibitor: improved isolation and preliminary structural
characterization.";
Biochemistry 22:5001-5007(1983).
[16]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 33-228.
PubMed=2154751; DOI=10.1073/pnas.87.4.1551;
Stoppa-Lyonnet D., Carter P.E., Meo T., Tosi M.;
"Clusters of intragenic Alu repeats predispose the human C1 inhibitor
locus to deleterious rearrangements.";
Proc. Natl. Acad. Sci. U.S.A. 87:1551-1555(1990).
[17]
NUCLEOTIDE SEQUENCE [MRNA] OF 213-500 (ISOFORM 1/2/3).
PubMed=3089875; DOI=10.1016/0378-1119(86)90230-1;
Tosi M., Duponchel C., Bourgarel P., Colomb M., Meo T.;
"Molecular cloning of human C1 inhibitor: sequence homologies with
alpha 1-antitrypsin and other members of the serpins superfamily.";
Gene 42:265-272(1986).
[18]
PROTEIN SEQUENCE OF 217-233.
PubMed=8618290; DOI=10.1016/S0022-5347(01)66050-6;
Pillai S., Wright D., Gupta A., Zhou G., Hull G., Jiang H., Zhang H.;
"Molecular weights and isoelectric points of sperm antigens relevant
to autoimmune infertility in men.";
J. Urol. 155:1928-1933(1996).
[19]
NUCLEOTIDE SEQUENCE [MRNA] OF 241-458 (ISOFORM 1/2/3), AND PARTIAL
PROTEIN SEQUENCE.
PubMed=3458172; DOI=10.1073/pnas.83.10.3161;
Davis A.E. III, Whitehead A.S., Harrison R.A., Dauphinias A.,
Bruns G.A., Cicardi M., Rosen F.S.;
"Human inhibitor of the first component of complement, C1:
characterization of cDNA clones and localization of the gene to
chromosome 11.";
Proc. Natl. Acad. Sci. U.S.A. 83:3161-3165(1986).
[20]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 418-500, AND VARIANTS HAE
MET-473; ARG-481; PRO-481; ARG-489 AND SER-498.
PubMed=7814636; DOI=10.1172/JCI117663;
Verpy E., Couture-Tosi E., Eldering E., Lopez-Trascasa M., Spath P.,
Meo T., Tosi M.;
"Crucial residues in the carboxy-terminal end of C1 inhibitor revealed
by pathogenic mutants impaired in secretion or function.";
J. Clin. Invest. 95:350-359(1995).
[21]
PROTEIN SEQUENCE OF 464-481, FUNCTION, AND REACTIVE SITE FOR
CHYMOTRYPSIN.
TISSUE=Plasma;
PubMed=8495195; DOI=10.1002/pro.5560020504;
Aulak K.S., Davis A.E. III, Donaldson V.H., Harrison R.A.;
"Chymotrypsin inhibitory activity of normal C1-inhibitor and a P1 Arg
to His mutant: evidence for the presence of overlapping reactive
centers.";
Protein Sci. 2:727-732(1993).
[22]
INTERACTION WITH MASP1.
PubMed=10946292; DOI=10.4049/jimmunol.165.5.2637;
Matsushita M., Thiel S., Jensenius J.C., Terai I., Fujita T.;
"Proteolytic activities of two types of mannose-binding lectin-
associated serine protease.";
J. Immunol. 165:2637-2642(2000).
[23]
INTERACTION WITH E.COLI STCE, AND PROTEOLYTIC PROCESSING BY E.COLI
STCE.
PubMed=12123444; DOI=10.1046/j.1365-2958.2002.02997.x;
Lathem W.W., Grys T.E., Witowski S.E., Torres A.G., Kaper J.B.,
Tarr P.I., Welch R.A.;
"StcE, a metalloprotease secreted by Escherichia coli O157:H7,
specifically cleaves C1 esterase inhibitor.";
Mol. Microbiol. 45:277-288(2002).
[24]
GLYCOSYLATION AT ASN-253.
PubMed=12754519; DOI=10.1038/nbt827;
Zhang H., Li X.-J., Martin D.B., Aebersold R.;
"Identification and quantification of N-linked glycoproteins using
hydrazide chemistry, stable isotope labeling and mass spectrometry.";
Nat. Biotechnol. 21:660-666(2003).
[25]
INTERACTION WITH E.COLI STCE, AND PROTEOLYTIC PROCESSING BY E.COLI
STCE.
PubMed=15096536; DOI=10.1084/jem.20030255;
Lathem W.W., Bergsbaken T., Welch R.A.;
"Potentiation of C1 esterase inhibitor by StcE, a metalloprotease
secreted by Escherichia coli O157:H7.";
J. Exp. Med. 199:1077-1087(2004).
[26]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-25; ASN-238; ASN-253 AND
ASN-352.
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).
[27]
GLYCOSYLATION AT ASN-25.
PubMed=16040958; DOI=10.1128/IAI.73.8.4478-4487.2005;
Liu D., Cramer C.C., Scafidi J., Davis A.E. III;
"N-linked glycosylation at Asn3 and the positively charged residues
within the amino-terminal domain of the c1 inhibitor are required for
interaction of the C1 Inhibitor with Salmonella enterica serovar
typhimurium lipopolysaccharide and lipid A.";
Infect. Immun. 73:4478-4487(2005).
[28]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-25; ASN-69; ASN-238;
ASN-253 AND ASN-352.
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).
[29]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-69; ASN-81; ASN-238;
ASN-253 AND ASN-352.
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).
[30]
GLYCOSYLATION AT ASN-238; ASN-253 AND ASN-352.
PubMed=19139490; DOI=10.1074/mcp.M800504-MCP200;
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F.,
Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y.,
Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.;
"A strategy for precise and large scale identification of core
fucosylated glycoproteins.";
Mol. Cell. Proteomics 8:913-923(2009).
[31]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-352, 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).
[32]
GLYCOSYLATION AT ASN-25; THR-47 AND THR-48, STRUCTURE OF
CARBOHYDRATES, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=22171320; DOI=10.1074/mcp.M111.013649;
Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
"Human urinary glycoproteomics; attachment site specific analysis of
N-and O-linked glycosylations by CID and ECD.";
Mol. Cell. Proteomics 11:1-17(2012).
[33]
GLYCOSYLATION AT THR-47 AND THR-48, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=23234360; DOI=10.1021/pr300963h;
Halim A., Ruetschi U., Larson G., Nilsson J.;
"LC-MS/MS characterization of O-glycosylation sites and glycan
structures of human cerebrospinal fluid glycoproteins.";
J. Proteome Res. 12:573-584(2013).
[34]
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).
[35]
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 119-500, DISULFIDE BONDS,
AND GLYCOSYLATION AT ASN-238.
PubMed=17488724; DOI=10.1074/jbc.M700841200;
Beinrohr L., Harmat V., Dobo J., Loerincz Z., Gal P., Zavodszky P.;
"C1 inhibitor serpin domain structure reveals the likely mechanism of
heparin potentiation and conformational disease.";
J. Biol. Chem. 282:21100-21109(2007).
[36]
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).
[37]
VARIANT HAE HIS-466.
PubMed=3178731; DOI=10.1042/bj2530615;
Aulak K.S., Pemberton P.A., Rosen F.S., Carrell R.W., Lachmann P.J.,
Harrison R.A.;
"Dysfunctional C1-inhibitor(At), isolated from a type II hereditary-
angio-oedema plasma, contains a P1 'reactive centre' (Arg444-->His)
mutation.";
Biochem. J. 253:615-618(1988).
[38]
VARIANT HAE SER-466.
PubMed=2365061; DOI=10.1016/0014-5793(90)81494-9;
Aulak K.S., Cicardi M., Harrison R.A.;
"Identification of a new P1 residue mutation (444Arg-->Ser) in a
dysfunctional C1 inhibitor protein contained in a type II hereditary
angioedema plasma.";
FEBS Lett. 266:13-16(1990).
[39]
VARIANT HAE THR-458.
PubMed=2296585; DOI=10.1073/pnas.87.1.265;
Levy N.J., Ramesh N., Cicardi M., Harrison R.A., Davis A.E. III;
"Type II hereditary angioneurotic edema that may result from a single
nucleotide change in the codon for alanine-436 in the C1 inhibitor
gene.";
Proc. Natl. Acad. Sci. U.S.A. 87:265-268(1990).
[40]
VARIANT HAE LYS-273 DEL.
PubMed=2118657; DOI=10.1073/pnas.87.17.6786;
Parad R.B., Kramer J., Strunk R.C., Rosen F.S., Davis A.E. III;
"Dysfunctional C1 inhibitor Ta: deletion of Lys-251 results in
acquisition of an N-glycosylation site.";
Proc. Natl. Acad. Sci. U.S.A. 87:6786-6790(1990).
[41]
VARIANTS HAE GLU-456 AND VAL-458.
Siddique Z.M., McPhaden A.R., Whaley K.;
"Identification of type II hereditary angio-oedema (HAE) mutations.";
Clin. Exp. Immunol. 86:11-12(1991).
[42]
VARIANT HAE LEU-466.
PubMed=1451784; DOI=10.1016/0014-5793(92)80204-T;
Frange D., Aulak K.S., Cicardi M., Harrison R.A., Davis A.E. III;
"A dysfunctional C1 inhibitor protein with a new reactive center
mutation (Arg-444-->Leu).";
FEBS Lett. 301:34-36(1992).
[43]
VARIANTS HAE GLU-454 AND THR-458.
PubMed=1363816; DOI=10.1038/ng0892-354;
Davis A.E. III, Aulak K., Parad R.B., Stecklein H.P., Eldering E.,
Hack C.E., Kramer J., Strunk R.C., Bissler J., Rosen F.S.;
"C1 inhibitor hinge region mutations produce dysfunction by different
mechanisms.";
Nat. Genet. 1:354-358(1992).
[44]
VARIANT HAE ARG-429.
PubMed=8172583;
Davis A.E. III, Bissler J.J., Cicardi M.;
"Mutations in the C1 inhibitor gene that result in hereditary
angioneurotic edema.";
Behring Inst. Mitt. 93:313-320(1993).
[45]
VARIANT HAE VAL-465.
PubMed=7883978; DOI=10.1172/JCI117780;
Zahedi R., Bissler J.J., Davis A.E. III, Andreadis C., Wisnieski J.J.;
"Unique C1 inhibitor dysfunction in a kindred without angioedema. II.
Identification of an Ala443-->Val substitution and functional analysis
of the recombinant mutant protein.";
J. Clin. Invest. 95:1299-1305(1995).
[46]
VARIANT HAE PRO-467.
PubMed=8529136;
Ocejo-Vinyals J.G., Leyva-Cobian F., Fernandez-Luna J.L.;
"A mutation unique in serine protease inhibitors (serpins) identified
in a family with type II hereditary angioneurotic edema.";
Mol. Med. 1:700-705(1995).
[47]
VARIANTS HAE.
PubMed=8755917;
Verpy E., Biasotto M., Brai M., Misiano G., Meo T., Tosi M.;
"Exhaustive mutation scanning by fluorescence-assisted mismatch
analysis discloses new genotype-phenotype correlations in angiodema.";
Am. J. Hum. Genet. 59:308-319(1996).
[48]
VARIANTS HAE TYR-130; PRO-394; VAL-408; CYS-466; GLU-473; GLU-493 AND
ARG-498.
PubMed=14635117; DOI=10.1002/humu.9202;
Kalmar L., Bors A., Farkas H., Vas S., Fandl B., Varga L., Fuest G.,
Tordai A.;
"Mutation screening of the C1 inhibitor gene among Hungarian patients
with hereditary angioedema.";
Hum. Mutat. 22:498-498(2003).
[49]
VARIANT HAE ARG-345, AND VARIANTS ALA-56 AND MET-480.
PubMed=16409206; DOI=10.1111/j.1398-9995.2006.01010.x;
Kang H.-R., Yim E.-Y., Oh S.-Y., Chang Y.-S., Kim Y.-K., Cho S.-H.,
Min K.-U., Kim Y.-Y.;
"Normal C1 inhibitor mRNA expression level in type I hereditary
angioedema patients: newly found C1 inhibitor gene mutations.";
Allergy 61:260-264(2006).
[50]
VARIANTS HAE ALA-118; CYS-154; PHE-170; ARG-184; PRO-230; LYS-232;
ASN-272 DEL; ARG-299; GLN-430; THR-441; PRO-447; SER-466; CYS-466;
LEU-466; GLY-473 AND GLY-497, AND VARIANTS ALA-56 AND MET-480.
PubMed=22994404; DOI=10.1111/all.12024;
Xu Y.Y., Zhi Y.X., Yin J., Wang L.L., Wen L.P., Gu J.Q., Guan K.,
Craig T., Zhang H.Y.;
"Mutational spectrum and geno-phenotype correlation in Chinese
families with Hereditary Angioedema.";
Allergy 67:1430-1436(2012).
[51]
VARIANTS HAE ARG-11; ARG-265; VAL-274; THR-458; CYS-466; HIS-466;
ARG-493 AND GLU-493.
PubMed=24456027; DOI=10.1111/ahg.12052;
Bafunno V., Bova M., Loffredo S., Divella C., Petraroli A., Marone G.,
Montinaro V., Margaglione M., Triggiani M.;
"Mutational spectrum of the c1 inhibitor gene in a cohort of Italian
patients with hereditary angioedema: description of nine novel
mutations.";
Ann. Hum. Genet. 78:73-82(2014).
-!- FUNCTION: Activation of the C1 complex is under control of the C1-
inhibitor. It forms a proteolytically inactive stoichiometric
complex with the C1r or C1s proteases. May play a potentially
crucial role in regulating important physiological pathways
including complement activation, blood coagulation, fibrinolysis
and the generation of kinins. Very efficient inhibitor of FXIIa.
Inhibits chymotrypsin and kallikrein.
{ECO:0000269|PubMed:8495195}.
-!- SUBUNIT: Binds to E.coli stcE which allows localization of
SERPING1 to cell membranes thus protecting the bacteria against
complement-mediated lysis. Interacts with MASP1.
{ECO:0000269|PubMed:10946292, ECO:0000269|PubMed:12123444,
ECO:0000269|PubMed:15096536}.
-!- INTERACTION:
O43889-2:CREB3; NbExp=3; IntAct=EBI-1223454, EBI-625022;
O82882:stcE (xeno); NbExp=3; IntAct=EBI-1223454, EBI-15979286;
-!- SUBCELLULAR LOCATION: Secreted.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P05155-1; Sequence=Displayed;
Name=2;
IsoId=P05155-2; Sequence=VSP_056662;
Note=No experimental confirmation available.;
Name=3;
IsoId=P05155-3; Sequence=VSP_056663;
Note=No experimental confirmation available.;
-!- PTM: Highly glycosylated (49%) with N- and O-glycosylation. O-
glycosylated with core 1 or possibly core 8 glycans. N-glycan
heterogeneity at Asn-25: Hex5HexNAc4 (minor), dHex1Hex5HexNAc4
(minor), Hex6HexNAc5 (major) and dHex1Hex6HexNAc5 (minor).
{ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:14760718,
ECO:0000269|PubMed:16040958, ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:17488724, ECO:0000269|PubMed:19139490,
ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169,
ECO:0000269|PubMed:22171320, ECO:0000269|PubMed:23234360,
ECO:0000269|PubMed:3756141}.
-!- PTM: Can be proteolytically cleaved by E.coli stcE.
{ECO:0000269|PubMed:12123444, ECO:0000269|PubMed:15096536}.
-!- POLYMORPHISM: Chymotrypsin uses Ala-465 as its reactive site in
normal plasma protease C1 inhibitor, and His-466 as its reactive
site in the variant His-466.
-!- DISEASE: Hereditary angioedema (HAE) [MIM:106100]: An autosomal
dominant disorder characterized by episodic local swelling
involving subcutaneous or submucous tissue of the upper
respiratory and gastrointestinal tracts, face, extremities, and
genitalia. Hereditary angioedema due to C1 esterase inhibitor
deficiency is comprised of two clinically indistinguishable forms.
In hereditary angioedema type 1, serum levels of C1 esterase
inhibitor are decreased, while in type 2, the levels are normal or
elevated, but the protein is non-functional.
{ECO:0000269|PubMed:12773530, ECO:0000269|PubMed:1363816,
ECO:0000269|PubMed:1451784, ECO:0000269|PubMed:14635117,
ECO:0000269|PubMed:16409206, ECO:0000269|PubMed:2118657,
ECO:0000269|PubMed:2296585, ECO:0000269|PubMed:22994404,
ECO:0000269|PubMed:2365061, ECO:0000269|PubMed:24456027,
ECO:0000269|PubMed:3178731, ECO:0000269|PubMed:7814636,
ECO:0000269|PubMed:7883978, ECO:0000269|PubMed:8172583,
ECO:0000269|PubMed:8529136, ECO:0000269|PubMed:8755917,
ECO:0000269|Ref.41}. Note=The disease is caused by mutations
affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA53096.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Wikipedia; Note=C1-inhibitor entry;
URL="https://en.wikipedia.org/wiki/C1-inhibitor";
-!- WEB RESOURCE: Name=SERPING1base; Note=SERPING1 mutation db;
URL="http://structure.bmc.lu.se/idbase/SERPING1base/";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/serping1/";
-----------------------------------------------------------------------
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EMBL; M13690; AAA35613.1; -; mRNA.
EMBL; M13656; AAB59387.1; -; mRNA.
EMBL; X07427; CAA30314.1; -; Genomic_DNA.
EMBL; X07428; CAA30314.1; JOINED; Genomic_DNA.
EMBL; X07429; CAA30314.1; JOINED; Genomic_DNA.
EMBL; X07430; CAA30314.1; JOINED; Genomic_DNA.
EMBL; X07431; CAA30314.1; JOINED; Genomic_DNA.
EMBL; X07432; CAA30314.1; JOINED; Genomic_DNA.
EMBL; X07433; CAA30314.1; JOINED; Genomic_DNA.
EMBL; X07577; CAA30469.1; -; mRNA.
EMBL; X54486; CAA38358.1; -; Genomic_DNA.
EMBL; AF435921; AAM21515.1; -; Genomic_DNA.
EMBL; AK293054; BAF85743.1; -; mRNA.
EMBL; AK303809; BAG64762.1; -; mRNA.
EMBL; AK303840; BAG64784.1; -; mRNA.
EMBL; AK312626; BAG35512.1; -; mRNA.
EMBL; BT006966; AAP35612.1; -; mRNA.
EMBL; AB209826; BAD93063.1; -; mRNA.
EMBL; AY904027; AAW69393.1; -; Genomic_DNA.
EMBL; AP000662; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP002893; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471076; EAW73764.1; -; Genomic_DNA.
EMBL; BC011171; AAH11171.1; -; mRNA.
EMBL; AY291075; AAQ19269.1; -; Genomic_DNA.
EMBL; M30688; AAA53096.1; ALT_SEQ; Genomic_DNA.
EMBL; M14036; AAA51848.1; -; mRNA.
EMBL; M13203; AAA51849.1; -; mRNA.
EMBL; S76944; AAB33044.2; -; Genomic_DNA.
CCDS; CCDS7962.1; -. [P05155-1]
PIR; S15386; ITHUC1.
RefSeq; NP_000053.2; NM_000062.2. [P05155-1]
RefSeq; NP_001027466.1; NM_001032295.1. [P05155-1]
UniGene; Hs.384598; -.
PDB; 1M6Q; Model; -; A=138-500.
PDB; 2OAY; X-ray; 2.35 A; A=119-500.
PDB; 5DU3; X-ray; 2.10 A; A/B=119-500.
PDB; 5DUQ; X-ray; 2.90 A; A/B=118-500.
PDBsum; 1M6Q; -.
PDBsum; 2OAY; -.
PDBsum; 5DU3; -.
PDBsum; 5DUQ; -.
ProteinModelPortal; P05155; -.
SMR; P05155; -.
BioGrid; 107171; 18.
DIP; DIP-45635N; -.
IntAct; P05155; 9.
STRING; 9606.ENSP00000278407; -.
DrugBank; DB05341; C1-INH.
MEROPS; I04.024; -.
iPTMnet; P05155; -.
PhosphoSitePlus; P05155; -.
UniCarbKB; P05155; -.
BioMuta; SERPING1; -.
DMDM; 124096; -.
PaxDb; P05155; -.
PeptideAtlas; P05155; -.
PRIDE; P05155; -.
TopDownProteomics; P05155-1; -. [P05155-1]
DNASU; 710; -.
Ensembl; ENST00000278407; ENSP00000278407; ENSG00000149131. [P05155-1]
Ensembl; ENST00000378323; ENSP00000367574; ENSG00000149131. [P05155-3]
Ensembl; ENST00000378324; ENSP00000367575; ENSG00000149131. [P05155-2]
GeneID; 710; -.
KEGG; hsa:710; -.
UCSC; uc001nkp.2; human. [P05155-1]
CTD; 710; -.
DisGeNET; 710; -.
EuPathDB; HostDB:ENSG00000149131.15; -.
GeneCards; SERPING1; -.
HGNC; HGNC:1228; SERPING1.
HPA; CAB026161; -.
HPA; HPA048738; -.
MalaCards; SERPING1; -.
MIM; 106100; phenotype.
MIM; 606860; gene.
neXtProt; NX_P05155; -.
OpenTargets; ENSG00000149131; -.
Orphanet; 100050; Hereditary angioedema type 1.
Orphanet; 100051; Hereditary angioedema type 2.
Orphanet; 169147; Immunodeficiency due to an early component of complement deficiency.
PharmGKB; PA35029; -.
eggNOG; KOG2392; Eukaryota.
eggNOG; COG4826; LUCA.
GeneTree; ENSGT00900000140788; -.
HOGENOM; HOG000231936; -.
HOVERGEN; HBG104060; -.
InParanoid; P05155; -.
KO; K04001; -.
PhylomeDB; P05155; -.
TreeFam; TF317350; -.
Reactome; R-HSA-114608; Platelet degranulation.
Reactome; R-HSA-140837; Intrinsic Pathway of Fibrin Clot Formation.
Reactome; R-HSA-977606; Regulation of Complement cascade.
ChiTaRS; SERPING1; human.
EvolutionaryTrace; P05155; -.
GeneWiki; C1-inhibitor; -.
GenomeRNAi; 710; -.
PMAP-CutDB; P05155; -.
PRO; PR:P05155; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000149131; -.
ExpressionAtlas; P05155; baseline and differential.
Genevisible; P05155; HS.
GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:UniProtKB.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0008015; P:blood circulation; TAS:ProtInc.
GO; GO:0007597; P:blood coagulation, intrinsic pathway; TAS:Reactome.
GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
GO; GO:0042730; P:fibrinolysis; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0001869; P:negative regulation of complement activation, lectin pathway; IDA:UniProtKB.
GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
GO; GO:0030449; P:regulation of complement activation; TAS:Reactome.
InterPro; IPR015553; C1-inh.
InterPro; IPR023795; Serpin_CS.
InterPro; IPR023796; Serpin_dom.
InterPro; IPR000215; Serpin_fam.
InterPro; IPR036186; Serpin_sf.
PANTHER; PTHR11461; PTHR11461; 1.
PANTHER; PTHR11461:SF159; PTHR11461:SF159; 1.
Pfam; PF00079; Serpin; 1.
SMART; SM00093; SERPIN; 1.
SUPFAM; SSF56574; SSF56574; 1.
PROSITE; PS00284; SERPIN; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Blood coagulation;
Complement pathway; Complete proteome; Direct protein sequencing;
Disease mutation; Disulfide bond; Fibrinolysis; Glycoprotein;
Hemostasis; Immunity; Innate immunity; Polymorphism;
Protease inhibitor; Reference proteome; Repeat; Secreted;
Serine protease inhibitor; Signal.
SIGNAL 1 22 {ECO:0000269|PubMed:6416294}.
CHAIN 23 500 Plasma protease C1 inhibitor.
{ECO:0000269|PubMed:3756141}.
/FTId=PRO_0000032514.
REPEAT 85 88 1.
REPEAT 89 92 2.
REPEAT 93 96 3.
REPEAT 97 100 4.
REPEAT 101 104 5.
REPEAT 105 108 6.
REPEAT 116 119 7.
REGION 85 119 7 X 4 AA tandem repeats of [QE]-P-T-[TQ].
SITE 465 466 Reactive bond for chymotrypsin.
SITE 466 467 Reactive bond.
CARBOHYD 25 25 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:14760718,
ECO:0000269|PubMed:16040958,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:22171320,
ECO:0000269|PubMed:3756141}.
CARBOHYD 47 47 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:22171320,
ECO:0000269|PubMed:23234360}.
CARBOHYD 48 48 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:22171320,
ECO:0000269|PubMed:23234360,
ECO:0000269|PubMed:3756141}.
CARBOHYD 64 64 O-linked (GalNAc...) serine.
{ECO:0000269|PubMed:3756141}.
CARBOHYD 69 69 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:3756141}.
CARBOHYD 71 71 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:3756141}.
CARBOHYD 81 81 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:3756141}.
CARBOHYD 83 83 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:3756141}.
CARBOHYD 88 88 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:3756141}.
CARBOHYD 92 92 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:3756141}.
CARBOHYD 96 96 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:3756141}.
CARBOHYD 238 238 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:14760718,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:17488724,
ECO:0000269|PubMed:19139490,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:3756141}.
CARBOHYD 253 253 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:12754519,
ECO:0000269|PubMed:14760718,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19139490,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:3756141}.
CARBOHYD 272 272 N-linked (GlcNAc...) asparagine; in
variant TA.
CARBOHYD 352 352 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:14760718,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19139490,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19838169,
ECO:0000269|PubMed:3756141}.
DISULFID 123 428 {ECO:0000269|PubMed:17488724,
ECO:0000269|PubMed:3756141}.
DISULFID 130 205 {ECO:0000269|PubMed:17488724,
ECO:0000269|PubMed:3756141}.
VAR_SEQ 1 52 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056662.
VAR_SEQ 17 17 G -> GFLEPQ (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056663.
VARIANT 11 11 L -> R (in HAE; phenotype consistent with
hereditary angioedema type 1).
{ECO:0000269|PubMed:24456027}.
/FTId=VAR_071701.
VARIANT 39 39 D -> E (in dbSNP:rs11229062).
/FTId=VAR_027374.
VARIANT 56 56 V -> A (in dbSNP:rs11546660).
{ECO:0000269|PubMed:16409206,
ECO:0000269|PubMed:22994404}.
/FTId=VAR_027375.
VARIANT 84 138 Missing (in HAE; phenotype consistent
with hereditary angioedema type 2).
{ECO:0000269|PubMed:12773530}.
/FTId=VAR_046202.
VARIANT 118 118 T -> A (in HAE; dbSNP:rs200534715).
{ECO:0000269|PubMed:22994404}.
/FTId=VAR_068832.
VARIANT 130 130 C -> Y (in HAE; phenotype consistent with
hereditary angioedema type 1).
{ECO:0000269|PubMed:14635117}.
/FTId=VAR_027379.
VARIANT 154 154 Y -> C (in HAE; dbSNP:rs281875168).
{ECO:0000269|PubMed:22994404}.
/FTId=VAR_068833.
VARIANT 170 170 S -> F (in HAE; dbSNP:rs281875169).
{ECO:0000269|PubMed:22994404}.
/FTId=VAR_068834.
VARIANT 184 184 G -> R (in HAE; dbSNP:rs281875170).
{ECO:0000269|PubMed:22994404}.
/FTId=VAR_068835.
VARIANT 230 230 L -> P (in HAE; dbSNP:rs281875171).
{ECO:0000269|PubMed:22994404}.
/FTId=VAR_068836.
VARIANT 232 232 I -> K (in HAE; dbSNP:rs281875172).
{ECO:0000269|PubMed:22994404}.
/FTId=VAR_068837.
VARIANT 265 265 W -> R (in HAE).
{ECO:0000269|PubMed:24456027}.
/FTId=VAR_071702.
VARIANT 272 272 Missing (in HAE).
{ECO:0000269|PubMed:22994404}.
/FTId=VAR_068838.
VARIANT 273 273 Missing (in HAE; phenotype consistent
with hereditary angioedema type 2;
creates a new glycosylation site).
{ECO:0000269|PubMed:2118657}.
/FTId=VAR_007012.
VARIANT 274 274 I -> V (in HAE; phenotype consistent with
hereditary angioedema type 2).
{ECO:0000269|PubMed:24456027}.
/FTId=VAR_071703.
VARIANT 299 299 W -> R (in HAE; dbSNP:rs281875173).
{ECO:0000269|PubMed:22994404}.
/FTId=VAR_068839.
VARIANT 308 308 T -> S (in dbSNP:rs1803212).
/FTId=VAR_011751.
VARIANT 345 345 G -> R (in HAE; phenotype consistent with
hereditary angioedema type 1).
{ECO:0000269|PubMed:16409206}.
/FTId=VAR_027376.
VARIANT 394 394 T -> P (in HAE; phenotype consistent with
hereditary angioedema type 1).
{ECO:0000269|PubMed:14635117}.
/FTId=VAR_027380.
VARIANT 408 408 D -> V (in HAE; phenotype consistent with
hereditary angioedema type 1).
{ECO:0000269|PubMed:14635117}.
/FTId=VAR_027381.
VARIANT 429 429 G -> R (in HAE; phenotype consistent with
hereditary angioedema type 2).
{ECO:0000269|PubMed:8172583}.
/FTId=VAR_007013.
VARIANT 430 430 L -> Q (in HAE; dbSNP:rs281875174).
{ECO:0000269|PubMed:22994404}.
/FTId=VAR_068840.
VARIANT 441 441 M -> T (in HAE; dbSNP:rs281875175).
{ECO:0000269|PubMed:22994404}.
/FTId=VAR_068841.
VARIANT 447 447 L -> P (in HAE; dbSNP:rs281875176).
{ECO:0000269|PubMed:22994404}.
/FTId=VAR_068842.
VARIANT 454 454 V -> E (in HAE; phenotype consistent with
hereditary angioedema type 2;
dbSNP:rs121907949).
{ECO:0000269|PubMed:1363816}.
/FTId=VAR_007014.
VARIANT 456 456 A -> E (in HAE; phenotype consistent with
hereditary angioedema type 2).
{ECO:0000269|Ref.41}.
/FTId=VAR_007015.
VARIANT 458 458 A -> T (in HAE; phenotype consistent with
hereditary angioedema type 2;
dbSNP:rs121907947).
{ECO:0000269|PubMed:1363816,
ECO:0000269|PubMed:2296585,
ECO:0000269|PubMed:24456027}.
/FTId=VAR_007016.
VARIANT 458 458 A -> V (in HAE; phenotype consistent with
hereditary angioedema type 2).
{ECO:0000269|Ref.41}.
/FTId=VAR_007017.
VARIANT 465 465 A -> V (in HAE; phenotype consistent with
hereditary angioedema type 2;
dbSNP:rs121907950).
{ECO:0000269|PubMed:7883978}.
/FTId=VAR_007018.
VARIANT 466 466 R -> C (in HAE; phenotype consistent with
hereditary angioedema type 2;
dbSNP:rs28940870).
{ECO:0000269|PubMed:14635117,
ECO:0000269|PubMed:22994404,
ECO:0000269|PubMed:24456027}.
/FTId=VAR_007019.
VARIANT 466 466 R -> H (in HAE; phenotype consistent with
hereditary angioedema type 2;
dbSNP:rs121907948).
{ECO:0000269|PubMed:24456027,
ECO:0000269|PubMed:3178731}.
/FTId=VAR_007020.
VARIANT 466 466 R -> L (in HAE; phenotype consistent with
hereditary angioedema type 2;
dbSNP:rs121907948).
{ECO:0000269|PubMed:1451784,
ECO:0000269|PubMed:22994404}.
/FTId=VAR_007021.
VARIANT 466 466 R -> S (in HAE; phenotype consistent with
hereditary angioedema type 2;
dbSNP:rs28940870).
{ECO:0000269|PubMed:22994404,
ECO:0000269|PubMed:2365061}.
/FTId=VAR_007022.
VARIANT 467 467 T -> P (in HAE; phenotype consistent with
hereditary angioedema type 2).
{ECO:0000269|PubMed:8529136}.
/FTId=VAR_007023.
VARIANT 473 473 V -> E (in HAE; phenotype consistent with
hereditary angioedema type 1).
{ECO:0000269|PubMed:14635117}.
/FTId=VAR_027382.
VARIANT 473 473 V -> G (in HAE; dbSNP:rs281875177).
{ECO:0000269|PubMed:22994404}.
/FTId=VAR_068843.
VARIANT 473 473 V -> M (in HAE; phenotype consistent with
hereditary angioedema type 2).
{ECO:0000269|PubMed:7814636}.
/FTId=VAR_007024.
VARIANT 474 474 Q -> E.
/FTId=VAR_007025.
VARIANT 477 477 F -> S (in HAE; phenotype consistent with
hereditary angioedema type 2).
/FTId=VAR_007026.
VARIANT 480 480 V -> M (in dbSNP:rs4926).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:16409206,
ECO:0000269|PubMed:22994404,
ECO:0000269|Ref.7, ECO:0000269|Ref.8,
ECO:0000269|Ref.9}.
/FTId=VAR_007027.
VARIANT 481 481 L -> P (in HAE; phenotype consistent with
hereditary angioedema type 2).
{ECO:0000269|PubMed:7814636}.
/FTId=VAR_007028.
VARIANT 481 481 L -> R (in HAE; phenotype consistent with
hereditary angioedema type 2).
{ECO:0000269|PubMed:7814636}.
/FTId=VAR_007029.
VARIANT 489 489 P -> R (in HAE; phenotype consistent with
hereditary angioedema type 2).
{ECO:0000269|PubMed:7814636}.
/FTId=VAR_007030.
VARIANT 493 493 G -> E (in HAE; phenotype consistent with
hereditary angioedema type 1).
{ECO:0000269|PubMed:14635117,
ECO:0000269|PubMed:24456027}.
/FTId=VAR_027383.
VARIANT 493 493 G -> R (in HAE; phenotype consistent with
hereditary angioedema type 2).
{ECO:0000269|PubMed:24456027}.
/FTId=VAR_071704.
VARIANT 497 497 D -> G (in HAE; dbSNP:rs281875178).
{ECO:0000269|PubMed:22994404}.
/FTId=VAR_068844.
VARIANT 498 498 P -> R (in HAE; phenotype consistent with
hereditary angioedema type 1).
{ECO:0000269|PubMed:14635117}.
/FTId=VAR_027384.
VARIANT 498 498 P -> S (in HAE; phenotype consistent with
hereditary angioedema type 2).
{ECO:0000269|PubMed:7814636}.
/FTId=VAR_007031.
CONFLICT 103 103 T -> S (in Ref. 6; BAF85743).
{ECO:0000305}.
CONFLICT 187 187 E -> Q (in Ref. 2; AAB59387).
{ECO:0000305}.
CONFLICT 306 306 K -> R (in Ref. 1; AAA35613).
{ECO:0000305}.
CONFLICT 314 320 HFKNSVI -> QLQKLSY (in Ref. 19; AA
sequence). {ECO:0000305}.
CONFLICT 322 322 V -> M (in Ref. 19; AA sequence).
{ECO:0000305}.
CONFLICT 332 332 V -> L (in Ref. 19; AA sequence).
{ECO:0000305}.
CONFLICT 370 375 MEQALS -> TGTGSQ (in Ref. 19; AA
sequence). {ECO:0000305}.
CONFLICT 417 417 E -> V (in Ref. 19; AA sequence).
{ECO:0000305}.
CONFLICT 439 439 S -> F (in Ref. 19; AA sequence).
{ECO:0000305}.
HELIX 132 137 {ECO:0000244|PDB:5DU3}.
HELIX 139 160 {ECO:0000244|PDB:5DU3}.
STRAND 167 169 {ECO:0000244|PDB:5DU3}.
HELIX 171 182 {ECO:0000244|PDB:5DU3}.
HELIX 187 197 {ECO:0000244|PDB:5DU3}.
HELIX 206 212 {ECO:0000244|PDB:5DU3}.
STRAND 218 226 {ECO:0000244|PDB:5DU3}.
HELIX 234 244 {ECO:0000244|PDB:5DU3}.
HELIX 255 269 {ECO:0000244|PDB:5DU3}.
TURN 270 272 {ECO:0000244|PDB:5DU3}.
STRAND 287 295 {ECO:0000244|PDB:5DU3}.
STRAND 299 301 {ECO:0000244|PDB:5DU3}.
HELIX 305 307 {ECO:0000244|PDB:5DU3}.
STRAND 309 315 {ECO:0000244|PDB:5DU3}.
STRAND 318 337 {ECO:0000244|PDB:5DU3}.
TURN 338 341 {ECO:0000244|PDB:5DU3}.
STRAND 342 350 {ECO:0000244|PDB:5DU3}.
STRAND 353 362 {ECO:0000244|PDB:5DU3}.
HELIX 367 373 {ECO:0000244|PDB:5DU3}.
HELIX 376 387 {ECO:0000244|PDB:5DU3}.
STRAND 392 399 {ECO:0000244|PDB:5DU3}.
STRAND 401 408 {ECO:0000244|PDB:5DU3}.
HELIX 409 415 {ECO:0000244|PDB:5DU3}.
STRAND 417 419 {ECO:0000244|PDB:2OAY}.
TURN 420 422 {ECO:0000244|PDB:5DU3}.
TURN 428 430 {ECO:0000244|PDB:5DU3}.
STRAND 440 449 {ECO:0000244|PDB:5DU3}.
STRAND 453 455 {ECO:0000244|PDB:5DU3}.
HELIX 458 461 {ECO:0000244|PDB:5DUQ}.
STRAND 469 472 {ECO:0000244|PDB:5DU3}.
STRAND 477 483 {ECO:0000244|PDB:5DU3}.
TURN 484 487 {ECO:0000244|PDB:5DU3}.
STRAND 488 496 {ECO:0000244|PDB:5DU3}.
SEQUENCE 500 AA; 55154 MW; 8B5E874833EA6C05 CRC64;
MASRLTLLTL LLLLLAGDRA SSNPNATSSS SQDPESLQDR GEGKVATTVI SKMLFVEPIL
EVSSLPTTNS TTNSATKITA NTTDEPTTQP TTEPTTQPTI QPTQPTTQLP TDSPTQPTTG
SFCPGPVTLC SDLESHSTEA VLGDALVDFS LKLYHAFSAM KKVETNMAFS PFSIASLLTQ
VLLGAGENTK TNLESILSYP KDFTCVHQAL KGFTTKGVTS VSQIFHSPDL AIRDTFVNAS
RTLYSSSPRV LSNNSDANLE LINTWVAKNT NNKISRLLDS LPSDTRLVLL NAIYLSAKWK
TTFDPKKTRM EPFHFKNSVI KVPMMNSKKY PVAHFIDQTL KAKVGQLQLS HNLSLVILVP
QNLKHRLEDM EQALSPSVFK AIMEKLEMSK FQPTLLTLPR IKVTTSQDML SIMEKLEFFD
FSYDLNLCGL TEDPDLQVSA MQHQTVLELT ETGVEAAAAS AISVARTLLV FEVQQPFLFV
LWDQQHKFPV FMGRVYDPRA


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