Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P05155 (IC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 176. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Plasma protease C1 inhibitor

Short name=C1 Inh
Short name=C1Inh
Alternative name(s):
C1 esterase inhibitor
C1-inhibiting factor
Serpin G1
Gene names
Name:SERPING1
Synonyms:C1IN, C1NH
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length500 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.21

Subunit structure

Binds to E.coli stcE which allows localization of SERPING1 to cell membranes thus protecting the bacteria against complement-mediated lysis. Interacts with MASP1. Ref.22 Ref.23 Ref.25

Subcellular location

Secreted.

Post-translational modification

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). Ref.2 Ref.24 Ref.27 Ref.30 Ref.32 Ref.33 Ref.34

Can be proteolytically cleaved by E.coli stcE. Ref.23 Ref.25

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.

Involvement in 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.14 Ref.20 Ref.36 Ref.37 Ref.38 Ref.39 Ref.40 Ref.41 Ref.42 Ref.43 Ref.44 Ref.45 Ref.46 Ref.47 Ref.48 Ref.49

Sequence similarities

Belongs to the serpin family.

Sequence caution

The sequence AAA53096.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processBlood coagulation
Complement pathway
Fibrinolysis
Hemostasis
Immunity
Innate immunity
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   DomainRepeat
Signal
   Molecular functionProtease inhibitor
Serine protease inhibitor
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processblood circulation

Traceable author statement Ref.37PubMed 2563376. Source: ProtInc

blood coagulation, intrinsic pathway

Traceable author statement. Source: Reactome

complement activation, classical pathway

Inferred from electronic annotation. Source: UniProtKB-KW

fibrinolysis

Inferred from electronic annotation. Source: UniProtKB-KW

innate immune response

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of complement activation, lectin pathway

Inferred from direct assay Ref.22. Source: UniProtKB

platelet activation

Traceable author statement. Source: Reactome

platelet degranulation

Traceable author statement. Source: Reactome

   Cellular_componentblood microparticle

Inferred from direct assay PubMed 22516433. Source: UniProt

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

platelet alpha granule lumen

Traceable author statement. Source: Reactome

   Molecular_functionserine-type endopeptidase inhibitor activity

Inferred from direct assay PubMed 11527969. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Ref.15
Chain23 – 500478Plasma protease C1 inhibitor Ref.2
PRO_0000032514

Regions

Repeat85 – 8841
Repeat89 – 9242
Repeat93 – 9643
Repeat97 – 10044
Repeat101 – 10445
Repeat105 – 10846
Repeat116 – 11947
Region85 – 119357 X 4 AA tandem repeats of [QE]-P-T-[TQ]

Sites

Site465 – 4662Reactive bond for chymotrypsin
Site466 – 4672Reactive bond

Amino acid modifications

Glycosylation251N-linked (GlcNAc...) (complex) Ref.2 Ref.26 Ref.27 Ref.28 Ref.32
Glycosylation471O-linked (GalNAc...) Ref.32 Ref.33
Glycosylation481O-linked (GalNAc...) Ref.2 Ref.32 Ref.33
Glycosylation641O-linked (GalNAc...) Ref.2
Glycosylation691N-linked (GlcNAc...) Ref.2 Ref.28 Ref.29
Glycosylation711O-linked (GalNAc...) Ref.2
Glycosylation811N-linked (GlcNAc...) Ref.2 Ref.29
Glycosylation831O-linked (GalNAc...) Ref.2
Glycosylation881O-linked (GalNAc...) Ref.2
Glycosylation921O-linked (GalNAc...) Ref.2
Glycosylation961O-linked (GalNAc...) Ref.2
Glycosylation2381N-linked (GlcNAc...) (complex) Ref.2 Ref.26 Ref.28 Ref.29 Ref.30 Ref.34
Glycosylation2531N-linked (GlcNAc...) (complex) Ref.2 Ref.24 Ref.26 Ref.28 Ref.29 Ref.30
Glycosylation2721N-linked (GlcNAc...); in variant TA
Glycosylation3521N-linked (GlcNAc...) (complex) Ref.2 Ref.26 Ref.28 Ref.29 Ref.30 Ref.31
Disulfide bond123 ↔ 428 Ref.2 Ref.34
Disulfide bond130 ↔ 205 Ref.2 Ref.34

Natural variations

Natural variant391D → E.
Corresponds to variant rs11229062 [ dbSNP | Ensembl ].
VAR_027374
Natural variant561V → A. Ref.48 Ref.49
Corresponds to variant rs11546660 [ dbSNP | Ensembl ].
VAR_027375
Natural variant84 – 13855Missing in HAE; phenotype consistent with hereditary angioedema type 2.
VAR_046202
Natural variant1181T → A in HAE. Ref.49
Corresponds to variant rs200534715 [ dbSNP | Ensembl ].
VAR_068832
Natural variant1301C → Y in HAE; phenotype consistent with hereditary angioedema type 1. Ref.47
VAR_027379
Natural variant1541Y → C in HAE. Ref.49
Corresponds to variant rs281875168 [ dbSNP | Ensembl ].
VAR_068833
Natural variant1701S → F in HAE. Ref.49
Corresponds to variant rs281875169 [ dbSNP | Ensembl ].
VAR_068834
Natural variant1841G → R in HAE. Ref.49
Corresponds to variant rs281875170 [ dbSNP | Ensembl ].
VAR_068835
Natural variant2301L → P in HAE. Ref.49
Corresponds to variant rs281875171 [ dbSNP | Ensembl ].
VAR_068836
Natural variant2321I → K in HAE. Ref.49
Corresponds to variant rs281875172 [ dbSNP | Ensembl ].
VAR_068837
Natural variant2721Missing in HAE. Ref.49
VAR_068838
Natural variant2731Missing in HAE; phenotype consistent with hereditary angioedema type 2; creates a new glycosylation site. Ref.39
VAR_007012
Natural variant2991W → R in HAE. Ref.49
Corresponds to variant rs281875173 [ dbSNP | Ensembl ].
VAR_068839
Natural variant3081T → S.
Corresponds to variant rs1803212 [ dbSNP | Ensembl ].
VAR_011751
Natural variant3451G → R in HAE; phenotype consistent with hereditary angioedema type 1. Ref.48
VAR_027376
Natural variant3941T → P in HAE; phenotype consistent with hereditary angioedema type 1. Ref.47
VAR_027380
Natural variant4081D → V in HAE; phenotype consistent with hereditary angioedema type 1. Ref.47
VAR_027381
Natural variant4291G → R in HAE; phenotype consistent with hereditary angioedema type 2. Ref.43
VAR_007013
Natural variant4301L → Q in HAE. Ref.49
Corresponds to variant rs281875174 [ dbSNP | Ensembl ].
VAR_068840
Natural variant4411M → T in HAE. Ref.49
Corresponds to variant rs281875175 [ dbSNP | Ensembl ].
VAR_068841
Natural variant4471L → P in HAE. Ref.49
Corresponds to variant rs281875176 [ dbSNP | Ensembl ].
VAR_068842
Natural variant4541V → E in HAE; phenotype consistent with hereditary angioedema type 2. Ref.42
VAR_007014
Natural variant4561A → E in HAE; phenotype consistent with hereditary angioedema type 2. Ref.40
VAR_007015
Natural variant4581A → T in HAE; phenotype consistent with hereditary angioedema type 2. Ref.38 Ref.42
VAR_007016
Natural variant4581A → V in HAE; phenotype consistent with hereditary angioedema type 2. Ref.40
VAR_007017
Natural variant4651A → V in HAE; phenotype consistent with hereditary angioedema type 2. Ref.44
VAR_007018
Natural variant4661R → C in HAE; phenotype consistent with hereditary angioedema type 2. Ref.47 Ref.49
Corresponds to variant rs28940870 [ dbSNP | Ensembl ].
VAR_007019
Natural variant4661R → H in HAE; phenotype consistent with hereditary angioedema type 2. Ref.36
VAR_007020
Natural variant4661R → L in HAE; phenotype consistent with hereditary angioedema type 2. Ref.41 Ref.49
Corresponds to variant rs121907948 [ dbSNP | Ensembl ].
VAR_007021
Natural variant4661R → S in HAE; phenotype consistent with hereditary angioedema type 2. Ref.37 Ref.49
Corresponds to variant rs28940870 [ dbSNP | Ensembl ].
VAR_007022
Natural variant4671T → P in HAE; phenotype consistent with hereditary angioedema type 2. Ref.45
VAR_007023
Natural variant4731V → E in HAE; phenotype consistent with hereditary angioedema type 1. Ref.47
VAR_027382
Natural variant4731V → G in HAE. Ref.49
Corresponds to variant rs281875177 [ dbSNP | Ensembl ].
VAR_068843
Natural variant4731V → M in HAE; phenotype consistent with hereditary angioedema type 2. Ref.20
VAR_007024
Natural variant4741Q → E.
VAR_007025
Natural variant4771F → S in HAE; phenotype consistent with hereditary angioedema type 2.
VAR_007026
Natural variant4801V → M. Ref.7 Ref.8 Ref.9 Ref.12 Ref.48 Ref.49
Corresponds to variant rs4926 [ dbSNP | Ensembl ].
VAR_007027
Natural variant4811L → P in HAE; phenotype consistent with hereditary angioedema type 2. Ref.20
VAR_007028
Natural variant4811L → R in HAE; phenotype consistent with hereditary angioedema type 2. Ref.20
VAR_007029
Natural variant4891P → R in HAE; phenotype consistent with hereditary angioedema type 2. Ref.20
VAR_007030
Natural variant4931G → E in HAE; phenotype consistent with hereditary angioedema type 1. Ref.47
VAR_027383
Natural variant4971D → G in HAE. Ref.49
Corresponds to variant rs281875178 [ dbSNP | Ensembl ].
VAR_068844
Natural variant4981P → R in HAE; phenotype consistent with hereditary angioedema type 1. Ref.47
VAR_027384
Natural variant4981P → S in HAE; phenotype consistent with hereditary angioedema type 2. Ref.20
VAR_007031

Experimental info

Sequence conflict1031T → S in BAF85743. Ref.6
Sequence conflict1871E → Q in AAB59387. Ref.2
Sequence conflict3061K → R in AAA35613. Ref.1
Sequence conflict314 – 3207HFKNSVI → QLQKLSY AA sequence Ref.19
Sequence conflict3221V → M AA sequence Ref.19
Sequence conflict3321V → L AA sequence Ref.19
Sequence conflict370 – 3756MEQALS → TGTGSQ AA sequence Ref.19
Sequence conflict4171E → V AA sequence Ref.19
Sequence conflict4391S → F AA sequence Ref.19

Secondary structure

..................................................... 500
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P05155 [UniParc].

Last modified February 1, 1991. Version 2.
Checksum: 8B5E874833EA6C05

FASTA50055,154
        10         20         30         40         50         60 
MASRLTLLTL LLLLLAGDRA SSNPNATSSS SQDPESLQDR GEGKVATTVI SKMLFVEPIL 

        70         80         90        100        110        120 
EVSSLPTTNS TTNSATKITA NTTDEPTTQP TTEPTTQPTI QPTQPTTQLP TDSPTQPTTG 

       130        140        150        160        170        180 
SFCPGPVTLC SDLESHSTEA VLGDALVDFS LKLYHAFSAM KKVETNMAFS PFSIASLLTQ 

       190        200        210        220        230        240 
VLLGAGENTK TNLESILSYP KDFTCVHQAL KGFTTKGVTS VSQIFHSPDL AIRDTFVNAS 

       250        260        270        280        290        300 
RTLYSSSPRV LSNNSDANLE LINTWVAKNT NNKISRLLDS LPSDTRLVLL NAIYLSAKWK 

       310        320        330        340        350        360 
TTFDPKKTRM EPFHFKNSVI KVPMMNSKKY PVAHFIDQTL KAKVGQLQLS HNLSLVILVP 

       370        380        390        400        410        420 
QNLKHRLEDM EQALSPSVFK AIMEKLEMSK FQPTLLTLPR IKVTTSQDML SIMEKLEFFD 

       430        440        450        460        470        480 
FSYDLNLCGL TEDPDLQVSA MQHQTVLELT ETGVEAAAAS AISVARTLLV FEVQQPFLFV 

       490        500 
LWDQQHKFPV FMGRVYDPRA 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and analysis of a cDNA coding for human C1 inhibitor."
Que B.G., Petra P.H.
Biochem. Biophys. Res. Commun. 137:620-625(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Human C1 inhibitor: primary structure, cDNA cloning, and chromosomal localization."
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.
Biochemistry 25:4292-4301(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, 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.
[3]"Genomic and cDNA cloning of the human C1 inhibitor. Intron-exon junctions and comparison with other serpins."
Carter P.E., Dunbar B., Fothergill J.E.
Eur. J. Biochem. 173:163-169(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[4]"Complete nucleotide sequence of the gene for human C1 inhibitor with an unusually high density of Alu elements."
Carter P.E., Duponchel C., Tosi M., Fothergill J.E.
Eur. J. Biochem. 197:301-308(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"Production of recombinant human C1 inhibitor in milk of transgenic rabbits for potential use in enzyme replacement therapy for hereditary angioedema."
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.
Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Foreskin.
[6]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Heart and Uterus.
[7]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
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.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT MET-480.
[8]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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT MET-480.
Tissue: Brain.
[9]SeattleSNPs variation discovery resource
Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT MET-480.
[10]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
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. expand/collapse author list , 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.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[12]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT MET-480.
Tissue: Brain.
[13]"Molecular cloning of the cDNA coding for human C1 inhibitor."
Rauth G., Schumacher G., Buckel P., Mueller-Esterl W.
Protein Seq. Data Anal. 1:251-257(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-500.
[14]"The functional integrity of the serpin domain of C1-inhibitor depends on the unique N-terminal domain, as revealed by a pathological mutant."
Bos I.G.A., Lubbers Y.T.P., Roem D., Abrahams J.P., Hack C.E., Eldering E.
J. Biol. Chem. 278:29463-29470(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 18-188, VARIANT HAE 84-ASP--THR-138 DEL.
Tissue: Blood.
[15]"Human C1 inhibitor: improved isolation and preliminary structural characterization."
Harrison R.A.
Biochemistry 22:5001-5007(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 23-62.
[16]"Clusters of intragenic Alu repeats predispose the human C1 inhibitor locus to deleterious rearrangements."
Stoppa-Lyonnet D., Carter P.E., Meo T., Tosi M.
Proc. Natl. Acad. Sci. U.S.A. 87:1551-1555(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 33-228.
[17]"Molecular cloning of human C1 inhibitor: sequence homologies with alpha 1-antitrypsin and other members of the serpins superfamily."
Tosi M., Duponchel C., Bourgarel P., Colomb M., Meo T.
Gene 42:265-272(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 213-500.
[18]"Molecular weights and isoelectric points of sperm antigens relevant to autoimmune infertility in men."
Pillai S., Wright D., Gupta A., Zhou G., Hull G., Jiang H., Zhang H.
J. Urol. 155:1928-1933(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 217-233.
[19]"Human inhibitor of the first component of complement, C1: characterization of cDNA clones and localization of the gene to chromosome 11."
Davis A.E. III, Whitehead A.S., Harrison R.A., Dauphinias A., Bruns G.A., Cicardi M., Rosen F.S.
Proc. Natl. Acad. Sci. U.S.A. 83:3161-3165(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 241-458, PARTIAL PROTEIN SEQUENCE.
[20]"Crucial residues in the carboxy-terminal end of C1 inhibitor revealed by pathogenic mutants impaired in secretion or function."
Verpy E., Couture-Tosi E., Eldering E., Lopez-Trascasa M., Spath P., Meo T., Tosi M.
J. Clin. Invest. 95:350-359(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 418-500, VARIANTS HAE MET-473; ARG-481; PRO-481; ARG-489 AND SER-498.
[21]"Chymotrypsin inhibitory activity of normal C1-inhibitor and a P1 Arg to His mutant: evidence for the presence of overlapping reactive centers."
Aulak K.S., Davis A.E. III, Donaldson V.H., Harrison R.A.
Protein Sci. 2:727-732(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 464-481, FUNCTION, REACTIVE SITE FOR CHYMOTRYPSIN.
Tissue: Plasma.
[22]"Proteolytic activities of two types of mannose-binding lectin-associated serine protease."
Matsushita M., Thiel S., Jensenius J.C., Terai I., Fujita T.
J. Immunol. 165:2637-2642(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MASP1.
[23]"StcE, a metalloprotease secreted by Escherichia coli O157:H7, specifically cleaves C1 esterase inhibitor."
Lathem W.W., Grys T.E., Witowski S.E., Torres A.G., Kaper J.B., Tarr P.I., Welch R.A.
Mol. Microbiol. 45:277-288(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH E.COLI STCE, PROTEOLYTIC PROCESSING BY E.COLI STCE.
[24]"Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry."
Zhang H., Li X.-J., Martin D.B., Aebersold R.
Nat. Biotechnol. 21:660-666(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-253.
[25]"Potentiation of C1 esterase inhibitor by StcE, a metalloprotease secreted by Escherichia coli O157:H7."
Lathem W.W., Bergsbaken T., Welch R.A.
J. Exp. Med. 199:1077-1087(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH E.COLI STCE, PROTEOLYTIC PROCESSING BY E.COLI STCE.
[26]"Screening for N-glycosylated proteins by liquid chromatography mass spectrometry."
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.
Proteomics 4:454-465(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-25; ASN-238; ASN-253 AND ASN-352.
Tissue: Plasma.
[27]"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."
Liu D., Cramer C.C., Scafidi J., Davis A.E. III
Infect. Immun. 73:4478-4487(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-25.
[28]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-25; ASN-69; ASN-238; ASN-253 AND ASN-352.
Tissue: Plasma.
[29]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-69; ASN-81; ASN-238; ASN-253 AND ASN-352.
Tissue: Liver.
[30]"A strategy for precise and large scale identification of core fucosylated glycoproteins."
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.
Mol. Cell. Proteomics 8:913-923(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-238; ASN-253 AND ASN-352.
[31]"Enrichment of glycopeptides for glycan structure and attachment site identification."
Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G., Larson G.
Nat. Methods 6:809-811(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-352, STRUCTURE OF CARBOHYDRATES.
Tissue: Cerebrospinal fluid.
[32]"Human urinary glycoproteomics; attachment site specific analysis of N-and O-linked glycosylations by CID and ECD."
Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.
Mol. Cell. Proteomics 0:0-0(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-25; THR-47 AND THR-48, STRUCTURE OF CARBOHYDRATES, MASS SPECTROMETRY.
[33]"LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins."
Halim A., Ruetschi U., Larson G., Nilsson J.
J. Proteome Res. 12:573-584(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT THR-47 AND THR-48, MASS SPECTROMETRY.
[34]"C1 inhibitor serpin domain structure reveals the likely mechanism of heparin potentiation and conformational disease."
Beinrohr L., Harmat V., Dobo J., Loerincz Z., Gal P., Zavodszky P.
J. Biol. Chem. 282:21100-21109(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 119-500, DISULFIDE BONDS, GLYCOSYLATION AT ASN-238.
[35]"What do dysfunctional serpins tell us about molecular mobility and disease?"
Stein P.E., Carrell R.W.
Nat. Struct. Biol. 2:96-113(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON VARIANTS.
[36]"Dysfunctional C1-inhibitor(At), isolated from a type II hereditary-angio-oedema plasma, contains a P1 'reactive centre' (Arg444-->His) mutation."
Aulak K.S., Pemberton P.A., Rosen F.S., Carrell R.W., Lachmann P.J., Harrison R.A.
Biochem. J. 253:615-618(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HAE HIS-466.
[37]"Identification of a new P1 residue mutation (444Arg-->Ser) in a dysfunctional C1 inhibitor protein contained in a type II hereditary angioedema plasma."
Aulak K.S., Cicardi M., Harrison R.A.
FEBS Lett. 266:13-16(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HAE SER-466.
[38]"Type II hereditary angioneurotic edema that may result from a single nucleotide change in the codon for alanine-436 in the C1 inhibitor gene."
Levy N.J., Ramesh N., Cicardi M., Harrison R.A., Davis A.E. III
Proc. Natl. Acad. Sci. U.S.A. 87:265-268(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HAE THR-458.
[39]"Dysfunctional C1 inhibitor Ta: deletion of Lys-251 results in acquisition of an N-glycosylation site."
Parad R.B., Kramer J., Strunk R.C., Rosen F.S., Davis A.E. III
Proc. Natl. Acad. Sci. U.S.A. 87:6786-6790(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HAE LYS-273 DEL.
[40]"Identification of type II hereditary angio-oedema (HAE) mutations."
Siddique Z.M., McPhaden A.R., Whaley K.
Clin. Exp. Immunol. 86:11-12(1991)
Cited for: VARIANTS HAE GLU-456 AND VAL-458.
[41]"A dysfunctional C1 inhibitor protein with a new reactive center mutation (Arg-444-->Leu)."
Frange D., Aulak K.S., Cicardi M., Harrison R.A., Davis A.E. III
FEBS Lett. 301:34-36(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HAE LEU-466.
[42]"C1 inhibitor hinge region mutations produce dysfunction by different mechanisms."
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.
Nat. Genet. 1:354-358(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HAE GLU-454 AND THR-458.
[43]"Mutations in the C1 inhibitor gene that result in hereditary angioneurotic edema."
Davis A.E. III, Bissler J.J., Cicardi M.
Behring Inst. Mitt. 93:313-320(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HAE ARG-429.
[44]"Unique C1 inhibitor dysfunction in a kindred without angioedema. II. Identification of an Ala443-->Val substitution and functional analysis of the recombinant mutant protein."
Zahedi R., Bissler J.J., Davis A.E. III, Andreadis C., Wisnieski J.J.
J. Clin. Invest. 95:1299-1305(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HAE VAL-465.
[45]"A mutation unique in serine protease inhibitors (serpins) identified in a family with type II hereditary angioneurotic edema."
Ocejo-Vinyals J.G., Leyva-Cobian F., Fernandez-Luna J.L.
Mol. Med. 1:700-705(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HAE PRO-467.
[46]"Exhaustive mutation scanning by fluorescence-assisted mismatch analysis discloses new genotype-phenotype correlations in angiodema."
Verpy E., Biasotto M., Brai M., Misiano G., Meo T., Tosi M.
Am. J. Hum. Genet. 59:308-319(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HAE.
[47]"Mutation screening of the C1 inhibitor gene among Hungarian patients with hereditary angioedema."
Kalmar L., Bors A., Farkas H., Vas S., Fandl B., Varga L., Fuest G., Tordai A.
Hum. Mutat. 22:498-498(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HAE TYR-130; PRO-394; VAL-408; CYS-466; GLU-473; GLU-493 AND ARG-498.
[48]"Normal C1 inhibitor mRNA expression level in type I hereditary angioedema patients: newly found C1 inhibitor gene mutations."
Kang H.-R., Yim E.-Y., Oh S.-Y., Chang Y.-S., Kim Y.-K., Cho S.-H., Min K.-U., Kim Y.-Y.
Allergy 61:260-264(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HAE ARG-345, VARIANTS ALA-56 AND MET-480.
[49]"Mutational spectrum and geno-phenotype correlation in Chinese families with Hereditary Angioedema."
Xu Y.Y., Zhi Y.X., Yin J., Wang L.L., Wen L.P., Gu J.Q., Guan K., Craig T., Zhang H.Y.
Allergy 67:1430-1436(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: 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, VARIANTS ALA-56 AND MET-480.
+Additional computationally mapped references.

Web resources

Wikipedia

C1-inhibitor entry

SERPING1base

SERPING1 mutation db

GeneReviews
SeattleSNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M13690 mRNA. Translation: AAA35613.1.
M13656 mRNA. Translation: AAB59387.1.
X07427 expand/collapse EMBL AC list , X07428, X07429, X07430, X07431, X07432, X07433 Genomic DNA. Translation: CAA30314.1.
X07577 mRNA. Translation: CAA30469.1.
X54486 Genomic DNA. Translation: CAA38358.1.
AF435921 Genomic DNA. Translation: AAM21515.1.
AK293054 mRNA. Translation: BAF85743.1.
AK312626 mRNA. Translation: BAG35512.1.
BT006966 mRNA. Translation: AAP35612.1.
AB209826 mRNA. Translation: BAD93063.1.
AY904027 Genomic DNA. Translation: AAW69393.1.
AP000662 Genomic DNA. No translation available.
AP002893 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW73764.1.
BC011171 mRNA. Translation: AAH11171.1.
AY291075 Genomic DNA. Translation: AAQ19269.1.
M30688 Genomic DNA. Translation: AAA53096.1. Sequence problems.
M14036 mRNA. Translation: AAA51848.1.
M13203 mRNA. Translation: AAA51849.1.
S76944 Genomic DNA. Translation: AAB33044.2.
PIRITHUC1. S15386.
RefSeqNP_000053.2. NM_000062.2.
NP_001027466.1. NM_001032295.1.
XP_005274262.1. XM_005274205.1.
UniGeneHs.384598.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1M6Qmodel-A138-500[»]
2OAYX-ray2.35A119-500[»]
ProteinModelPortalP05155.
SMRP05155. Positions 126-498.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107171. 12 interactions.
DIPDIP-45635N.
IntActP05155. 6 interactions.

Protein family/group databases

MEROPSI04.024.

PTM databases

PhosphoSiteP05155.

Polymorphism databases

DMDM124096.

Proteomic databases

PaxDbP05155.
PeptideAtlasP05155.
PRIDEP05155.

Protocols and materials databases

DNASU710.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000278407; ENSP00000278407; ENSG00000149131.
GeneID710.
KEGGhsa:710.
UCSCuc001nkp.1. human.

Organism-specific databases

CTD710.
GeneCardsGC11P057364.
HGNCHGNC:1228. SERPING1.
HPACAB026161.
HPA048738.
MIM106100. phenotype.
606860. gene.
neXtProtNX_P05155.
Orphanet100050. Hereditary angioedema type 1.
100051. Hereditary angioedema type 2.
169147. Immunodeficiency due to an early component of complement deficiency.
PharmGKBPA35029.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG4826.
HOVERGENHBG104060.
KOK04001.
PhylomeDBP05155.
TreeFamTF317350.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.

Gene expression databases

ArrayExpressP05155.
BgeeP05155.
GenevestigatorP05155.

Family and domain databases

InterProIPR015553. C1-inh.
IPR023795. Serpin_CS.
IPR023796. Serpin_dom.
IPR000215. Serpin_fam.
[Graphical view]
PANTHERPTHR11461. PTHR11461. 1 hit.
PTHR11461:SF21. PTHR11461:SF21. 1 hit.
PfamPF00079. Serpin. 1 hit.
[Graphical view]
SMARTSM00093. SERPIN. 1 hit.
[Graphical view]
SUPFAMSSF56574. SSF56574. 1 hit.
PROSITEPS00284. SERPIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSERPING1. human.
EvolutionaryTraceP05155.
GeneWikiC1-inhibitor.
GenomeRNAi710.
NextBio2886.
PMAP-CutDBP05155.
PROP05155.
SOURCESearch...

Entry information

Entry nameIC1_HUMAN
AccessionPrimary (citable) accession number: P05155
Secondary accession number(s): A6NMU0 expand/collapse secondary AC list , A8KAI9, B2R6L5, Q16304, Q547W3, Q59EI5, Q7Z455, Q96FE0, Q9UC49, Q9UCF9
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: February 1, 1991
Last modified: March 19, 2014
This is version 176 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM