IC1_MOUSE
ID IC1_MOUSE Reviewed; 504 AA.
AC P97290; A2ATR7; O88330; Q99M43; Q9QX09;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Plasma protease C1 inhibitor;
DE Short=C1 Inh;
DE Short=C1Inh;
DE AltName: Full=C1 esterase inhibitor;
DE AltName: Full=C1-inhibiting factor;
DE AltName: Full=Serpin G1;
DE Flags: Precursor;
GN Name=Serping1; Synonyms=C1nh;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=9199246; DOI=10.1016/s0167-4781(97)00056-0;
RA Russell J.A., Whaley K., Heaphy S.;
RT "The sequence of a cDNA encoding functional murine C1-inhibitor protein.";
RL Biochim. Biophys. Acta 1352:156-160(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=129/Sv, and BALB/cJ;
RX PubMed=9652403; DOI=10.1046/j.1432-1327.1998.2540117.x;
RA Lener M., Vinci G., Duponchel C., Meo T., Tosi M.;
RT "Molecular cloning, gene structure and expression profile of mouse C1
RT inhibitor.";
RL Eur. J. Biochem. 254:117-122(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-243.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=16944957; DOI=10.1021/pr060186m;
RA Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.;
RT "Proteome-wide characterization of N-glycosylation events by diagonal
RT chromatography.";
RL J. Proteome Res. 5:2438-2447(2006).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-243.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=17330941; DOI=10.1021/pr0604559;
RA Bernhard O.K., Kapp E.A., Simpson R.J.;
RT "Enhanced analysis of the mouse plasma proteome using cysteine-containing
RT tryptic glycopeptides.";
RL J. Proteome Res. 6:987-995(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Activation of the C1 complex is under control of the C1-
CC inhibitor. It forms a proteolytically inactive stoichiometric complex
CC with the C1r or C1s proteases. May play a potentially crucial role in
CC regulating important physiological pathways including complement
CC activation, blood coagulation, fibrinolysis and the generation of
CC kinins. Very efficient inhibitor of FXIIa. May inhibit chymotrypsin and
CC kallikrein.
CC -!- SUBUNIT: Interacts with MASP1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Y10386; CAA71412.1; -; mRNA.
DR EMBL; AF010254; AAC40136.1; -; mRNA.
DR EMBL; AF052039; AAC40149.1; -; Genomic_DNA.
DR EMBL; AL928914; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002026; AAH02026.1; -; mRNA.
DR CCDS; CCDS16193.1; -.
DR RefSeq; NP_033906.2; NM_009776.3.
DR RefSeq; XP_006498686.1; XM_006498623.3.
DR AlphaFoldDB; P97290; -.
DR SMR; P97290; -.
DR STRING; 10090.ENSMUSP00000023994; -.
DR MEROPS; I04.024; -.
DR GlyGen; P97290; 5 sites.
DR iPTMnet; P97290; -.
DR PhosphoSitePlus; P97290; -.
DR CPTAC; non-CPTAC-3370; -.
DR jPOST; P97290; -.
DR MaxQB; P97290; -.
DR PaxDb; P97290; -.
DR PeptideAtlas; P97290; -.
DR PRIDE; P97290; -.
DR ProteomicsDB; 267209; -.
DR Antibodypedia; 14214; 594 antibodies from 39 providers.
DR DNASU; 12258; -.
DR Ensembl; ENSMUST00000023994; ENSMUSP00000023994; ENSMUSG00000023224.
DR GeneID; 12258; -.
DR KEGG; mmu:12258; -.
DR UCSC; uc008kjd.2; mouse.
DR CTD; 710; -.
DR MGI; MGI:894696; Serping1.
DR VEuPathDB; HostDB:ENSMUSG00000023224; -.
DR eggNOG; KOG2392; Eukaryota.
DR GeneTree; ENSGT00940000159681; -.
DR HOGENOM; CLU_023330_3_0_1; -.
DR InParanoid; P97290; -.
DR OMA; EFFDFTY; -.
DR OrthoDB; 1124079at2759; -.
DR PhylomeDB; P97290; -.
DR TreeFam; TF317350; -.
DR Reactome; R-MMU-114608; Platelet degranulation.
DR Reactome; R-MMU-140837; Intrinsic Pathway of Fibrin Clot Formation.
DR Reactome; R-MMU-977606; Regulation of Complement cascade.
DR BioGRID-ORCS; 12258; 2 hits in 70 CRISPR screens.
DR ChiTaRS; Serping1; mouse.
DR PRO; PR:P97290; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P97290; protein.
DR Bgee; ENSMUSG00000023224; Expressed in left lobe of liver and 222 other tissues.
DR ExpressionAtlas; P97290; baseline and differential.
DR Genevisible; P97290; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:MGI.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR GO; GO:0042730; P:fibrinolysis; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0001869; P:negative regulation of complement activation, lectin pathway; ISS:UniProtKB.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
DR Gene3D; 2.30.39.10; -; 1.
DR Gene3D; 3.30.497.10; -; 1.
DR InterPro; IPR015553; C1-inh.
DR InterPro; IPR023795; Serpin_CS.
DR InterPro; IPR023796; Serpin_dom.
DR InterPro; IPR000215; Serpin_fam.
DR InterPro; IPR036186; Serpin_sf.
DR InterPro; IPR042178; Serpin_sf_1.
DR InterPro; IPR042185; Serpin_sf_2.
DR PANTHER; PTHR11461; PTHR11461; 1.
DR PANTHER; PTHR11461:SF159; PTHR11461:SF159; 1.
DR Pfam; PF00079; Serpin; 1.
DR SMART; SM00093; SERPIN; 1.
DR SUPFAM; SSF56574; SSF56574; 1.
DR PROSITE; PS00284; SERPIN; 1.
PE 1: Evidence at protein level;
KW Blood coagulation; Complement pathway; Disulfide bond; Fibrinolysis;
KW Glycoprotein; Hemostasis; Immunity; Innate immunity; Protease inhibitor;
KW Reference proteome; Secreted; Serine protease inhibitor; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000250"
FT CHAIN 23..504
FT /note="Plasma protease C1 inhibitor"
FT /id="PRO_0000032515"
FT REGION 22..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 470..471
FT /note="Reactive bond"
FT /evidence="ECO:0000250"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957,
FT ECO:0000269|PubMed:17330941"
FT CARBOHYD 356
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 128..432
FT /evidence="ECO:0000250"
FT DISULFID 135..210
FT /evidence="ECO:0000250"
FT CONFLICT 291
FT /note="C -> R (in Ref. 2; AAC40136)"
FT /evidence="ECO:0000305"
FT CONFLICT 421
FT /note="E -> K (in Ref. 1; CAA71412)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 504 AA; 55585 MW; B27BBDC05D318E62 CRC64;
MASRLTPLTL LLLLLAGDRA FSDPEATSHS TQDPLEAQAK SRESFPERDD SWSPPEPTVL
PSTWPTTSVA ITITNDTMGK VANESFSQHS QPAAQLPTDS PGQPPLNSSS QPSTASDLPT
QATTEPFCPE PLAQCSDSDR DSSEAKLSEA LTDFSVKLYH AFSATKMAKT NMAFSPFSIA
SLLTQVLLGA GDSTKSNLES ILSYPKDFAC VHQALKGFSS KGVTSVSQIF HSPDLAIRDT
YVNASQSLYG SSPRVLGPDS AANLELINTW VAENTNHKIR KLLDSLPSDT CLVLLNAVYL
SAKWKITFEP KKMMAPFFYK NSMIKVPMMS SVKYPVAQFD DHTLKAKVGQ LQLSHNLSFV
IVVPVFPKHQ LKDVEKALNP TVFKAIMKKL ELSKFLPTYL TMPHIKVKSS QDMLSVMEKL
EFFDFTYDLN LCGLTEDPDL QVSAMKHETV LELTESGVEA AAASAISFGR SLPIFEVQRP
FLFLLWDQQH RFPVFMGRVY DPRG
