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

 IC1_MOUSE               Reviewed;         504 AA.
P97290; A2ATR7; O88330; Q99M43; Q9QX09;
27-APR-2001, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 3.
20-JUN-2018, entry version 163.
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=C1nh;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=9199246; DOI=10.1016/S0167-4781(97)00056-0;
Russell J.A., Whaley K., Heaphy S.;
"The sequence of a cDNA encoding functional murine C1-inhibitor
protein.";
Biochim. Biophys. Acta 1352:156-160(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
STRAIN=129/Sv, and BALB/cJ;
PubMed=9652403; DOI=10.1046/j.1432-1327.1998.2540117.x;
Lener M., Vinci G., Duponchel C., Meo T., Tosi M.;
"Molecular cloning, gene structure and expression profile of mouse C1
inhibitor.";
Eur. J. Biochem. 254:117-122(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Mammary tumor;
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).
[5]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-243.
STRAIN=C57BL/6J; TISSUE=Plasma;
PubMed=16944957; DOI=10.1021/pr060186m;
Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J.,
Gevaert K.;
"Proteome-wide characterization of N-glycosylation events by diagonal
chromatography.";
J. Proteome Res. 5:2438-2447(2006).
[6]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-243.
STRAIN=C57BL/6J; TISSUE=Plasma;
PubMed=17330941; DOI=10.1021/pr0604559;
Bernhard O.K., Kapp E.A., Simpson R.J.;
"Enhanced analysis of the mouse plasma proteome using cysteine-
containing tryptic glycopeptides.";
J. Proteome Res. 6:987-995(2007).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- 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.
May inhibit chymotrypsin and kallikrein.
-!- SUBUNIT: Interacts with MASP1. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; Y10386; CAA71412.1; -; mRNA.
EMBL; AF010254; AAC40136.1; -; mRNA.
EMBL; AF052039; AAC40149.1; -; Genomic_DNA.
EMBL; AL928914; CAM23311.1; -; Genomic_DNA.
EMBL; BC002026; AAH02026.1; -; mRNA.
CCDS; CCDS16193.1; -.
RefSeq; NP_033906.2; NM_009776.3.
RefSeq; XP_006498686.1; XM_006498623.3.
UniGene; Mm.38888; -.
ProteinModelPortal; P97290; -.
SMR; P97290; -.
IntAct; P97290; 1.
MINT; P97290; -.
STRING; 10090.ENSMUSP00000023994; -.
MEROPS; I04.024; -.
iPTMnet; P97290; -.
PhosphoSitePlus; P97290; -.
MaxQB; P97290; -.
PaxDb; P97290; -.
PeptideAtlas; P97290; -.
PRIDE; P97290; -.
Ensembl; ENSMUST00000023994; ENSMUSP00000023994; ENSMUSG00000023224.
GeneID; 12258; -.
KEGG; mmu:12258; -.
UCSC; uc008kjd.2; mouse.
CTD; 710; -.
MGI; MGI:894696; Serping1.
eggNOG; KOG2392; Eukaryota.
eggNOG; COG4826; LUCA.
GeneTree; ENSGT00920000149046; -.
HOGENOM; HOG000231936; -.
HOVERGEN; HBG104060; -.
InParanoid; P97290; -.
KO; K04001; -.
OMA; IYLSAKW; -.
OrthoDB; EOG091G03BW; -.
TreeFam; TF317350; -.
Reactome; R-MMU-114608; Platelet degranulation.
Reactome; R-MMU-140837; Intrinsic Pathway of Fibrin Clot Formation.
Reactome; R-MMU-977606; Regulation of Complement cascade.
ChiTaRS; Serping1; mouse.
PRO; PR:P97290; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000023224; -.
ExpressionAtlas; P97290; baseline and differential.
Genevisible; P97290; MM.
GO; GO:0005615; C:extracellular space; IDA:MGI.
GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:MGI.
GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
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; ISS:UniProtKB.
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;
Blood coagulation; Complement pathway; Complete proteome;
Disulfide bond; Fibrinolysis; Glycoprotein; Hemostasis; Immunity;
Innate immunity; Protease inhibitor; Reference proteome; Secreted;
Serine protease inhibitor; Signal.
SIGNAL 1 22 {ECO:0000250}.
CHAIN 23 504 Plasma protease C1 inhibitor.
/FTId=PRO_0000032515.
SITE 470 471 Reactive bond. {ECO:0000250}.
CARBOHYD 75 75 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 83 83 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 107 107 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 243 243 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16944957,
ECO:0000269|PubMed:17330941}.
CARBOHYD 356 356 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 128 432 {ECO:0000250}.
DISULFID 135 210 {ECO:0000250}.
CONFLICT 291 291 C -> R (in Ref. 2; AAC40136).
{ECO:0000305}.
CONFLICT 421 421 E -> K (in Ref. 1; CAA71412).
{ECO:0000305}.
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


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