IC1_RAT
ID IC1_RAT Reviewed; 504 AA.
AC Q6P734;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 125.
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;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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).
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. Inhibits chymotrypsin and
CC kallikrein (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with MASP1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
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DR EMBL; BC061860; AAH61860.1; -; mRNA.
DR RefSeq; NP_954524.1; NM_199093.1.
DR RefSeq; XP_006234509.1; XM_006234447.2.
DR AlphaFoldDB; Q6P734; -.
DR SMR; Q6P734; -.
DR STRING; 10116.ENSRNOP00000009817; -.
DR GlyGen; Q6P734; 5 sites.
DR PaxDb; Q6P734; -.
DR PRIDE; Q6P734; -.
DR Ensembl; ENSRNOT00000009817; ENSRNOP00000009817; ENSRNOG00000007457.
DR GeneID; 295703; -.
DR KEGG; rno:295703; -.
DR UCSC; RGD:735225; rat.
DR CTD; 710; -.
DR RGD; 735225; Serping1.
DR eggNOG; KOG2392; Eukaryota.
DR GeneTree; ENSGT00940000159681; -.
DR HOGENOM; CLU_023330_3_0_1; -.
DR InParanoid; Q6P734; -.
DR OMA; EFFDFTY; -.
DR OrthoDB; 1124079at2759; -.
DR PhylomeDB; Q6P734; -.
DR TreeFam; TF317350; -.
DR Reactome; R-RNO-114608; Platelet degranulation.
DR Reactome; R-RNO-140837; Intrinsic Pathway of Fibrin Clot Formation.
DR Reactome; R-RNO-977606; Regulation of Complement cascade.
DR PRO; PR:Q6P734; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000007457; Expressed in liver and 19 other tissues.
DR Genevisible; Q6P734; RN.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0001848; F:complement binding; ISO:RGD.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; ISS:UniProtKB.
DR GO; GO:0007568; P:aging; IEP:RGD.
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 2: Evidence at transcript level;
KW Blood coagulation; Complement pathway; Fibrinolysis; Glycoprotein;
KW 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_0000248966"
FT REGION 23..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 469..470
FT /note="Reactive bond for chymotrypsin"
FT /evidence="ECO:0000250"
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:0000255"
FT CARBOHYD 356
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 504 AA; 55611 MW; 5EADC6331BEA730D CRC64;
MASKLTPLTL LLLLLAGDRA FSDSEVTSHS SQDPLVVQEG SRDSVPERDG SRSPIEHTGQ
SSTWPTTSGS TKISNDTMDQ VANESFIQHV QPAAQLPEDS PSQSPVNSSS PPSTASAPPT
QAPTEPLCPE PLAWCSDSDR DSSEATLSEA LTDFSVKLYH AFSATKKAET NMAFSPFSIA
SLLTQVLLGA GDSTKSNLED ILSYPKDFAC VHQTLKAFSS KGVTSVSQIF HSPDLAIRDT
YVNASLSLYG SSPRVLGPDG DANLKLINTW VAENTNHKIN ELLDSLPSDT RLVLLNAVYL
SAKWKKTFEQ KKMMASFLYK NSMIKVPMLS SKKYPLALFN DQTLKAKVGQ LQLSHNLSFV
IMVPQSPTHQ LEDMEKALNP TVFKAILKKL ELSKFQPTYV MMPRIKVKSS QDMLSIMEKL
EFFDFTYDLN LCGLTEDPDL QVSSMKHETV LELTETGVEA AAASTISVAR NLLIFEVQQP
FLFLLWDQRH KFPVFMGRVY DPRA
