ID   ANT3_MOUSE              Reviewed;         465 AA.
AC   P32261;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   27-MAR-2024, entry version 183.
DE   RecName: Full=Antithrombin-III;
DE            Short=ATIII;
DE   AltName: Full=Serpin C1;
DE   Flags: Precursor;
GN   Name=Serpinc1; Synonyms=At3;
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].
RX   PubMed=1440494;
RA   Wu J.K., Sheffield W.P., Blajchman M.A.;
RT   "Molecular cloning and cell-free expression of mouse antithrombin III.";
RL   Thromb. Haemost. 68:291-296(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver;
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   [3]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-188.
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   [4]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-129; ASN-168 AND ASN-188.
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   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC   Spleen, and 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: Most important serine protease inhibitor in plasma that
CC       regulates the blood coagulation cascade. AT-III inhibits thrombin,
CC       matriptase-3/TMPRSS7, as well as factors IXa, Xa and XIa. Its
CC       inhibitory activity is greatly enhanced in the presence of heparin (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Forms protease inhibiting heterodimer with TMPRSS7.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Plasma.
CC   -!- PTM: Phosphorylated by FAM20C in the extracellular medium.
CC       {ECO:0000250|UniProtKB:P01008}.
CC   -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
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DR   EMBL; S47225; AAB23965.1; -; mRNA.
DR   EMBL; BC019447; AAH19447.1; -; mRNA.
DR   EMBL; BC033377; AAH33377.1; -; mRNA.
DR   CCDS; CCDS15411.1; -.
DR   RefSeq; NP_543120.1; NM_080844.4.
DR   RefSeq; XP_006496689.1; XM_006496626.2.
DR   AlphaFoldDB; P32261; -.
DR   SMR; P32261; -.
DR   BioGRID; 198229; 6.
DR   IntAct; P32261; 1.
DR   MINT; P32261; -.
DR   STRING; 10090.ENSMUSP00000068971; -.
DR   MEROPS; I04.018; -.
DR   GlyCosmos; P32261; 4 sites, No reported glycans.
DR   GlyGen; P32261; 5 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; P32261; -.
DR   PhosphoSitePlus; P32261; -.
DR   SwissPalm; P32261; -.
DR   CPTAC; non-CPTAC-3338; -.
DR   jPOST; P32261; -.
DR   PaxDb; 10090-ENSMUSP00000068971; -.
DR   PeptideAtlas; P32261; -.
DR   ProteomicsDB; 282124; -.
DR   Pumba; P32261; -.
DR   Antibodypedia; 793; 908 antibodies from 42 providers.
DR   DNASU; 11905; -.
DR   Ensembl; ENSMUST00000064725.11; ENSMUSP00000068971.6; ENSMUSG00000026715.13.
DR   GeneID; 11905; -.
DR   KEGG; mmu:11905; -.
DR   UCSC; uc007dem.2; mouse.
DR   AGR; MGI:88095; -.
DR   CTD; 462; -.
DR   MGI; MGI:88095; Serpinc1.
DR   VEuPathDB; HostDB:ENSMUSG00000026715; -.
DR   eggNOG; KOG2392; Eukaryota.
DR   GeneTree; ENSGT00940000157967; -.
DR   HOGENOM; CLU_023330_0_2_1; -.
DR   InParanoid; P32261; -.
DR   OMA; CQVPTMY; -.
DR   OrthoDB; 3218836at2759; -.
DR   PhylomeDB; P32261; -.
DR   TreeFam; TF343094; -.
DR   Reactome; R-MMU-140837; Intrinsic Pathway of Fibrin Clot Formation.
DR   Reactome; R-MMU-140875; Common Pathway of Fibrin Clot Formation.
DR   Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR   Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
DR   BioGRID-ORCS; 11905; 2 hits in 77 CRISPR screens.
DR   ChiTaRS; Serpinc1; mouse.
DR   PRO; PR:P32261; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; P32261; Protein.
DR   Bgee; ENSMUSG00000026715; Expressed in left lobe of liver and 87 other cell types or tissues.
DR   ExpressionAtlas; P32261; baseline and differential.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0005615; C:extracellular space; ISO:MGI.
DR   GO; GO:0008201; F:heparin binding; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0002020; F:protease binding; ISO:MGI.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; ISO:MGI.
DR   GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR   GO; GO:0030193; P:regulation of blood coagulation; IEA:InterPro.
DR   GO; GO:0007584; P:response to nutrient; ISO:MGI.
DR   CDD; cd02045; serpinC1_AT3; 1.
DR   Gene3D; 2.30.39.10; Alpha-1-antitrypsin, domain 1; 1.
DR   Gene3D; 3.30.497.10; Antithrombin, subunit I, domain 2; 1.
DR   InterPro; IPR033829; Antithrombin_3_serpin_domain.
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:SF53; ANTITHROMBIN-III; 1.
DR   PANTHER; PTHR11461; SERINE PROTEASE INHIBITOR, SERPIN; 1.
DR   Pfam; PF00079; Serpin; 1.
DR   SMART; SM00093; SERPIN; 1.
DR   SUPFAM; SSF56574; Serpins; 1.
DR   PROSITE; PS00284; SERPIN; 1.
DR   Genevisible; P32261; MM.
PE   1: Evidence at protein level;
KW   Blood coagulation; Disulfide bond; Glycoprotein; Hemostasis;
KW   Heparin-binding; Phosphoprotein; Protease inhibitor; Reference proteome;
KW   Secreted; Serine protease inhibitor; Signal.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000250"
FT   CHAIN           33..465
FT                   /note="Antithrombin-III"
FT                   /id="PRO_0000032490"
FT   BINDING         82
FT                   /ligand="heparin"
FT                   /ligand_id="ChEBI:CHEBI:28304"
FT                   /evidence="ECO:0000250"
FT   BINDING         162
FT                   /ligand="heparin"
FT                   /ligand_id="ChEBI:CHEBI:28304"
FT                   /evidence="ECO:0000250"
FT   BINDING         178
FT                   /ligand="heparin"
FT                   /ligand_id="ChEBI:CHEBI:28304"
FT                   /evidence="ECO:0000250"
FT   SITE            426..427
FT                   /note="Reactive bond"
FT   MOD_RES         64
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P01008"
FT   MOD_RES         69
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P01008"
FT   CARBOHYD        129
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:17330941"
FT   CARBOHYD        168
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:17330941"
FT   CARBOHYD        188
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16944957,
FT                   ECO:0000269|PubMed:17330941"
FT   CARBOHYD        225
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        41..161
FT                   /evidence="ECO:0000250"
FT   DISULFID        54..128
FT                   /evidence="ECO:0000250"
FT   DISULFID        280..463
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   465 AA;  52004 MW;  5CE087E98874E35D CRC64;
     MYSPGAGSGA AGERKLCLLS LLLIGALGCA ICHGNPVDDI CIAKPRDIPV NPLCIYRSPG
     KKATEEDGSE QKVPEATNRR VWELSKANSR FATNFYQHLA DSKNDNDNIF LSPLSISTAF
     AMTKLGACND TLKQLMEVFK FDTISEKTSD QIHFFFAKLN CRLYRKANKS SDLVSANRLF
     GDKSLTFNES YQDVSEVVYG AKLQPLDFKE NPEQSRVTIN NWVANKTEGR IKDVIPQGAI
     NELTALVLVN TIYFKGLWKS KFSPENTRKE PFYKVDGQSC PVPMMYQEGK FKYRRVAEGT
     QVLELPFKGD DITMVLILPK PEKSLAKVEQ ELTPELLQEW LDELSETMLV VHMPRFRTED
     GFSLKEQLQD MGLIDLFSPE KSQLPGIVAG GRDDLYVSDA FHKAFLEVNE EGSEAAASTS
     VVITGRSLNP NRVTFKANRP FLVLIREVAL NTIIFMGRVA NPCVN
//