ANT3_MOUSE
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 03-AUG-2022, entry version 174.
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, Spleen,
RC 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 STRING; 10090.ENSMUSP00000068971; -.
DR MEROPS; I04.018; -.
DR GlyGen; P32261; 4 sites.
DR iPTMnet; P32261; -.
DR PhosphoSitePlus; P32261; -.
DR SwissPalm; P32261; -.
DR CPTAC; non-CPTAC-3338; -.
DR jPOST; P32261; -.
DR PaxDb; P32261; -.
DR PeptideAtlas; P32261; -.
DR PRIDE; P32261; -.
DR ProteomicsDB; 282124; -.
DR Antibodypedia; 793; 861 antibodies from 42 providers.
DR DNASU; 11905; -.
DR Ensembl; ENSMUST00000064725; ENSMUSP00000068971; ENSMUSG00000026715.
DR GeneID; 11905; -.
DR KEGG; mmu:11905; -.
DR UCSC; uc007dem.2; mouse.
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; PICIYRN; -.
DR OrthoDB; 1124079at2759; -.
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 72 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 85 other tissues.
DR ExpressionAtlas; P32261; baseline and differential.
DR Genevisible; P32261; MM.
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:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
DR GO; GO:2000266; P:regulation of blood coagulation, intrinsic pathway; IEA:InterPro.
DR GO; GO:0007584; P:response to nutrient; ISO:MGI.
DR CDD; cd02045; serpinC1_AT3; 1.
DR Gene3D; 2.30.39.10; -; 1.
DR Gene3D; 3.30.497.10; -; 1.
DR InterPro; IPR033829; Antithrombin_3_serpin_domain.
DR InterPro; IPR015555; AT-III.
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:SF53; PTHR11461:SF53; 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; 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
