ID ANT3_BOVIN Reviewed; 465 AA. AC P41361; Q3SZQ7; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 27-JUN-2006, sequence version 2. DT 24-JAN-2024, entry version 144. DE RecName: Full=Antithrombin-III; DE Short=ATIII; DE AltName: Full=Serpin C1; DE Flags: Precursor; GN Name=SERPINC1; Synonyms=AT3; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Hereford; TISSUE=Testis; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. RN [2] RP PROTEIN SEQUENCE OF 33-465. RX PubMed=1930634; DOI=10.1007/bf01024785; RA Mejdoub H., le Ret M., Boulanger Y., Maman M., Choay J., Reinbolt J.; RT "The complete amino acid sequence of bovine antithrombin (ATIII)."; RL J. Protein Chem. 10:205-212(1991). RN [3] RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 33-465. RX PubMed=8331659; DOI=10.1006/jmbi.1993.1378; RA Mourey L., Samama J.-P., Delarue M., Petitou M., Choay J., Moras D.; RT "Crystal structure of cleaved bovine antithrombin III at 3.2-A RT resolution."; RL J. Mol. Biol. 232:223-241(1993). 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}. 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; BC102747; AAI02748.1; -; mRNA. DR PIR; A61435; A61435. DR RefSeq; NP_001029870.1; NM_001034698.2. DR PDB; 1ATT; X-ray; 3.20 A; A/B=37-465. DR PDBsum; 1ATT; -. DR AlphaFoldDB; P41361; -. DR SMR; P41361; -. DR STRING; 9913.ENSBTAP00000072452; -. DR ChEMBL; CHEMBL2150842; -. DR MEROPS; I04.018; -. DR GlyCosmos; P41361; 4 sites, No reported glycans. DR PaxDb; 9913-ENSBTAP00000005713; -. DR PeptideAtlas; P41361; -. DR GeneID; 540261; -. DR KEGG; bta:540261; -. DR CTD; 462; -. DR eggNOG; KOG2392; Eukaryota. DR InParanoid; P41361; -. DR OrthoDB; 3218836at2759; -. DR EvolutionaryTrace; P41361; -. DR PRO; PR:P41361; -. DR Proteomes; UP000009136; Unplaced. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW. DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW. DR GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW. DR GO; GO:0030193; P:regulation of blood coagulation; IEA:InterPro. 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; 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. PE 1: Evidence at protein level; KW 3D-structure; Blood coagulation; Direct protein sequencing; Disulfide bond; KW Glycoprotein; Hemostasis; Heparin-binding; Phosphoprotein; KW Protease inhibitor; Reference proteome; Secreted; KW Serine protease inhibitor; Signal. FT SIGNAL 1..32 FT /evidence="ECO:0000269|PubMed:1930634" FT CHAIN 33..465 FT /note="Antithrombin-III" FT /id="PRO_0000094123" 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 CARBOHYD 168 FT /note="N-linked (GlcNAc...) asparagine" FT CARBOHYD 188 FT /note="N-linked (GlcNAc...) asparagine" FT CARBOHYD 225 FT /note="N-linked (GlcNAc...) asparagine" FT DISULFID 41..161 FT DISULFID 54..128 FT DISULFID 280..463 FT CONFLICT 129 FT /note="N -> D (in Ref. 1; AAI02748)" FT /evidence="ECO:0000305" FT CONFLICT 133 FT /note="K -> T (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 182 FT /note="G -> D (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 441 FT /note="I -> F (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT TURN 39..42 FT /evidence="ECO:0007829|PDB:1ATT" FT TURN 77..80 FT /evidence="ECO:0007829|PDB:1ATT" FT HELIX 81..102 FT /evidence="ECO:0007829|PDB:1ATT" FT STRAND 109..111 FT /evidence="ECO:0007829|PDB:1ATT" FT HELIX 113..123 FT /evidence="ECO:0007829|PDB:1ATT" FT TURN 124..126 FT /evidence="ECO:0007829|PDB:1ATT" FT HELIX 129..138 FT /evidence="ECO:0007829|PDB:1ATT" FT HELIX 141..143 FT /evidence="ECO:0007829|PDB:1ATT" FT HELIX 149..161 FT /evidence="ECO:0007829|PDB:1ATT" FT TURN 168..170 FT /evidence="ECO:0007829|PDB:1ATT" FT STRAND 178..182 FT /evidence="ECO:0007829|PDB:1ATT" FT HELIX 189..199 FT /evidence="ECO:0007829|PDB:1ATT" FT STRAND 202..206 FT /evidence="ECO:0007829|PDB:1ATT" FT HELIX 208..226 FT /evidence="ECO:0007829|PDB:1ATT" FT TURN 227..229 FT /evidence="ECO:0007829|PDB:1ATT" FT STRAND 244..260 FT /evidence="ECO:0007829|PDB:1ATT" FT STRAND 266..273 FT /evidence="ECO:0007829|PDB:1ATT" FT STRAND 279..296 FT /evidence="ECO:0007829|PDB:1ATT" FT TURN 297..299 FT /evidence="ECO:0007829|PDB:1ATT" FT STRAND 300..307 FT /evidence="ECO:0007829|PDB:1ATT" FT STRAND 310..319 FT /evidence="ECO:0007829|PDB:1ATT" FT HELIX 325..330 FT /evidence="ECO:0007829|PDB:1ATT" FT HELIX 337..342 FT /evidence="ECO:0007829|PDB:1ATT" FT STRAND 345..363 FT /evidence="ECO:0007829|PDB:1ATT" FT HELIX 364..371 FT /evidence="ECO:0007829|PDB:1ATT" FT HELIX 375..377 FT /evidence="ECO:0007829|PDB:1ATT" FT TURN 379..381 FT /evidence="ECO:0007829|PDB:1ATT" FT STRAND 387..391 FT /evidence="ECO:0007829|PDB:1ATT" FT STRAND 396..409 FT /evidence="ECO:0007829|PDB:1ATT" FT STRAND 412..425 FT /evidence="ECO:0007829|PDB:1ATT" FT STRAND 441..447 FT /evidence="ECO:0007829|PDB:1ATT" FT TURN 448..450 FT /evidence="ECO:0007829|PDB:1ATT" FT STRAND 453..459 FT /evidence="ECO:0007829|PDB:1ATT" SQ SEQUENCE 465 AA; 52347 MW; B674E579154F291F CRC64; MISNGIGTVT AGKRSICLLP LLLIGLWGCV TCHRSPVEDV CTAKPRDIPV NPMCIYRSSE KKATEGQGSE QKIPGATNRR VWELSKANSH FATAFYQHLA DSKNNNDNIF LSPLSISTAF AMTKLGACNN TLKQLMEVFK FDTISEKTSD QIHFFFAKLN CRLYRKANKS SELVSANRLF GGKSITFNET YQDISEVVYG AKLQPLDFKG NAEQSRLTIN QWISNKTEGR ITDVIPPQAI NEFTVLVLVN TIYFKGLWKS KFSPENTRKE LFYKADGESC SVLMMYQESK FRYRRVAEST QVLELPFKGD DITMVLILPK LEKTLAKVEQ ELTPDMLQEW LDELTETLLV VHMPRFRIED SFSVKEQLQD MGLEDLFSPE KSRLPGIVAE GRSDLYVSDA FHKAFLEVNE EGSEAAASTV ISIAGRSLNS DRVTFKANRP ILVLIREVAL NTIIFMGRVA NPCVD //