ANT3_BOVIN
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 03-AUG-2022, entry version 139.
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}.
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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.ENSBTAP00000005713; -.
DR ChEMBL; CHEMBL2150842; -.
DR MEROPS; I04.018; -.
DR PaxDb; P41361; -.
DR PeptideAtlas; P41361; -.
DR PRIDE; P41361; -.
DR GeneID; 540261; -.
DR KEGG; bta:540261; -.
DR CTD; 462; -.
DR eggNOG; KOG2392; Eukaryota.
DR InParanoid; P41361; -.
DR OrthoDB; 1124079at2759; -.
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; IBA:GO_Central.
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 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; 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.
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
