ANT3_SHEEP
ID ANT3_SHEEP Reviewed; 465 AA.
AC P32262;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Antithrombin-III;
DE Short=ATIII;
DE AltName: Full=Serpin C1;
DE Flags: Precursor;
GN Name=SERPINC1; Synonyms=AT3;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1482684; DOI=10.1016/0167-4781(92)90123-h;
RA Niessen R.W.L.M., Sturk A., Hordijk P.L., Michiels F., Peters M.;
RT "Sequence characterization of a sheep cDNA for antithrombin III.";
RL Biochim. Biophys. Acta 1171:207-210(1992).
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; X68287; CAA48347.1; -; mRNA.
DR PIR; S28219; S28219.
DR RefSeq; NP_001009393.1; NM_001009393.1.
DR AlphaFoldDB; P32262; -.
DR SMR; P32262; -.
DR STRING; 9940.ENSOARP00000013845; -.
DR MEROPS; I04.018; -.
DR PRIDE; P32262; -.
DR Ensembl; ENSOART00020023586; ENSOARP00020019560; ENSOARG00020015384.
DR GeneID; 443407; -.
DR KEGG; oas:443407; -.
DR CTD; 462; -.
DR eggNOG; KOG2392; Eukaryota.
DR OrthoDB; 1124079at2759; -.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0002020; F:protease binding; IEA:Ensembl.
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: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; 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 2: Evidence at transcript 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_0000032492"
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:0000255"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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; 52499 MW; E075EFAE51D5F118 CRC64;
MISNGIGTVT TGKRSMCLFP LLLIGLWGCV TCHRSPVEDI CTAKPRDIPV NPMCIYRSPE
KKATEGEGSE QKIPGATNRR VWELSKANSH FATAFYQHLA DSKNNNDNIF LSPLSISTAF
AMTKLGACNN TLKQLMEVFK FDTISEKTSD QIHFFFAKLN CRLYRKANKS SELVSANRLF
GDKSITFNET YQDISEVVYG AKLQPLDFKG NAEQSRLTIN QWISNKTEGR ITDVIPPQAI
DEFTVLVLVN TIYFKGLWKS KFSPENTKKE LFYKADGESC SVPMMYQEGK FRYRRVAEGT
QVLELPFKGD DITMVLILPK LEKPLAKVER ELTPDMLQEW LDELTETLLV VHMPHFRIED
SFSVKEQLQD MGLEDLFSPE KSRLPGIVAE GRNDLYVSDA FHKAFLEVNE EGSEAAASTV
ISIAGRSLNL NRVTFQANRP FLVLIREVAL NTIIFMGRVA NPCVN
