ID   ANT3_PONAB              Reviewed;         464 AA.
AC   Q5R5A3;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Antithrombin-III;
DE            Short=ATIII;
DE   AltName: Full=Serpin C1;
DE   Flags: Precursor;
GN   Name=SERPINC1; Synonyms=AT3;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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; CR860961; CAH93063.1; -; mRNA.
DR   RefSeq; NP_001126813.1; NM_001133341.1.
DR   AlphaFoldDB; Q5R5A3; -.
DR   SMR; Q5R5A3; -.
DR   STRING; 9601.ENSPPYP00000000566; -.
DR   MEROPS; I04.018; -.
DR   PRIDE; Q5R5A3; -.
DR   Ensembl; ENSPPYT00000040391; ENSPPYP00000030713; ENSPPYG00000000491.
DR   GeneID; 100173818; -.
DR   KEGG; pon:100173818; -.
DR   CTD; 462; -.
DR   eggNOG; KOG2392; Eukaryota.
DR   GeneTree; ENSGT00940000157967; -.
DR   HOGENOM; CLU_023330_0_2_1; -.
DR   InParanoid; Q5R5A3; -.
DR   OrthoDB; 1124079at2759; -.
DR   TreeFam; TF343094; -.
DR   Proteomes; UP000001595; Chromosome 1.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
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: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..464
FT                   /note="Antithrombin-III"
FT                   /id="PRO_0000032491"
FT   BINDING         81
FT                   /ligand="heparin"
FT                   /ligand_id="ChEBI:CHEBI:28304"
FT                   /evidence="ECO:0000250"
FT   BINDING         161
FT                   /ligand="heparin"
FT                   /ligand_id="ChEBI:CHEBI:28304"
FT                   /evidence="ECO:0000250"
FT   BINDING         177
FT                   /ligand="heparin"
FT                   /ligand_id="ChEBI:CHEBI:28304"
FT                   /evidence="ECO:0000250"
FT   SITE            425..426
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         63
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P01008"
FT   MOD_RES         68
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P01008"
FT   CARBOHYD        128
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        167
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        187
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        224
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        40..160
FT                   /evidence="ECO:0000250"
FT   DISULFID        53..127
FT                   /evidence="ECO:0000250"
FT   DISULFID        279..462
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   464 AA;  52639 MW;  D2C02CE9625AD2B0 CRC64;
     MYSNVIGTIT SGKRKVYLLS LLLIGFWDCV TCHGSPVDIC IAKPRDIPMN PMCIYRSPEK
     KATEDEGSEQ KIPEATNRRV WELSKANSRF ATTFYQHLAD SKNDNDNIFL SPLSISTAFA
     MTKLGACNDT LQQLMEVFKF DTISEKTSDQ IHFFFAKLNC RLYRKANKSS KLVSANRLFG
     DKSLTFNETY QDISELVYGA KLQPLDFKEN AEQSRAAINK WVSNKTEGRI TDVIPPEAIN
     ELTVLVLVNT IYFKGLWKSK FSPENTRKEL FYKADGESCS ASMMYQEGKF RYRRVAEGTQ
     VLELPFKGDD ITMVLILPKP EKSLAKVEKE LTPEVLQEWL DELEEMMLVV HMPRFRIEDG
     FSLKEQLQDM GLVDLFSPEK SKLPGIVAEG RDDLYVSDAF HKAFLEVNEE GSEAAASTAV
     VIAGRSLNPN RVTFKANRPF LVFIREVPLN TIIFMGRVAN PCVK