ID A0A2Y9DDZ2_TRIMA Unreviewed; 465 AA.
AC A0A2Y9DDZ2;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Antithrombin-III {ECO:0000256|ARBA:ARBA00015267};
DE AltName: Full=Serpin C1 {ECO:0000256|ARBA:ARBA00033153};
GN Name=LOC101343760 {ECO:0000313|RefSeq:XP_004372886.1};
OS Trichechus manatus latirostris (Florida manatee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_004372886.1};
RN [1] {ECO:0000313|RefSeq:XP_004372886.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBUNIT: Forms protease inhibiting heterodimer with TMPRSS7.
CC {ECO:0000256|ARBA:ARBA00011096}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000256|ARBA:ARBA00004239}.
CC -!- SIMILARITY: Belongs to the serpin family.
CC {ECO:0000256|ARBA:ARBA00009500, ECO:0000256|RuleBase:RU000411}.
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DR RefSeq; XP_004372886.1; XM_004372829.2.
DR AlphaFoldDB; A0A2Y9DDZ2; -.
DR STRING; 127582.A0A2Y9DDZ2; -.
DR GeneID; 101343760; -.
DR KEGG; tmu:101343760; -.
DR InParanoid; A0A2Y9DDZ2; -.
DR OrthoDB; 3218836at2759; -.
DR Proteomes; UP000248480; Unplaced.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
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; 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: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.
DR PROSITE; PS00284; SERPIN; 1.
PE 3: Inferred from homology;
KW Blood coagulation {ECO:0000256|ARBA:ARBA00023084};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hemostasis {ECO:0000256|ARBA:ARBA00022696};
KW Heparin-binding {ECO:0000256|ARBA:ARBA00022674};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000248480};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..465
FT /note="Antithrombin-III"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016163970"
FT DOMAIN 93..462
FT /note="Serpin"
FT /evidence="ECO:0000259|SMART:SM00093"
SQ SEQUENCE 465 AA; 52715 MW; 5DC467196CB1835C CRC64;
MFSNGEGTAA AGKRKVCLLS LLLVGLWSCA TCHWNLVEDI CTAKPRDIPV NPMCIYRSPE
KKAIEEEGPE QKIPEATNRR VWELSKANTR FATAFYQHLA DSKNDNDNIF LSPLSISTAF
AMTKLGACDN TLKQLMEVFK FDTISEKTSD QVHFFFAKLN CRLYRKANKS SELVSANRLF
GDKSLTFNET YQDISEVVYG AKLQPLDFKE NAEQSRVTIN NWVANKTEGR ITDVIPEKAI
NELTVLVLVN TIYFKGLWKS KFSPENTRKE LFYKDDGESC PVSMMYQEGK FRYRRVAEGT
QVLELPFKGD DITMVLILPK PEKRLAKVEQ QLSPEVQQEW LDELEETMLV VHMPRFRIED
SFSVKEQLQD MGLVDLFSPE KARLPGIVAE GREDLYVSDA FHKAFLEVNE EGSEAAASTA
IVIAGRSLNP SRVTFKANRP FLVLIREVAL NTVIFMGRVA NPCVN
//
