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Database: UniProt
Entry: A0A026WI68_OOCBI
LinkDB: A0A026WI68_OOCBI
Original site: A0A026WI68_OOCBI 
ID   A0A026WI68_OOCBI        Unreviewed;       438 AA.
AC   A0A026WI68;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Antithrombin-III {ECO:0000313|EMBL:EZA54804.1};
GN   ORFNames=X777_05089 {ECO:0000313|EMBL:EZA54804.1};
OS   Ooceraea biroi (Clonal raider ant) (Cerapachys biroi).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Dorylinae; Ooceraea.
OX   NCBI_TaxID=2015173 {ECO:0000313|EMBL:EZA54804.1, ECO:0000313|Proteomes:UP000053097};
RN   [1] {ECO:0000313|EMBL:EZA54804.1, ECO:0000313|Proteomes:UP000053097}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24508170; DOI=10.1016/j.cub.2014.01.018;
RA   Oxley P.R., Ji L., Fetter-Pruneda I., McKenzie S.K., Li C., Hu H.,
RA   Zhang G., Kronauer D.J.;
RT   "The genome of the clonal raider ant Cerapachys biroi.";
RL   Curr. Biol. 24:451-458(2014).
CC   -!- SIMILARITY: Belongs to the serpin family.
CC       {ECO:0000256|RuleBase:RU000411}.
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DR   EMBL; KK107238; EZA54804.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A026WI68; -.
DR   EnsemblMetazoa; XM_026971155.1; XP_026826956.1; LOC113562280.
DR   OMA; MTKGHIR; -.
DR   OrthoDB; 3218836at2759; -.
DR   Proteomes; UP000053097; Unassembled WGS sequence.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   CDD; cd19594; serpin_crustaceans_chelicerates_insects; 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; 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:SF278; SERINE PROTEASE INHIBITOR 88EA; 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   Protease inhibitor {ECO:0000256|ARBA:ARBA00022690};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053097};
KW   Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..438
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001541135"
FT   DOMAIN          47..431
FT                   /note="Serpin"
FT                   /evidence="ECO:0000259|SMART:SM00093"
SQ   SEQUENCE   438 AA;  49720 MW;  C2793F1A91AC9235 CRC64;
     MFLLTAVPLL LAISRISAQC LTGNDVPSLM DPASKISLTD ARYNFALDSL KKAALIETRD
     NVFFSPHSLH QALSLAYFGA RGTTEESLKT ALRIPEHLSK VDVQRYYAFE RSINEMRSQI
     NSSESYEYNV ANRFWITNTK KLRECMLDFF NDQLQVTDFR TNPAQVRNHI NEWISNMTKG
     HIRELLPPNS ISEDTDLVLA NAVYFKGLWA HRFDPKNSQR DIFYSSGMQN SVITFMRQKG
     QFHHHVSEDL GAYVLELPYK GNEISMFVLL PPFSIMYSGQ NPSNEPQDGI RQLVERLATE
     RGSQLLREML QDRMTYREVE VSLPRFELER ELPVAQLLSQ LGAGELFSNS ADLRGFLADG
     EQSLTLGDAV HRARIEVTEE GTTAAAATAI LTFRSSRPMD PAVFKANHPF VYLIYDKTSN
     TILFTGIFRK PETQQPAA
//
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