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Database: UniProt
Entry: E2A358_CAMFO
LinkDB: E2A358_CAMFO
Original site: E2A358_CAMFO 
ID   E2A358_CAMFO            Unreviewed;       481 AA.
AC   E2A358;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=Antithrombin-III {ECO:0000313|EMBL:EFN72133.1};
GN   ORFNames=EAG_01413 {ECO:0000313|EMBL:EFN72133.1};
OS   Camponotus floridanus (Florida carpenter ant).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Formicinae; Camponotus.
OX   NCBI_TaxID=104421 {ECO:0000313|Proteomes:UP000000311};
RN   [1] {ECO:0000313|EMBL:EFN72133.1, ECO:0000313|Proteomes:UP000000311}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C129 {ECO:0000313|Proteomes:UP000000311};
RX   PubMed=20798317; DOI=10.1126/science.1192428;
RA   Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA   Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA   Wang J., Liebig J.;
RT   "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT   saltator.";
RL   Science 329:1068-1071(2010).
CC   -!- SIMILARITY: Belongs to the serpin family.
CC       {ECO:0000256|RuleBase:RU000411}.
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DR   EMBL; GL436277; EFN72133.1; -; Genomic_DNA.
DR   RefSeq; XP_011250693.1; XM_011252391.2.
DR   AlphaFoldDB; E2A358; -.
DR   STRING; 104421.E2A358; -.
DR   MEROPS; I04.083; -.
DR   EnsemblMetazoa; XM_011252391.3; XP_011250693.1; LOC105247925.
DR   GeneID; 105247925; -.
DR   KEGG; cfo:105247925; -.
DR   InParanoid; E2A358; -.
DR   OMA; MTKGHIR; -.
DR   OrthoDB; 3218836at2759; -.
DR   Proteomes; UP000000311; 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:UP000000311};
KW   Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900}.
FT   DOMAIN          89..472
FT                   /note="Serpin"
FT                   /evidence="ECO:0000259|SMART:SM00093"
SQ   SEQUENCE   481 AA;  53925 MW;  FF84948BA8A72FBA CRC64;
     MVARNLQSCF FSIETRTCCN NRSTNIIADL PIAGISRKCP TMSFFTAMLS LSLAIGMISA
     QCLTGNDVPT MMDPMSKISL TNARIDFALD SLKKAALIES KDNIFFSPHS IHQALSLAYF
     GARGTTESSL KQALRIPEQL SKVDMQRFYA YEKFLNQPRS QNESTDYEYK VANKFWITNS
     RKLRDCMFDF FGDQMQVTDF RTNPAEVRTR INDWVSNMTK GHIRDLLPPN SISGDTDLVL
     ANAAYFKGLW AQRFDPKNSK RDIFYVSGTQ NSVITFMRQK GNFNHVVSEE LGVYILELPY
     KGNDISMFVL LPPFSNARAL SQDSEPQDGI RQLVERLATE KGSRELRQLL DDGMPPREVE
     VNLPRFELER ELQLNQLLYA LGAGELLSPG AADLRGFVAD GESSLHLGDA IHRARIEVTE
     EGTTAAAATA IFTFRSSRPT EPAIFNANHP FVYLIYDKRD HIVLFAGIFR SPANSLASGA
     V
//
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