ID A0A226EZ78_FOLCA Unreviewed; 444 AA.
AC A0A226EZ78;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Antithrombin-III {ECO:0000313|EMBL:OXA62839.1};
GN ORFNames=Fcan01_04011 {ECO:0000313|EMBL:OXA62839.1};
OS Folsomia candida (Springtail).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC Entomobryomorpha; Isotomoidea; Isotomidae; Proisotominae; Folsomia.
OX NCBI_TaxID=158441 {ECO:0000313|EMBL:OXA62839.1, ECO:0000313|Proteomes:UP000198287};
RN [1] {ECO:0000313|EMBL:OXA62839.1, ECO:0000313|Proteomes:UP000198287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VU population {ECO:0000313|EMBL:OXA62839.1,
RC ECO:0000313|Proteomes:UP000198287};
RC TISSUE=Whole body {ECO:0000313|EMBL:OXA62839.1};
RA Faddeeva A., Derks M.F., Anvar Y., Smit S., Van Straalen N., Roelofs D.;
RT "The genome of Folsomia candida.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the serpin family.
CC {ECO:0000256|RuleBase:RU000411}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OXA62839.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LNIX01000001; OXA62839.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A226EZ78; -.
DR OMA; MTKGHIR; -.
DR OrthoDB; 3218836at2759; -.
DR Proteomes; UP000198287; 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:UP000198287};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..444
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013008350"
FT DOMAIN 55..414
FT /note="Serpin"
FT /evidence="ECO:0000259|SMART:SM00093"
FT REGION 414..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..438
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 444 AA; 48440 MW; 7511F92D72A00493 CRC64;
MNSRVVARSA ILSLILTCAT IMATDTDKCF GAGDVPIDGH NLTGNWTESK LEFTLAMFHS
LYAGENLFFS PHSIHQALVV ALMGARGKTE AQLRSLLNLE NVPKVSLLQH LRADGMHRDS
ICPSSPGVEL RVANKIFVDK SEPLQACVLT HLGPEVEQLD LVNDTEGSRA IMNKWVEEIT
HNKIYSLVPP LPPNSRLAIV NGAYFRGVWE HQFKKSKTKL GLFYSSPTEV VPTYMMHTKG
YYHHGASPEL GAYVLELPYE GDSMSLVLLL PPFSPGAITR TVTALGRGGL KRAMEELAGT
SLEVVLPRFS LSHTLPLTQA LTDLGLTSLF NRSGAELGDF STKPEGLFVE EAIHKAFLEV
NEEGASAGGG TALIGTRSGR PLDQSRFVAN HPFIMGVWDK CRETMLFMGV LHRPQTKGQG
GEGSEENATT TTTTEQVNVN EKKV
//
