ID   ALLT_ICTTR              Reviewed;         413 AA.
AC   O54762;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Alpha-1-antitrypsin-like protein GS55-LT;
DE   Flags: Precursor;
OS   Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS   tridecemlineatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC   Xerinae; Marmotini; Ictidomys.
OX   NCBI_TaxID=43179;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=9434174; DOI=10.1016/s0378-1119(97)00532-5;
RA   Takamatsu N., Kojima M., Taniyama M., Ohba K., Uematsu T., Segawa C.,
RA   Tsutou S., Watanabe M., Kondo J., Kondo N., Shiba T.;
RT   "Expression of multiple alpha1-antitrypsin-like genes in hibernating
RT   species of the squirrel family.";
RL   Gene 204:127-132(1997).
CC   -!- FUNCTION: Inhibitor of serine proteases. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- DOMAIN: The reactive center loop (RCL) extends out from the body of the
CC       protein and directs binding to the target protease. The protease
CC       cleaves the serpin at the reactive site within the RCL, establishing a
CC       covalent linkage between the serpin reactive site and the active site
CC       of the protease. The resulting inactive serpin-protease complex is
CC       highly stable (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
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DR   EMBL; AB000551; BAA24421.1; -; mRNA.
DR   RefSeq; NP_001299613.1; NM_001312684.1.
DR   AlphaFoldDB; O54762; -.
DR   SMR; O54762; -.
DR   MEROPS; I04.001; -.
DR   GeneID; 101963508; -.
DR   OrthoDB; 1124079at2759; -.
DR   Proteomes; UP000005215; 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   Gene3D; 2.30.39.10; -; 1.
DR   Gene3D; 3.30.497.10; -; 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; PTHR11461; 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   Glycoprotein; Protease inhibitor; Reference proteome; Secreted;
KW   Serine protease inhibitor; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..413
FT                   /note="Alpha-1-antitrypsin-like protein GS55-LT"
FT                   /id="PRO_0000032401"
FT   REGION          368..387
FT                   /note="RCL"
FT   SITE            377..378
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        65
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        102
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        123
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   413 AA;  46025 MW;  8E18A4DD16AD2CA5 CRC64;
     MPSSISWGLL LLAGLSCLAT GCLIEDSEKS DAPKHDQENS ASHKIAPNLA EFAFSLYRVL
     AHESNTTNIF FSPVSIATAL GSLSLGTKAD THTQIMEGVG FNLTEISEAE IHQGFQHLLQ
     NLNKSNSQLQ LTTGNGLFID HNMKLLDKFL EDIKNLYHSE AFSTDFTNTE EAKKQINTYV
     EKGTQGKIVD LVKDLDRDSG LALVNYIFFK GTLEKPFKAD HTMEQDFHVD EATTVRVPMM
     NRLGMFDLHY CPTLSSMVLK MKYLGDITAI FIMPKVGRME YVEETLTKEF LDKLLKKDYT
     GKNTVHFPKL SISGTIDLKP VLTRLGITKV FSHEADLSGI TEDAPLRVSQ ALHKAVLTID
     EKGTEAERHT VKGPMALTLA PEVKFNRPFL VTLYDRSTKS PLFVGRVVNP TLH