ID   ALMS_ICTTR              Reviewed;         413 AA.
AC   O54761;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Alpha-1-antitrypsin-like protein GS55-MS;
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. Its primary target is
CC       elastase, but it also has a moderate affinity for plasmin and thrombin
CC       (By similarity). {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; AB000550; BAA24420.1; -; mRNA.
DR   AlphaFoldDB; O54761; -.
DR   SMR; O54761; -.
DR   MEROPS; I04.001; -.
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..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..413
FT                   /note="Alpha-1-antitrypsin-like protein GS55-MS"
FT                   /id="PRO_0000032400"
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        266
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   413 AA;  45954 MW;  B08D2544695EE0F4 CRC64;
     MPSSISWGLL LLAGLSCLVA GSLAEDAQET GASKHDQEHP ASHRIAPNLA EFALSLYRVL
     AHESNTTNIF FSPVSIAMAL ASLSLGTKAD THTQIMEGLG FNLTETAESD IHQGFQHLLQ
     TLNKPNSQLQ LTTGNGLFID HNLKLLDKFL QDVKNLYHSE AFSTDFTNTE EAKKQINTYV
     EKGTQGKIVD LVKDLNRDSV LALVNYIFFK GKWEKPFEVD HTKEEDFHVD QVTTVRVPMM
     NRMGMFEVHY CSTLASWVLQ MDYLGNATAI FLLPDEGKLQ HLEDTITKEI LAKFLKNRES
     SSVNLHFPKL NISGTMDLKP VLTRLGITNV FSYKADLSGI TEDDPLRVSQ ALHKAVLTID
     ERGTEAAGAT FLEMMPMSLP PEVKFDKPFL VVIIEHSTKS PLFVGKVVNP TLH