ID   ALST_TAMSI              Reviewed;         413 AA.
AC   O54759;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Alpha-1-antitrypsin-like protein CM55-ST;
DE   Flags: Precursor;
OS   Tamias sibiricus (Siberian chipmunk) (Eutamias sibiricus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC   Xerinae; Marmotini; Tamias.
OX   NCBI_TaxID=64680;
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   -!- TISSUE SPECIFICITY: Expressed in liver.
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; AB000548; BAA24418.1; -; mRNA.
DR   AlphaFoldDB; O54759; -.
DR   SMR; O54759; -.
DR   MEROPS; I04.001; -.
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; Pyrrolidone carboxylic acid;
KW   Serine protease inhibitor; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..413
FT                   /note="Alpha-1-antitrypsin-like protein CM55-ST"
FT                   /id="PRO_0000032405"
FT   REGION          368..387
FT                   /note="RCL"
FT   SITE            377..378
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         25
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000255"
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        165
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;  46152 MW;  7A04BFD5C520A55A CRC64;
     MPSSISWGLL LLAALSCLGP GSLAQDAQET EASKQDQEHP ASHRIAPHLA EFALSFYRVL
     ARQSNTTNIF FSPVSIATAL AMLSLGTKGD THTQILEGLD FNLTEMAEAD IHQGFQNLLQ
     TLNRPNTQLQ LTSGNGLFID RNLKLLDKFL EDVKSLYHSE AFSTNFTNTQ EARQQINSYV
     EKGTQGKIVE LLKELDRDTV LALVNYIFFK GKWKQPFNEE QTREKDFHVD EATTVRVPMM
     NRLGMFHLHH CSTLASWVLQ MDYLGNATAI FLLPDKGKMQ HLEDTVTTEI LTKFLKNRQT
     TKSQLYFPKV SISGTYDLKD VLSSLGITKV FSSEADLSGV TEEAPLSVSK ALHKAVLDID
     EEGTEAAGGT VLGNIRSTLR YEVIFDRPFL VVIYEHHTKS PLFVGKVVNP TQQ