ALMM_TAMSI
ID ALMM_TAMSI Reviewed; 413 AA.
AC O54757;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=Alpha-1-antitrypsin-like protein CM55-MM;
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], AND TISSUE SPECIFICITY.
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: Protease inhibitor. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in liver. {ECO:0000269|PubMed:9434174}.
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; AB000546; BAA24416.1; -; mRNA.
DR AlphaFoldDB; O54757; -.
DR SMR; O54757; -.
DR MEROPS; I04.001; -.
DR PRIDE; O54757; -.
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; 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 CM55-MM"
FT /id="PRO_0000032403"
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; 46212 MW; D1C37B899BB20B69 CRC64;
MPSSISWGLL LLAALSCLGP GSLAQDAQET EASKKDQEHP ASHRIAPHLA EFALSLYRVL
AHQSNTTNIF FSPVSIATAL AMLSLGTKGD THTQILEGLD FNLTEMAEAD IHQGFQNLLQ
TLNRPNTQLQ LTSGNGLFIH QNLKLLDKFL EDVKSLYHSE ALPTNFTNTE EARQQINSYV
EKGTQGKIVE LVKELHRDTV LALVNYIFFK GKWEEPFNEE DTKEEDFHVD EATTVRVPMM
NRLGMFHLHH CSTLASWVLQ MDYLGNATAI FLLPDKGKMQ HLEDTVTMEI LSKFLKNRET
TLVDLYFPKV SISGTYDLKT VLHSLGITRV FSQEADLSGV TEDAPLTVSK ALHKAVLDIH
EKGTDAAGAT FLEMIPMMLP PDMKFDRPFL VVIYEHHTKS PLFVGKVVNP TLQ
