ID   A1AT_CYPCA              Reviewed;         372 AA.
AC   P32759;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Alpha-1-antitrypsin homolog;
DE   Flags: Precursor;
OS   Cyprinus carpio (Common carp).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Cyprininae; Cyprinus.
OX   NCBI_TaxID=7962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Cerebrospinal fluid;
RX   PubMed=7891100; DOI=10.1046/j.1471-4159.1995.64041721.x;
RA   Huang C.-J., Lee M.S., Huang F.-L., Chang G.D.;
RT   "A protease inhibitor of the serpin family is a major protein in carp
RT   perimeningeal fluid: II. cDNA cloning, sequence analysis, and Escherichia
RT   coli expression.";
RL   J. Neurochem. 64:1721-1727(1995).
CC   -!- SUBCELLULAR LOCATION: Secreted.
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; L08689; AAA73953.1; -; mRNA.
DR   PIR; I50492; I50492.
DR   AlphaFoldDB; P32759; -.
DR   SMR; P32759; -.
DR   Proteomes; UP000694384; Unplaced.
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..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..372
FT                   /note="Alpha-1-antitrypsin homolog"
FT                   /id="PRO_0000032407"
FT   REGION          328..347
FT                   /note="RCL"
FT   SITE            337..338
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        214
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        226
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   372 AA;  41900 MW;  D5D67E3E40A91EE9 CRC64;
     MPATCLLHTM LTLPSPSTRN LRSIQMPRAR TFSSPSRYRN GFEHAGCRCQ GSTLSQIYSS
     LGYSGLQASQ VNEGYEHLIH MLGHSREAMQ LEAGAGVAIR EGFKVVDQFL KDVQHYYNSE
     AFSVDFSKPE IAAEEINQFI AKKTNDKITN MVKDLDSDTV MMLINYMYFR GKWDKPFDAQ
     LTHKADFKVD EDTTVQVDMM KRTGRYDIYQ DPVNQTTVMM VPYKGNTSMM IIFPDDGKMK
     ELEESISRHH LKNWHDKLFR SSVDLFMPKF SITATSKLKG ILEDMGVTDA FGDTADLSGL
     TEEVKVKVSQ VVHKAVLSVD EKGTEAAAAT TIEIMPMSLP DTVILNRPFL VLIVEDTTKS
     ILFMGKITNP TE