ID   A1AT_SHEEP              Reviewed;         416 AA.
AC   P12725;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Alpha-1-antiproteinase;
DE   AltName: Full=Alpha-1-antitrypsin;
DE   AltName: Full=Alpha-1-proteinase inhibitor;
DE   Flags: Precursor;
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=2788872; DOI=10.1093/nar/17.15.6398;
RA   Brown W.M., Dziegielewska K.D., Foreman R.C., Saunders N.R., Wu Y.;
RT   "Nucleotide and deduced amino acid sequence of sheep alpha 1 antitrypsin.";
RL   Nucleic Acids Res. 17:6398-6398(1989).
RN   [2]
RP   PROTEIN SEQUENCE OF 25-55.
RC   TISSUE=Plasma;
RX   PubMed=1899999; DOI=10.1042/bj2730685;
RA   Mistry R., Snashall P.D., Totty N., Guz A., Tetley T.D.;
RT   "Isolation and characterization of sheep alpha 1-proteinase inhibitor.";
RL   Biochem. J. 273:685-690(1991).
CC   -!- FUNCTION: Inhibits human leukocyte elastase, pig pancreatic elastase
CC       and bovine trypsin on a 1:1 molar basis.
CC   -!- SUBUNIT: Interacts with CELA2A (By similarity). Interacts with ERGIC3
CC       and LMAN1/ERGIC53 (By similarity). Interacts with PRSS1/Trypsin (By
CC       similarity). {ECO:0000250|UniProtKB:P01009}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Plasma.
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 carboxyl group of the serpin reactive site
CC       and the serine hydroxyl of the protease. The resulting inactive serpin-
CC       protease complex is highly stable (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
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DR   EMBL; X15555; CAA33561.1; -; mRNA.
DR   PIR; S05312; ITSH.
DR   RefSeq; NP_001009799.1; NM_001009799.2.
DR   AlphaFoldDB; P12725; -.
DR   SMR; P12725; -.
DR   STRING; 9940.ENSOARP00000015963; -.
DR   MEROPS; I04.001; -.
DR   PRIDE; P12725; -.
DR   GeneID; 443388; -.
DR   KEGG; oas:443388; -.
DR   CTD; 5265; -.
DR   eggNOG; KOG2392; Eukaryota.
DR   OrthoDB; 1124079at2759; -.
DR   Proteomes; UP000002356; 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   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Phosphoprotein;
KW   Protease inhibitor; Reference proteome; Secreted;
KW   Serine protease inhibitor; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000269|PubMed:1899999"
FT   CHAIN           25..416
FT                   /note="Alpha-1-antiproteinase"
FT                   /id="PRO_0000032399"
FT   REGION          371..390
FT                   /note="RCL"
FT   SITE            380..381
FT                   /note="Reactive bond"
FT   MOD_RES         381
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P01009"
FT   CARBOHYD        68
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        105
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        143
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        269
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        39
FT                   /note="A -> S (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        45
FT                   /note="C -> A (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   416 AA;  45985 MW;  0B4702C0527321BF CRC64;
     MALSITRGLL LLAALCCLAP TSLAGVLQGH AVQETDDTAH QEAACHKIAP NLANFAFSIY
     HKLAHQSNTS NIFFSPVSIA SAFAMLSLGA KGNTHTEILE GLGFNLTELA EAEIHKGFQH
     LLHTLNQPNH QLQLTTGNGL FINESAKLVD TFLEDVKNLH HSKAFSINFR DAEEAKKKIN
     DYVEKGSHGK IVDLVKDLDQ DTVFALVNYI SFKGKWEKPF EVEHTTERDF HVNEQTTVKV
     PMMNRLGMFD LHYCDKLASW VLLLDYVGNV TACFILPDLG KLQQLEDKLN NELLAKFLEK
     KYASSANLHL PKLSISETYD LKTVLGELGI NRVFSNGADL SGITEEQPLM VSKALHKAAL
     TIDEKGTEAA GATFLEAIPM SLPPDVEFNR PFLCILYDRN TKSPLFVGKV VNPTQA