ID   A1AT_BOVIN              Reviewed;         416 AA.
AC   P34955; Q3SZS3;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   24-JAN-2024, entry version 159.
DE   RecName: Full=Alpha-1-antiproteinase;
DE   AltName: Full=Alpha-1-antitrypsin;
DE   AltName: Full=Alpha-1-proteinase inhibitor;
DE   AltName: Full=Serpin A1;
DE   Flags: Precursor;
GN   Name=SERPINA1; Synonyms=PI;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=1562597; DOI=10.1016/0167-4781(92)90530-d;
RA   Sinha D., Bakhshi M.R., Kirby E.P.;
RT   "Complete cDNA sequence of bovine alpha 1-antitrypsin.";
RL   Biochim. Biophys. Acta 1130:209-212(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   CHARACTERIZATION.
RX   PubMed=8056747; DOI=10.1093/oxfordjournals.jbchem.a124348;
RA   Sinha D., Yang X., Emig F., Kirby E.P.;
RT   "Isolation and characterization of two protease inhibitors from bovine
RT   plasma.";
RL   J. Biochem. 115:387-391(1994).
RN   [5]
RP   INTERACTION WITH PRSS1.
RX   PubMed=11057674; DOI=10.1038/35038119;
RA   Huntington J.A., Read R.J., Carrell R.W.;
RT   "Structure of a serpin-protease complex shows inhibition by deformation.";
RL   Nature 407:923-926(2000).
CC   -!- FUNCTION: Inhibitor of serine proteases. Its primary target is
CC       elastase, but it also has a moderate affinity for plasmin and thrombin.
CC       Inhibits trypsin, chymotrypsin and plasminogen activator (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with CELA2A (By similarity). Interacts with ERGIC3
CC       and LMAN1/ERGIC53 (By similarity). Interacts with PRSS1/Trypsin
CC       (PubMed:11057674). {ECO:0000250|UniProtKB:P01009,
CC       ECO:0000269|PubMed:11057674}.
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; X63129; CAA44840.1; -; mRNA.
DR   EMBL; BT025459; ABF57415.1; -; mRNA.
DR   EMBL; BC102730; AAI02731.1; -; mRNA.
DR   PIR; S21097; S21097.
DR   RefSeq; NP_776307.1; NM_173882.2.
DR   RefSeq; XP_005222164.1; XM_005222107.2.
DR   AlphaFoldDB; P34955; -.
DR   SMR; P34955; -.
DR   STRING; 9913.ENSBTAP00000065816; -.
DR   MEROPS; I04.001; -.
DR   GlyCosmos; P34955; 4 sites, No reported glycans.
DR   PaxDb; 9913-ENSBTAP00000004927; -.
DR   PeptideAtlas; P34955; -.
DR   Ensembl; ENSBTAT00000004927.4; ENSBTAP00000004927.3; ENSBTAG00000018843.6.
DR   Ensembl; ENSBTAT00000072441.1; ENSBTAP00000065816.1; ENSBTAG00000018843.6.
DR   GeneID; 280699; -.
DR   KEGG; bta:280699; -.
DR   CTD; 5265; -.
DR   VEuPathDB; HostDB:ENSBTAG00000018843; -.
DR   VGNC; VGNC:53953; SERPINA1.
DR   eggNOG; KOG2392; Eukaryota.
DR   GeneTree; ENSGT00940000154493; -.
DR   HOGENOM; CLU_023330_2_1_1; -.
DR   InParanoid; P34955; -.
DR   OMA; MEIMPMS; -.
DR   OrthoDB; 3218836at2759; -.
DR   TreeFam; TF343201; -.
DR   Reactome; R-BTA-114608; Platelet degranulation.
DR   Reactome; R-BTA-204005; COPII-mediated vesicle transport.
DR   Reactome; R-BTA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR   Reactome; R-BTA-5694530; Cargo concentration in the ER.
DR   Reactome; R-BTA-6798695; Neutrophil degranulation.
DR   Reactome; R-BTA-8957275; Post-translational protein phosphorylation.
DR   Proteomes; UP000009136; Chromosome 21.
DR   Bgee; ENSBTAG00000018843; Expressed in liver and 72 other cell types or tissues.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0002020; F:protease binding; IEA:Ensembl.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central.
DR   CDD; cd02056; serpinA1_A1AT; 1.
DR   Gene3D; 2.30.39.10; Alpha-1-antitrypsin, domain 1; 1.
DR   Gene3D; 3.30.497.10; Antithrombin, subunit I, domain 2; 1.
DR   Gene3D; 2.10.310.10; Serpins superfamily; 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:SF165; ALPHA-1-ANTITRYPSIN; 1.
DR   PANTHER; PTHR11461; SERINE PROTEASE INHIBITOR, SERPIN; 1.
DR   Pfam; PF00079; Serpin; 1.
DR   SMART; SM00093; SERPIN; 1.
DR   SUPFAM; SSF56574; Serpins; 1.
DR   PROSITE; PS00284; SERPIN; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Phosphoprotein; Protease inhibitor; Reference proteome;
KW   Secreted; Serine protease inhibitor; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000250"
FT   CHAIN           25..416
FT                   /note="Alpha-1-antiproteinase"
FT                   /id="PRO_0000032380"
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"
SQ   SEQUENCE   416 AA;  46104 MW;  3280CDAF42DA35E2 CRC64;
     MALSITRGLL LLAALCCLAP ISLAGVLQGH AVQETDDTSH QEAACHKIAP NLANFAFSIY
     HHLAHQSNTS NIFFSPVSIA SAFAMLSLGA KGNTHTEILK GLGFNLTELA EAEIHKGFQH
     LLHTLNQPNH QLQLTTGNGL FINESAKLVD TFLEDVKNLY HSEAFSINFR DAEEAKKKIN
     DYVEKGSHGK IVELVKVLDP NTVFALVNYI SFKGKWEKPF EMKHTTERDF HVDEQTTVKV
     PMMNRLGMFD LHYCDKLASW VLLLDYVGNV TACFILPDLG KLQQLEDKLN NELLAKFLEK
     KYASSANLHL PKLSISETYD LKSVLGDVGI TEVFSDRADL SGITKEQPLK VSKALHKAAL
     TIDEKGTEAV GSTFLEAIPM SLPPDVEFNR PFLCILYDRN TKSPLFVGKV VNPTQA
//