A1AT_BOVIN
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 03-AUG-2022, entry version 152.
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.ENSBTAP00000004927; -.
DR MEROPS; I04.001; -.
DR PaxDb; P34955; -.
DR PeptideAtlas; P34955; -.
DR PRIDE; P34955; -.
DR Ensembl; ENSBTAT00000004927; ENSBTAP00000004927; ENSBTAG00000018843.
DR Ensembl; ENSBTAT00000072441; ENSBTAP00000065816; ENSBTAG00000018843.
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; MEAIPMS; -.
DR OrthoDB; 1124079at2759; -.
DR TreeFam; TF343201; -.
DR Reactome; R-BTA-114608; Platelet degranulation.
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-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 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 GO; GO:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
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 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
