ID   SPA32_BOVIN             Reviewed;         411 AA.
AC   A2I7M9;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 54.
DE   RecName: Full=Serpin A3-2;
DE   Flags: Precursor;
GN   Name=SERPINA3-2 {ECO:0000312|EMBL:ABM55496.1};
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 [GENOMIC DNA], AND NOMENCLATURE.
RX   PubMed=18384666; DOI=10.1186/1471-2164-9-151;
RA   Pelissier P., Delourme D., Germot A., Blanchet X., Becila S., Maftah A.,
RA   Leveziel H., Ouali A., Bremaud L.;
RT   "An original SERPINA3 gene cluster: elucidation of genomic organization and
RT   gene expression in the Bos taurus 21q24 region.";
RL   BMC Genomics 9:151-151(2008).
CC   -!- FUNCTION: Serine protease inhibitor. {ECO:0000250|UniProtKB:Q9TTE1}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9TTE1}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle,
CC       chromaffin granule {ECO:0000250|UniProtKB:Q9TTE1}. Secreted
CC       {ECO:0000250|UniProtKB:Q9TTE1}.
CC   -!- SIMILARITY: Belongs to the serpin family. {ECO:0000255}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; EF153626; ABM55496.1; -; Genomic_DNA.
DR   RefSeq; NP_001139773.1; NM_001146301.1.
DR   AlphaFoldDB; A2I7M9; -.
DR   SMR; A2I7M9; -.
DR   MEROPS; I04.027; -.
DR   PeptideAtlas; A2I7M9; -.
DR   PRIDE; A2I7M9; -.
DR   GeneID; 100272170; -.
DR   CTD; 396686; -.
DR   InParanoid; A2I7M9; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0042583; C:chromaffin granule; IEA:UniProtKB-SubCell.
DR   GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; ISS:UniProtKB.
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   3: Inferred from homology;
KW   Cytoplasmic vesicle; Glycoprotein; Protease inhibitor; Reference proteome;
KW   Secreted; Serine protease inhibitor; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000250"
FT   CHAIN           25..411
FT                   /note="Serpin A3-2"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000401157"
FT   SITE            377..378
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250|UniProtKB:Q9TTE1"
FT   CARBOHYD        100
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        180
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        230
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        264
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   411 AA;  46237 MW;  9C13FC47AB2597EE CRC64;
     MRAERTSFLL ALGLLVAGIR SVHCLPENVV VKDQHRRVDG HTLASSNTDF AFSLYKQLAL
     KNPNKNVILS PLSVSIALAF LSLGARGSTL TEILEGLKFN LTEIQEKEIH HSFQHLLQAL
     NQPSNQLQLS VGNAMFVQEE LKLLDKFIED AQVLYSSEAF PTNFRDSEAA RSLINDYVKN
     KTQGKIEELF KYLSPRTELV LVNYIYFKAQ WKTPFDPKHT EQAEFHVSDN KTVEVPMMTL
     DLETPYFRDE ELGCTLVELT YTSNDSALFI LPDEGKMRDL EAKLTPETLT RWRNSLQPRR
     IHELYLPKFS IKSNYELNDI LSQLGIRKIF ANADLSGITG TADLVVSQVV HGAALDVDEE
     GTEGVAATGI GIERTFLRII VRVNRPFLIA VVLKDTQSII FLGKVTNPSE A