ID   SPA34_BOVIN             Reviewed;         411 AA.
AC   A2I7N0;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=Serpin A3-4;
DE   Flags: Precursor;
GN   Name=SERPINA3-4 {ECO:0000312|EMBL:ABM55497.1};
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}.
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DR   EMBL; EF153627; ABM55497.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2I7N0; -.
DR   SMR; A2I7N0; -.
DR   MEROPS; I04.027; -.
DR   PeptideAtlas; A2I7N0; -.
DR   PRIDE; A2I7N0; -.
DR   InParanoid; A2I7N0; -.
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 A3-4"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000401158"
FT   SITE            377..378
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250|UniProtKB:Q9TTE1"
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"
FT   CARBOHYD        318
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   411 AA;  46311 MW;  905F034685847C35 CRC64;
     MRAERLSPLL ALGLLVAGIR SVHCLPENVV VKDRHRRVDG HTLASSNTDF AFSLYKQLAL
     KDPNKNVMFS PLSVSMALAF LSLGARGPTL TEILEGLKFN PTEIQETQIH QGFQHLLQAL
     NRPRNQLQLS VGNAMFVQEE LKLLDKFIED ARVLYSSEAF PTNFRDPEAA KSLINDYVKN
     KTQGKIEELF KDLSPRTELV LVNYVYFKAQ WKTRFDPKHT EQAEFHVSDN KTVEVPMMTL
     DLETPYFRDE ELGCTLVELT YTSNDSALFI LPDKGKMQDL EAKLTPEMLT RWRNSLQPRR
     IHELYLPKFS IKSNYELNDT LSQMGIKKIF TDADLSGITG TADLVVSQVV HGAALDVDEE
     GTEGAAATGI GIERTFLRII VRVNRPFLIA VVLKDTQSII FLGKVTNPSE A