ID   SPA35_BOVIN             Reviewed;         411 AA.
AC   A2I7N1;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 57.
DE   RecName: Full=Serpin A3-5;
DE   Flags: Precursor;
GN   Name=SERPINA3-5 {ECO:0000312|EMBL:ABM55498.1};
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; EF153628; ABM55498.1; -; Genomic_DNA.
DR   RefSeq; NP_001075213.1; NM_001081744.1.
DR   AlphaFoldDB; A2I7N1; -.
DR   SMR; A2I7N1; -.
DR   STRING; 9913.ENSBTAP00000009264; -.
DR   MEROPS; I04.027; -.
DR   PaxDb; A2I7N1; -.
DR   PeptideAtlas; A2I7N1; -.
DR   PRIDE; A2I7N1; -.
DR   GeneID; 617667; -.
DR   CTD; 12; -.
DR   eggNOG; KOG2392; Eukaryota.
DR   InParanoid; A2I7N1; -.
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 A3-5"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000401159"
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"
FT   CARBOHYD        318
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   411 AA;  46397 MW;  09CC2860390D7004 CRC64;
     MRAERTSFLL ALGLLMAGIR SVHCLPENVV VKDQRRRVDS HTLASSNTDF AFSLYKQLAL
     KNPNKNVMFS PLSVSMALAF LSLGARGPTL TEILEGLKFN LTEIQETQIH QGFQHLLQAL
     NRPSNQLQLS VGNAMFVQEE LKLLDKFIED ARVLYSSEAF PTNFRDSEAA RSLINDYVKN
     KTQGKIEELF KYLSPRTVLV LVNYIYFKAQ WKTRFDPKHT EQAEFHVSKN KTVEVPMMTL
     DLETPYFRDK ELGCMLVELT YSSNDSALFI LPDEGKMQDL EAKLTPETLT RWRNSLQPRR
     IHELYLPKFS IKSNYELNDT LSQMGIKKIF TDADLSGITG TADLVVSQVV HGAALDVDEE
     GTEGAAATGI GIERTFLRII VRVNRPFLIA VVLKDTQSII FLGKVTNPSE A