SPA32_BOVIN
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}.
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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