SPA35_BOVIN
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