SPA36_BOVIN
ID SPA36_BOVIN Reviewed; 414 AA.
AC A2I7N2;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 52.
DE RecName: Full=Serpin A3-6;
DE Flags: Precursor;
GN Name=SERPINA3-6 {ECO:0000312|EMBL:ABM55499.1};
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; EF153629; ABM55499.1; -; Genomic_DNA.
DR RefSeq; NP_001139774.1; NM_001146302.1.
DR AlphaFoldDB; A2I7N2; -.
DR SMR; A2I7N2; -.
DR MEROPS; I04.027; -.
DR PRIDE; A2I7N2; -.
DR GeneID; 100272171; -.
DR CTD; 100272171; -.
DR InParanoid; A2I7N2; -.
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..25
FT /evidence="ECO:0000250"
FT CHAIN 26..414
FT /note="Serpin A3-6"
FT /evidence="ECO:0000255"
FT /id="PRO_0000401160"
FT SITE 380..381
FT /note="Reactive bond"
FT /evidence="ECO:0000250|UniProtKB:Q9TTE1"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 414 AA; 46390 MW; 5219AA0735B88A82 CRC64;
MRTERVSPLL ALGILVAGLC SRVHCLPENV TPEEQHKVTS VDGHSLASSN TDFAFSLYKQ
LALKDPNKNV IFSPLSVSIA LAFLSLGAHG PTVTEILEGL KFNLTETPET EIHQGFQHLL
QTFNQPSNQL QLSVGNAIFV QEELKLLDKF IEDARVLYSS EAFPTNFRDP EAAKSLINDY
VKNKTQGKIE ELFKDLSPRT ELVLVNYVYF KAQWKTRFDP KHTEKTEFHV SDNKTVEVPM
MTLDLETPYF RDEELGCTLV ELTYTSNDSA LFILPDKGKM QDLEAKLTPE MLTRWRNSLQ
PRRIHELYLP KFSIKSNYEL NDTLSQMGIK KIFTDADLSG ITGTADLVVS QVVHGAALDV
DEEGTEGAAA TGIGIERTFL RIIVRVNRPF LIAVVLKDTQ SIIFLGKVTN PSEA